Wikipedia

FAM110A

Protein FAM110A, also known as protein family with sequence similarity 110, A, C20orf55[5] or BA371L19.3[6] is encoded by the FAM110A gene. FAM110A is located on chromosome 20[6] and is a part of the greater FAM110 gene family,[7] consisting of FAM110A, FAM110B, and FAM110C.

FAM110A
Identifiers
AliasesFAM110A, C20orf55, F10, bA371L19.3, family with sequence similarity 110 member A
External IDsOMIM: 611393; MGI: 1921097; HomoloGene: 12862; GeneCards: FAM110A; OMA:FAM110A - orthologs
Orthologs
SpeciesHumanMouse
Entrez

83541

73847

Ensembl

ENSG00000125898

ENSMUSG00000027459

UniProt

Q9BQ89

Q8R184

RefSeq (mRNA)

NM_001289150
NM_001289151
NM_028666
NM_146127

RefSeq (protein)

NP_001276079
NP_001276080
NP_082942
NP_666239
NP_001393330

Location (UCSC)Chr 20: 0.83 – 0.86 MbChr 2: 151.81 – 151.82 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gene

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Overview

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In humans, FAM110A is located on the plus strand at 20p13.[6] The gene transcript is found from base pairs 833,715 to 846,279, with a total transcript length of 12,564 base pairs.[5] The FAM110A mRNA transcript is predicted to contain two exons.[5] An upstream promoter region for FAM110A is predicted to be 1,111 base pairs long.[8] Six different mRNA transcripts of FAM110A are predicted, all differing in their 5' untranslated regions.[5]

 
FAM110A genomic location on chromosome 20 (pictured in red).[6]

Homology

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219 organisms have been reported to have orthologs with the human FAM110A gene.[5]

FAM110A orthologs (relative to human FAM110A)[5]
Species Taxonomic group Date of divergence (MYA) Accession Sequence length Sequence identity Sequence similarity
Thirteen-lined ground squirrel (Ictidomys tridecemlineatus) Mammal 90 XP_005320619.1 295 92% 94%
Domesticated dog (Canis lupus familiaris) Mammal 96 XP_005634952.1 295 91% 93%
Armadillo (Dasypus novemcinctus) Mammal 105 XP_023446141.1 284 85% 85%
Garter snake (Thamnophis sirtalis) Reptile 312 XP_013922001.1 360 46% 58%
Painted turtle (Chrysemys picta bellii) Reptile 312 XP_005304966.1 362 48% 59%
Hummingbird (Calypte anna) Bird 312 XP_030319175.1 337 53% 61%
Chicken (Gallus gallus) Bird 312 XP_003642512.1 331 56% 62%
Worm (Microcaecilia unicolor) Amphibian 351.8 XP_030068004.1 381 39% 49%
Sterlet (Acipenser ruthenus) Fish 435 XP_033863480.2 350 43% 54%
Zebrafish (Danio rerio) Fish 435 XP_003201231.1 446 59% 71%
Deer tick (Ixodes scapularis) Arthropod 797 XP_029825208.1 337 31% 40%

Regulation

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FAM110A transcription factor binding sites[8]
Matrix family Matrix information Start position End position Strand Matrix similarity
TGF-β induced apoptosis proteins Cysteine-serine-rich nuclear protein 1 (AXUD1, AXIN1 up-regulated 1) 277 283 (+) 1.00
CAS interacting zinc finger protein Zinc finger protein 384 (Cas-interacting zinc finger protein - CIZ) 305 315 (+) 1.00
Lim homeodomain factors LIM homeobox transcription factor 1, alpha 342 364 (-) 1.00
SWI/SNF related nucleophosphoproteins with a RING finger DNA binding motif SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 3 354 364 (-) 1.00
SWI/SNF related nucleophosphoproteins with a RING finger DNA binding motif SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 3 357 367 (+) 1.00
Cart-1 (cartilage homeoprotein 1) Binding site for S8 type homeodomains 421 441 (-) 1.00
NKX homeodomain factors Homeo domain factor Nkx-2.5/Csx, tinman homolog low affinity sites 423 441 (-) 1.00
TCF11 transcription factor TCF11/LCR-F1/Nrf1 homodimers 559 565 (+) 1.00
EVI1-myleoid transforming protein MEL1 (MDS1/EVI1-like gene 1) DNA-binding domain 2 612 628 (-) 1.00
C2H2 zinc finger transcription factors 37 Zinc finger protein 37 alpha (KOX21) 770 778 (-) 1.00
C2H2 zinc finger transcription factors 2 Zinc finger with KRAB and SCAN domains 3 819 841 (-) 1.00
Myeloid zinc finger 1 factors Myeloid zinc finger protein MZF1 1002 1012 (-) 1.00
C2H2 zinc finger transcription factors 2 KRAB-containing zinc finger protein 300 1014 1036 (+) 1.00
C2H2 zinc finger transcription factors 2 Zinc finger with KRAB and SCAN domains 3 1029 1051 (-) 1.00

Protein

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Overview

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All human FAM110A transcript variants encode the same protein, which is 295 amino acids in length.[5] The human FAM110A protein is projected to weigh 31.3 kiladaltons and have an isoelectric point of 10.5.[9]

