RNA binding motif protein, Y-linked, family 1, member A1

RBMY1A1
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2FY1
Identifiers
Aliases	RBMY1A1 , RBM, RBM1, RBM2, RBMY, RBMY1C, YRRM1, YRRM2, RNA binding motif protein, Y-linked, family 1, member A1, RNA binding motif protein Y-linked family 1 member A1
External IDs	OMIM: 400006 HomoloGene: 121598 GeneCards: RBMY1A1
Gene location (Human)
Chr.	Y chromosome (human)
End	21,549,326 bp
Gene ontology
Molecular function	• GO:0001948 protein binding ; • mRNA binding ; • RNA binding ; • nucleic acid binding ;
Cellular component	• nucleus ; • nuclear speck ;
Biological process	• mRNA processing ; • regulation of alternative mRNA splicing, via spliceosome ; • RNA splicing ; • mRNA cis splicing, via spliceosome ;
	Sources:Amigo / QuickGO
Orthologs
	5940
	n/a
	ENSG00000234414
	n/a
	P0DJD3
	n/a
	NM_005058 ; NM_001320944 ; NM_001320945
	n/a
NP_001307873 ; NP_001307874 ; NP_005049 ; NP_001006120 ; NP_001307878 ;
	NP_001307879
	n/a
	Wikidata
View/Edit Human

Last updated September 16, 2021

RNA-binding motif protein, Y chromosome, family 1 member A1/C is a protein that in humans is encoded by the RBMY1A1 gene.^[3]^[4]^[5]

This gene encodes a protein containing an RNA-binding motif in the N-terminus and four SRGY (serine, arginine, glycine, tyrosine) boxes in the C-terminus. Multiple copies of this gene are found in the AZFb azoospermia factor region of chromosome Y and the encoded protein is thought to be involved in spermatogenesis. Most copies of this locus are pseudogenes, although six highly similar copies have full-length ORFs and are considered functional. Four functional copies of this gene are found within inverted repeat IR2; two functional copies of this gene are found in palindrome P3, along with two copies of PTPN13-like, Y-linked. Alternative splicing of transcripts results in two transcript variants that encode different proteins.^[5]

Related Research Articles

RNA-binding proteins are proteins that bind to the double or single stranded RNA in cells and participate in forming ribonucleoprotein complexes. RBPs contain various structural motifs, such as RNA recognition motif (RRM), dsRNA binding domain, zinc finger and others. They are cytoplasmic and nuclear proteins. However, since most mature RNA is exported from the nucleus relatively quickly, most RBPs in the nucleus exist as complexes of protein and pre-mRNA called heterogeneous ribonucleoprotein particles (hnRNPs). RBPs have crucial roles in various cellular processes such as: cellular function, transport and localization. They especially play a major role in post-transcriptional control of RNAs, such as: splicing, polyadenylation, mRNA stabilization, mRNA localization and translation. Eukaryotic cells encode diverse RBPs, approximately 500 genes, with unique RNA-binding activity and protein–protein interaction. During evolution, the diversity of RBPs greatly increased with the increase in the number of introns. Diversity enabled eukaryotic cells to utilize RNA exons in various arrangements, giving rise to a unique RNP (ribonucleoprotein) for each RNA. Although RBPs have a crucial role in post-transcriptional regulation in gene expression, relatively few RBPs have been studied systematically.

TIA1 or Tia1 cytotoxic granule-associated rna binding protein is a 3'UTR mRNA binding protein that can bind the 5'TOP sequence of 5'TOP mRNAs. It is associated with programmed cell death (apoptosis) and regulates alternative splicing of the gene encoding the Fas receptor, an apoptosis-promoting protein. Under stress conditions, TIA1 localizes to cellular RNA-protein conglomerations called stress granules. It is encoded by the TIA1 gene.

Deleted in azoospermia-like is a protein that in humans is encoded by the DAZL gene.

