- INFO: Beginning work on ANXA5... {November 14, 2007 4:51:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:52:00 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ANXA5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a8a.
| PDB = {{PDB2|1a8a}}, {{PDB2|1a8b}}, {{PDB2|1anw}}, {{PDB2|1anx}}, {{PDB2|1avh}}, {{PDB2|1avr}}, {{PDB2|1bc0}}, {{PDB2|1bc1}}, {{PDB2|1bc3}}, {{PDB2|1bcw}}, {{PDB2|1bcy}}, {{PDB2|1bcz}}, {{PDB2|1g5n}}, {{PDB2|1hak}}, {{PDB2|1hvd}}, {{PDB2|1hve}}, {{PDB2|1hvf}}, {{PDB2|1hvg}}, {{PDB2|1n41}}, {{PDB2|1n42}}, {{PDB2|1n44}}, {{PDB2|1sav}}, {{PDB2|2ie6}}, {{PDB2|2ie7}}, {{PDB2|2ran}}
| Name = Annexin A5
| HGNCid = 543
| Symbol = ANXA5
| AltSymbols =; ANX5; ENX2; PP4
| OMIM = 131230
| ECnumber =
| Homologene = 20312
| MGIid = 106008
| GeneAtlas_image1 = PBB_GE_ANXA5_200782_at_tn.png
| Function = {{GNF_GO|id=GO:0004859 |text = phospholipase inhibitor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005544 |text = calcium-dependent phospholipid binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0050819 |text = negative regulation of coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 308
| Hs_Ensembl = ENSG00000164111
| Hs_RefseqProtein = NP_001145
| Hs_RefseqmRNA = NM_001154
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 122808598
| Hs_GenLoc_end = 122837626
| Hs_Uniprot = P08758
| Mm_EntrezGene = 11747
| Mm_Ensembl = ENSMUSG00000027712
| Mm_RefseqmRNA = NM_009673
| Mm_RefseqProtein = NP_033803
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 36640893
| Mm_GenLoc_end = 36656884
| Mm_Uniprot = Q3U5Q1
}}
}}
'''Annexin A5''', also known as '''ANXA5''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the annexin family of calcium-dependent phospholipid binding proteins some of which have been implicated in membrane-related events along exocytotic and endocytotic pathways. Annexin 5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel activity and a potential role in cellular signal transduction, inflammation, growth and differentiation. Annexin 5 has also been described as placental anticoagulant protein I, vascular anticoagulant-alpha, endonexin II, lipocortin V, placental protein 4 and anchorin CII. The gene spans 29 kb containing 13 exons, and encodes a single transcript of approximately 1.6 kb and a protein product with a molecular weight of about 35 kDa.<ref>{{cite web | title = Entrez Gene: ANXA5 annexin A5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=308| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cederholm A, Frostegård J |title=Annexin A5 as a novel player in prevention of atherothrombosis in SLE and in the general population. |journal=Ann. N. Y. Acad. Sci. |volume=1108 |issue= |pages= 96-103 |year= 2007 |pmid= 17893975 |doi= }}
*{{cite journal | author=Schlaepfer DD, Jones J, Haigler HT |title=Inhibition of protein kinase C by annexin V. |journal=Biochemistry |volume=31 |issue= 6 |pages= 1886-91 |year= 1992 |pmid= 1310621 |doi= }}
*{{cite journal | author=Huber R, Berendes R, Burger A, ''et al.'' |title=Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. |journal=J. Mol. Biol. |volume=223 |issue= 3 |pages= 683-704 |year= 1992 |pmid= 1311770 |doi= }}
*{{cite journal | author=Kirsch T, Pfäffle M |title=Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins. |journal=FEBS Lett. |volume=310 |issue= 2 |pages= 143-7 |year= 1992 |pmid= 1397263 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Tait JF, Frankenberry DA, Shiang R, ''et al.'' |title=Chromosomal localization of the human gene for annexin V (placental anticoagulant protein I) to 4q26----q28. |journal=Cytogenet. Cell Genet. |volume=57 |issue= 4 |pages= 187-92 |year= 1992 |pmid= 1683830 |doi= }}
*{{cite journal | author=Huber R, Römisch J, Paques EP |title=The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. |journal=EMBO J. |volume=9 |issue= 12 |pages= 3867-74 |year= 1991 |pmid= 2147412 |doi= }}
*{{cite journal | author=Huber R, Schneider M, Mayr I, ''et al.'' |title=The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. |journal=FEBS Lett. |volume=275 |issue= 1-2 |pages= 15-21 |year= 1991 |pmid= 2148156 |doi= }}
*{{cite journal | author=Maurer-Fogy I, Reutelingsperger CP, Pieters J, ''et al.'' |title=Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein. |journal=Eur. J. Biochem. |volume=174 |issue= 4 |pages= 585-92 |year= 1988 |pmid= 2455636 |doi= }}
*{{cite journal | author=Rothhut B, Coméra C, Cortial S, ''et al.'' |title=A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation. |journal=Biochem. J. |volume=263 |issue= 3 |pages= 929-35 |year= 1990 |pmid= 2532007 |doi= }}
*{{cite journal | author=Schlaepfer DD, Mehlman T, Burgess WH, Haigler HT |title=Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 17 |pages= 6078-82 |year= 1987 |pmid= 2957692 |doi= }}
*{{cite journal | author=Funakoshi T, Heimark RL, Hendrickson LE, ''et al.'' |title=Human placental anticoagulant protein: isolation and characterization. |journal=Biochemistry |volume=26 |issue= 17 |pages= 5572-8 |year= 1987 |pmid= 2960376 |doi= }}
*{{cite journal | author=Iwasaki A, Suda M, Nakao H, ''et al.'' |title=Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 1261-73 |year= 1988 |pmid= 2963810 |doi= }}
*{{cite journal | author=Funakoshi T, Hendrickson LE, McMullen BA, Fujikawa K |title=Primary structure of human placental anticoagulant protein. |journal=Biochemistry |volume=26 |issue= 25 |pages= 8087-92 |year= 1988 |pmid= 2964863 |doi= }}
*{{cite journal | author=Kaplan R, Jaye M, Burgess WH, ''et al.'' |title=Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein. |journal=J. Biol. Chem. |volume=263 |issue= 17 |pages= 8037-43 |year= 1988 |pmid= 2967291 |doi= }}
*{{cite journal | author=Grundmann U, Abel KJ, Bohn H, ''et al.'' |title=Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3708-12 |year= 1988 |pmid= 2967495 |doi= }}
*{{cite journal | author=Pepinsky RB, Tizard R, Mattaliano RJ, ''et al.'' |title=Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. |journal=J. Biol. Chem. |volume=263 |issue= 22 |pages= 10799-811 |year= 1988 |pmid= 2968983 |doi= }}
*{{cite journal | author=Ahn NG, Teller DC, Bienkowski MJ, ''et al.'' |title=Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18657-63 |year= 1989 |pmid= 2974032 |doi= }}
*{{cite journal | author=Demange P, Voges D, Benz J, ''et al.'' |title=Annexin V: the key to understanding ion selectivity and voltage regulation? |journal=Trends Biochem. Sci. |volume=19 |issue= 7 |pages= 272-6 |year= 1994 |pmid= 7519374 |doi= }}
*{{cite journal | author=Fernández MP, Morgan RO, Fernández MR, Carcedo MT |title=The gene encoding human annexin V has a TATA-less promoter with a high G+C content. |journal=Gene |volume=149 |issue= 2 |pages= 253-60 |year= 1994 |pmid= 7958998 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ARF6... {November 14, 2007 4:52:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:52:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ARF6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e0s.
| PDB = {{PDB2|1e0s}}, {{PDB2|2a5d}}, {{PDB2|2a5f}}, {{PDB2|2a5g}}, {{PDB2|2j5x}}
| Name = ADP-ribosylation factor 6
| HGNCid = 659
| Symbol = ARF6
| AltSymbols =;
| OMIM = 600464
| ECnumber =
| Homologene = 1256
| MGIid = 99435
| GeneAtlas_image1 = PBB_GE_ARF6_203311_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARF6_203312_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005938 |text = cell cortex}}
| Process = {{GNF_GO|id=GO:0006888 |text = ER to Golgi vesicle-mediated transport}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}} {{GNF_GO|id=GO:0030838 |text = positive regulation of actin filament polymerization}} {{GNF_GO|id=GO:0030866 |text = cortical actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0031529 |text = ruffle organization and biogenesis}} {{GNF_GO|id=GO:0035020 |text = regulation of Rac protein signal transduction}} {{GNF_GO|id=GO:0048261 |text = negative regulation of receptor mediated endocytosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 382
| Hs_Ensembl = ENSG00000165527
| Hs_RefseqProtein = NP_001654
| Hs_RefseqmRNA = NM_001663
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 49429589
| Hs_GenLoc_end = 49431484
| Hs_Uniprot = P62330
| Mm_EntrezGene = 11845
| Mm_Ensembl = ENSMUSG00000044147
| Mm_RefseqmRNA = NM_007481
| Mm_RefseqProtein = NP_031507
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 70290755
| Mm_GenLoc_end = 70292386
| Mm_Uniprot = Q3U0D7
}}
}}
'''ADP-ribosylation factor 6''', also known as '''ARF6''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the human ARF gene family, which is part of the RAS superfamily. The ARF genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The product of this gene is localized to the plasma membrane, and regulates vesicular trafficking, remodelling of membrane lipids, and signaling pathways that lead to actin remodeling. A pseudogene of this gene is located on chromosome 7.<ref>{{cite web | title = Entrez Gene: ARF6 ADP-ribosylation factor 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=382| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sabe H |title=Requirement for Arf6 in cell adhesion, migration, and cancer cell invasion. |journal=J. Biochem. |volume=134 |issue= 4 |pages= 485-9 |year= 2004 |pmid= 14607973 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Tsuchiya M, Price SR, Tsai SC, ''et al.'' |title=Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. |journal=J. Biol. Chem. |volume=266 |issue= 5 |pages= 2772-7 |year= 1991 |pmid= 1993656 |doi= }}
*{{cite journal | author=Stearns T, Willingham MC, Botstein D, Kahn RA |title=ADP-ribosylation factor is functionally and physically associated with the Golgi complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 1238-42 |year= 1990 |pmid= 2105501 |doi= }}
*{{cite journal | author=D'Souza-Schorey C, Stahl PD |title=Myristoylation is required for the intracellular localization and endocytic function of ARF6. |journal=Exp. Cell Res. |volume=221 |issue= 1 |pages= 153-9 |year= 1995 |pmid= 7589240 |doi= 10.1006/excr.1995.1362 }}
*{{cite journal | author=D'Souza-Schorey C, Li G, Colombo MI, Stahl PD |title=A regulatory role for ARF6 in receptor-mediated endocytosis. |journal=Science |volume=267 |issue= 5201 |pages= 1175-8 |year= 1995 |pmid= 7855600 |doi= }}
*{{cite journal | author=Welsh CF, Moss J, Vaughan M |title=ADP-ribosylation factors: a family of approximately 20-kDa guanine nucleotide-binding proteins that activate cholera toxin. |journal=Mol. Cell. Biochem. |volume=138 |issue= 1-2 |pages= 157-66 |year= 1995 |pmid= 7898460 |doi= }}
*{{cite journal | author=Amor JC, Harrison DH, Kahn RA, Ringe D |title=Structure of the human ADP-ribosylation factor 1 complexed with GDP. |journal=Nature |volume=372 |issue= 6507 |pages= 704-8 |year= 1995 |pmid= 7990966 |doi= 10.1038/372704a0 }}
*{{cite journal | author=Orcl L, Palmer DJ, Amherdt M, Rothman JE |title=Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. |journal=Nature |volume=364 |issue= 6439 |pages= 732-4 |year= 1993 |pmid= 8355790 |doi= 10.1038/364732a0 }}
*{{cite journal | author=Helms JB, Palmer DJ, Rothman JE |title=Two distinct populations of ARF bound to Golgi membranes. |journal=J. Cell Biol. |volume=121 |issue= 4 |pages= 751-60 |year= 1993 |pmid= 8491770 |doi= }}
*{{cite journal | author=Cavenagh MM, Whitney JA, Carroll K, ''et al.'' |title=Intracellular distribution of Arf proteins in mammalian cells. Arf6 is uniquely localized to the plasma membrane. |journal=J. Biol. Chem. |volume=271 |issue= 36 |pages= 21767-74 |year= 1996 |pmid= 8702973 |doi= }}
*{{cite journal | author=D'Souza-Schorey C, Boshans RL, McDonough M, ''et al.'' |title=A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. |journal=EMBO J. |volume=16 |issue= 17 |pages= 5445-54 |year= 1997 |pmid= 9312003 |doi= 10.1093/emboj/16.17.5445 }}
*{{cite journal | author=Frank S, Upender S, Hansen SH, Casanova JE |title=ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6. |journal=J. Biol. Chem. |volume=273 |issue= 1 |pages= 23-7 |year= 1998 |pmid= 9417041 |doi= }}
*{{cite journal | author=Yang CZ, Heimberg H, D'Souza-Schorey C, ''et al.'' |title=Subcellular distribution and differential expression of endogenous ADP-ribosylation factor 6 in mammalian cells. |journal=J. Biol. Chem. |volume=273 |issue= 7 |pages= 4006-11 |year= 1998 |pmid= 9461590 |doi= }}
*{{cite journal | author=Mao M, Fu G, Wu JS, ''et al.'' |title=Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 14 |pages= 8175-80 |year= 1998 |pmid= 9653160 |doi= }}
*{{cite journal | author=Andreev J, Simon JP, Sabatini DD, ''et al.'' |title=Identification of a new Pyk2 target protein with Arf-GAP activity. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 2338-50 |year= 1999 |pmid= 10022920 |doi= }}
*{{cite journal | author=Radhakrishna H, Al-Awar O, Khachikian Z, Donaldson JG |title=ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. |journal=J. Cell. Sci. |volume=112 ( Pt 6) |issue= |pages= 855-66 |year= 1999 |pmid= 10036235 |doi= }}
*{{cite journal | author=Kim HS |title=Assignment of the human ADP-ribosylation factor 6 (ARF6) gene to chromosome 7q22.1 by radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 94 |year= 1999 |pmid= 10343114 |doi= }}
*{{cite journal | author=Langille SE, Patki V, Klarlund JK, ''et al.'' |title=ADP-ribosylation factor 6 as a target of guanine nucleotide exchange factor GRP1. |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 27099-104 |year= 1999 |pmid= 10480924 |doi= }}
*{{cite journal | author=Honda A, Nogami M, Yokozeki T, ''et al.'' |title=Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. |journal=Cell |volume=99 |issue= 5 |pages= 521-32 |year= 1999 |pmid= 10589680 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATP7A... {November 14, 2007 4:52:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:53:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ATP7A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aw0.
