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I am WeigelaPen and I have started editing pages of protein domains, making links to the Pfam database of protein families/domains.

Please feel free to add more up-to-date annotation for any protein domains if you think the current annotation is old and where more recent work gives better explanation of function.


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Notes

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Template for Pfam-box or info-box Template:Infobox protein family

Glucose-6-phosphate dehydrogenase, NAD binding domain
 
glucose 6-phosphate dehydrogenase from leuconostoc mesenteroides
Identifiers
SymbolG6PD_N
PfamPF00479
Pfam clanCL0063
InterProIPR022674
PROSITEPDOC00067
SCOP21dpg / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Template for Table Table cell templates provide a set of templates to configure text and color in cells in a standard way, using phrases such as Yes, No or n/a.

Table

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Col 1 Human gene C. elegans gene D. melanogaster gene S. cerevisiae gene Sch. pombe gene
Ex for col 1, row1 Ex for col 2 Ex for col3 Ex for col4 Ex for col5 Ex for col6
Ex col1 row 2 a
CDK8 CDK8 cdk-8 Cdk8 SSN3 srb10
  • a Fungal-specific
  • b Protein-name in Sch. pombe

Table of conserved subunits of cytochrome oxidase c complex

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No. Subunit name Human protein Protein description from UniProt Pfam family with Human protein


1 Cox1 COX1_HUMAN Cytochrome c oxidase subunit 1 Pfam PF00115
2 Cox2 COX2_HUMAN Cytochrome c oxidase subunit 2 Pfam PF02790, Pfam PF00116
3 Cox3 COX3_HUMAN Cytochrome c oxidase subunit 3 Pfam PF00510
4 Cox4i1 COX41_HUMAN Cytochrome c oxidase subunit 4 isoform 1, mitochondrial Pfam PF02936
5 Cox4a2 COX42_HUMAN Cytochrome c oxidase subunit 4 isoform 2, mitochondrial Pfam PF02936
6 Cox5a COX5A_HUMAN Cytochrome c oxidase subunit 5A, mitochondrial Pfam PF02284
7 Cox5b COX5B_HUMAN Cytochrome c oxidase subunit 5B, mitochondrial Pfam PF01215
8 Cox6a1 CX6A1_HUMAN Cytochrome c oxidase subunit 6A1, mitochondrial Pfam PF02046
9 Cox6a2 CX6A2_HUMAN Cytochrome c oxidase subunit 6A2, mitochondrial Pfam PF02046
10 Cox6b1 CX6B1_HUMAN Cytochrome c oxidase subunit 6B1 Pfam PF02297
11 Cox6b2 CX6B2_HUMAN Cytochrome c oxidase subunit 6B2 Pfam PF02297
12 Cox6c COX6C_HUMAN Cytochrome c oxidase subunit 6C Pfam PF02937
13 Cox7a1 CX7A1_HUMAN Cytochrome c oxidase subunit 7A1, mitochondrial Pfam PF02238
14 Cox7a2 CX7A2_HUMAN Cytochrome c oxidase subunit 7A2, mitochondrial Pfam PF02238
15 Cox7a3 COX7S_HUMAN Putative cytochrome c oxidase subunit 7A3, mitochondrial Pfam PF02238
16 Cox7b COX7B_HUMAN Cytochrome c oxidase subunit 7B, mitochondrial Pfam PF05392
17 Cox7c COX7C_HUMAN Cytochrome c oxidase subunit 7C, mitochondrial Pfam PF02935
18 Cox7r COX7R_HUMAN Cytochrome c oxidase subunit 7A-related protein, mitochondrial Pfam PF02238
19 Cox8a COX8A_HUMAN Cytochrome c oxidase subunit 8A, mitochondrial P Pfam PF02285
20 Cox8c COX8C_HUMAN Cytochrome c oxidase subunit 8C, mitochondrial Pfam PF02285
Assembly subunits[1][2][3]
1 Coa1 COA1_HUMAN Cytochrome c oxidase assembly factor 1 homolog Pfam PF08695
2 Coa3 COA3_HUMAN Cytochrome c oxidase assembly factor 3 homolog, mitochondrial Pfam PF09813
3 Coa4 COA4_HUMAN Cytochrome c oxidase assembly factor 4 homolog, mitochondrial Pfam PF06747
4 Coa5 COA5_HUMAN Cytochrome c oxidase assembly factor 5 Pfam PF10203
5 Coa6 COA6_HUMAN Cytochrome c oxidase assembly factor 6 homolog Pfam PF02297
6 Coa7 COA7_HUMAN Cytochrome c oxidase assembly factor 7, Pfam PF08238
7 Cox11 COX11_HUMAN Cytochrome c oxidase assembly protein COX11 mitochondrial Pfam PF04442
8 Cox14 COX14_HUMAN Cytochrome c oxidase assembly protein Pfam PF14880
9 Cox15 COX15_HUMAN Cytochrome c oxidase assembly protein COX15 homolog Pfam PF02628
10 Cox16 COX16_HUMAN Cytochrome c oxidase assembly protein COX16 homolog mitochondrial Pfam PF14138
11 Cox17 COX17_HUMAN Cytochrome c oxidase copper chaperone Pfam PF05051
12 Cox18[4] COX18_HUMAN Mitochondrial inner membrane protein (Cytochrome c oxidase assembly protein 18) Pfam PF02096
13 Cox19 COX19_HUMAN Cytochrome c oxidase assembly protein Pfam PF06747
14 Cox20 COX20_HUMAN Cytochrome c oxidase protein 20 homolog Pfam PF12597