FAM110A repetitive structures[10]
Species Accession Repeating structures Positions
Human (Homo sapiens) NP_001035812.1 SPARP 162-166; 177-181
Chimpanzee (Pan troglodytes) XP_003316845.1 SPARP 162-166; 177-181
Mouse (Mus musculus) NP_001276079.1 PATP 11-14; 139-142
Chicken (Gallus gallus) XP_015151953.1 AVRR 88-91; 168-171
PRSA 104-107; 285-288
SAGR 106-109; 147-150
PAAP 158-161; 199-202
Zebrafish (Danio rerio) XP_009302562.1 LARP 88-91; 348-351
 
Immunofluorescent staining of FAM110A localization.[11]

Human FAM110A is predicted to contain one standard deviation less than average frequencies of methionine, asparagine, and isoleucine residues, while containing one standard deviation higher frequencies of serine and proline residues.[10] Human FAM110A is also predicted to contain a frequency of arginine residues two standard deviations higher than average.[10] The presence of a high frequency of arginine residues is also apparent in the FAM110A chimpanzee, mouse, chicken and zebrafish orthologs,[10] indicating that it may play a vital role to the function of the gene due to its high conservation.

FAM110A is predicted to be hydrophilic and soluble.[12]

 
Predicted FAM110A tertiary structure (C-score: -2.81).[13]

The tertiary structure of FAM110A is predicted to be 80% disordered.[14]

Post-translational modification

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The N-terminal glycine residue FAM110A is not predicted to be myristolated (confidence: 0.97),[15] indicating that FAM110A is not membrane-associated.

It is predicted that FAM110A contains no sulfation of tyrosine residues,[16] suggesting that FAM110A is not secreted.

Phosphorylation analysis indicates FAM110A to be associated with the AGC and Akt kinase families.[17]

Immunofluorescent analysis of FAM110A reveals the protein to be localized in the nucleoplasm, cytosol, and vesicles.[11]

Interacting proteins

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Proteins predicted to interact with FAM110A
Protein abbreviation Protein name Association type
CSNK1E Casein kinase 1 isoform ε Two hybrid
DYNA1I1 Cytoplasmic dynein 1 intermediate chain Two hybrid
KRT15 Type 1 cytoskeletal keratin Two hybrid
TRIM23 E3 ubiquitin-protein ligase Two hybrid
GOLGA2 Member 2 Golgin (subfamily A) Two hybrid

Clinical significance

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Cancer pathogenesis

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FAM110A has been observed to be abnormally expressed in prostate cancer metastasis, where it co-localizes with E-cadherin and β-catenin at cell-cell adherens junctions,[18] suggesting FAM110A’s involvement in the epithelial-to-mesenchymal transition in cancer pathogenesis. The greater FAM110 gene family is aberrantly methylated in breast cancer cells,[19] and has been shown to be associated with reduced time to distant metastasis in breast cancer patients.[19]

Cell cycle involvement

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FAM110A has been found to localize to centrosomes and accumulate at the microtubule organizing center in interphase and at spindle poles in mitosis.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125898 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027459 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d e f g "FAM110A family with sequence similarity 110 member A [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 19 December 2020.
  6. ^ a b c d "FAM110A Gene". GeneCards. Retrieved 19 December 2020.
  7. ^ a b Hauge H, Patzke S, Aasheim HC (July 2007). "Characterization of the FAM110 gene family". Genomics. 90 (1): 14–27. doi:10.1016/j.ygeno.2007.03.002. PMID 17499476.
  8. ^ a b "Genomatix". Archived from the original on 24 February 2001. Retrieved 19 December 2020.
  9. ^ "ExPASy - Compute pI/Mw tool". web.expasy.org. Swiss Institute of Bioinformatics. Retrieved 19 December 2020.
  10. ^ a b c d "SAPS: Statistical Analysis of Protein Sequences". EMBL-EBI. European Molecular Biology Laboratory. Retrieved 19 December 2020.
  11. ^ a b "Anti-FAM110A Antibody (HPA069240) - Atlas Antibodies". www.atlasantibodies.com. Atlas Antibodies. Retrieved 19 December 2020.
  12. ^ "SOSUI: Classification and secondary structure prediction for membrane proteins". harrier.nagahama-i-bio.ac.jp. Retrieved 19 December 2020.
  13. ^ "I-TASSER server for protein structure and function prediction". zhanglab.ccmb.med.umich.edu. Zhang Lab, University of Michigan.
  14. ^ "PHYRE2 Protein Fold Recognition Server". www.sbg.bio.ic.ac.uk. Structural Bioinformatics Group, Imperial College, London. Retrieved 19 December 2020.
  15. ^ "ExPASy - Myristoylation tool". web.expasy.org. Swiss Institute of Bioinformatics. Retrieved 19 December 2020.
  16. ^ "ExPASy - Sulfinator tool". web.expasy.org. Swiss Institute of Bioinformatics. Retrieved 19 December 2020.
  17. ^ "GPS 5.0 - Kinase-specific Phosphorylation Site Prediction". gps.biocuckoo.cn. The CUCKOO Workgroup.
  18. ^ Tsuruta, H.; Verhaegh, G.W.; Schalken, J.A. (April 2014). "The expression and function of FAM110A in human prostate cancer". European Urology Supplements. 13 (1): e303. doi:10.1016/S1569-9056(14)60298-0.
  19. ^ a b Locke WJ, Clark SJ (November 2012). "Epigenome remodelling in breast cancer: insights from an early in vitro model of carcinogenesis". Breast Cancer Research. 14 (6): 215. doi:10.1186/bcr3237. PMC 4053120. PMID 23168266.
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