| PDB = {{PDB2|1aw0}}, {{PDB2|1kvi}}, {{PDB2|1kvj}}, {{PDB2|1q8l}}, {{PDB2|1s6o}}, {{PDB2|1s6u}}, {{PDB2|1y3j}}, {{PDB2|1y3k}}, {{PDB2|1yjr}}, {{PDB2|1yjt}}, {{PDB2|1yju}}, {{PDB2|1yjv}}, {{PDB2|2aw0}}, {{PDB2|2g9o}}, {{PDB2|2ga7}}
| Name = ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome)
| HGNCid = 869
| Symbol = ATP7A
| AltSymbols =; MK; MNK
| OMIM = 300011
| ECnumber =
| Homologene = 35
| MGIid = 99400
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004008 |text = copper-exporting ATPase activity}} {{GNF_GO|id=GO:0005375 |text = copper ion transmembrane transporter activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015097 |text = mercury ion transmembrane transporter activity}} {{GNF_GO|id=GO:0015662 |text = ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}} {{GNF_GO|id=GO:0032767 |text = copper-dependent protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046873 |text = metal ion transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005770 |text = late endosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005802 |text = trans-Golgi network}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0030140 |text = trans-Golgi network transport vesicle}} {{GNF_GO|id=GO:0030173 |text = integral to Golgi membrane}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006825 |text = copper ion transport}} {{GNF_GO|id=GO:0006878 |text = cellular copper ion homeostasis}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0015694 |text = mercury ion transport}} {{GNF_GO|id=GO:0030001 |text = metal ion transport}} {{GNF_GO|id=GO:0051353 |text = positive regulation of oxidoreductase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 538
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000043
| Hs_RefseqmRNA = NM_000052
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11977
| Mm_Ensembl = ENSMUSG00000033792
| Mm_RefseqmRNA = NM_009726
| Mm_RefseqProtein = NP_033856
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 102230043
| Mm_GenLoc_end = 102327470
| Mm_Uniprot = Q3T9Y7
}}
}}
'''ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome)''', also known as '''ATP7A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Harris ED, Reddy MC, Qian Y, ''et al.'' |title=Multiple forms of the Menkes Cu-ATPase. |journal=Adv. Exp. Med. Biol. |volume=448 |issue= |pages= 39-51 |year= 1999 |pmid= 10079814 |doi= }}
*{{cite journal | author=Tümer Z, Møller LB, Horn N |title=Mutation spectrum of ATP7A, the gene defective in Menkes disease. |journal=Adv. Exp. Med. Biol. |volume=448 |issue= |pages= 83-95 |year= 1999 |pmid= 10079817 |doi= }}
*{{cite journal | author=Cox DW, Moore SD |title=Copper transporting P-type ATPases and human disease. |journal=J. Bioenerg. Biomembr. |volume=34 |issue= 5 |pages= 333-8 |year= 2003 |pmid= 12539960 |doi= }}
*{{cite journal | author=Voskoboinik I, Camakaris J |title=Menkes copper-translocating P-type ATPase (ATP7A): biochemical and cell biology properties, and role in Menkes disease. |journal=J. Bioenerg. Biomembr. |volume=34 |issue= 5 |pages= 363-71 |year= 2003 |pmid= 12539963 |doi= }}
*{{cite journal | author=La Fontaine S, Mercer JF |title=Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis. |journal=Arch. Biochem. Biophys. |volume=463 |issue= 2 |pages= 149-67 |year= 2007 |pmid= 17531189 |doi= 10.1016/j.abb.2007.04.021 }}
*{{cite journal | author=Lutsenko S, LeShane ES, Shinde U |title=Biochemical basis of regulation of human copper-transporting ATPases. |journal=Arch. Biochem. Biophys. |volume=463 |issue= 2 |pages= 134-48 |year= 2007 |pmid= 17562324 |doi= 10.1016/j.abb.2007.04.013 }}
*{{cite journal | author=Dierick HA, Ambrosini L, Spencer J, ''et al.'' |title=Molecular structure of the Menkes disease gene (ATP7A). |journal=Genomics |volume=28 |issue= 3 |pages= 462-9 |year= 1996 |pmid= 7490081 |doi= 10.1006/geno.1995.1175 }}
*{{cite journal | author=Tümer Z, Vural B, Tønnesen T, ''et al.'' |title=Characterization of the exon structure of the Menkes disease gene using vectorette PCR. |journal=Genomics |volume=26 |issue= 3 |pages= 437-42 |year= 1995 |pmid= 7607665 |doi= }}
*{{cite journal | author=Kaler SG, Gallo LK, Proud VK, ''et al.'' |title=Occipital horn syndrome and a mild Menkes phenotype associated with splice site mutations at the MNK locus. |journal=Nat. Genet. |volume=8 |issue= 2 |pages= 195-202 |year= 1995 |pmid= 7842019 |doi= 10.1038/ng1094-195 }}
*{{cite journal | author=Das S, Levinson B, Whitney S, ''et al.'' |title=Diverse mutations in patients with Menkes disease often lead to exon skipping. |journal=Am. J. Hum. Genet. |volume=55 |issue= 5 |pages= 883-9 |year= 1994 |pmid= 7977350 |doi= }}
*{{cite journal | author=Chelly J, Tümer Z, Tønnesen T, ''et al.'' |title=Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein. |journal=Nat. Genet. |volume=3 |issue= 1 |pages= 14-9 |year= 1993 |pmid= 8490646 |doi= 10.1038/ng0193-14 }}
*{{cite journal | author=Mercer JF, Livingston J, Hall B, ''et al.'' |title=Isolation of a partial candidate gene for Menkes disease by positional cloning. |journal=Nat. Genet. |volume=3 |issue= 1 |pages= 20-5 |year= 1993 |pmid= 8490647 |doi= 10.1038/ng0193-20 }}
*{{cite journal | author=Vulpe C, Levinson B, Whitney S, ''et al.'' |title=Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. |journal=Nat. Genet. |volume=3 |issue= 1 |pages= 7-13 |year= 1993 |pmid= 8490659 |doi= 10.1038/ng0193-7 }}
*{{cite journal | author=Levinson B, Conant R, Schnur R, ''et al.'' |title=A repeated element in the regulatory region of the MNK gene and its deletion in a patient with occipital horn syndrome. |journal=Hum. Mol. Genet. |volume=5 |issue= 11 |pages= 1737-42 |year= 1997 |pmid= 8923001 |doi= }}
*{{cite journal | author=Yamaguchi Y, Heiny ME, Suzuki M, Gitlin JD |title=Biochemical characterization and intracellular localization of the Menkes disease protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 24 |pages= 14030-5 |year= 1997 |pmid= 8943055 |doi= }}
*{{cite journal | author=Petris MJ, Mercer JF, Culvenor JG, ''et al.'' |title=Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. |journal=EMBO J. |volume=15 |issue= 22 |pages= 6084-95 |year= 1997 |pmid= 8947031 |doi= }}
*{{cite journal | author=Tümer Z, Lund C, Tolshave J, ''et al.'' |title=Identification of point mutations in 41 unrelated patients affected with Menkes disease. |journal=Am. J. Hum. Genet. |volume=60 |issue= 1 |pages= 63-71 |year= 1997 |pmid= 8981948 |doi= }}
*{{cite journal | author=Dierick HA, Adam AN, Escara-Wilke JF, Glover TW |title=Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network. |journal=Hum. Mol. Genet. |volume=6 |issue= 3 |pages= 409-16 |year= 1997 |pmid= 9147644 |doi= }}
*{{cite journal | author=Ronce N, Moizard MP, Robb L, ''et al.'' |title=A C2055T transition in exon 8 of the ATP7A gene is associated with exon skipping in an occipital horn syndrome family. |journal=Am. J. Hum. Genet. |volume=61 |issue= 1 |pages= 233-8 |year= 1997 |pmid= 9246006 |doi= }}
*{{cite journal | author=Gitschier J, Moffat B, Reilly D, ''et al.'' |title=Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. |journal=Nat. Struct. Biol. |volume=5 |issue= 1 |pages= 47-54 |year= 1998 |pmid= 9437429 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BMPR2... {November 14, 2007 4:53:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:54:00 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BMPR2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2hlq.
| PDB = {{PDB2|2hlq}}, {{PDB2|2hlr}}
| Name = Bone morphogenetic protein receptor, type II (serine/threonine kinase)
| HGNCid = 1078
| Symbol = BMPR2
| AltSymbols =; BMPR-II; BMPR3; BMR2; BRK-3; T-ALK
| OMIM = 600799
| ECnumber =
| Homologene = 929
| MGIid = 1095407
| GeneAtlas_image1 = PBB_GE_BMPR2_209920_at_tn.png
| GeneAtlas_image2 = PBB_GE_BMPR2_210214_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005024 |text = transforming growth factor beta receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007178 |text = transmembrane receptor protein serine/threonine kinase signaling pathway}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 659
| Hs_Ensembl = ENSG00000204217
| Hs_RefseqProtein = NP_001195
| Hs_RefseqmRNA = NM_001204
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 202949916
| Hs_GenLoc_end = 203140719
| Hs_Uniprot = Q13873
| Mm_EntrezGene = 12168
| Mm_Ensembl = ENSMUSG00000067336
| Mm_RefseqmRNA = NM_007561
| Mm_RefseqProtein = NP_031587
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 59709199
| Mm_GenLoc_end = 59815028
| Mm_Uniprot = Q3UER5
}}
}}
'''Bone morphogenetic protein receptor, type II (serine/threonine kinase)''', also known as '''BMPR2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the bone morphogenetic protein (BMP) receptor family of transmembrane serine/threonine kinases. The ligands of this receptor are BMPs, which are members of the TGF-beta superfamily. BMPs are involved in endochondral bone formation and embryogenesis. These proteins transduce their signals through the formation of heteromeric complexes of 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding. Mutations in this gene have been associated with primary pulmonary hypertension.<ref>{{cite web | title = Entrez Gene: BMPR2 bone morphogenetic protein receptor, type II (serine/threonine kinase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=659| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=De Caestecker M, Meyrick B |title=Bone morphogenetic proteins, genetics and the pathophysiology of primary pulmonary hypertension. |journal=Respir. Res. |volume=2 |issue= 4 |pages= 193-7 |year= 2002 |pmid= 11686884 |doi= }}
*{{cite journal | author=Sztrymf B, Yaïci A, Girerd B, Humbert M |title=Genes and pulmonary arterial hypertension. |journal=Respiration; international review of thoracic diseases |volume=74 |issue= 2 |pages= 123-32 |year= 2007 |pmid= 17318011 |doi= 10.1159/000098818 }}
*{{cite journal | author=Rosenzweig BL, Imamura T, Okadome T, ''et al.'' |title=Cloning and characterization of a human type II receptor for bone morphogenetic proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7632-6 |year= 1995 |pmid= 7644468 |doi= }}
*{{cite journal | author=Nohno T, Ishikawa T, Saito T, ''et al.'' |title=Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22522-6 |year= 1995 |pmid= 7673243 |doi= }}
*{{cite journal | author=Liu F, Ventura F, Doody J, Massagué J |title=Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. |journal=Mol. Cell. Biol. |volume=15 |issue= 7 |pages= 3479-86 |year= 1995 |pmid= 7791754 |doi= }}
*{{cite journal | author=Kawabata M, Chytil A, Moses HL |title=Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 5625-30 |year= 1995 |pmid= 7890683 |doi= }}
*{{cite journal | author=Ishidou Y, Kitajima I, Obama H, ''et al.'' |title=Enhanced expression of type I receptors for bone morphogenetic proteins during bone formation. |journal=J. Bone Miner. Res. |volume=10 |issue= 11 |pages= 1651-9 |year= 1996 |pmid= 8592941 |doi= }}
*{{cite journal | author=Nishitoh H, Ichijo H, Kimura M, ''et al.'' |title=Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21345-52 |year= 1996 |pmid= 8702914 |doi= }}
*{{cite journal | author=Wu X, Robinson CE, Fong HW, Gimble JM |title=Analysis of the native murine bone morphogenetic protein serine threonine kinase type I receptor (ALK-3). |journal=J. Cell. Physiol. |volume=168 |issue= 2 |pages= 453-61 |year= 1996 |pmid= 8707881 |doi= 10.1002/(SICI)1097-4652(199608)168:2<453::AID-JCP24>3.0.CO;2-2 }}
*{{cite journal | author=Nichols WC, Koller DL, Slovis B, ''et al.'' |title=Localization of the gene for familial primary pulmonary hypertension to chromosome 2q31-32. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 277-80 |year= 1997 |pmid= 9054941 |doi= 10.1038/ng0397-277 }}
*{{cite journal | author=Morse JH, Jones AC, Barst RJ, ''et al.'' |title=Mapping of familial primary pulmonary hypertension locus (PPH1) to chromosome 2q31-q32. |journal=Circulation |volume=95 |issue= 12 |pages= 2603-6 |year= 1997 |pmid= 9193425 |doi= }}
*{{cite journal | author=Erlacher L, McCartney J, Piek E, ''et al.'' |title=Cartilage-derived morphogenetic proteins and osteogenic protein-1 differentially regulate osteogenesis. |journal=J. Bone Miner. Res. |volume=13 |issue= 3 |pages= 383-92 |year= 1998 |pmid= 9525338 |doi= }}
*{{cite journal | author=Aström AK, Jin D, Imamura T, ''et al.'' |title=Chromosomal localization of three human genes encoding bone morphogenetic protein receptors. |journal=Mamm. Genome |volume=10 |issue= 3 |pages= 299-302 |year= 1999 |pmid= 10051328 |doi= }}
*{{cite journal | author=Gilboa L, Nohe A, Geissendörfer T, ''et al.'' |title=Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. |journal=Mol. Biol. Cell |volume=11 |issue= 3 |pages= 1023-35 |year= 2000 |pmid= 10712517 |doi= }}
*{{cite journal | author=Kirsch T, Nickel J, Sebald W |title=BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II. |journal=EMBO J. |volume=19 |issue= 13 |pages= 3314-24 |year= 2000 |pmid= 10880444 |doi= 10.1093/emboj/19.13.3314 }}
*{{cite journal | author=Deng Z, Morse JH, Slager SL, ''et al.'' |title=Familial primary pulmonary hypertension (gene PPH1) is caused by mutations in the bone morphogenetic protein receptor-II gene. |journal=Am. J. Hum. Genet. |volume=67 |issue= 3 |pages= 737-44 |year= 2000 |pmid= 10903931 |doi= }}
*{{cite journal | author=Machado RD, Pauciulo MW, Fretwell N, ''et al.'' |title=A physical and transcript map based upon refinement of the critical interval for PPH1, a gene for familial primary pulmonary hypertension. The International PPH Consortium. |journal=Genomics |volume=68 |issue= 2 |pages= 220-8 |year= 2001 |pmid= 10964520 |doi= 10.1006/geno.2000.6291 }}
*{{cite journal | author=Lane KB, Machado RD, Pauciulo MW, ''et al.'' |title=Heterozygous germline mutations in BMPR2, encoding a TGF-beta receptor, cause familial primary pulmonary hypertension. The International PPH Consortium. |journal=Nat. Genet. |volume=26 |issue= 1 |pages= 81-4 |year= 2000 |pmid= 10973254 |doi= 10.1038/79226 }}
*{{cite journal | author=Thomson JR, Machado RD, Pauciulo MW, ''et al.'' |title=Sporadic primary pulmonary hypertension is associated with germline mutations of the gene encoding BMPR-II, a receptor member of the TGF-beta family. |journal=J. Med. Genet. |volume=37 |issue= 10 |pages= 741-5 |year= 2001 |pmid= 11015450 |doi= }}
*{{cite journal | author=Machado RD, Pauciulo MW, Thomson JR, ''et al.'' |title=BMPR2 haploinsufficiency as the inherited molecular mechanism for primary pulmonary hypertension. |journal=Am. J. Hum. Genet. |volume=68 |issue= 1 |pages= 92-102 |year= 2001 |pmid= 11115378 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CFL1... {November 14, 2007 4:54:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:54:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CFL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1q8g.
