RBY1A_HUMAN
ID RBY1A_HUMAN Reviewed; 496 AA.
AC P0DJD3; Q15376; Q15377; Q15414; Q6NSB5; Q86VU6; Q8NHR0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=RNA-binding motif protein, Y chromosome, family 1 member A1;
DE AltName: Full=RNA-binding motif protein 1;
DE AltName: Full=RNA-binding motif protein 2;
DE AltName: Full=Y chromosome RNA recognition motif 1;
DE Short=hRBMY;
GN Name=RBMY1A1; Synonyms=RBM1, RBM2, YRRM1, YRRM2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8269511; DOI=10.1016/0092-8674(93)90616-x;
RA Ma K., Inglis J.D., Sharkey A., Bickmore W.A., Hill R.E., Prosser E.J.,
RA Speedson R.M., Thomson E.J., Jobling M.;
RT "A Y chromosome gene family with RNA-binding protein homology: candidates
RT for the azoospermia factor AZF controlling human spermatogenesis.";
RL Cell 75:1287-1295(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [4]
RP IDENTIFICATION.
RX PubMed=9598316; DOI=10.1006/geno.1998.5255;
RA Chai N.-N., Zhou H., Hernandez J., Najmabadi H., Bhasin S., Yen P.H.;
RT "Structure and organization of the RBMY genes on the human Y chromosome:
RT transposition and amplification of an ancestral autosomal hnRNPG gene.";
RL Genomics 49:283-289(1998).
RN [5]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9108067; DOI=10.1073/pnas.94.8.3848;
RA Elliott D.J., Millar M.R., Oghene K., Ross A., Kiesewetter F., Pryor J.,
RA McIntyre M., Hargreave T.B., Saunders P.T.K., Vogt P.H., Chandley A.C.,
RA Cooke H.;
RT "Expression of RBM in the nuclei of human germ cells is dependent on a
RT critical region of the Y chromosome long arm.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3848-3853(1997).
RN [6]
RP INTERACTION WITH KHDRBS3.
RX PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J.,
RA Cooke H.J., Artzt K., Eperon I.C.;
RT "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT binding protein implicated in spermatogenesis.";
RL Hum. Mol. Genet. 8:959-969(1999).
RN [7]
RP INTERACTION WITH TRA2B.
RC TISSUE=Testis;
RX PubMed=10749975; DOI=10.1093/hmg/9.5.685;
RA Venables J.P., Elliott D.J., Makarova O.V., Makarov E.M., Cooke H.J.,
RA Eperon E.C.;
RT "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins
RT interact with Tra2beta and affect splicing.";
RL Hum. Mol. Genet. 9:685-694(2000).
RN [8]
RP FUNCTION, INTERACTION WITH TRA2B, AND RNA-BINDING.
RX PubMed=12165565; DOI=10.1093/hmg/11.17.2037;
RA Hofmann Y., Wirth B.;
RT "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via
RT direct interaction with Htra2-beta1.";
RL Hum. Mol. Genet. 11:2037-2049(2002).
RN [9]
RP INTERACTION WITH KHDRBS1.
RX PubMed=15595951; DOI=10.1111/j.1365-2605.2004.00496.x;
RA Elliott D.J.;
RT "The role of potential splicing factors including RBMY, RBMX, hnRNPG-T and
RT STAR proteins in spermatogenesis.";
RL Int. J. Androl. 27:328-334(2004).
RN [10]
RP STRUCTURE BY NMR OF 1-109 IN COMPLEX WITH RNA.
RX PubMed=17318228; DOI=10.1038/sj.embor.7400910;
RA Skrisovska L., Bourgeois C.F., Stefl R., Grellscheid S.-N., Kister L.,
RA Wenter P., Elliott D.J., Stevenin J., Allain F.H.-T.;
RT "The testis-specific human protein RBMY recognizes RNA through a novel mode
RT of interaction.";
RL EMBO Rep. 8:372-379(2007).
CC -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required
CC for sperm development. Acts additively with TRA2B to promote exon 7
CC inclusion of the survival motor neuron SMN. Binds non-specifically to
CC mRNAs. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:8269511}.
CC -!- SUBUNIT: Interacts with splicing factor proteins SFRS3/SRP20,
CC TRA2B/SFRS10, KHDRBS1/SAM68 and KHDRBS3. {ECO:0000269|PubMed:10332027,
CC ECO:0000269|PubMed:10749975, ECO:0000269|PubMed:12165565,
CC ECO:0000269|PubMed:15595951, ECO:0000269|PubMed:17318228}.