Table of Subunit composition of Complex III

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The bc1 complex, or Complex III, contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1.[5][6]

No. Subunit name Human protein Protein description from UniProt Pfam family with Human protein
Respiratory subunit proteins
1 MT-CYB / Cyt b CYB_HUMAN Cytochrome b PF13631
2 CYC1 / Cyt c1 CY1_HUMAN Cytochrome c1, heme protein, mitochondrial PF02167
3 Rieske / UCR1 UCRI_HUMAN Cytochrome b-c1 complex subunit Rieske, mitochondrial EC=1.10.2.2 PF02921 , PF00355
Core protein subunits
4 QCR1 / SU1 QCR1_HUMAN Cytochrome b-c1 complex subunit 1, mitochondrial PF00675, PF05193
5 QCR2 / SU2 QCR2_HUMAN Cytochrome b-c1 complex subunit 2, mitochondrial PF00675, PF05193
Low-molucular weight protein subunits
6 QCR6 / SU6 QCR6_HUMAN Cytochrome b-c1 complex subunit 6, mitochondrial PF02320
7 QCR7 / SU7 QCR7_HUMAN Cytochrome b-c1 complex subunit 7 PF02271
8 QCR8 / SU8 QCR8_HUMAN Cytochrome b-c1 complex subunit 8 PF02939
9 QCR9 / SU9 / UCRC QCR9_HUMAN Cytochrome b-c1 complex subunit 9 PF05365
10 QCR10 / SU10 QCR10_HUMAN Cytochrome b-c1 complex subunit 10 PF08997
11 QCR11 / SU11 a UCRI_HUMAN Cytochrome b-c1 complex subunit 11 PF09165
  • a A cleavage product of 8 kDa from the N-terminus of Rieske








|- | 1 || SdhA || SDHA_HUMAN || Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial ||PF00890, PF02910 |-

| 2 || SdhB || SDHB_HUMAN || Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial ||PF13085, PF13183 |-


| 3 || SdhC || C560_HUMAN || Succinate dehydrogenase cytochrome b560 subunit, mitochondrial ||PF01127 |-


| 4 || SdhD || DHSD_HUMAN || Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial ||PF05328 |-