| PDB = {{PDB2|1q8g}}, {{PDB2|1q8x}}
| Name = Cofilin 1 (non-muscle)
| HGNCid = 1874
| Symbol = CFL1
| AltSymbols =; CFL
| OMIM = 601442
| ECnumber =
| Homologene = 39624
| MGIid = 101757
| GeneAtlas_image1 = PBB_GE_CFL1_200021_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1072
| Hs_Ensembl = ENSG00000172757
| Hs_RefseqProtein = NP_005498
| Hs_RefseqmRNA = NM_005507
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 65378884
| Hs_GenLoc_end = 65383462
| Hs_Uniprot = P23528
| Mm_EntrezGene = 12631
| Mm_Ensembl = ENSMUSG00000056201
| Mm_RefseqmRNA = XM_979959
| Mm_RefseqProtein = XP_985053
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 5492497
| Mm_GenLoc_end = 5495201
| Mm_Uniprot = Q544Y7
}}
}}
'''Cofilin 1 (non-muscle)''', also known as '''CFL1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: CFL1 cofilin 1 (non-muscle)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1072| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Maciver SK, Hussey PJ |title=The ADF/cofilin family: actin-remodeling proteins. |journal=Genome Biol. |volume=3 |issue= 5 |pages= reviews3007 |year= 2002 |pmid= 12049672 |doi= }}
*{{cite journal | author=Samstag Y, Nebl G |title=Interaction of cofilin with the serine phosphatases PP1 and PP2A in normal and neoplastic human T lymphocytes. |journal=Adv. Enzyme Regul. |volume=43 |issue= |pages= 197-211 |year= 2004 |pmid= 12791392 |doi= }}
*{{cite journal | author=Ogawa K, Tashima M, Yumoto Y, ''et al.'' |title=Coding sequence of human placenta cofilin cDNA. |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7169 |year= 1991 |pmid= 2263493 |doi= }}
*{{cite journal | author=van der Steege G, Draaijers TG, Grootscholten PM, ''et al.'' |title=A provisional transcript map of the spinal muscular atrophy (SMA) critical region. |journal=Eur. J. Hum. Genet. |volume=3 |issue= 2 |pages= 87-95 |year= 1995 |pmid= 7552146 |doi= }}
*{{cite journal | author=Davidson MM, Haslam RJ |title=Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+. |journal=Biochem. J. |volume=301 ( Pt 1) |issue= |pages= 41-7 |year= 1994 |pmid= 8037689 |doi= }}
*{{cite journal | author=Ono S, Minami N, Abe H, Obinata T |title=Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. |journal=J. Biol. Chem. |volume=269 |issue= 21 |pages= 15280-6 |year= 1994 |pmid= 8195165 |doi= }}
*{{cite journal | author=Abe H, Nagaoka R, Obinata T |title=Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes. |journal=Exp. Cell Res. |volume=206 |issue= 1 |pages= 1-10 |year= 1993 |pmid= 8482351 |doi= 10.1006/excr.1993.1113 }}
*{{cite journal | author=Gillett GT, Fox MF, Rowe PS, ''et al.'' |title=Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and muscle-type cofilin (CFL2) to chromosome 14. |journal=Ann. Hum. Genet. |volume=60 |issue= Pt 3 |pages= 201-11 |year= 1996 |pmid= 8800436 |doi= }}
*{{cite journal | author=Okada K, Takano-Ohmuro H, Obinata T, Abe H |title=Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood. |journal=Exp. Cell Res. |volume=227 |issue= 1 |pages= 116-22 |year= 1996 |pmid= 8806458 |doi= 10.1006/excr.1996.0256 }}
*{{cite journal | author=Nebl G, Meuer SC, Samstag Y |title=Dephosphorylation of serine 3 regulates nuclear translocation of cofilin. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26276-80 |year= 1996 |pmid= 8824278 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Ott DE, Coren LV, Kane BP, ''et al.'' |title=Cytoskeletal proteins inside human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=70 |issue= 11 |pages= 7734-43 |year= 1996 |pmid= 8892894 |doi= }}
*{{cite journal | author=Yang N, Higuchi O, Ohashi K, ''et al.'' |title=Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. |journal=Nature |volume=393 |issue= 6687 |pages= 809-12 |year= 1998 |pmid= 9655398 |doi= 10.1038/31735 }}
*{{cite journal | author=Rodal AA, Tetreault JW, Lappalainen P, ''et al.'' |title=Aip1p interacts with cofilin to disassemble actin filaments. |journal=J. Cell Biol. |volume=145 |issue= 6 |pages= 1251-64 |year= 1999 |pmid= 10366597 |doi= }}
*{{cite journal | author=Maekawa M, Ishizaki T, Boku S, ''et al.'' |title=Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. |journal=Science |volume=285 |issue= 5429 |pages= 895-8 |year= 1999 |pmid= 10436159 |doi= }}
*{{cite journal | author=Sumi T, Matsumoto K, Takai Y, Nakamura T |title=Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2. |journal=J. Cell Biol. |volume=147 |issue= 7 |pages= 1519-32 |year= 2000 |pmid= 10613909 |doi= }}
*{{cite journal | author=Adachi R, Matsui S, Kinoshita M, ''et al.'' |title=Nitric oxide induces chemotaxis of neutrophil-like HL-60 cells and translocation of cofilin to plasma membranes. |journal=Int. J. Immunopharmacol. |volume=22 |issue= 11 |pages= 855-64 |year= 2001 |pmid= 11090694 |doi= }}
*{{cite journal | author=Lee K, Jung J, Kim M, Guidotti G |title=Interaction of the alpha subunit of Na,K-ATPase with cofilin. |journal=Biochem. J. |volume=353 |issue= Pt 2 |pages= 377-85 |year= 2001 |pmid= 11139403 |doi= }}
*{{cite journal | author=Toshima J, Toshima JY, Amano T, ''et al.'' |title=Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. |journal=Mol. Biol. Cell |volume=12 |issue= 4 |pages= 1131-45 |year= 2001 |pmid= 11294912 |doi= }}
*{{cite journal | author=Sumi T, Matsumoto K, Shibuya A, Nakamura T |title=Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 23092-6 |year= 2001 |pmid= 11340065 |doi= 10.1074/jbc.C100196200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYBB... {November 14, 2007 4:54:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:55:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome b-245, beta polypeptide (chronic granulomatous disease)
| HGNCid = 2578
| Symbol = CYBB
| AltSymbols =; CGD; GP91-1; GP91-PHOX; GP91PHOX; NOX2
| OMIM = 300481
| ECnumber =
| Homologene = 68054
| MGIid = 88574
| GeneAtlas_image1 = PBB_GE_CYBB_203923_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYBB_203922_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005244 |text = voltage-gated ion channel activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050660 |text = FAD binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1536
| Hs_Ensembl = ENSG00000165168
| Hs_RefseqProtein = NP_000388
| Hs_RefseqmRNA = NM_000397
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 37524208
| Hs_GenLoc_end = 37557658
| Hs_Uniprot = P04839
| Mm_EntrezGene = 13058
| Mm_Ensembl = ENSMUSG00000015340
| Mm_RefseqmRNA = NM_007807
| Mm_RefseqProtein = NP_031833
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 8592987
| Mm_GenLoc_end = 8626250
| Mm_Uniprot = Q3TVP4
}}
}}
'''Cytochrome b-245, beta polypeptide (chronic granulomatous disease)''', also known as '''CYBB''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Cytochrome b (-245) is composed of cytochrome b alpha (CYBA) and beta (CYBB) chain. It has been proposed as a primary component of the microbicidal oxidase system of phagocytes. CYBB deficiency is one of five described biochemical defects associated with chronic granulomatous disease (CGD). In this disorder, there is decreased activity of phagocyte NADPH oxidase; neutrophils are able to phagocytize bacteria but cannot kill them in the phagocytic vacuoles. The cause of the killing defect is an inability to increase the cell's respiration and consequent failure to deliver activated oxygen into the phagocytic vacuole.<ref>{{cite web | title = Entrez Gene: CYBB cytochrome b-245, beta polypeptide (chronic granulomatous disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1536| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bolscher BG, de Boer M, de Klein A, ''et al.'' |title=Point mutations in the beta-subunit of cytochrome b558 leading to X-linked chronic granulomatous disease. |journal=Blood |volume=77 |issue= 11 |pages= 2482-7 |year= 1991 |pmid= 1710153 |doi= }}
*{{cite journal | author=Nong Y, Kandil O, Tobin EH, ''et al.'' |title=The HIV core protein p24 inhibits interferon-gamma-induced increase of HLA-DR and cytochrome b heavy chain mRNA levels in the human monocyte-like cell line THP1. |journal=Cell. Immunol. |volume=132 |issue= 1 |pages= 10-6 |year= 1991 |pmid= 1905983 |doi= }}
*{{cite journal | author=Dinauer MC, Pierce EA, Bruns GA, ''et al.'' |title=Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1729-37 |year= 1990 |pmid= 2243141 |doi= }}
*{{cite journal | author=Royer-Pokora B, Kunkel LM, Monaco AP, ''et al.'' |title=Cloning the gene for an inherited human disorder--chronic granulomatous disease--on the basis of its chromosomal location. |journal=Nature |volume=322 |issue= 6074 |pages= 32-8 |year= 1986 |pmid= 2425263 |doi= 10.1038/322032a0 }}
*{{cite journal | author=Dinauer MC, Curnutte JT, Rosen H, Orkin SH |title=A missense mutation in the neutrophil cytochrome b heavy chain in cytochrome-positive X-linked chronic granulomatous disease. |journal=J. Clin. Invest. |volume=84 |issue= 6 |pages= 2012-6 |year= 1990 |pmid= 2556453 |doi= }}
*{{cite journal | author=Dinauer MC, Orkin SH, Brown R, ''et al.'' |title=The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex. |journal=Nature |volume=327 |issue= 6124 |pages= 717-20 |year= 1987 |pmid= 3600768 |doi= 10.1038/327717a0 }}
*{{cite journal | author=Teahan C, Rowe P, Parker P, ''et al.'' |title=The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome b-245. |journal=Nature |volume=327 |issue= 6124 |pages= 720-1 |year= 1987 |pmid= 3600769 |doi= 10.1038/327720a0 }}
*{{cite journal | author=Rabbani H, de Boer M, Ahlin A, ''et al.'' |title=A 40-base-pair duplication in the gp91-phox gene leading to X-linked chronic granulomatous disease. |journal=Eur. J. Haematol. |volume=51 |issue= 4 |pages= 218-22 |year= 1994 |pmid= 7694872 |doi= }}
*{{cite journal | author=Pollock JD, Williams DA, Gifford MA, ''et al.'' |title=Mouse model of X-linked chronic granulomatous disease, an inherited defect in phagocyte superoxide production. |journal=Nat. Genet. |volume=9 |issue= 2 |pages= 202-9 |year= 1995 |pmid= 7719350 |doi= 10.1038/ng0295-202 }}
*{{cite journal | author=Ariga T, Sakiyama Y, Matsumoto S |title=Two novel point mutations in the cytochrome b 558 heavy chain gene, detected in two Japanese patients with X-linked chronic granulomatous disease. |journal=Hum. Genet. |volume=94 |issue= 4 |pages= 441 |year= 1994 |pmid= 7927345 |doi= }}
*{{cite journal | author=Leto TL, Adams AG, de Mendez I |title=Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 22 |pages= 10650-4 |year= 1994 |pmid= 7938008 |doi= }}
*{{cite journal | author=Ariga T, Sakiyama Y, Tomizawa K, ''et al.'' |title=A newly recognized point mutation in the cytochrome b558 heavy chain gene replacing alanine57 by glutamic acid, in a patient with cytochrome b positive X-linked chronic granulomatous disease. |journal=Eur. J. Pediatr. |volume=152 |issue= 6 |pages= 469-72 |year= 1993 |pmid= 8101486 |doi= }}
*{{cite journal | author=Leusen JH, de Boer M, Bolscher BG, ''et al.'' |title=A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox. |journal=J. Clin. Invest. |volume=93 |issue= 5 |pages= 2120-6 |year= 1994 |pmid= 8182143 |doi= }}
*{{cite journal | author=Meindl A, Carvalho MR, Herrmann K, ''et al.'' |title=A gene (SRPX) encoding a sushi-repeat-containing protein is deleted in patients with X-linked retinitis pigmentosa. |journal=Hum. Mol. Genet. |volume=4 |issue= 12 |pages= 2339-46 |year= 1996 |pmid= 8634708 |doi= }}
*{{cite journal | author=Sathyamoorthy M, de Mendez I, Adams AG, Leto TL |title=p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9141-6 |year= 1997 |pmid= 9083043 |doi= }}
*{{cite journal | author=Eklund EA, Kakar R |title=Identification and characterization of TF1(phox), a DNA-binding protein that increases expression of gp91(phox) in PLB985 myeloid leukemia cells. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9344-55 |year= 1997 |pmid= 9083071 |doi= }}
*{{cite journal | author=Jendrossek V, Ritzel A, Neubauer B, ''et al.'' |title=An in-frame triplet deletion within the gp91-phox gene in an adult X-linked chronic granulomatous disease patient with residual NADPH-oxidase activity. |journal=Eur. J. Haematol. |volume=58 |issue= 2 |pages= 78-85 |year= 1997 |pmid= 9111587 |doi= }}
*{{cite journal | author=Rae J, Newburger PE, Dinauer MC, ''et al.'' |title=X-Linked chronic granulomatous disease: mutations in the CYBB gene encoding the gp91-phox component of respiratory-burst oxidase. |journal=Am. J. Hum. Genet. |volume=62 |issue= 6 |pages= 1320-31 |year= 1998 |pmid= 9585602 |doi= }}
*{{cite journal | author=Ariga T, Furuta H, Cho K, Sakiyama Y |title=Genetic analysis of 13 families with X-linked chronic granulomatous disease reveals a low proportion of sporadic patients and a high proportion of sporadic carriers. |journal=Pediatr. Res. |volume=44 |issue= 1 |pages= 85-92 |year= 1998 |pmid= 9667376 |doi= }}
*{{cite journal | author=Kumatori A, Faizunnessa NN, Suzuki S, ''et al.'' |title=Nonhomologous recombination between the cytochrome b558 heavy chain gene (CYBB) and LINE-1 causes an X-linked chronic granulomatous disease. |journal=Genomics |volume=53 |issue= 2 |pages= 123-8 |year= 1998 |pmid= 9790760 |doi= 10.1006/geno.1998.5510 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DNM1... {November 14, 2007 4:55:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:55:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DNM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dyn.
| PDB = {{PDB2|1dyn}}, {{PDB2|2aka}}, {{PDB2|2dyn}}
| Name = Dynamin 1
| HGNCid = 2972
| Symbol = DNM1
| AltSymbols =; DNM
| OMIM = 602377
| ECnumber =
| Homologene = 68397
| MGIid = 107384
| GeneAtlas_image1 = PBB_GE_DNM1_215116_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0005905 |text = coated pit}}
| Process = {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1759
| Hs_Ensembl = ENSG00000106976
| Hs_RefseqProtein = NP_001005336
| Hs_RefseqmRNA = NM_001005336
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 130005479
| Hs_GenLoc_end = 130057348
| Hs_Uniprot = Q05193
| Mm_EntrezGene = 13429
| Mm_Ensembl = ENSMUSG00000026825
| Mm_RefseqmRNA = NM_010065
| Mm_RefseqProtein = NP_034195
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 32130480
| Mm_GenLoc_end = 32175293
| Mm_Uniprot = Q6PDM5
}}
}}
'''Dynamin 1''', also known as '''DNM1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the dynamin subfamily of GTP-binding proteins. The encoded protein possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the encoded protein, which can also self-assemble leading to stimulation of GTPase activity. More than sixty highly conserved copies of the 3' region of this gene are found elsewhere in the genome, particularly on chromosomes Y and 15. Alternatively spliced transcript variants encoding different isoforms have been described.<ref>{{cite web | title = Entrez Gene: DNM1 dynamin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1759| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sever S |title=Dynamin and endocytosis. |journal=Curr. Opin. Cell Biol. |volume=14 |issue= 4 |pages= 463-7 |year= 2003 |pmid= 12383797 |doi= }}
*{{cite journal | author=Wiejak J, Wyroba E |title=Dynamin: characteristics, mechanism of action and function. |journal=Cell. Mol. Biol. Lett. |volume=7 |issue= 4 |pages= 1073-80 |year= 2003 |pmid= 12511974 |doi= }}
*{{cite journal | author=Orth JD, McNiven MA |title=Dynamin at the actin-membrane interface. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 1 |pages= 31-9 |year= 2003 |pmid= 12517701 |doi= }}
*{{cite journal | author=Obar RA, Collins CA, Hammarback JA, ''et al.'' |title=Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. |journal=Nature |volume=347 |issue= 6290 |pages= 256-61 |year= 1990 |pmid= 2144893 |doi= 10.1038/347256a0 }}