Deleted in azoospermia 1, also known as DAZ1, is a protein which in humans is encoded by the DAZ1 gene.

Probable ATP-dependent RNA helicase DDX5 also known as DEAD box protein 5 or RNA helicase p68 is an enzyme that in humans is encoded by the DDX5 gene.

Transformer-2 protein homolog beta, also known as TRA2B previously known as splicing factor, arginine/serine-rich 10 (SFRS10), is a protein that in humans is encoded by the TRA2B gene.

Heterogeneous nuclear ribonucleoprotein G is a protein that in humans is encoded by the RBMX gene.

Splicing factor, arginine/serine-rich 3 is a protein that in humans is encoded by the SFRS3 gene.

Deleted in azoospermia protein 3 is a protein that in humans is encoded by the DAZ3 gene.

Splicing factor, arginine/serine-rich 9, also known as SFRS9, is a human gene encoding an SR protein involved in splice site selection in alternative splicing.

Deleted in azoospermia protein 2 is a protein that in humans is encoded by the DAZ2 gene.

Probable ATP-dependent RNA helicase DDX6 is an enzyme that in humans is encoded by the DDX6 gene.

Quaking homolog, KH domain RNA binding (mouse), also known as QKI, is a protein which in humans is encoded by the QKI gene.

KH domain-containing, RNA-binding, signal transduction-associated protein 3 is a protein that in humans is encoded by the KHDRBS3 gene.

ATP-dependent RNA helicase DDX3Y is an enzyme that in humans is encoded by the DDX3Y gene.

Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 is an enzyme that in humans is encoded by the DHX38 gene.

RNA binding motif protein 9 (RBM9), also known as Rbfox2, is a protein which in humans is encoded by the RBM9 gene.

Probable ATP-dependent RNA helicase DDX10 is an enzyme that in humans is encoded by the DDX10 gene.

Polypyrimidine tract-binding protein 1 is a protein that in humans is encoded by the PTBP1 gene.

The DAZprotein family is a group of three highly conserved RNA-binding proteins that are important in gametogenesis and meiosis. Therefore, mutations in the genes that encode for the DAZ proteins can have detrimental consequences for fertility.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000234414 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Ma K, Inglis JD, Sharkey A, Bickmore WA, Hill RE, Prosser EJ, Speed RM, Thomson EJ, Jobling M, Taylor K, et al. (Jan 1994). "A Y chromosome gene family with RNA-binding protein homology: candidates for the azoospermia factor AZF controlling human spermatogenesis". Cell. 75 (7): 1287–95. doi:10.1016/0092-8674(93)90616-X. PMID 8269511. S2CID 24678568.
↑ Chai NN, Zhou H, Hernandez J, Najmabadi H, Bhasin S, Yen PH (Aug 1998). "Structure and organization of the RBMY genes on the human Y chromosome: transposition and amplification of an ancestral autosomal hnRNPG gene". Genomics. 49 (2): 283–9. doi:10.1006/geno.1998.5255. PMID 9598316.
1 2 "Entrez Gene: RBMY1A1 RNA binding motif protein, Y-linked, family 1, member A1".

