Putative uncharacterized protein C6orf52

C6orf52
Identifiers
AliasesC6orf52, chromosome 6 open reading frame 52
External IDsGeneCards: C6orf52
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

347744

n/a

Ensembl

ENSG00000137434
ENSG00000285312

n/a

UniProt

Q5T4I8

n/a

RefSeq (mRNA)

NM_001145020
NM_001354357
NM_001388310
NM_001388311

n/a

RefSeq (protein)

NP_001138492
NP_001341286

n/a

Location (UCSC)Chr 6: 10.67 – 10.69 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Putative uncharacterized protein C6orf52 (C6orf52) is a protein in humans that is encoded by the gene "C6orf52" and has six known isoforms.[3] C6orf52 was identified in 2002 by The National Institutes of Health Mammalian Gene Collection (MGC) Program.[4] C6orf52 has one known paralog, tRNA selenocysteine 1-associated protein 1 (TRNAU1AP).[5]

Gene

The cytogenetic location of C6orf52 is 6p24.2 on the shorthand of chromosome 6.[6] It is 23,379 nucleotides long, spanning from nucleotide 10671418 to 10694797 and has a molecular weight of 17,383 Da with 9 different exons. C6orf52 has no common aliases although the major protein product is sometimes referred to as "Q5T4I8".[7]

Location of C6orf52 on shorthand of chromosome 6.

mRNA

C6orf52 is known to undergo alternative splicing and has six known isoforms of varying length.

Homology

Paralogs

C6orf52 has one identified paralog, tRNA selenocysteine 1-associated protein 1 (TRNAU1AP), which is located on chromosome one at 1p35.3.[5] TRNAU1AP is involved selenocysteine biosynthesis, selenoproteins synthesis efficiency enhancement and may be involved in the methylation of tRNA(Sec).[8]

Orthologs

C6orf52 is conserved through many species. It can be found it many mammals, reptiles, and birds, such as the Zebra Finch.[9]

Scientific nameNameAccessionSequence Similarity % Date of Divergence (Estimated MYA)[10]
Sus scrofaWild BoarNP_001138494.160.976 96
Taeniopygia guttataZebra FinchXP_004175377.156.90 312
Ailuropoda melanoleucaGiant PandaXP_019651607.164.43 96
Pelodiscus sinensisChinese Softshell TurtleXP_006138812.142.55 312
Canis lupus familiarisDogXP_005640089.164.29 96
Pan troglodytesCommon ChimpanzeeXP_009448762.298.03 6.65
Macaca mulattaRhesus macaqueNP_001180810.194.08 29.44

There is a domain of high conservation across species starting near the last third of the polypeptide.

Multiple sequence alignment for multiple orthologs of C6orf52. A high conservation domain begins near the last third of the polypeptide sequence.

Isoforms

Q5T4I8 has six known isoforms of varying amino acid length.

IsoformPolypeptide Length
X1207
X2182
X3177
X4176
X5126
X693

Tissue distribution

Tissue expression is highest within the oocyte, with high expression in the testes and female gonad.[7]

Tissue expression of Q5T4I8 in humans. Expression is highest in the oocyte.

Expression is extremely high (2000-3000 transcripts per million) in the first stages of embryonic development up until the blastocyst.

C6orf52 expression levels during preimplantation embryonic development, measured in transcripts per million (TPM)

Subcellular localization

It is predicted to be a non-transmembrane protein that is located within the nucleus.[11]

Structure

The protein composition is relatively high in glutamic acid and serine residue levels and is relatively low in tryptophan and arginine when compared to the average human protein composition.[12][13]

The secondary structure of C6orf52 consists mostly of coiled regions, however there is an extended alpha helix region within the highly conserved domain.[14][15]

Post-translational modifications

C6orf52 has two commonly predicted post-translational modifications present in the highly conserved domain.[16][17] The lysine at position 123 (of the major protein) within the highly conserved domain is expected to undergo sumoylation often, while the tyrosine at position 128 is expected to undergo phosphorylation. Sumoylation sites allow for the binding of SUMO (small ubiquitin-like modifier protein) which are known to alter different functional parameters of proteins such as subcellular localization, protein parenting, DNA binding and transactivation functions of transcription factors.[18] Tyrosine phosphorylation is associated with many things, namely growth factor signaling and cell differentiation during development which are recurring aspects of C6orf52.[19]

Clinical significance

Two proteins in cattle that have been linked to fat or energy metabolism were predicted to be similar to C6orf52, however there is no known clinical study done examining C6orf52.[20]

References

  1. 1 2 3 ENSG00000285312 GRCh38: Ensembl release 89: ENSG00000137434, ENSG00000285312 – Ensembl, May 2017
  2. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ "NCBI(National Center for Biotechnology Information)". Retrieved 2019-02-22.
  4. ↑ "NCBI(National Center for Biotechnology Information)". Virginia Medical. 105 (4): 272–277. April 1978. Retrieved 2019-02-25.
  5. 1 2 "NCBI(National Center for Biotechnology Information)". Retrieved 2019-02-25.
  6. ↑ "HUGO Gene Symbol Report". Retrieved 2019-02-25.
  7. 1 2 "UniProt". Retrieved 2019-02-25.
  8. ↑ "UniProt - TRNAU1AP - tRNA selenosysteine 1-associated protein 1 - Homo sapiens". UniProt. Retrieved 2019-05-06.
  9. ↑ "Blast NCBI". Retrieved 2019-02-25.
  10. ↑ "TimeTree: The Timescale of Life". Retrieved 2019-02-25.
  11. ↑ "PSORT II Prediction". Retrieved 2019-05-05.
  12. ↑ "The Institute for Environmental Modeling (TIEM)". Retrieved 2019-05-05.
  13. ↑ "ProtScale - Amino Acid Composition (in UniProKB/Swiss-Prot data bank)". Retrieved 2019-05-05.
  14. ↑ "NPS@: Network Protein Sequence Analysis - SOPMA". Retrieved 2019-05-05.
  15. ↑ "I-TASSER server for protein structure and function prediction". Retrieved 2019-05-05.
  16. ↑ "NetPhos 3.1 Server". Retrieved 2019-05-05.
  17. ↑ "SUMOplot Analysis Program - Abgent". Retrieved 2019-05-05.
  18. ↑ Hilgarth RS, Murphy LA, Skaggs HS, Wilkerson DC, Xing H, Sarge KD (December 2004). "Regulation and function of SUMO modification". The Journal of Biological Chemistry. 279 (52): 53899–53902. doi:10.1074/jbc.R400021200. PMID 15448161.
  19. ↑ Pasantes-Morales H, Franco R (April 2002). "Influence of protein tyrosine kinases on cell volume change-induced taurine release". Cerebellum. 1 (2). London, England: 103–109. doi:10.1080/147342202753671231. PMID 12882359. S2CID 9909209.
  20. ↑ Chow YW, Pietranico R, Mukerji A (1975). "NCBI(National Center for Biotechnology Information)". Biochemical and Biophysical Research Communications. 66 (4): 1424–1431. doi:10.1016/0006-291x(75)90518-5. PMID 6.
This page is issued from Wikipedia. The text is available under Creative Commons Attribution-Share Alike 4.0 unless otherwise noted. Additional terms may apply for the media files.