*{{cite journal | author=Timm D, Salim K, Gout I, ''et al.'' |title=Crystal structure of the pleckstrin homology domain from dynamin. |journal=Nat. Struct. Biol. |volume=1 |issue= 11 |pages= 782-8 |year= 1995 |pmid= 7634088 |doi= }}
*{{cite journal | author=Downing AK, Driscoll PC, Gout I, ''et al.'' |title=Three-dimensional solution structure of the pleckstrin homology domain from dynamin. |journal=Curr. Biol. |volume=4 |issue= 10 |pages= 884-91 |year= 1995 |pmid= 7850421 |doi= }}
*{{cite journal | author=Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB |title=Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. |journal=Cell |volume=79 |issue= 2 |pages= 199-209 |year= 1994 |pmid= 7954789 |doi= }}
*{{cite journal | author=van der Bliek AM, Redelmeier TE, Damke H, ''et al.'' |title=Mutations in human dynamin block an intermediate stage in coated vesicle formation. |journal=J. Cell Biol. |volume=122 |issue= 3 |pages= 553-63 |year= 1993 |pmid= 8101525 |doi= }}
*{{cite journal | author=Miki H, Miura K, Matuoka K, ''et al.'' |title=Association of Ash/Grb-2 with dynamin through the Src homology 3 domain. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 5489-92 |year= 1994 |pmid= 8119878 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Sontag JM, Fykse EM, Ushkaryov Y, ''et al.'' |title=Differential expression and regulation of multiple dynamins. |journal=J. Biol. Chem. |volume=269 |issue= 6 |pages= 4547-54 |year= 1994 |pmid= 8308025 |doi= }}
*{{cite journal | author=Newman-Smith ED, Shurland DL, van der Bliek AM |title=Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis. |journal=Genomics |volume=41 |issue= 2 |pages= 286-9 |year= 1997 |pmid= 9143509 |doi= 10.1006/geno.1996.4596 }}
*{{cite journal | author=Grabs D, Slepnev VI, Songyang Z, ''et al.'' |title=The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13419-25 |year= 1997 |pmid= 9148966 |doi= }}
*{{cite journal | author=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700-6 |year= 1997 |pmid= 9195986 |doi= }}
*{{cite journal | author=Ringstad N, Nemoto Y, De Camilli P |title=The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8569-74 |year= 1997 |pmid= 9238017 |doi= }}
*{{cite journal | author=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319-22 |year= 1997 |pmid= 9280305 |doi= }}
*{{cite journal | author=Wigge P, Köhler K, Vallis Y, ''et al.'' |title=Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. |journal=Mol. Biol. Cell |volume=8 |issue= 10 |pages= 2003-15 |year= 1997 |pmid= 9348539 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Witke W, Podtelejnikov AV, Di Nardo A, ''et al.'' |title=In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. |journal=EMBO J. |volume=17 |issue= 4 |pages= 967-76 |year= 1998 |pmid= 9463375 |doi= 10.1093/emboj/17.4.967 }}
*{{cite journal | author=Slepnev VI, Ochoa GC, Butler MH, ''et al.'' |title=Role of phosphorylation in regulation of the assembly of endocytic coat complexes. |journal=Science |volume=281 |issue= 5378 |pages= 821-4 |year= 1998 |pmid= 9694653 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EEF1A1... {November 14, 2007 4:55:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:57:01 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Eukaryotic translation elongation factor 1 alpha 1
| HGNCid = 3189
| Symbol = EEF1A1
| AltSymbols =; CCS-3; CCS3; EEF-1; EEF1A; EF-Tu; EF1A; FLJ25721; GRAF-1EF; HNGC:16303; LENG7; MGC102687; MGC131894; MGC16224; PTI1; eEF1A-1
| OMIM = 130590
| ECnumber =
| Homologene = 68181
| MGIid = 1096881
| GeneAtlas_image1 = PBB_GE_EEF1A1_204892_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_EEF1A1_206559_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_EEF1A1_213477_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003746 |text = translation elongation factor activity}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005853 |text = eukaryotic translation elongation factor 1 complex}}
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0006414 |text = translational elongation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1915
| Hs_Ensembl = ENSG00000156508
| Hs_RefseqProtein = NP_001393
| Hs_RefseqmRNA = NM_001402
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 74282194
| Hs_GenLoc_end = 74288344
| Hs_Uniprot = P68104
| Mm_EntrezGene = 13627
| Mm_Ensembl = ENSMUSG00000037742
| Mm_RefseqmRNA = NM_010106
| Mm_RefseqProtein = NP_034236
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 78264142
| Mm_GenLoc_end = 78266338
| Mm_Uniprot = Q3TII3
}}
}}
'''Eukaryotic translation elongation factor 1 alpha 1''', also known as '''EEF1A1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. This isoform is identified as an autoantigen in 66% of patients with Felty syndrome. This gene has been found to have multiple copies on many chromosomes, some of which, if not all, represent different pseudogenes.<ref>{{cite web | title = Entrez Gene: EEF1A1 eukaryotic translation elongation factor 1 alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1915| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Madsen HO, Poulsen K, Dahl O, ''et al.'' |title=Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family. |journal=Nucleic Acids Res. |volume=18 |issue= 6 |pages= 1513-6 |year= 1990 |pmid= 2183196 |doi= }}
*{{cite journal | author=Bec G, Kerjan P, Zha XD, Waller JP |title=Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1. |journal=J. Biol. Chem. |volume=264 |issue= 35 |pages= 21131-7 |year= 1990 |pmid= 2556394 |doi= }}
*{{cite journal | author=Uetsuki T, Naito A, Nagata S, Kaziro Y |title=Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha. |journal=J. Biol. Chem. |volume=264 |issue= 10 |pages= 5791-8 |year= 1989 |pmid= 2564392 |doi= }}
*{{cite journal | author=Whiteheart SW, Shenbagamurthi P, Chen L, ''et al.'' |title=Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. |journal=J. Biol. Chem. |volume=264 |issue= 24 |pages= 14334-41 |year= 1989 |pmid= 2569467 |doi= }}
*{{cite journal | author=Motorin YuA , Wolfson AD, Orlovsky AF, Gladilin KL |title=Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. |journal=FEBS Lett. |volume=238 |issue= 2 |pages= 262-4 |year= 1988 |pmid= 3169261 |doi= }}
*{{cite journal | author=Ann DK, Wu MM, Huang T, ''et al.'' |title=Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha. |journal=J. Biol. Chem. |volume=263 |issue= 8 |pages= 3546-9 |year= 1988 |pmid= 3346208 |doi= }}
*{{cite journal | author=Brands JH, Maassen JA, van Hemert FJ, ''et al.'' |title=The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. |journal=Eur. J. Biochem. |volume=155 |issue= 1 |pages= 167-71 |year= 1986 |pmid= 3512269 |doi= }}
*{{cite journal | author=Opdenakker G, Cabeza-Arvelaiz Y, Fiten P, ''et al.'' |title=Human elongation factor 1 alpha: a polymorphic and conserved multigene family with multiple chromosomal localizations. |journal=Hum. Genet. |volume=75 |issue= 4 |pages= 339-44 |year= 1987 |pmid= 3570288 |doi= }}
*{{cite journal | author=Rao TR, Slobin LI |title=Structure of the amino-terminal end of mammalian elongation factor Tu. |journal=Nucleic Acids Res. |volume=14 |issue= 5 |pages= 2409 |year= 1986 |pmid= 3960725 |doi= }}
*{{cite journal | author=Carvalho MD, Carvalho JF, Merrick WC |title=Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes. |journal=Arch. Biochem. Biophys. |volume=234 |issue= 2 |pages= 603-11 |year= 1984 |pmid= 6568109 |doi= }}
*{{cite journal | author=Shen R, Su ZZ, Olsson CA, Fisher PB |title=Identification of the human prostatic carcinoma oncogene PTI-1 by rapid expression cloning and differential RNA display. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 15 |pages= 6778-82 |year= 1995 |pmid= 7542776 |doi= }}
*{{cite journal | author=Reed VS, Wastney ME, Yang DC |title=Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha. |journal=J. Biol. Chem. |volume=269 |issue= 52 |pages= 32932-6 |year= 1995 |pmid= 7806521 |doi= }}
*{{cite journal | author=Kielbassa K, Müller HJ, Meyer HE, ''et al.'' |title=Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6156-62 |year= 1995 |pmid= 7890750 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Wu-Baer F, Lane WS, Gaynor RB |title=Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA. |journal=J. Biol. Chem. |volume=271 |issue= 8 |pages= 4201-8 |year= 1996 |pmid= 8626763 |doi= }}
*{{cite journal | author=Sanders J, Brandsma M, Janssen GM, ''et al.'' |title=Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. |journal=J. Cell. Sci. |volume=109 ( Pt 5) |issue= |pages= 1113-7 |year= 1996 |pmid= 8743958 |doi= }}
*{{cite journal | author=Lund A, Knudsen SM, Vissing H, ''et al.'' |title=Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3. |journal=Genomics |volume=36 |issue= 2 |pages= 359-61 |year= 1997 |pmid= 8812466 |doi= 10.1006/geno.1996.0475 }}
*{{cite journal | author=Welle S, Thornton C, Bhatt K, Krym M |title=Expression of elongation factor-1 alpha and S1 in young and old human skeletal muscle. |journal=J. Gerontol. A Biol. Sci. Med. Sci. |volume=52 |issue= 5 |pages= B235-9 |year= 1997 |pmid= 9310071 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Sheu GT, Traugh JA |title=Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33290-7 |year= 1998 |pmid= 9407120 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ELK1... {November 14, 2007 4:57:01 PM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 14, 2007 4:57:33 PM PST}
- AMBIGUITY: More than one potential page found for updating, ELK1 ELK1 {November 14, 2007 4:57:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ELK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dux.
| PDB = {{PDB2|1dux}}
| Name = ELK1, member of ETS oncogene family
| HGNCid = 3321
| Symbol = ELK1
| AltSymbols =;
| OMIM = 311040
| ECnumber =
| Homologene = 3832
| MGIid = 101833
| GeneAtlas_image1 = PBB_GE_ELK1_203617_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_ELK1_210376_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2002
| Hs_Ensembl = ENSG00000126767
| Hs_RefseqProtein = NP_005220
| Hs_RefseqmRNA = NM_005229
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 47379864
| Hs_GenLoc_end = 47394964
| Hs_Uniprot = P19419
| Mm_EntrezGene = 13712
| Mm_Ensembl = ENSMUSG00000009406
| Mm_RefseqmRNA = NM_007922
| Mm_RefseqProtein = NP_031948
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 20092248
| Mm_GenLoc_end = 20107547
| Mm_Uniprot = Q3V1M9
}}
}}
'''ELK1, member of ETS oncogene family''', also known as '''ELK1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the Ets family of transcription factors and of the ternary complex factor (TCF) subfamily. Proteins of the TCF subfamily form a ternary complex by binding to the the serum response factor and the serum reponse element in the promoter of the c-fos proto-oncogene. The protein encoded by this gene is a nuclear target for the ras-raf-MAPK signaling cascade.<ref>{{cite web | title = Entrez Gene: ELK1 ELK1, member of ETS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2002| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sharrocks AD, Brown AL, Ling Y, Yates PR |title=The ETS-domain transcription factor family. |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 12 |pages= 1371-87 |year= 1998 |pmid= 9570133 |doi= }}
*{{cite journal | author=Wasylyk B, Hagman J, Gutierrez-Hartmann A |title=Ets transcription factors: nuclear effectors of the Ras-MAP-kinase signaling pathway. |journal=Trends Biochem. Sci. |volume=23 |issue= 6 |pages= 213-6 |year= 1998 |pmid= 9644975 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Ron D, Habener JF |title=CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. |journal=Genes Dev. |volume=6 |issue= 3 |pages= 439-53 |year= 1992 |pmid= 1547942 |doi= }}
*{{cite journal | author=Janknecht R, Nordheim A |title=Elk-1 protein domains required for direct and SRF-assisted DNA-binding. |journal=Nucleic Acids Res. |volume=20 |issue= 13 |pages= 3317-24 |year= 1992 |pmid= 1630903 |doi= }}
*{{cite journal | author=Rao VN, Huebner K, Isobe M, ''et al.'' |title=elk, tissue-specific ets-related genes on chromosomes X and 14 near translocation breakpoints. |journal=Science |volume=244 |issue= 4900 |pages= 66-70 |year= 1989 |pmid= 2539641 |doi= }}
*{{cite journal | author=Price MA, Rogers AE, Treisman R |title=Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET). |journal=EMBO J. |volume=14 |issue= 11 |pages= 2589-601 |year= 1995 |pmid= 7540136 |doi= }}
*{{cite journal | author=Gille H, Kortenjann M, Thomae O, ''et al.'' |title=ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. |journal=EMBO J. |volume=14 |issue= 5 |pages= 951-62 |year= 1995 |pmid= 7889942 |doi= }}
*{{cite journal | author=Janz M, Lehmann U, Olde Weghuis D, ''et al.'' |title=Refined mapping of the human Ets-related gene Elk-1 to Xp11.2-p11.4, distal to the OATL1 region. |journal=Hum. Genet. |volume=94 |issue= 4 |pages= 442-4 |year= 1994 |pmid= 7927346 |doi= }}
*{{cite journal | author=Rao VN, Reddy ES |title=elk-1 proteins interact with MAP kinases. |journal=Oncogene |volume=9 |issue= 7 |pages= 1855-60 |year= 1994 |pmid= 8208531 |doi= }}
*{{cite journal | author=Marais R, Wynne J, Treisman R |title=The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. |journal=Cell |volume=73 |issue= 2 |pages= 381-93 |year= 1993 |pmid= 8386592 |doi= }}
*{{cite journal | author=Gille H, Strahl T, Shaw PE |title=Activation of ternary complex factor Elk-1 by stress-activated protein kinases. |journal=Curr. Biol. |volume=5 |issue= 10 |pages= 1191-200 |year= 1996 |pmid= 8548291 |doi= }}
*{{cite journal | author=Giovane A, Sobieszczuk P, Mignon C, ''et al.'' |title=Locations of the ets subfamily members net, elk1, and sap1 (ELK3, ELK1, and ELK4) on three homologous regions of the mouse and human genomes. |journal=Genomics |volume=29 |issue= 3 |pages= 769-72 |year= 1996 |pmid= 8575773 |doi= 10.1006/geno.1995.9938 }}
*{{cite journal | author=Cano E, Hazzalin CA, Kardalinou E, ''et al.'' |title=Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction. |journal=J. Cell. Sci. |volume=108 ( Pt 11) |issue= |pages= 3599-609 |year= 1996 |pmid= 8586671 |doi= }}
*{{cite journal | author=Raingeaud J, Whitmarsh AJ, Barrett T, ''et al.'' |title=MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. |journal=Mol. Cell. Biol. |volume=16 |issue= 3 |pages= 1247-55 |year= 1996 |pmid= 8622669 |doi= }}
*{{cite journal | author=Stein E, Cerretti DP, Daniel TO |title=Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23588-93 |year= 1996 |pmid= 8798570 |doi= }}
*{{cite journal | author=Janknecht R, Nordheim A |title=MAP kinase-dependent transcriptional coactivation by Elk-1 and its cofactor CBP. |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 3 |pages= 831-7 |year= 1997 |pmid= 8941362 |doi= 10.1006/bbrc.1996.1740 }}
*{{cite journal | author=Watson DK, Robinson L, Hodge DR, ''et al.'' |title=FLI1 and EWS-FLI1 function as ternary complex factors and ELK1 and SAP1a function as ternary and quaternary complex factors on the Egr1 promoter serum response elements. |journal=Oncogene |volume=14 |issue= 2 |pages= 213-21 |year= 1997 |pmid= 9010223 |doi= 10.1038/sj.onc.1200839 }}
*{{cite journal | author=Janknecht R, Hunter T |title=Activation of the Sap-1a transcription factor by the c-Jun N-terminal kinase (JNK) mitogen-activated protein kinase. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4219-24 |year= 1997 |pmid= 9020136 |doi= }}
*{{cite journal | author=Janknecht R, Hunter T |title=Convergence of MAP kinase pathways on the ternary complex factor Sap-1a. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1620-7 |year= 1997 |pmid= 9130707 |doi= 10.1093/emboj/16.7.1620 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GP6... {November 14, 2007 5:08:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:09:10 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GP6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2gi7.