CC -!- INTERACTION:
CC P0DJD3; Q8WTP8: AEN; NbExp=3; IntAct=EBI-8638511, EBI-8637627;
CC P0DJD3; Q9NRW3: APOBEC3C; NbExp=3; IntAct=EBI-8638511, EBI-1044593;
CC P0DJD3; Q14781: CBX2; NbExp=3; IntAct=EBI-8638511, EBI-745934;
CC P0DJD3; Q14011: CIRBP; NbExp=3; IntAct=EBI-8638511, EBI-538850;
CC P0DJD3; P49761: CLK3; NbExp=3; IntAct=EBI-8638511, EBI-745579;
CC P0DJD3; P61978: HNRNPK; NbExp=3; IntAct=EBI-8638511, EBI-304185;
CC P0DJD3; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-8638511, EBI-739832;
CC P0DJD3; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-8638511, EBI-10329013;
CC P0DJD3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-8638511, EBI-1567797;
CC P0DJD3; P79522: PRR3; NbExp=3; IntAct=EBI-8638511, EBI-2803328;
CC P0DJD3; P98179: RBM3; NbExp=4; IntAct=EBI-8638511, EBI-2949699;
CC P0DJD3; P38159: RBMX; NbExp=3; IntAct=EBI-8638511, EBI-743526;
CC P0DJD3; P54274: TERF1; NbExp=2; IntAct=EBI-8638511, EBI-710997;
CC P0DJD3; Q96PQ6: ZNF317; NbExp=5; IntAct=EBI-8638511, EBI-1210473;
CC P0DJD3-2; Q6P158: DHX57; NbExp=3; IntAct=EBI-11994018, EBI-1051531;
CC P0DJD3-2; P02008: HBZ; NbExp=3; IntAct=EBI-11994018, EBI-719843;
CC P0DJD3-2; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-11994018, EBI-7060731;
CC P0DJD3-2; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-11994018, EBI-12028858;
CC P0DJD3-2; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-11994018, EBI-2858213;
CC P0DJD3-2; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-11994018, EBI-10329013;
CC P0DJD3-2; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-11994018, EBI-1567797;
CC P0DJD3-2; P79522: PRR3; NbExp=3; IntAct=EBI-11994018, EBI-2803328;
CC P0DJD3-2; Q9Y272: RASD1; NbExp=3; IntAct=EBI-11994018, EBI-740818;
CC P0DJD3-2; P98179: RBM3; NbExp=3; IntAct=EBI-11994018, EBI-2949699;
CC P0DJD3-2; P38159: RBMX; NbExp=4; IntAct=EBI-11994018, EBI-743526;
CC P0DJD3-2; Q15415: RBMY1J; NbExp=3; IntAct=EBI-11994018, EBI-8642021;
CC P0DJD3-2; P09012: SNRPA; NbExp=4; IntAct=EBI-11994018, EBI-607085;
CC P0DJD3-2; P07101-3: TH; NbExp=3; IntAct=EBI-11994018, EBI-12001016;
CC P0DJD3-2; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-11994018, EBI-2849854;
CC P0DJD3-2; Q96PQ6: ZNF317; NbExp=3; IntAct=EBI-11994018, EBI-1210473;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9108067}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P0DJD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DJD3-2; Sequence=VSP_042316;
CC Name=3;
CC IsoId=P0DJD3-3; Sequence=VSP_042315;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8269511}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all of the transcriptionally active
CC stages of germ cell development from spermatogonia through
CC spermatocytes to round spermatids. {ECO:0000269|PubMed:9108067}.
CC -!- MISCELLANEOUS: The RBMY1 proteins are encoded by repeated regions of
CC the Y chromosome, mostly within the AZFb region. The exact number of
CC functional copies is unclear and may vary between individuals, and some
CC of them may represent pseudogenes. The proteins are very similar, which
CC makes the characterization of each protein difficult. Thus, most
CC experiments do not discriminate between the different members. One can
CC therefore suppose that reported interactions with a RBMY1 protein
CC involve all the proteins.
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DR EMBL; X76059; CAA53659.1; -; mRNA.
DR EMBL; BC047768; AAH47768.1; -; mRNA.
DR EMBL; BC070298; AAH70298.1; -; mRNA.
DR EMBL; AC010141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14796.1; -. [P0DJD3-1]
DR PIR; A49418; A49418.
DR RefSeq; NP_001307873.1; NM_001320944.1. [P0DJD3-2]
DR RefSeq; NP_001307874.1; NM_001320945.1. [P0DJD3-3]
DR RefSeq; NP_005049.1; NM_005058.3. [P0DJD3-1]
DR RefSeq; XP_011529792.1; XM_011531490.1. [P0DJD3-3]
DR PDB; 2FY1; NMR; -; A=1-109.