|}


Table of E.coli small Ribosomal subunits

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Subunit No. Subunit name E.coli protein Pfam family with E.coli protein
1 30S ribosomal protein S1 RS1_ECOLI PF00575
2 30S ribosomal protein S2 RS2_ECOLI PF00318
3 30S ribosomal protein S3 RS3_ECOLI PF00189 ,PF07650
4 30S ribosomal protein S4 RS4_ECOLI PF00163 ,PF01479
5 30S ribosomal protein S5 RS5_ECOLI PF00333 ,PF03719
6 30S ribosomal protein S6 RS6_ECOLI PF01250
7 30S ribosomal protein S7 RS7_ECOLI PF00177
8 30S ribosomal protein S8 RS8_ECOLI PF00410
9 30S ribosomal protein S9 RS9_ECOLI PF00380
10 30S ribosomal protein S10 RS10_ECOLI PF00338
11 30S ribosomal protein S11 RS11_ECOLI PF00411
12 30S ribosomal protein S12 RS12_ECOLI PF00164
13 30S ribosomal protein S13 RS13_ECOLI PF00416
14 30S ribosomal protein S14 RS14_ECOLI PF00253
15 30S ribosomal protein S15 RS15_ECOLI PF00312
16 30S ribosomal protein S16 RS16_ECOLI PF00886
27 30S ribosomal protein S17 RS17_ECOLI PF00366
28 30S ribosomal protein S18 RS18_ECOLI PF01084
29 30S ribosomal protein S19 RS19_ECOLI PF00203
20 30S ribosomal protein S20 RS20_ECOLI PF01649
21 30S ribosomal protein S21 RS21_ECOLI PF01165
22 aStationary-phase-induced ribosome-associated protein SRA_ECOLI PF08136

a : Alternative name 30S ribosomal protein S22 - Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein. It is not essential for bacterial growth.[7]

Table of Human small Ribosomal subunits

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Subunit No. Subunit name Human protein Pfam family with Human protein Pfam family description


2 ribosomal protein S2 RS2_HUMAN PF03719 Ribosomal protein S5, C-terminal domain
2 ribosomal protein S2 RS2_HUMAN PF00333 Ribosomal protein S5, N-terminal domain
3 ribosomal protein S3 RS3_HUMAN PF00189 Ribosomal protein S3, C-terminal domain
3a ribosomal protein S3a RS3A_HUMAN PF01015 Ribosomal S3Ae family
4 ribosomal protein S4, X isoform RS4X_HUMAN PF08071 RS4NT (NUC023) domain
4 ribosomal protein S4, X isoform RS4X_HUMAN PF01479 S4 domain
4 ribosomal protein S4, X isoform RS4X_HUMAN PF00900 Ribosomal family S4e
4 ribosomal protein S4, X isoform RS4X_HUMAN PF16121 40S ribosomal protein S4 C-terminus
4 ribosomal protein S4, Y isoform 1 RS4Y1_HUMAN PF08071 RS4NT (NUC023) domain
4 ribosomal protein S4, Y isoform 1 RS4Y1_HUMAN PF00900 Ribosomal family S4e
4 ribosomal protein S4, Y isoform 1 RS4Y1_HUMAN PF16121 40S ribosomal protein S4 C-terminus
4 ribosomal protein S4, Y isoform 2 RS4Y2_HUMAN PF08071 RS4NT (NUC023) domain
4 ribosomal protein S4, Y isoform 2 RS4Y2_HUMAN PF00900 Ribosomal family S4e
4 ribosomal protein S4, Y isoform 2 RS4Y2_HUMAN PF16121 40S ribosomal protein S4 C-terminus
5 ribosomal protein S5 RS5_HUMAN PF00177 Ribosomal protein S7p/S5e
6 ribosomal protein S6 RS6_HUMAN PF01092 Ribosomal protein S6e
7 ribosomal protein S7 RS7_HUMAN PF01251 Ribosomal protein S7e
8 ribosomal protein S8 RS8_HUMAN PF01201 Ribosomal protein S8e
9 ribosomal protein S9 RS9_HUMAN PF01479 S4 domain
9 ribosomal protein S9 RS9_HUMAN PF00163 Ribosomal protein S4/S9 N-terminal domain
10 ribosomal protein S10 RS10_HUMAN PF03501 Plectin/S10 domain
11 ribosomal protein S11 RS11_HUMAN PF16205 Ribosomal_S17 N-terminal
11 ribosomal protein S11 RS11_HUMAN PF00366 Ribosomal protein S17
12 ribosomal protein S12 RS12_HUMAN PF01248 Ribosomal protein L7Ae/L30e/S12e/Gadd45 family
13 ribosomal protein S13 RS13_HUMAN PF08069 Ribosomal S13/S15 N-terminal domain
13 ribosomal protein S13 RS13_HUMAN PF00312 Ribosomal protein S15
14 ribosomal protein S14 RS14_HUMAN PF00411 Ribosomal protein S11
15 ribosomal protein S15 RS15_HUMAN PF00203 Ribosomal protein S19
15a ribosomal protein S15a RS15A_HUMAN PF00410 Ribosomal protein S8
16 ribosomal protein S16 RS16_HUMAN PF00380 Ribosomal protein S9/S16
17 ribosomal protein S17 RS17_HUMAN PF00833 Ribosomal S17
18 ribosomal protein S18 RS18_HUMAN PF00416 Ribosomal protein S13/S18
19 ribosomal protein S19 RS19_HUMAN PF01090 Ribosomal protein S19e
20 ribosomal protein S20 RS20_HUMAN PF00338 Ribosomal protein S10p/S20e
21 ribosomal protein S21 RS21_HUMAN PF01249 Ribosomal protein S21e
23 ribosomal protein S23 RS23_HUMAN PF00164 Ribosomal protein S12/S23
24 ribosomal protein S24 RS24_HUMAN PF01282 Ribosomal protein S24e
25 ribosomal protein S25 RS25_HUMAN PF03297 S25 ribosomal protein
26 ribosomal protein S26 RS26_HUMAN PF01283 Ribosomal protein S26e
27 ribosomal protein S27 RS27_HUMAN PF01667 Ribosomal protein S27
28 ribosomal protein S28 RS28_HUMAN PF01200 Ribosomal protein S28e
29 ribosomal protein S29 RS29_HUMAN PF00253 Ribosomal protein S14p/S29e
30 ribosomal protein S30 RS30_HUMAN PF04758 Ribosomal protein S30
A ribosomal protein SA RSSA_HUMAN PF16122 40S ribosomal protein SA C-terminus
A ribosomal protein SA RSSA_HUMAN PF00318 Ribosomal protein S2