| PDB = {{PDB2|2gi7}}
| Name = Glycoprotein VI (platelet)
| HGNCid = 14388
| Symbol = GP6
| AltSymbols =; GPIV; GPVI; MGC138168
| OMIM = 605546
| ECnumber =
| Homologene = 9488
| MGIid = 1889810
| GeneAtlas_image1 = PBB_GE_GP6_220336_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005518 |text = collagen binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007167 |text = enzyme linked receptor protein signaling pathway}} {{GNF_GO|id=GO:0030168 |text = platelet activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 51206
| Hs_Ensembl = ENSG00000088053
| Hs_RefseqProtein = NP_057447
| Hs_RefseqmRNA = NM_016363
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 60216885
| Hs_GenLoc_end = 60241444
| Hs_Uniprot = Q9HCN6
| Mm_EntrezGene = 243816
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_145298
| Mm_RefseqProtein = XP_145298
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Glycoprotein VI (platelet)''', also known as '''GP6''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Glycoprotein VI (GP6) is a 58-kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. Upon injury to the vessel wall and subsequent damage to the endothelial lining, exposure of the subendothelial matrix to blood flow results in deposition of platelets. Collagen fibers are the most thrombogenic macromolecular components of the extracellular matrix, with collagen types I, III, and VI being the major forms found in blood vessels. Platelet interaction with collagen occurs as a 2-step procedure: (1) the initial adhesion to collagen is followed by (2) an activation step leading to platelet secretion, recruitment of additional platelets, and aggregation. In physiologic conditions, the resulting platelet plug is the initial hemostatic event limiting blood loss. However, exposure of collagen after rupture of atherosclerotic plaques is a major stimulus of thrombus formation associated with myocardial infarction or stroke (Jandrot-Perrus et al., 2000).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: GP6 glycoprotein VI (platelet)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51206| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nieswandt B, Watson SP |title=Platelet-collagen interaction: is GPVI the central receptor? |journal=Blood |volume=102 |issue= 2 |pages= 449-61 |year= 2003 |pmid= 12649139 |doi= 10.1182/blood-2002-12-3882 }}
*{{cite journal | author=Watson SP, Auger JM, McCarty OJ, Pearce AC |title=GPVI and integrin alphaIIb beta3 signaling in platelets. |journal=J. Thromb. Haemost. |volume=3 |issue= 8 |pages= 1752-62 |year= 2005 |pmid= 16102042 |doi= 10.1111/j.1538-7836.2005.01429.x }}
*{{cite journal | author=Huang MM, Bolen JB, Barnwell JW, ''et al.'' |title=Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7844-8 |year= 1991 |pmid= 1715582 |doi= }}
*{{cite journal | author=Moroi M, Jung SM, Okuma M, Shinmyozu K |title=A patient with platelets deficient in glycoprotein VI that lack both collagen-induced aggregation and adhesion. |journal=J. Clin. Invest. |volume=84 |issue= 5 |pages= 1440-5 |year= 1989 |pmid= 2808700 |doi= }}
*{{cite journal | author=Polgár J, Clemetson JM, Kehrel BE, ''et al.'' |title=Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13576-83 |year= 1997 |pmid= 9153205 |doi= }}
*{{cite journal | author=Gibbins JM, Okuma M, Farndale R, ''et al.'' |title=Glycoprotein VI is the collagen receptor in platelets which underlies tyrosine phosphorylation of the Fc receptor gamma-chain. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 255-9 |year= 1997 |pmid= 9280292 |doi= }}
*{{cite journal | author=Tsuji M, Ezumi Y, Arai M, Takayama H |title=A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23528-31 |year= 1997 |pmid= 9295288 |doi= }}
*{{cite journal | author=Clemetson JM, Polgar J, Magnenat E, ''et al.'' |title=The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcalphaR and the natural killer receptors. |journal=J. Biol. Chem. |volume=274 |issue= 41 |pages= 29019-24 |year= 1999 |pmid= 10506151 |doi= }}
*{{cite journal | author=Miura Y, Ohnuma M, Jung SM, Moroi M |title=Cloning and expression of the platelet-specific collagen receptor glycoprotein VI. |journal=Thromb. Res. |volume=98 |issue= 4 |pages= 301-9 |year= 2000 |pmid= 10822077 |doi= }}
*{{cite journal | author=Nieswandt B, Bergmeier W, Schulte V, ''et al.'' |title=Expression and function of the mouse collagen receptor glycoprotein VI is strictly dependent on its association with the FcRgamma chain. |journal=J. Biol. Chem. |volume=275 |issue= 31 |pages= 23998-4002 |year= 2000 |pmid= 10825177 |doi= 10.1074/jbc.M003803200 }}
*{{cite journal | author=Jandrot-Perrus M, Busfield S, Lagrue AH, ''et al.'' |title=Cloning, characterization, and functional studies of human and mouse glycoprotein VI: a platelet-specific collagen receptor from the immunoglobulin superfamily. |journal=Blood |volume=96 |issue= 5 |pages= 1798-807 |year= 2000 |pmid= 10961879 |doi= }}
*{{cite journal | author=Ezumi Y, Uchiyama T, Takayama H |title=Molecular cloning, genomic structure, chromosomal localization, and alternative splice forms of the platelet collagen receptor glycoprotein VI. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 1 |pages= 27-36 |year= 2000 |pmid= 11027634 |doi= 10.1006/bbrc.2000.3624 }}
*{{cite journal | author=Barry FA, Gibbins JM |title=Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12874-8 |year= 2002 |pmid= 11825911 |doi= 10.1074/jbc.M200482200 }}
*{{cite journal | author=Suzuki-Inoue K, Tulasne D, Shen Y, ''et al.'' |title=Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 21561-6 |year= 2002 |pmid= 11943772 |doi= 10.1074/jbc.M201012200 }}
*{{cite journal | author=Quinton TM, Ozdener F, Dangelmaier C, ''et al.'' |title=Glycoprotein VI-mediated platelet fibrinogen receptor activation occurs through calcium-sensitive and PKC-sensitive pathways without a requirement for secreted ADP. |journal=Blood |volume=99 |issue= 9 |pages= 3228-34 |year= 2002 |pmid= 11964287 |doi= }}
*{{cite journal | author=Saving KL, Mankin PE, Gorman MJ |title=Differences in adhesion receptor expression between immature and older platelets and red blood cells of neonates and adults. |journal=J. Pediatr. Hematol. Oncol. |volume=24 |issue= 2 |pages= 120-4 |year= 2002 |pmid= 11990697 |doi= }}
*{{cite journal | author=Andrews RK, Suzuki-Inoue K, Shen Y, ''et al.'' |title=Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI. |journal=Blood |volume=99 |issue= 11 |pages= 4219-21 |year= 2002 |pmid= 12010829 |doi= 10.1182/blood-2001-11-0008 }}
*{{cite journal | author=Wonerow P, Obergfell A, Wilde JI, ''et al.'' |title=Differential role of glycolipid-enriched membrane domains in glycoprotein VI- and integrin-mediated phospholipase Cgamma2 regulation in platelets. |journal=Biochem. J. |volume=364 |issue= Pt 3 |pages= 755-65 |year= 2002 |pmid= 12049640 |doi= 10.1042/BJ20020128 }}
*{{cite journal | author=Miura Y, Takahashi T, Jung SM, Moroi M |title=Analysis of the interaction of platelet collagen receptor glycoprotein VI (GPVI) with collagen. A dimeric form of GPVI, but not the monomeric form, shows affinity to fibrous collagen. |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46197-204 |year= 2003 |pmid= 12356768 |doi= 10.1074/jbc.M204029200 }}
*{{cite journal | author=Holmes ML, Bartle N, Eisbacher M, Chong BH |title=Cloning and analysis of the thrombopoietin-induced megakaryocyte-specific glycoprotein VI promoter and its regulation by GATA-1, Fli-1, and Sp1. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48333-41 |year= 2003 |pmid= 12359731 |doi= 10.1074/jbc.M206127200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HMBS... {November 14, 2007 4:57:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:58:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Hydroxymethylbilane synthase
| HGNCid = 4982
| Symbol = HMBS
| AltSymbols =; PBG-D; PBGD; UPS
| OMIM = 609806
| ECnumber =
| Homologene = 158
| MGIid = 96112
| GeneAtlas_image1 = PBB_GE_HMBS_203040_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HMBS_213344_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_HMBS_212524_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004418 |text = hydroxymethylbilane synthase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006783 |text = heme biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3145
| Hs_Ensembl = ENSG00000149397
| Hs_RefseqProtein = NP_000181
| Hs_RefseqmRNA = NM_000190
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 118460797
| Hs_GenLoc_end = 118469469
| Hs_Uniprot = P08397
| Mm_EntrezGene = 15288
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_013551
| Mm_RefseqProtein = NP_038579
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Hydroxymethylbilane synthase''', also known as '''HMBS''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the hydroxymethylbilane synthase superfamily. The encoded protein is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane. Mutations in this gene are associated with the autosomal dominant disease acute intermittent porphyria. Alternatively spliced transcript variants encoding different isoforms have been described.<ref>{{cite web | title = Entrez Gene: HMBS hydroxymethylbilane synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3145| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Deybach JC, Puy H |title=Porphobilinogen deaminase gene structure and molecular defects. |journal=J. Bioenerg. Biomembr. |volume=27 |issue= 2 |pages= 197-205 |year= 1995 |pmid= 7592566 |doi= }}
*{{cite journal | author=Astrin KH, Desnick RJ |title=Molecular basis of acute intermittent porphyria: mutations and polymorphisms in the human hydroxymethylbilane synthase gene. |journal=Hum. Mutat. |volume=4 |issue= 4 |pages= 243-52 |year= 1995 |pmid= 7866402 |doi= 10.1002/humu.1380040403 }}
*{{cite journal | author=Helliwell JR, Nieh YP, Habash J, ''et al.'' |title=Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase. |journal=Faraday Discuss. |volume=122 |issue= |pages= 131-44; discussion 171-90 |year= 2003 |pmid= 12555854 |doi= }}
*{{cite journal | author=Hessels J, Voortman G, van der Wagen A, ''et al.'' |title=Homozygous acute intermittent porphyria in a 7-year-old boy with massive excretions of porphyrins and porphyrin precursors. |journal=J. Inherit. Metab. Dis. |volume=27 |issue= 1 |pages= 19-27 |year= 2004 |pmid= 14970743 |doi= 10.1023/B:BOLI.0000016613.75677.05 }}
*{{cite journal | author=Kauppinen R |title=Molecular diagnostics of acute intermittent porphyria. |journal=Expert Rev. Mol. Diagn. |volume=4 |issue= 2 |pages= 243-9 |year= 2004 |pmid= 14995910 |doi= 10.1586/14737159.4.2.243 }}
*{{cite journal | author=Hrdinka M, Puy H, Martasek P |title=May 2006 update in porphobilinogen deaminase gene polymorphisms and mutations causing acute intermittent porphyria: comparison with the situation in Slavic population. |journal=Physiological research / Academia Scientiarum Bohemoslovaca |volume=55 Suppl 2 |issue= |pages= S119-36 |year= 2007 |pmid= 17298216 |doi= }}
*{{cite journal | author=Kauppinen R, Peltonen L, Pihlaja H, Mustajoki P |title=CRIM-positive mutations of acute intermittent porphyria in Finland. |journal=Hum. Mutat. |volume=1 |issue= 5 |pages= 392-6 |year= 1993 |pmid= 1301948 |doi= 10.1002/humu.1380010508 }}
*{{cite journal | author=Mgone CS, Lanyon WG, Moore MR, Connor JM |title=Detection of seven point mutations in the porphobilinogen deaminase gene in patients with acute intermittent porphyria, by direct sequencing of in vitro amplified cDNA. |journal=Hum. Genet. |volume=90 |issue= 1-2 |pages= 12-6 |year= 1992 |pmid= 1427766 |doi= }}
*{{cite journal | author=Gu XF, de Rooij F, Voortman G, ''et al.'' |title=High frequency of mutations in exon 10 of the porphobilinogen deaminase gene in patients with a CRIM-positive subtype of acute intermittent porphyria. |journal=Am. J. Hum. Genet. |volume=51 |issue= 3 |pages= 660-5 |year= 1992 |pmid= 1496994 |doi= }}
*{{cite journal | author=Delfau MH, Picat C, De Rooij F, ''et al.'' |title=Molecular heterogeneity of acute intermittent porphyria: identification of four additional mutations resulting in the CRIM-negative subtype of the disease. |journal=Am. J. Hum. Genet. |volume=49 |issue= 2 |pages= 421-8 |year= 1991 |pmid= 1714233 |doi= }}
*{{cite journal | author=Namba H, Narahara K, Tsuji K, ''et al.'' |title=Assignment of human porphobilinogen deaminase to 11q24.1----q24.2 by in situ hybridization and gene dosage studies. |journal=Cytogenet. Cell Genet. |volume=57 |issue= 2-3 |pages= 105-8 |year= 1991 |pmid= 1914516 |doi= }}
*{{cite journal | author=Lee JS, Anvret M |title=Identification of the most common mutation within the porphobilinogen deaminase gene in Swedish patients with acute intermittent porphyria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10912-5 |year= 1992 |pmid= 1961762 |doi= }}
*{{cite journal | author=Tunnacliffe A, McGuire RS |title=A physical linkage group in human chromosome band 11q23 covering a region implicated in leukocyte neoplasia. |journal=Genomics |volume=8 |issue= 3 |pages= 447-53 |year= 1991 |pmid= 1981047 |doi= }}
*{{cite journal | author=Lander M, Pitt AR, Alefounder PR, ''et al.'' |title=Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding. |journal=Biochem. J. |volume=275 ( Pt 2) |issue= |pages= 447-52 |year= 1991 |pmid= 2025226 |doi= }}
*{{cite journal | author=Scobie GA, Llewellyn DH, Urquhart AJ, ''et al.'' |title=Acute intermittent porphyria caused by a C----T mutation that produces a stop codon in the porphobilinogen deaminase gene. |journal=Hum. Genet. |volume=85 |issue= 6 |pages= 631-4 |year= 1990 |pmid= 2227955 |doi= }}
*{{cite journal | author=Delfau MH, Picat C, de Rooij FW, ''et al.'' |title=Two different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyria. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1511-6 |year= 1990 |pmid= 2243128 |doi= }}
*{{cite journal | author=Lannfelt L, Wetterberg L, Lilius L, ''et al.'' |title=Porphobilinogen deaminase in human erythrocytes: purification of two forms with apparent molecular weights of 40 kDa and 42 kDa. |journal=Scand. J. Clin. Lab. Invest. |volume=49 |issue= 7 |pages= 677-84 |year= 1990 |pmid= 2609111 |doi= }}
*{{cite journal | author=Grandchamp B, Picat C, de Rooij F, ''et al.'' |title=A point mutation G----A in exon 12 of the porphobilinogen deaminase gene results in exon skipping and is responsible for acute intermittent porphyria. |journal=Nucleic Acids Res. |volume=17 |issue= 16 |pages= 6637-49 |year= 1989 |pmid= 2789372 |doi= }}
*{{cite journal | author=Raich N, Romeo PH, Dubart A, ''et al.'' |title=Molecular cloning and complete primary sequence of human erythrocyte porphobilinogen deaminase. |journal=Nucleic Acids Res. |volume=14 |issue= 15 |pages= 5955-68 |year= 1986 |pmid= 2875434 |doi= }}
*{{cite journal | author=Vidaud M, Gattoni R, Stevenin J, ''et al.'' |title=A 5' splice-region G----C mutation in exon 1 of the human beta-globin gene inhibits pre-mRNA splicing: a mechanism for beta+-thalassemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 1041-5 |year= 1989 |pmid= 2915972 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IDS... {November 14, 2007 4:58:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:58:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Iduronate 2-sulfatase (Hunter syndrome)
| HGNCid = 5389
| Symbol = IDS
| AltSymbols =; MPS2; SIDS
| OMIM = 309900
| ECnumber =
| Homologene = 169
| MGIid = 96417
| Function = {{GNF_GO|id=GO:0004423 |text = iduronate-2-sulfatase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008484 |text = sulfuric ester hydrolase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0030203 |text = glycosaminoglycan metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3423
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000193
| Hs_RefseqmRNA = NM_000202
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15931
| Mm_Ensembl = ENSMUSG00000035847
| Mm_RefseqmRNA = NM_001038990
| Mm_RefseqProtein = NP_001034079
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 66603734
| Mm_GenLoc_end = 66625640
| Mm_Uniprot = Q8CJ15
}}
}}
'''Iduronate 2-sulfatase (Hunter syndrome)''', also known as '''IDS''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Iduronate-2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in this X-chromosome gene that result in enzymatic deficiency lead to the sex-linked Mucopolysaccharidosis Type II, also known as Hunter Syndrome. Iduronate-2-sulfatase has a strong sequence homology with human arylsulfatases A, B, and C, and human glucosamine-6-sulfatase. A splice variant of this gene has been described.<ref>{{cite web | title = Entrez Gene: IDS iduronate 2-sulfatase (Hunter syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3423| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hopwood JJ, Bunge S, Morris CP, ''et al.'' |title=Molecular basis of mucopolysaccharidosis type II: mutations in the iduronate-2-sulphatase gene. |journal=Hum. Mutat. |volume=2 |issue= 6 |pages= 435-42 |year= 1994 |pmid= 8111411 |doi= 10.1002/humu.1380020603 }}