Lavery R, Glennon M, Houghton J, et al. (2007). "Investigation of DAZ and RBMY1 gene expression in human testis by quantitative real-time PCR". Arch. Androl. 53 (2): 71–3. doi: 10.1080/01485010600915228 . PMID 17453684.
Skrisovska L, Bourgeois CF, Stefl R, et al. (2007). "The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction". EMBO Rep. 8 (4): 372–9. doi:10.1038/sj.embor.7400910. PMC 1852761 . PMID 17318228.
Lindtner S, Zolotukhin AS, Uranishi H, et al. (2007). "RNA-binding motif protein 15 binds to the RNA transport element RTÉ and provides a direct link to the NXF1 export pathway". J. Biol. Chem. 281 (48): 36915–28. doi: 10.1074/jbc.M608745200 . PMID 17001072.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Tsuei DJ, Hsu HC, Lee PH, et al. (2004). "RBMY, a male germ cell-specific RNA-binding protein, activated in human liver cancers and transforms rodent fibroblasts". Oncogene. 23 (34): 5815–22. doi: 10.1038/sj.onc.1207773 . PMID 15184870.
Skaletsky H, Kuroda-Kawaguchi T, Minx PJ, et al. (2003). "The male-specific region of the human Y chromosome is a mosaic of discrete sequence classes". Nature. 423 (6942): 825–37. Bibcode:2003Natur.423..825S. doi: 10.1038/nature01722 . PMID 12815422.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Tsuei DJ, Chang MH, Chen PJ, et al. (2003). "Characterization of integration patterns and flanking cellular sequences of hepatitis B virus in childhood hepatocellular carcinomas". J. Med. Virol. 68 (4): 513–21. doi:10.1002/jmv.10240. PMID 12376959. S2CID 26869562.
Friel A, Houghton JA, Glennon M, et al. (2002). "A preliminary report on the implication of RT-PCR detection of DAZ, RBMY1, USP9Y and Protamine-2 mRNA in testicular biopsy samples from azoospermic men". Int. J. Androl. 25 (1): 59–64. doi: 10.1046/j.1365-2605.2002.00326.x . PMID 11869379.
Pellizzoni L, Charroux B, Rappsilber J, et al. (2001). "A functional interaction between the survival motor neuron complex and RNA polymerase II". J. Cell Biol. 152 (1): 75–85. doi:10.1083/jcb.152.1.75. PMC 2193649 . PMID 11149922.
Elliott DJ, Bourgeois CF, Klink A, et al. (2000). "A mammalian germ cell-specific RNA-binding protein interacts with ubiquitously expressed proteins involved in splice site selection". Proc. Natl. Acad. Sci. U.S.A. 97 (11): 5717–22. Bibcode:2000PNAS...97.5717E. doi: 10.1073/pnas.97.11.5717 . PMC 18499 . PMID 10823932.
Venables JP, Elliott DJ, Makarova OV, et al. (2000). "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing". Hum. Mol. Genet. 9 (5): 685–94. doi: 10.1093/hmg/9.5.685 . PMID 10749975.
Elliott DJ, Oghene K, Makarov G, et al. (1998). "Dynamic changes in the subnuclear organisation of pre-mRNA splicing proteins and RBM during human germ cell development". J. Cell Sci. 111 (9): 1255–65. doi:10.1242/jcs.111.9.1255. PMID 9547301.
Prosser J, Inglis JD, Condie A, et al. (1997). "Degeneracy in human multicopy RBM (YRRM), a candidate spermatogenesis gene". Mamm. Genome. 7 (11): 835–42. doi:10.1007/s003359900246. PMID 8875892. S2CID 23907707.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000234414 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8269511-3] Ma K, Inglis JD, Sharkey A, Bickmore WA, Hill RE, Prosser EJ, Speed RM, Thomson EJ, Jobling M, Taylor K, et al. (Jan 1994). "A Y chromosome gene family with RNA-binding protein homology: candidates for the azoospermia factor AZF controlling human spermatogenesis". Cell. 75 (7): 1287–95. doi:10.1016/0092-8674(93)90616-X. PMID 8269511. S2CID 24678568.

[pmid9598316-4] Chai NN, Zhou H, Hernandez J, Najmabadi H, Bhasin S, Yen PH (Aug 1998). "Structure and organization of the RBMY genes on the human Y chromosome: transposition and amplification of an ancestral autosomal hnRNPG gene". Genomics. 49 (2): 283–9. doi:10.1006/geno.1998.5255. PMID 9598316.

[entrez-5] 1 2 "Entrez Gene: RBMY1A1 RNA binding motif protein, Y-linked, family 1, member A1".

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RNA binding motif protein, Y-linked, family 1, member A1

Related Research Articles

References

Further reading