Assembly of the ribosome in eukaryotes

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Ribosomes, which synthesize the proteome of cells, are complex ribonucleoproteins that, in eukaryotes, contain 79–80 proteins and four ribosomal RNAs(rRNAs). General or specialized chaperones solubilize the ribosomal proteins and facilitate their import into the nucleus. Assembly of the eukaryotic ribosome appears to be driven by the ribosomal proteins in vivo when assembly is also aided by chaperones. Most ribosomal proteins assemble with rRNA co-transcriptionally, becoming associated more stably as assembly proceeds, and the active sites of both subunits are constructed last.[8]

Recent de novo proteomics experiments where the authors characterized in vivo ribosome-assembly intermediates and associated assembly factors from wild-type Escherichia coli cells using a general quantitative mass spectrometry (qMS) approach have confirmed the presence of all the known small and large subunit components and have identified a total of 21 known and potentially new ribosome-assembly-factors that co-localise with various ribosomal particles.[9]

Bacterial and eukaryotic ribosomes, which share an evolutionarily conserved core, are thought to have evolved from a common ancestor by addition of proteins and RNA that bestow different functionalities to ribosomes from different domains of life.[10] The term 'the core' refers to the structurally conserved part of the 70S ribosomes (from T. thermophilus and Escherichia coli) and the 80S ribosomes (from S. cerevisiae), deduced by a standard procedure of structural alignment.[11]