*{{cite journal | author=Gort L, Chabás A, Coll MJ |title=Hunter disease in the Spanish population: molecular analysis in 31 families. |journal=J. Inherit. Metab. Dis. |volume=21 |issue= 6 |pages= 655-61 |year= 1998 |pmid= 9762601 |doi= }}
*{{cite journal | author=Crotty PL, Braun SE, Anderson RA, Whitley CB |title=Mutation R468W of the iduronate-2-sulfatase gene in mild Hunter syndrome (mucopolysaccharidosis type II) confirmed by in vitro mutagenesis and expression. |journal=Hum. Mol. Genet. |volume=1 |issue= 9 |pages= 755-7 |year= 1993 |pmid= 1284597 |doi= }}
*{{cite journal | author=Bunge S, Steglich C, Beck M, ''et al.'' |title=Mutation analysis of the iduronate-2-sulfatase gene in patients with mucopolysaccharidosis type II (Hunter syndrome). |journal=Hum. Mol. Genet. |volume=1 |issue= 5 |pages= 335-9 |year= 1993 |pmid= 1303211 |doi= }}
*{{cite journal | author=Beck M, Steglich C, Zabel B, ''et al.'' |title=Deletion of the Hunter gene and both DXS466 and DXS304 in a patient with mucopolysaccharidosis type II. |journal=Am. J. Med. Genet. |volume=44 |issue= 1 |pages= 100-3 |year= 1992 |pmid= 1355630 |doi= 10.1002/ajmg.1320440123 }}
*{{cite journal | author=Sukegawa K, Tomatsu S, Tamai K, ''et al.'' |title=Intermediate form of mucopolysaccharidosis type II (Hunter disease): a C1327 to T substitution in the iduronate sulfatase gene. |journal=Biochem. Biophys. Res. Commun. |volume=183 |issue= 2 |pages= 809-13 |year= 1992 |pmid= 1550586 |doi= }}
*{{cite journal | author=Flomen RH, Green PM, Bentley DR, ''et al.'' |title=Detection of point mutations and a gross deletion in six Hunter syndrome patients. |journal=Genomics |volume=13 |issue= 3 |pages= 543-50 |year= 1992 |pmid= 1639384 |doi= }}
*{{cite journal | author=Wilson PJ, Suthers GK, Callen DF, ''et al.'' |title=Frequent deletions at Xq28 indicate genetic heterogeneity in Hunter syndrome. |journal=Hum. Genet. |volume=86 |issue= 5 |pages= 505-8 |year= 1991 |pmid= 1901826 |doi= }}
*{{cite journal | author=Wraith JE, Cooper A, Thornley M, ''et al.'' |title=The clinical phenotype of two patients with a complete deletion of the iduronate-2-sulphatase gene (mucopolysaccharidosis II--Hunter syndrome). |journal=Hum. Genet. |volume=87 |issue= 2 |pages= 205-6 |year= 1991 |pmid= 1906048 |doi= }}
*{{cite journal | author=Wilson PJ, Morris CP, Anson DS, ''et al.'' |title=Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 21 |pages= 8531-5 |year= 1990 |pmid= 2122463 |doi= }}
*{{cite journal | author=Bielicki J, Freeman C, Clements PR, Hopwood JJ |title=Human liver iduronate-2-sulphatase. Purification, characterization and catalytic properties. |journal=Biochem. J. |volume=271 |issue= 1 |pages= 75-86 |year= 1990 |pmid= 2222422 |doi= }}
*{{cite journal | author=Daniele A, Di Natale P |title=Hunter syndrome: presence of material cross-reacting with antibodies against iduronate sulfatase. |journal=Hum. Genet. |volume=75 |issue= 3 |pages= 234-8 |year= 1987 |pmid= 3104200 |doi= }}
*{{cite journal | author=Mossman J, Blunt S, Stephens R, ''et al.'' |title=Hunter's disease in a girl: association with X:5 chromosomal translocation disrupting the Hunter gene. |journal=Arch. Dis. Child. |volume=58 |issue= 11 |pages= 911-5 |year= 1984 |pmid= 6418082 |doi= }}
*{{cite journal | author=Sukegawa K, Tomatsu S, Fukao T, ''et al.'' |title=Mucopolysaccharidosis type II (Hunter disease): identification and characterization of eight point mutations in the iduronate-2-sulfatase gene in Japanese patients. |journal=Hum. Mutat. |volume=6 |issue= 2 |pages= 136-43 |year= 1995 |pmid= 7581397 |doi= 10.1002/humu.1380060206 }}
*{{cite journal | author=Li P, Huffman P, Thompson JN |title=Mutations of the iduronate-2-sulfatase gene on a T146T background in three patients with Hunter syndrome. |journal=Hum. Mutat. |volume=5 |issue= 3 |pages= 272-4 |year= 1995 |pmid= 7599640 |doi= 10.1002/humu.1380050314 }}
*{{cite journal | author=Popowska E, Rathmann M, Tylki-Szymanska A, ''et al.'' |title=Mutations of the iduronate-2-sulfatase gene in 12 Polish patients with mucopolysaccharidosis type II (Hunter syndrome). |journal=Hum. Mutat. |volume=5 |issue= 1 |pages= 97-100 |year= 1995 |pmid= 7728156 |doi= 10.1002/humu.1380050114 }}
*{{cite journal | author=Ben Simon-Schiff E, Bach G, Hopwood JJ, Abeliovich D |title=Mutation analysis of Jewish Hunter patients in Israel. |journal=Hum. Mutat. |volume=4 |issue= 4 |pages= 263-70 |year= 1995 |pmid= 7866405 |doi= 10.1002/humu.1380040406 }}
*{{cite journal | author=Jonsson JJ, Aronovich EL, Braun SE, Whitley CB |title=Molecular diagnosis of mucopolysaccharidosis type II (Hunter syndrome) by automated sequencing and computer-assisted interpretation: toward mutation mapping of the iduronate-2-sulfatase gene. |journal=Am. J. Hum. Genet. |volume=56 |issue= 3 |pages= 597-607 |year= 1995 |pmid= 7887413 |doi= }}
*{{cite journal | author=Schröder W, Wulff K, Wehnert M, ''et al.'' |title=Mutations of the iduronate-2-sulfatase (IDS) gene in patients with Hunter syndrome (mucopolysaccharidosis II). |journal=Hum. Mutat. |volume=4 |issue= 2 |pages= 128-31 |year= 1994 |pmid= 7981716 |doi= 10.1002/humu.1380040206 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IGFBP2... {November 14, 2007 4:58:31 PM PST}
- SEARCH REDIRECT: Control Box Found: IGFBP2 {November 14, 2007 4:59:01 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:59:02 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:59:02 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:59:02 PM PST}
- UPDATED: Updated protein page: IGFBP2 {November 14, 2007 4:59:08 PM PST}
- INFO: Beginning work on IL7... {November 14, 2007 4:59:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:59:43 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| update_protein_box = yes
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| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Interleukin 7
| HGNCid = 6023
| Symbol = IL7
| AltSymbols =; IL-7
| OMIM = 146660
| ECnumber =
| Homologene = 680
| MGIid = 96561
| GeneAtlas_image1 = PBB_GE_IL7_206693_at_tn.png
| Function = {{GNF_GO|id=GO:0005139 |text = interleukin-7 receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030890 |text = positive regulation of B cell proliferation}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0045453 |text = bone resorption}} {{GNF_GO|id=GO:0045582 |text = positive regulation of T cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3574
| Hs_Ensembl = ENSG00000104432
| Hs_RefseqProtein = NP_000871
| Hs_RefseqmRNA = NM_000880
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 79807564
| Hs_GenLoc_end = 79880313
| Hs_Uniprot = P13232
| Mm_EntrezGene = 16196
| Mm_Ensembl = ENSMUSG00000040329
| Mm_RefseqmRNA = NM_008371
| Mm_RefseqProtein = NP_032397
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 7556913
| Mm_GenLoc_end = 7587247
| Mm_Uniprot = Q3UT18
}}
}}
'''Interleukin 7''', also known as '''IL7''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.<ref>{{cite web | title = Entrez Gene: IL7 interleukin 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3574| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Möller P, Böhm M, Czarnetszki BM, Schadendorf D |title=Interleukin-7. Biology and implications for dermatology. |journal=Exp. Dermatol. |volume=5 |issue= 3 |pages= 129-37 |year= 1997 |pmid= 8840152 |doi= }}
*{{cite journal | author=Appasamy PM |title=Biological and clinical implications of interleukin-7 and lymphopoiesis. |journal=Cytokines Cell. Mol. Ther. |volume=5 |issue= 1 |pages= 25-39 |year= 1999 |pmid= 10390077 |doi= }}
*{{cite journal | author=Fry TJ, Mackall CL |title=Interleukin-7: from bench to clinic. |journal=Blood |volume=99 |issue= 11 |pages= 3892-904 |year= 2002 |pmid= 12010786 |doi= }}
*{{cite journal | author=Fry TJ, Mackall CL |title=Interleukin-7 and immunorestoration in HIV: beyond the thymus. |journal=J. Hematother. Stem Cell Res. |volume=11 |issue= 5 |pages= 803-7 |year= 2003 |pmid= 12427286 |doi= 10.1089/152581602760404603 }}
*{{cite journal | author=Al-Rawi MA, Mansel RE, Jiang WG |title=Interleukin-7 (IL-7) and IL-7 receptor (IL-7R) signalling complex in human solid tumours. |journal=Histol. Histopathol. |volume=18 |issue= 3 |pages= 911-23 |year= 2004 |pmid= 12792903 |doi= }}
*{{cite journal | author=Aspinall R, Henson S, Pido-Lopez J, Ngom PT |title=Interleukin-7: an interleukin for rejuvenating the immune system. |journal=Ann. N. Y. Acad. Sci. |volume=1019 |issue= |pages= 116-22 |year= 2004 |pmid= 15247003 |doi= 10.1196/annals.1297.021 }}
*{{cite journal | author=Snyder KM, Mackall CL, Fry TJ |title=IL-7 in allogeneic transplant: clinical promise and potential pitfalls. |journal=Leuk. Lymphoma |volume=47 |issue= 7 |pages= 1222-8 |year= 2007 |pmid= 16923550 |doi= 10.1080/10428190600555876 }}
*{{cite journal | author=Brunton LL, Lupton SD |title=An STS in the human IL7 gene located at 8q12-13. |journal=Nucleic Acids Res. |volume=18 |issue= 5 |pages= 1315 |year= 1990 |pmid= 2320434 |doi= }}
*{{cite journal | author=Lupton SD, Gimpel S, Jerzy R, ''et al.'' |title=Characterization of the human and murine IL-7 genes. |journal=J. Immunol. |volume=144 |issue= 9 |pages= 3592-601 |year= 1990 |pmid= 2329282 |doi= }}
*{{cite journal | author=Goodwin RG, Lupton S, Schmierer A, ''et al.'' |title=Human interleukin 7: molecular cloning and growth factor activity on human and murine B-lineage cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 1 |pages= 302-6 |year= 1989 |pmid= 2643102 |doi= }}
*{{cite journal | author=Sutherland GR, Baker E, Fernandez KE, ''et al.'' |title=The gene for human interleukin 7 (IL7) is at 8q12-13. |journal=Hum. Genet. |volume=82 |issue= 4 |pages= 371-2 |year= 1989 |pmid= 2786840 |doi= }}
*{{cite journal | author=Muegge K, Vila MP, Durum SK |title=Interleukin-7: a cofactor for V(D)J rearrangement of the T cell receptor beta gene. |journal=Science |volume=261 |issue= 5117 |pages= 93-5 |year= 1993 |pmid= 7686307 |doi= }}
*{{cite journal | author=Watanabe M, Ueno Y, Yajima T, ''et al.'' |title=Interleukin 7 is produced by human intestinal epithelial cells and regulates the proliferation of intestinal mucosal lymphocytes. |journal=J. Clin. Invest. |volume=95 |issue= 6 |pages= 2945-53 |year= 1995 |pmid= 7769137 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Noguchi M, Nakamura Y, Russell SM, ''et al.'' |title=Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor. |journal=Science |volume=262 |issue= 5141 |pages= 1877-80 |year= 1994 |pmid= 8266077 |doi= }}
*{{cite journal | author=Sica D, Rayman P, Stanley J, ''et al.'' |title=Interleukin 7 enhances the proliferation and effector function of tumor-infiltrating lymphocytes from renal-cell carcinoma. |journal=Int. J. Cancer |volume=53 |issue= 6 |pages= 941-7 |year= 1993 |pmid= 8473051 |doi= }}
*{{cite journal | author=Kroemer RT, Doughty SW, Robinson AJ, Richards WG |title=Prediction of the three-dimensional structure of human interleukin-7 by homology modeling. |journal=Protein Eng. |volume=9 |issue= 6 |pages= 493-8 |year= 1996 |pmid= 8862549 |doi= }}
*{{cite journal | author=Kroemer RT, Richards WG |title=Homology modeling study of the human interleukin-7 receptor complex. |journal=Protein Eng. |volume=9 |issue= 12 |pages= 1135-42 |year= 1997 |pmid= 9010926 |doi= }}
*{{cite journal | author=Kim JH, Loveland JE, Sitz KV, ''et al.'' |title=Expansion of restricted cellular immune responses to HIV-1 envelope by vaccination: IL-7 and IL-12 differentially augment cellular proliferative responses to HIV-1. |journal=Clin. Exp. Immunol. |volume=108 |issue= 2 |pages= 243-50 |year= 1997 |pmid= 9158092 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on INDO... {November 14, 2007 4:59:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:00:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_INDO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2d0t.
| PDB = {{PDB2|2d0t}}, {{PDB2|2d0u}}
| Name = Indoleamine-pyrrole 2,3 dioxygenase
| HGNCid = 6059
| Symbol = INDO
| AltSymbols =; CD107B; IDO
| OMIM = 147435
| ECnumber =
| Homologene = 48082
| MGIid = 96416
| GeneAtlas_image1 = PBB_GE_INDO_210029_at_tn.png
| Function = {{GNF_GO|id=GO:0004426 |text = tryptophan 2,3-dioxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0019441 |text = tryptophan catabolic process to kynurenine}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3620
| Hs_Ensembl = ENSG00000131203
| Hs_RefseqProtein = NP_002155
| Hs_RefseqmRNA = NM_002164
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 39890545
| Hs_GenLoc_end = 39905120
| Hs_Uniprot = P14902
| Mm_EntrezGene = 15930
| Mm_Ensembl = ENSMUSG00000031551
| Mm_RefseqmRNA = NM_008324
| Mm_RefseqProtein = NP_032350
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 26049686
| Mm_GenLoc_end = 26062554
| Mm_Uniprot = P28776
}}
}}
'''Indoleamine-pyrrole 2,3 dioxygenase''', also known as '''INDO''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Gamma-interferon (IFNG; MIM 147570) has an antiproliferative effect on many tumor cells and inhibits intracellular pathogens such as Toxoplasma and Chlamydia, at least partly because of the induction of indoleamine 2,3-dioxygenase (INDO; EC 1.13.11.42). This enzyme catalyzes the degradation of the essential amino acid L-tryptophan to N-formylkynurenine.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: INDO indoleamine-pyrrole 2,3 dioxygenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3620| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Grohmann U, Fallarino F, Puccetti P |title=Tolerance, DCs and tryptophan: much ado about IDO. |journal=Trends Immunol. |volume=24 |issue= 5 |pages= 242-8 |year= 2004 |pmid= 12738417 |doi= }}
*{{cite journal | author=Takikawa O |title=Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism. |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 1 |pages= 12-9 |year= 2005 |pmid= 16176799 |doi= 10.1016/j.bbrc.2005.09.032 }}
*{{cite journal | author=Puccetti P |title=On watching the watchers: IDO and type I/II IFN. |journal=Eur. J. Immunol. |volume=37 |issue= 4 |pages= 876-9 |year= 2007 |pmid= 17393386 |doi= 10.1002/eji.200737184 }}
*{{cite journal | author=Kadoya A, Tone S, Maeda H, ''et al.'' |title=Gene structure of human indoleamine 2,3-dioxygenase. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 1 |pages= 530-6 |year= 1992 |pmid= 1449503 |doi= }}
*{{cite journal | author=Kamimura S, Eguchi K, Yonezawa M, Sekiba K |title=Localization and developmental change of indoleamine 2,3-dioxygenase activity in the human placenta. |journal=Acta Med. Okayama |volume=45 |issue= 3 |pages= 135-9 |year= 1991 |pmid= 1716396 |doi= }}
*{{cite journal | author=Dai W, Gupta SL |title=Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=168 |issue= 1 |pages= 1-8 |year= 1990 |pmid= 2109605 |doi= }}
*{{cite journal | author=Tone S, Takikawa O, Habara-Ohkubo A, ''et al.'' |title=Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA. |journal=Nucleic Acids Res. |volume=18 |issue= 2 |pages= 367 |year= 1990 |pmid= 2326172 |doi= }}
*{{cite journal | author=Werner-Felmayer G, Werner ER, Fuchs D, ''et al.'' |title=Tumour necrosis factor-alpha and lipopolysaccharide enhance interferon-induced tryptophan degradation and pteridine synthesis in human cells. |journal=Biol. Chem. Hoppe-Seyler |volume=370 |issue= 9 |pages= 1063-9 |year= 1990 |pmid= 2482041 |doi= }}
*{{cite journal | author=Carlin JM, Borden EC, Byrne GI |title=Interferon-induced indoleamine 2,3-dioxygenase activity inhibits Chlamydia psittaci replication in human macrophages. |journal=J. Interferon Res. |volume=9 |issue= 3 |pages= 329-37 |year= 1989 |pmid= 2501398 |doi= }}
*{{cite journal | author=Kobayashi K, Hayashi K, Sono M |title=Effects of tryptophan and pH on the kinetics of superoxide radical binding to indoleamine 2,3-dioxygenase studied by pulse radiolysis. |journal=J. Biol. Chem. |volume=264 |issue= 26 |pages= 15280-3 |year= 1989 |pmid= 2549057 |doi= }}
*{{cite journal | author=Daley-Yates PT, Powell AP, Smith LL |title=Pulmonary indoleamine 2,3-dioxygenase activity and its significance in the response of rats, mice, and rabbits to oxidative stress. |journal=Toxicol. Appl. Pharmacol. |volume=96 |issue= 2 |pages= 222-32 |year= 1989 |pmid= 2848333 |doi= }}