DR PDBsum; 2FY1; -.
DR AlphaFoldDB; P0DJD3; -.
DR SMR; P0DJD3; -.
DR BioGRID; 111875; 28.
DR IntAct; P0DJD3; 25.
DR MINT; P0DJD3; -.
DR iPTMnet; P0DJD3; -.
DR PhosphoSitePlus; P0DJD3; -.
DR BioMuta; RBMY1A1; -.
DR DMDM; 378522864; -.
DR jPOST; P0DJD3; -.
DR MassIVE; P0DJD3; -.
DR PaxDb; P0DJD3; -.
DR PeptideAtlas; P0DJD3; -.
DR PRIDE; P0DJD3; -.
DR ProteomicsDB; 52542; -. [P0DJD3-3]
DR Antibodypedia; 34794; 198 antibodies from 24 providers.
DR DNASU; 5940; -.
DR Ensembl; ENST00000303902.9; ENSP00000303712.6; ENSG00000234414.7. [P0DJD3-2]
DR Ensembl; ENST00000382707.6; ENSP00000372154.2; ENSG00000234414.7. [P0DJD3-1]
DR Ensembl; ENST00000439108.6; ENSP00000388006.3; ENSG00000234414.7. [P0DJD3-1]
DR GeneID; 378949; -.
DR GeneID; 5940; -.
DR KEGG; hsa:5940; -.
DR MANE-Select; ENST00000382707.6; ENSP00000372154.2; NM_005058.4; NP_005049.1.
DR UCSC; uc004fuq.4; human. [P0DJD3-1]
DR CTD; 378949; -.
DR CTD; 5940; -.
DR DisGeNET; 378949; -.
DR DisGeNET; 5940; -.
DR GeneCards; RBMY1A1; -.
DR GeneReviews; RBMY1A1; -.
DR HGNC; HGNC:9912; RBMY1A1.
DR HPA; ENSG00000234414; Tissue enriched (testis).
DR MalaCards; RBMY1A1; -.
DR MIM; 400006; gene.
DR neXtProt; NX_P0DJD3; -.
DR OpenTargets; ENSG00000234414; -.
DR Orphanet; 1646; Partial chromosome Y deletion.
DR VEuPathDB; HostDB:ENSG00000234414; -.
DR GeneTree; ENSGT00940000163524; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; P0DJD3; -.
DR OMA; AVCTEEM; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; P0DJD3; -.
DR TreeFam; TF331833; -.
DR PathwayCommons; P0DJD3; -.
DR SignaLink; P0DJD3; -.
DR BioGRID-ORCS; 378949; 7 hits in 212 CRISPR screens.
DR BioGRID-ORCS; 5940; 10 hits in 209 CRISPR screens.
DR Pharos; P0DJD3; Tbio.
DR PRO; PR:P0DJD3; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; P0DJD3; protein.
DR Bgee; ENSG00000234414; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; P0DJD3; baseline.
DR Genevisible; P0DJD3; HS.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..496
FT /note="RNA-binding motif protein, Y chromosome, family 1
FT member A1"
FT /id="PRO_0000081899"
FT DOMAIN 8..85
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 78..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042315"
FT VAR_SEQ 327..363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042316"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2FY1"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2FY1"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:2FY1"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2FY1"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2FY1"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2FY1"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:2FY1"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2FY1"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2FY1"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2FY1"
SQ SEQUENCE 496 AA; 55784 MW; 3E493C52C7BA9E7E CRC64;
MVEADHPGKL FIGGLNRETN EKMLKAVFGK HGPISEVLLI KDRTSKSRGF AFITFENPAD
AKNAAKDMNG KSLHGKAIKV EQAKKPSFQS GGRRRPPASS RNRSPSGSLR SARGSRGGTR
GWLPSHEGHL DDGGYTPDLK MSYSRGLIPV KRGPSSRSGG PPPKKSAPSA VARSNSWMGS
QGPMSQRREN YGVPPRRATI SSWRNDRMST RHDGYATNDG NHPSCQETRD YAPPSRGYAY
RDNGHSNRDE HSSRGYRNHR SSRETRDYAP PSRGHAYRDY GHSRRDESYS RGYRNRRSSR
ETREYAPPSR GHGYRDYGHS RRHESYSRGY RNHPSSRETR DYAPPHRDYA YRDYGHSSWD
EHSSRGYSYH DGYGEALGRD HSEHLSGSSY RDALQRYGTS HGAPPARGPR MSYGGSTCHA
YSNTRDRYGR SWESYSSCGD FHYCDREHVC RKDQRNPPSL GRVLPDPREA CGSSSYVASI
VDGGESRSEK GDSSRY