Table of Human 60S large subunit components

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infoboxes lost to ComplexI

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NADH-Ubiquinone/plastoquinone (complex I), various chains
Identifiers
SymbolOxidored_q1
PfamPF00361
Pfam clanCL0425
InterProIPR001750
TCDB3.D.9
OPM superfamily279
OPM protein3rko
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH-Ubiquinone oxidoreductase (complex I) subunit C-terminus
Identifiers
SymbolOxidored_q1_C
PfamPF01010
InterProIPR002128
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus
Identifiers
SymbolOxidored_q1_N
PfamPF00662
InterProIPR001516
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH-ubiquinone/plastoquinone oxidoreductase chain 4L
Identifiers
SymbolOxidored_q2
PfamPF00420
InterProIPR001133
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH-ubiquinone/plastoquinone oxidoreductase chain 6
Identifiers
SymbolOxidored_q3
PfamPF00499
InterProIPR001457
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH-ubiquinone/plastoquinone oxidoreductase, chain 3
Identifiers
SymbolOxidored_q4
PfamPF00507
InterProIPR000440
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH-ubiquinone oxidoreductase chain 4, amino terminus
Identifiers
SymbolOxidored_q5_N
PfamPF01059
InterProIPR000260
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NADH ubiquinone oxidoreductase, 20 Kd subunit
Identifiers
SymbolOxidored_q6
PfamPF01058
InterProIPR006137
PROSITEPDOC00858
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Reference management

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  • plagiarism checker. If you are doing any of Chris's wikipedia articles this is the best plagiarism checker I have found to use:
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Table of Conserved subunits of ComplexI[12][13]

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No. Human/Bovine subunit Human protein Protein description (UniProt) Pfam family with Human protein
Core Subunitsa
1 NDUFS7 / PSST / NUKM NDUS7_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF01058
2 NDUFS8 / TYKY / NUIM NDUS8_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF12838
3 NDUFV2 / 24kD / NUHM NDUV2_HUMAN NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF01257
4 NDUFS3 / 30kD / NUGM NDUS3_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF00329
5 NDUFS2 / 49kD / NUCM NDUS2_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF00346
6 NDUFV1 / 51kD / NUBM NDUV1_HUMAN NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF01512
7 NDUFS1 / 75kD / NUAM NDUS1_HUMAN NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial EC=1.6.5.3 EC=1.6.99.3 PF00384
8 ND1 / NU1M NU1M_HUMAN NADH-ubiquinone oxidoreductase chain 1 EC=1.6.5.3 PF00146
9 ND2 / NU2M NU2M_HUMAN NADH-ubiquinone oxidoreductase chain 2 EC=1.6.5.3 PF00361, PF06444
10 ND3 / NU3M NU3M_HUMAN NADH-ubiquinone oxidoreductase chain 3 EC=1.6.5.3 PF00507
11 ND4 / NU4M NU4M_HUMAN NADH-ubiquinone oxidoreductase chain 4 EC=1.6.5.3 PF01059,PF00361
12 ND4L / NULM NU4LM_HUMAN NADH-ubiquinone oxidoreductase chain 4L EC=1.6.5.3 PF00420
13 ND5 / NU5M NU5M_HUMAN NADH-ubiquinone oxidoreductase chain 5 EC=1.6.5.3 PF00361
14 ND6 / NU6M NU6M_HUMAN NADH-ubiquinone oxidoreductase chain 6 EC=1.6.5.3 PF00499
Core accessory subunitsb
15 NDUFS6 / 13A NDUS6_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial PF10276
16 NDUFA12 / B17.2 NDUAC_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 PF05071
17 NDUFS4 / AQDQ NDUS4_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial PF04800
18 NDUFA9 / 39kDa NDUA9_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial PF01370
19 NDUFAB1 / ACPM ACPM_HUMAN Acyl carrier protein, mitochondrial PF00550
20 NDUFA2 / B8 NDUA2_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 PF05047
21 NDUFA1 / MFWE NDUA1_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 PF15879
22 NDUFB3 / B12 NDUB3_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 PF08122
23 NDUFA5 / AB13 NDUA5_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 -
24 NDUFA6 / B14 NDUA6_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 PF05347
25 NDUFA11 / B14.7 NDUAB_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 PF02466
26 NDUFB11 / ESSS NDUBB_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial PF10183
27 NDUFS5 / PFFD NDUS5_HUMAN NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 PF10200
28 NDUFB4 / B15 NDUB4_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 PF07225
29 NDUFA13 /A13 NDUAD_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 PF06212
30 NDUFB7 / B18 NDUB7_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 PF05676
31 NDUFA8 / PGIV NDUA8_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 PF06747
32 NDUFB9 / B22 NDUB9_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 PF05347
33 NDUFB10 / PDSW NDUBA_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 PF10249
34 NDUFB8 / ASHI NDUB8_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial PF05821
35 NDUFC2 / B14.5B NDUC2_HUMAN NADH dehydrogenase [ubiquinone] 1 subunit C2 PF06374
36 NDUFB2 / AGGG NDUB2_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial PF14813
37 NDUFA7 / B14.5A NDUA7_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 PF07347
38 NDUFA3 / B9 NDUA3_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 PF14987
39 NDUFA4 / MLRQ NDUA4_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4 PF06522
40 NDUFB5 / SGDH NDUB5_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial PF09781
41 NDUFB1 / MNLL NDUB1_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 PF08040
42 NDUFC1 / KFYI NDUC1_HUMAN NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial PF15088
43 NDUFA10 / 42kD NDUAA_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial PF01712
44 NDUFA4L2 NUA4L_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2 PF15880
45 NDUFV3 NDUV3_HUMAN NADH dehydrogenase [ubiquinone] flavoprotein 3, 10kDa -
46 NDUFB6 NDUB6_HUMAN NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 PF09782
Assembly factor proteins[14]
47 NDUFAF1 CIA30_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, assembly factor 1 PF08547
48 NDUFAF2 MIMIT_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, assembly factor 2 PF05071
49 NDUFAF3 NDUF3_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3 PF05071
50 NDUFAF4 NDUF4_HUMAN NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, assembly factor 4 PF06784
  • a Found in all species
  • b May or may not be present in any species