*{{cite journal | author=Najfeld V, Menninger J, Muhleman D, ''et al.'' |title=Localization of indoleamine 2,3-dioxygenase gene (INDO) to chromosome 8p12-->p11 by fluorescent in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3-4 |pages= 231-2 |year= 1993 |pmid= 8404046 |doi= }}
*{{cite journal | author=Burkin DJ, Kimbro KS, Barr BL, ''et al.'' |title=Localization of the human indoleamine 2,3-dioxygenase (IDO) gene to the pericentromeric region of human chromosome 8. |journal=Genomics |volume=17 |issue= 1 |pages= 262-3 |year= 1993 |pmid= 8406467 |doi= }}
*{{cite journal | author=Malina HZ, Martin XD |title=Indoleamine 2,3-dioxygenase: antioxidant enzyme in the human eye. |journal=Graefes Arch. Clin. Exp. Ophthalmol. |volume=234 |issue= 7 |pages= 457-62 |year= 1996 |pmid= 8817290 |doi= }}
*{{cite journal | author=Munn DH, Zhou M, Attwood JT, ''et al.'' |title=Prevention of allogeneic fetal rejection by tryptophan catabolism. |journal=Science |volume=281 |issue= 5380 |pages= 1191-3 |year= 1998 |pmid= 9712583 |doi= }}
*{{cite journal | author=Takikawa O, Littlejohn TK, Truscott RJ |title=Indoleamine 2,3-dioxygenase in the human lens, the first enzyme in the synthesis of UV filters. |journal=Exp. Eye Res. |volume=72 |issue= 3 |pages= 271-7 |year= 2001 |pmid= 11180976 |doi= 10.1006/exer.2000.0951 }}
*{{cite journal | author=Kudo Y, Boyd CA |title=The role of L-tryptophan transport in L-tryptophan degradation by indoleamine 2,3-dioxygenase in human placental explants. |journal=J. Physiol. (Lond.) |volume=531 |issue= Pt 2 |pages= 417-23 |year= 2001 |pmid= 11230514 |doi= }}
*{{cite journal | author=Terentis AC, Thomas SR, Takikawa O, ''et al.'' |title=The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15788-94 |year= 2002 |pmid= 11867636 |doi= 10.1074/jbc.M200457200 }}
*{{cite journal | author=Kvirkvelia N, Vojnovic I, Warner TD, ''et al.'' |title=Placentally derived prostaglandin E2 acts via the EP4 receptor to inhibit IL-2-dependent proliferation of CTLL-2 T cells. |journal=Clin. Exp. Immunol. |volume=127 |issue= 2 |pages= 263-9 |year= 2002 |pmid= 11876748 |doi= }}
*{{cite journal | author=Sedlmayr P, Blaschitz A, Wintersteiger R, ''et al.'' |title=Localization of indoleamine 2,3-dioxygenase in human female reproductive organs and the placenta. |journal=Mol. Hum. Reprod. |volume=8 |issue= 4 |pages= 385-91 |year= 2002 |pmid= 11912287 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LIPC... {November 14, 2007 5:00:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:01:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Lipase, hepatic
| HGNCid = 6619
| Symbol = LIPC
| AltSymbols =; HL; HTGL; LIPH
| OMIM = 151670
| ECnumber =
| Homologene = 199
| MGIid = 96216
| GeneAtlas_image1 = PBB_GE_LIPC_206606_at_tn.png
| Function = {{GNF_GO|id=GO:0004806 |text = triacylglycerol lipase activity}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006487 |text = protein amino acid N-linked glycosylation}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3990
| Hs_Ensembl = ENSG00000166035
| Hs_RefseqProtein = NP_000227
| Hs_RefseqmRNA = NM_000236
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 56511467
| Hs_GenLoc_end = 56648364
| Hs_Uniprot = P11150
| Mm_EntrezGene = 15450
| Mm_Ensembl = ENSMUSG00000032207
| Mm_RefseqmRNA = NM_008280
| Mm_RefseqProtein = NP_032306
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 70597343
| Mm_GenLoc_end = 70734025
| Mm_Uniprot = Q3TYU0
}}
}}
'''Lipase, hepatic''', also known as '''LIPC''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = LIPC encodes hepatic triglyceride lipase, which is expressed in liver. LIPC has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake.<ref>{{cite web | title = Entrez Gene: LIPC lipase, hepatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3990| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Santamarina-Fojo S, Haudenschild C, Amar M |title=The role of hepatic lipase in lipoprotein metabolism and atherosclerosis. |journal=Curr. Opin. Lipidol. |volume=9 |issue= 3 |pages= 211-9 |year= 1998 |pmid= 9645503 |doi= }}
*{{cite journal | author=Jansen H, Verhoeven AJ, Sijbrands EJ |title=Hepatic lipase: a pro- or anti-atherogenic protein? |journal=J. Lipid Res. |volume=43 |issue= 9 |pages= 1352-62 |year= 2003 |pmid= 12235167 |doi= }}
*{{cite journal | author=Zambon A, Deeb SS, Pauletto P, ''et al.'' |title=Hepatic lipase: a marker for cardiovascular disease risk and response to therapy. |journal=Curr. Opin. Lipidol. |volume=14 |issue= 2 |pages= 179-89 |year= 2003 |pmid= 12642787 |doi= 10.1097/01.mol.0000064055.08840.77 }}
*{{cite journal | author=Hegele RA, Tu L, Connelly PW |title=Human hepatic lipase mutations and polymorphisms. |journal=Hum. Mutat. |volume=1 |issue= 4 |pages= 320-4 |year= 1993 |pmid= 1301939 |doi= 10.1002/humu.1380010410 }}
*{{cite journal | author=Hegele RA, Vezina C, Moorjani S, ''et al.'' |title=A hepatic lipase gene mutation associated with heritable lipolytic deficiency. |journal=J. Clin. Endocrinol. Metab. |volume=72 |issue= 3 |pages= 730-2 |year= 1991 |pmid= 1671786 |doi= }}
*{{cite journal | author=Hegele RA, Little JA, Connelly PW |title=Compound heterozygosity for mutant hepatic lipase in familial hepatic lipase deficiency. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 1 |pages= 78-84 |year= 1991 |pmid= 1883393 |doi= }}
*{{cite journal | author=Ameis D, Stahnke G, Kobayashi J, ''et al.'' |title=Isolation and characterization of the human hepatic lipase gene. |journal=J. Biol. Chem. |volume=265 |issue= 12 |pages= 6552-5 |year= 1990 |pmid= 2324091 |doi= }}
*{{cite journal | author=Datta S, Luo CC, Li WH, ''et al.'' |title=Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. |journal=J. Biol. Chem. |volume=263 |issue= 3 |pages= 1107-10 |year= 1988 |pmid= 2447084 |doi= }}
*{{cite journal | author=Cai SJ, Wong DM, Chen SH, Chan L |title=Structure of the human hepatic triglyceride lipase gene. |journal=Biochemistry |volume=28 |issue= 23 |pages= 8966-71 |year= 1990 |pmid= 2605236 |doi= }}
*{{cite journal | author=Stahnke G, Sprengel R, Augustin J, Will H |title=Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. |journal=Differentiation |volume=35 |issue= 1 |pages= 45-52 |year= 1988 |pmid= 2828141 |doi= }}
*{{cite journal | author=Martin GA, Busch SJ, Meredith GD, ''et al.'' |title=Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. |journal=J. Biol. Chem. |volume=263 |issue= 22 |pages= 10907-14 |year= 1988 |pmid= 2839510 |doi= }}
*{{cite journal | author=Sparkes RS, Zollman S, Klisak I, ''et al.'' |title=Human genes involved in lipolysis of plasma lipoproteins: mapping of loci for lipoprotein lipase to 8p22 and hepatic lipase to 15q21. |journal=Genomics |volume=1 |issue= 2 |pages= 138-44 |year= 1988 |pmid= 3692485 |doi= }}
*{{cite journal | author=Kounnas MZ, Chappell DA, Wong H, ''et al.'' |title=The cellular internalization and degradation of hepatic lipase is mediated by low density lipoprotein receptor-related protein and requires cell surface proteoglycans. |journal=J. Biol. Chem. |volume=270 |issue= 16 |pages= 9307-12 |year= 1995 |pmid= 7721852 |doi= }}
*{{cite journal | author=Mori A, Takagi A, Ikeda Y, ''et al.'' |title=An AvaII polymorphism in exon 5 of the human hepatic triglyceride lipase gene. |journal=Mol. Cell. Probes |volume=10 |issue= 4 |pages= 309-11 |year= 1996 |pmid= 8865179 |doi= 10.1006/mcpr.1996.0040 }}
*{{cite journal | author=Takagi A, Ikeda Y, Mori A, ''et al.'' |title=Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. |journal=Mol. Cell. Probes |volume=10 |issue= 4 |pages= 313-4 |year= 1996 |pmid= 8865180 |doi= 10.1006/mcpr.1996.0041 }}
*{{cite journal | author=Choi SY, Goldberg IJ, Curtiss LK, Cooper AD |title=Interaction between ApoB and hepatic lipase mediates the uptake of ApoB-containing lipoproteins. |journal=J. Biol. Chem. |volume=273 |issue= 32 |pages= 20456-62 |year= 1998 |pmid= 9685400 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Tiebel O, Gehrisch S, Pietzsch J, ''et al.'' |title=18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. |journal=Hum. Mutat. |volume=12 |issue= 3 |pages= 216 |year= 2000 |pmid= 10660332 |doi= }}
*{{cite journal | author=Yamakawa-Kobayashi K, Somekawa Y, Fujimura M, ''et al.'' |title=Relation of the -514C/T polymorphism in the hepatic lipase gene to serum HDL and LDL cholesterol levels in postmenopausal women under hormone replacement therapy. |journal=Atherosclerosis |volume=162 |issue= 1 |pages= 17-21 |year= 2002 |pmid= 11947893 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MEFV... {November 14, 2007 5:01:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:01:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Mediterranean fever
| HGNCid = 6998
| Symbol = MEFV
| AltSymbols =; MEF; FMF; MGC126560; MGC126586; TRIM20
| OMIM = 608107
| ECnumber =
| Homologene = 32441
| MGIid = 1859396
| GeneAtlas_image1 = PBB_GE_MEFV_208262_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0005875 |text = microtubule associated complex}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4210
| Hs_Ensembl = ENSG00000103313
| Hs_RefseqProtein = NP_000234
| Hs_RefseqmRNA = NM_000243
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 3232029
| Hs_GenLoc_end = 3246628
| Hs_Uniprot = O15553
| Mm_EntrezGene = 54483
| Mm_Ensembl = ENSMUSG00000022534
| Mm_RefseqmRNA = NM_019453
| Mm_RefseqProtein = NP_062326
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 3622450
| Mm_GenLoc_end = 3633325
| Mm_Uniprot = Q32MT1
}}
}}
'''Mediterranean fever''', also known as '''MEFV''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = MEFV was identified as the gene that when mutated causes Mediterranean fever, a hereditary periodic fever syndrome. MEFV is expressed in granulocytes and myeloid bone marrow precursors.<ref>{{cite web | title = Entrez Gene: MEFV Mediterranean fever| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4210| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NES... {November 14, 2007 5:06:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:07:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Nestin
| HGNCid = 7756
| Symbol = NES
| AltSymbols =; FLJ21841; Nbla00170
| OMIM = 600915
| ECnumber =
| Homologene = 31391
| MGIid = 101784
| GeneAtlas_image1 = PBB_GE_NES_218678_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0005882 |text = intermediate filament}}
| Process = {{GNF_GO|id=GO:0007417 |text = central nervous system development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10763
| Hs_Ensembl = ENSG00000132688
| Hs_RefseqProtein = NP_006608
| Hs_RefseqmRNA = NM_006617
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 154905179
| Hs_GenLoc_end = 154913813
| Hs_Uniprot = P48681
| Mm_EntrezGene = 18008
| Mm_Ensembl = ENSMUSG00000004891
| Mm_RefseqmRNA = NM_016701
| Mm_RefseqProtein = NP_057910
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 88057020
| Mm_GenLoc_end = 88066378
| Mm_Uniprot =
}}
}}
'''Nestin''', also known as '''NES''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Nestin is an intermediate filament protein that was first identified with a monoclonal antibody by Hockfield and McKay (1985). It is expressed predominantly in stem cells of the central nervous system in the neural tube. Upon terminal neural differentiation, nestin is downregulated and replaced by neurofilaments.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: NES nestin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10763| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wiese C, Rolletschek A, Kania G, ''et al.'' |title=Nestin expression--a property of multi-lineage progenitor cells? |journal=Cell. Mol. Life Sci. |volume=61 |issue= 19-20 |pages= 2510-22 |year= 2004 |pmid= 15526158 |doi= 10.1007/s00018-004-4144-6 }}
*{{cite journal | author=Dahlstrand J, Zimmerman LB, McKay RD, Lendahl U |title=Characterization of the human nestin gene reveals a close evolutionary relationship to neurofilaments. |journal=J. Cell. Sci. |volume=103 ( Pt 2) |issue= |pages= 589-97 |year= 1993 |pmid= 1478958 |doi= }}
*{{cite journal | author=Hockfield S, McKay RD |title=Identification of major cell classes in the developing mammalian nervous system. |journal=J. Neurosci. |volume=5 |issue= 12 |pages= 3310-28 |year= 1986 |pmid= 4078630 |doi= }}
*{{cite journal | author=Lothian C, Lendahl U |title=An evolutionarily conserved region in the second intron of the human nestin gene directs gene expression to CNS progenitor cells and to early neural crest cells. |journal=Eur. J. Neurosci. |volume=9 |issue= 3 |pages= 452-62 |year= 1997 |pmid= 9104587 |doi= }}
*{{cite journal | author=Yaworsky PJ, Kappen C |title=Heterogeneity of neural progenitor cells revealed by enhancers in the nestin gene. |journal=Dev. Biol. |volume=205 |issue= 2 |pages= 309-21 |year= 1999 |pmid= 9917366 |doi= 10.1006/dbio.1998.9035 }}
*{{cite journal | author=Cassiman D, van Pelt J, De Vos R, ''et al.'' |title=Synaptophysin: A novel marker for human and rat hepatic stellate cells. |journal=Am. J. Pathol. |volume=155 |issue= 6 |pages= 1831-9 |year= 1999 |pmid= 10595912 |doi= }}
*{{cite journal | author=Messam CA, Hou J, Major EO |title=Coexpression of nestin in neural and glial cells in the developing human CNS defined by a human-specific anti-nestin antibody. |journal=Exp. Neurol. |volume=161 |issue= 2 |pages= 585-96 |year= 2000 |pmid= 10686078 |doi= 10.1006/exnr.1999.7319 }}
*{{cite journal | author=About I, Bottero MJ, de Denato P, ''et al.'' |title=Human dentin production in vitro. |journal=Exp. Cell Res. |volume=258 |issue= 1 |pages= 33-41 |year= 2000 |pmid= 10912785 |doi= 10.1006/excr.2000.4909 }}
*{{cite journal | author=Sanchez-Ramos J, Song S, Cardozo-Pelaez F, ''et al.'' |title=Adult bone marrow stromal cells differentiate into neural cells in vitro. |journal=Exp. Neurol. |volume=164 |issue= 2 |pages= 247-56 |year= 2000 |pmid= 10915564 |doi= 10.1006/exnr.2000.7389 }}
*{{cite journal | author=Woodbury D, Schwarz EJ, Prockop DJ, Black IB |title=Adult rat and human bone marrow stromal cells differentiate into neurons. |journal=J. Neurosci. Res. |volume=61 |issue= 4 |pages= 364-70 |year= 2000 |pmid= 10931522 |doi= }}
*{{cite journal | author=Akiyama Y, Honmou O, Kato T, ''et al.'' |title=Transplantation of clonal neural precursor cells derived from adult human brain establishes functional peripheral myelin in the rat spinal cord. |journal=Exp. Neurol. |volume=167 |issue= 1 |pages= 27-39 |year= 2001 |pmid= 11161590 |doi= 10.1006/exnr.2000.7539 }}
*{{cite journal | author=Sahlgren CM, Mikhailov A, Hellman J, ''et al.'' |title=Mitotic reorganization of the intermediate filament protein nestin involves phosphorylation by cdc2 kinase. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16456-63 |year= 2001 |pmid= 11278541 |doi= 10.1074/jbc.M009669200 }}
*{{cite journal | author=Messam CA, Hou J, Berman JW, Major EO |title=Analysis of the temporal expression of nestin in human fetal brain derived neuronal and glial progenitor cells. |journal=Brain Res. Dev. Brain Res. |volume=134 |issue= 1-2 |pages= 87-92 |year= 2002 |pmid= 11947939 |doi= }}
*{{cite journal | author=Safford KM, Hicok KC, Safford SD, ''et al.'' |title=Neurogenic differentiation of murine and human adipose-derived stromal cells. |journal=Biochem. Biophys. Res. Commun. |volume=294 |issue= 2 |pages= 371-9 |year= 2002 |pmid= 12051722 |doi= 10.1016/S0006-291X(02)00469-2 }}
*{{cite journal | author=Gu H, Wang S, Messam CA, Yao Z |title=Distribution of nestin immunoreactivity in the normal adult human forebrain. |journal=Brain Res. |volume=943 |issue= 2 |pages= 174-80 |year= 2002 |pmid= 12101039 |doi= }}
*{{cite journal | author=Vanderwinden JM, Gillard K, De Laet MH, ''et al.'' |title=Distribution of the intermediate filament nestin in the muscularis propria of the human gastrointestinal tract. |journal=Cell Tissue Res. |volume=309 |issue= 2 |pages= 261-8 |year= 2003 |pmid= 12172785 |doi= 10.1007/s00441-002-0590-3 }}
*{{cite journal | author=Piper K, Ball SG, Turnpenny LW, ''et al.'' |title=Beta-cell differentiation during human development does not rely on nestin-positive precursors: implications for stem cell-derived replacement therapy. |journal=Diabetologia |volume=45 |issue= 7 |pages= 1045-7 |year= 2003 |pmid= 12187925 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=About I, Mitsiadis TA |title=Molecular aspects of tooth pathogenesis and repair: in vivo and in vitro models. |journal=Adv. Dent. Res. |volume=15 |issue= |pages= 59-62 |year= 2003 |pmid= 12640742 |doi= }}