Pages under construction

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  • User:WeigelaPen/Sandpit
Cyclin
 
Structure of the Pho85-Pho80 CDK-cyclin Complex of the Phosphate-responsive Signal Transduction Pathway *************needs reference
Identifiers
Symbol?
PfamPF08613
Pfam clanCL0065
InterProIPR013922
PROSITEPDOC00264
SCOP247954 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB2pk9
Cyclin, N-terminal domain
 
Structure of bovine cyclin A.[17]
Identifiers
SymbolCyclin_N

For Article on WINE, to add:See also

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[[Category:Oenology| ]] [[Category:Natural polyphenols|*]] [[de:Phenole im Wein]]

External links

  1. ^ Szklarczyk R, Wanschers BF, Cuypers TD, Esseling JJ, Riemersma M, van den Brand MA; et al. (2012). "Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase". Genome Biol. 13 (2): R12. doi:10.1186/gb-2012-13-2-r12. PMC 3334569. PMID 22356826. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  2. ^ Mick DU, Dennerlein S, Wiese H, Reinhold R, Pacheu-Grau D, Lorenzi I; et al. (2012). "MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation". Cell. 151 (7): 1528–41. doi:10.1016/j.cell.2012.11.053. PMID 23260140. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  3. ^ Kozjak-Pavlovic V, Prell F, Thiede B, Götz M, Wosiek D, Ott C; et al. (2014). "C1orf163/RESA1 is a novel mitochondrial intermembrane space protein connected to respiratory chain assembly". J Mol Biol. 426 (4): 908–20. doi:10.1016/j.jmb.2013.12.001. PMID 24333015. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  4. ^ Gaisne M, Bonnefoy N (2006). "The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast". FEMS Yeast Res. 6 (6): 869–82. doi:10.1111/j.1567-1364.2006.00083.x. PMID 16911509.
  5. ^ Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW; et al. (1998). "Electron transfer by domain movement in cytochrome bc1". Nature. 392 (6677): 677–84. doi:10.1038/33612. PMID 9565029. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  6. ^ Hao GF, Wang F, Li H, Zhu XL, Yang WC, Huang LS; et al. (2012). "Computational discovery of picomolar Q(o) site inhibitors of cytochrome bc1 complex". J Am Chem Soc. 134 (27): 11168–76. doi:10.1021/ja3001908. PMID 22690928. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
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