*{{cite journal | author=Hao HN, Zhao J, Thomas RL, ''et al.'' |title=Fetal human hematopoietic stem cells can differentiate sequentially into neural stem cells and then astrocytes in vitro. |journal=J. Hematother. Stem Cell Res. |volume=12 |issue= 1 |pages= 23-32 |year= 2003 |pmid= 12662433 |doi= 10.1089/152581603321210109 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NTRK2... {November 14, 2007 5:01:59 PM PST}
- SEARCH REDIRECT: Control Box Found: NTRK2 {November 14, 2007 5:02:49 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:02:50 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:02:50 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:02:50 PM PST}
- UPDATED: Updated protein page: NTRK2 {November 14, 2007 5:03:00 PM PST}
- INFO: Beginning work on PAK2... {November 14, 2007 5:03:00 PM PST}
- SEARCH REDIRECT: Control Box Found: PAK2 {November 14, 2007 5:03:47 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:03:48 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:03:48 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:03:48 PM PST}
- UPDATED: Updated protein page: PAK2 {November 14, 2007 5:03:57 PM PST}
- INFO: Beginning work on PARK7... {November 14, 2007 5:07:39 PM PST}
- SEARCH REDIRECT: Control Box Found: PARK7 {November 14, 2007 5:08:19 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:08:20 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:08:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:08:20 PM PST}
- UPDATED: Updated protein page: PARK7 {November 14, 2007 5:08:27 PM PST}
- INFO: Beginning work on POLG... {November 14, 2007 5:03:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:04:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Polymerase (DNA directed), gamma
| HGNCid = 9179
| Symbol = POLG
| AltSymbols =; FLJ27114; PEO; POLG1; POLGA; SANDO; SCAE
| OMIM = 174763
| ECnumber =
| Homologene = 2016
| MGIid = 1196389
| GeneAtlas_image1 = PBB_GE_POLG_203366_at_tn.png
| GeneAtlas_image2 = PBB_GE_POLG_217635_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003891 |text = delta DNA polymerase activity}} {{GNF_GO|id=GO:0003895 |text = gamma DNA-directed DNA polymerase activity}} {{GNF_GO|id=GO:0004527 |text = exonuclease activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005760 |text = gamma DNA polymerase complex}}
| Process = {{GNF_GO|id=GO:0006264 |text = mitochondrial DNA replication}} {{GNF_GO|id=GO:0006287 |text = base-excision repair, gap-filling}} {{GNF_GO|id=GO:0007568 |text = aging}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5428
| Hs_Ensembl = ENSG00000140521
| Hs_RefseqProtein = NP_002684
| Hs_RefseqmRNA = NM_002693
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 87660577
| Hs_GenLoc_end = 87679030
| Hs_Uniprot = P54098
| Mm_EntrezGene = 18975
| Mm_Ensembl = ENSMUSG00000039176
| Mm_RefseqmRNA = NM_017462
| Mm_RefseqProtein = NP_059490
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 79322896
| Mm_GenLoc_end = 79339786
| Mm_Uniprot = P54099
}}
}}
'''Polymerase (DNA directed), gamma''', also known as '''POLG''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Graziewicz MA, Longley MJ, Copeland WC |title=DNA polymerase gamma in mitochondrial DNA replication and repair. |journal=Chem. Rev. |volume=106 |issue= 2 |pages= 383-405 |year= 2006 |pmid= 16464011 |doi= 10.1021/cr040463d }}
*{{cite journal | author=Hudson G, Chinnery PF |title=Mitochondrial DNA polymerase-gamma and human disease. |journal=Hum. Mol. Genet. |volume=15 Spec No 2 |issue= |pages= R244-52 |year= 2006 |pmid= 16987890 |doi= 10.1093/hmg/ddl233 }}
*{{cite journal | author=Lestienne P |title=Evidence for a direct role of the DNA polymerase gamma in the replication of the human mitochondrial DNA in vitro. |journal=Biochem. Biophys. Res. Commun. |volume=146 |issue= 3 |pages= 1146-53 |year= 1987 |pmid= 3619920 |doi= }}
*{{cite journal | author=Ropp PA, Copeland WC |title=Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. |journal=Genomics |volume=36 |issue= 3 |pages= 449-58 |year= 1997 |pmid= 8884268 |doi= 10.1006/geno.1996.0490 }}
*{{cite journal | author=Lecrenier N, Van Der Bruggen P, Foury F |title=Mitochondrial DNA polymerases from yeast to man: a new family of polymerases. |journal=Gene |volume=185 |issue= 1 |pages= 147-52 |year= 1997 |pmid= 9034326 |doi= }}
*{{cite journal | author=Walker RL, Anziano P, Meltzer PS |title=A PAC containing the human mitochondrial DNA polymerase gamma gene (POLG) maps to chromosome 15q25. |journal=Genomics |volume=40 |issue= 2 |pages= 376-8 |year= 1997 |pmid= 9119411 |doi= 10.1006/geno.1996.4580 }}
*{{cite journal | author=Zullo SJ, Butler L, Zahorchak RJ, ''et al.'' |title=Localization by fluorescence in situ hybridization (FISH) of human mitochondrial polymerase gamma (POLG) to human chromosome band 15q24-->q26, and of mouse mitochondrial polymerase gamma (Polg) to mouse chromosome band 7E, with confirmation by direct sequence analysis of bacterial artificial chromosomes (BACs). |journal=Cytogenet. Cell Genet. |volume=78 |issue= 3-4 |pages= 281-4 |year= 1998 |pmid= 9465903 |doi= }}
*{{cite journal | author=Kapsa RM, Quigley AF, Han TF, ''et al.'' |title=mtDNA replicative potential remains constant during ageing: polymerase gamma activity does not correlate with age related cytochrome oxidase activity decline in platelets. |journal=Nucleic Acids Res. |volume=26 |issue= 19 |pages= 4365-73 |year= 1998 |pmid= 9742236 |doi= }}
*{{cite journal | author=Spelbrink JN, Toivonen JM, Hakkaart GA, ''et al.'' |title=In vivo functional analysis of the human mitochondrial DNA polymerase POLG expressed in cultured human cells. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24818-28 |year= 2000 |pmid= 10827171 |doi= 10.1074/jbc.M000559200 }}
*{{cite journal | author=Van Goethem G, Dermaut B, Löfgren A, ''et al.'' |title=Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions. |journal=Nat. Genet. |volume=28 |issue= 3 |pages= 211-2 |year= 2001 |pmid= 11431686 |doi= 10.1038/90034 }}
*{{cite journal | author=Hirano M, DiMauro S |title=ANT1, Twinkle, POLG, and TP: new genes open our eyes to ophthalmoplegia. |journal=Neurology |volume=57 |issue= 12 |pages= 2163-5 |year= 2003 |pmid= 11756592 |doi= }}
*{{cite journal | author=Ponamarev MV, Longley MJ, Nguyen D, ''et al.'' |title=Active site mutation in DNA polymerase gamma associated with progressive external ophthalmoplegia causes error-prone DNA synthesis. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15225-8 |year= 2002 |pmid= 11897778 |doi= 10.1074/jbc.C200100200 }}
*{{cite journal | author=Nitanai Y, Satow Y, Adachi H, Tsujimoto M |title=Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. |journal=J. Mol. Biol. |volume=321 |issue= 2 |pages= 177-84 |year= 2002 |pmid= 12144777 |doi= }}
*{{cite journal | author=Lamantea E, Tiranti V, Bordoni A, ''et al.'' |title=Mutations of mitochondrial DNA polymerase gammaA are a frequent cause of autosomal dominant or recessive progressive external ophthalmoplegia. |journal=Ann. Neurol. |volume=52 |issue= 2 |pages= 211-9 |year= 2002 |pmid= 12210792 |doi= 10.1002/ana.10278 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Van Goethem G, Martin JJ, Dermaut B, ''et al.'' |title=Recessive POLG mutations presenting with sensory and ataxic neuropathy in compound heterozygote patients with progressive external ophthalmoplegia. |journal=Neuromuscul. Disord. |volume=13 |issue= 2 |pages= 133-42 |year= 2003 |pmid= 12565911 |doi= }}
*{{cite journal | author=Jazayeri M, Andreyev A, Will Y, ''et al.'' |title=Inducible expression of a dominant negative DNA polymerase-gamma depletes mitochondrial DNA and produces a rho0 phenotype. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9823-30 |year= 2003 |pmid= 12645575 |doi= }}
*{{cite journal | author=Garrido N, Griparic L, Jokitalo E, ''et al.'' |title=Composition and dynamics of human mitochondrial nucleoids. |journal=Mol. Biol. Cell |volume=14 |issue= 4 |pages= 1583-96 |year= 2003 |pmid= 12686611 |doi= 10.1091/mbc.E02-07-0399 }}
*{{cite journal | author=Agostino A, Valletta L, Chinnery PF, ''et al.'' |title=Mutations of ANT1, Twinkle, and POLG1 in sporadic progressive external ophthalmoplegia (PEO). |journal=Neurology |volume=60 |issue= 8 |pages= 1354-6 |year= 2004 |pmid= 12707443 |doi= }}
*{{cite journal | author=Van Goethem G, Schwartz M, Löfgren A, ''et al.'' |title=Novel POLG mutations in progressive external ophthalmoplegia mimicking mitochondrial neurogastrointestinal encephalomyopathy. |journal=Eur. J. Hum. Genet. |volume=11 |issue= 7 |pages= 547-9 |year= 2004 |pmid= 12825077 |doi= 10.1038/sj.ejhg.5201002 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POLR2J... {November 14, 2007 5:04:40 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2J {November 14, 2007 5:05:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:05:25 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:05:25 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:05:25 PM PST}
- UPDATED: Updated protein page: POLR2J {November 14, 2007 5:05:31 PM PST}
- INFO: Beginning work on PSAP... {November 14, 2007 5:05:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:06:13 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSAP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m12.
| PDB = {{PDB2|1m12}}, {{PDB2|1n69}}, {{PDB2|1sn6}}, {{PDB2|2dob}}, {{PDB2|2gtg}}
| Name = Prosaposin (variant Gaucher disease and variant metachromatic leukodystrophy)
| HGNCid = 9498
| Symbol = PSAP
| AltSymbols =; SAP1; FLJ00245; GLBA; MGC110993
| OMIM = 176801
| ECnumber =
| Homologene = 37680
| MGIid = 97783
| GeneAtlas_image1 = PBB_GE_PSAP_200866_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSAP_200871_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004098 |text = cerebroside-sulfatase activity}} {{GNF_GO|id=GO:0004336 |text = galactosylceramidase activity}} {{GNF_GO|id=GO:0004348 |text = glucosylceramidase activity}} {{GNF_GO|id=GO:0004557 |text = alpha-galactosidase activity}} {{GNF_GO|id=GO:0004565 |text = beta-galactosidase activity}} {{GNF_GO|id=GO:0004767 |text = sphingomyelin phosphodiesterase activity}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008289 |text = lipid binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006665 |text = sphingolipid metabolic process}} {{GNF_GO|id=GO:0006687 |text = glycosphingolipid metabolic process}} {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0007040 |text = lysosome organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5660
| Hs_Ensembl = ENSG00000197746
| Hs_RefseqProtein = NP_001035930
| Hs_RefseqmRNA = NM_001042465
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 73246061
| Hs_GenLoc_end = 73281132
| Hs_Uniprot = P07602
| Mm_EntrezGene = 19156
| Mm_Ensembl = ENSMUSG00000004207
| Mm_RefseqmRNA = NM_011179
| Mm_RefseqProtein = NP_035309
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 59673071
| Mm_GenLoc_end = 59697954
| Mm_Uniprot = Q3TID4
}}
}}
'''Prosaposin (variant Gaucher disease and variant metachromatic leukodystrophy)''', also known as '''PSAP''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a highly conserved glycoprotein which is a precursor for 4 cleavage products: saposins A, B, C, and D. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Mutations in this gene have been associated with Gaucher disease, Tay-Sachs disease, and metachromatic leukodystrophy. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref>{{cite web | title = Entrez Gene: PSAP prosaposin (variant Gaucher disease and variant metachromatic leukodystrophy)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5660| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gieselmann V, Zlotogora J, Harris A, ''et al.'' |title=Molecular genetics of metachromatic leukodystrophy. |journal=Hum. Mutat. |volume=4 |issue= 4 |pages= 233-42 |year= 1995 |pmid= 7866401 |doi= 10.1002/humu.1380040402 }}
*{{cite journal | author=Schnabel D, Schröder M, Fürst W, ''et al.'' |title=Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. |journal=J. Biol. Chem. |volume=267 |issue= 5 |pages= 3312-5 |year= 1992 |pmid= 1371116 |doi= }}
*{{cite journal | author=Hiraiwa M, Soeda S, Kishimoto Y, O'Brien JS |title=Binding and transport of gangliosides by prosaposin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 23 |pages= 11254-8 |year= 1993 |pmid= 1454804 |doi= }}
*{{cite journal | author=Rorman EG, Scheinker V, Grabowski GA |title=Structure and evolution of the human prosaposin chromosomal gene. |journal=Genomics |volume=13 |issue= 2 |pages= 312-8 |year= 1992 |pmid= 1612590 |doi= }}
*{{cite journal | author=Kondoh K, Hineno T, Sano A, Kakimoto Y |title=Isolation and characterization of prosaposin from human milk. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 1 |pages= 286-92 |year= 1992 |pmid= 1958198 |doi= }}
*{{cite journal | author=Holtschmidt H, Sandhoff K, Fürst W, ''et al.'' |title=The organization of the gene for the human cerebroside sulfate activator protein. |journal=FEBS Lett. |volume=280 |issue= 2 |pages= 267-70 |year= 1991 |pmid= 2013321 |doi= }}
*{{cite journal | author=Holtschmidt H, Sandhoff K, Kwon HY, ''et al.'' |title=Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. |journal=J. Biol. Chem. |volume=266 |issue= 12 |pages= 7556-60 |year= 1991 |pmid= 2019586 |doi= }}
*{{cite journal | author=Hineno T, Sano A, Kondoh K, ''et al.'' |title=Secretion of sphingolipid hydrolase activator precursor, prosaposin. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 2 |pages= 668-74 |year= 1991 |pmid= 2025281 |doi= }}
*{{cite journal | author=Schnabel D, Schröder M, Sandhoff K |title=Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. |journal=FEBS Lett. |volume=284 |issue= 1 |pages= 57-9 |year= 1991 |pmid= 2060627 |doi= }}
*{{cite journal | author=Zhang XL, Rafi MA, DeGala G, Wenger DA |title=The mechanism for a 33-nucleotide insertion in mRNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy. |journal=Hum. Genet. |volume=87 |issue= 2 |pages= 211-5 |year= 1991 |pmid= 2066109 |doi= }}
*{{cite journal | author=Fürst W, Schubert J, Machleidt W, ''et al.'' |title=The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein. |journal=Eur. J. Biochem. |volume=192 |issue= 3 |pages= 709-14 |year= 1990 |pmid= 2209618 |doi= }}
*{{cite journal | author=Rafi MA, Zhang XL, DeGala G, Wenger DA |title=Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 2 |pages= 1017-23 |year= 1990 |pmid= 2302219 |doi= }}
*{{cite journal | author=Kretz KA, Carson GS, Morimoto S, ''et al.'' |title=Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 7 |pages= 2541-4 |year= 1990 |pmid= 2320574 |doi= }}
*{{cite journal | author=Nakano T, Sandhoff K, Stümper J, ''et al.'' |title=Structure of full-length cDNA coding for sulfatide activator, a Co-beta-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. |journal=J. Biochem. |volume=105 |issue= 2 |pages= 152-4 |year= 1989 |pmid= 2498298 |doi= }}
*{{cite journal | author=Rorman EG, Grabowski GA |title=Molecular cloning of a human co-beta-glucosidase cDNA: evidence that four sphingolipid hydrolase activator proteins are encoded by single genes in humans and rats. |journal=Genomics |volume=5 |issue= 3 |pages= 486-92 |year= 1990 |pmid= 2515150 |doi= }}
*{{cite journal | author=Morimoto S, Martin BM, Yamamoto Y, ''et al.'' |title=Saposin A: second cerebrosidase activator protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3389-93 |year= 1989 |pmid= 2717620 |doi= }}
*{{cite journal | author=Dewji NN, Wenger DA, O'Brien JS |title=Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 23 |pages= 8652-6 |year= 1988 |pmid= 2825202 |doi= }}
*{{cite journal | author=O'Brien JS, Kretz KA, Dewji N, ''et al.'' |title=Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. |journal=Science |volume=241 |issue= 4869 |pages= 1098-101 |year= 1988 |pmid= 2842863 |doi= }}
*{{cite journal | author=Morimoto S, Martin BM, Kishimoto Y, O'Brien JS |title=Saposin D: a sphingomyelinase activator. |journal=Biochem. Biophys. Res. Commun. |volume=156 |issue= 1 |pages= 403-10 |year= 1988 |pmid= 2845979 |doi= }}
*{{cite journal | author=Dewji N, Wenger D, Fujibayashi S, ''et al.'' |title=Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator. |journal=Biochem. Biophys. Res. Commun. |volume=134 |issue= 2 |pages= 989-94 |year= 1986 |pmid= 2868718 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPA1... {November 14, 2007 5:06:14 PM PST}
- SEARCH REDIRECT: Control Box Found: RPA1 {November 14, 2007 5:06:51 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:06:52 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:06:52 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:06:52 PM PST}
- UPDATED: Updated protein page: RPA1 {November 14, 2007 5:06:59 PM PST}
end log.
