RBY1C_HUMAN
ID RBY1C_HUMAN Reviewed; 496 AA.
AC P0DJD4; Q15376; Q15377; Q15414; Q6NSB5; Q86VU6; Q8NHR0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=RNA-binding motif protein, Y chromosome, family 1 member C;
GN Name=RBMY1C;
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 [GENOMIC DNA] OF 1-220 AND 332-496.
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 [2]
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 [3]
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 [4]
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 [5]
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).
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.
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:15595951}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9108067}.
CC -!- TISSUE SPECIFICITY: Testis-specific.
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; U36608; AAC16917.1; -; Genomic_DNA.
DR EMBL; U36604; AAC16917.1; JOINED; Genomic_DNA.
DR EMBL; U36605; AAC16917.1; JOINED; Genomic_DNA.
DR EMBL; U36606; AAC16917.1; JOINED; Genomic_DNA.
DR EMBL; U36607; AAC16917.1; JOINED; Genomic_DNA.
DR EMBL; U36610; AAC16918.1; -; Genomic_DNA.
DR EMBL; U36609; AAC16918.1; JOINED; Genomic_DNA.
DR PIR; A49418; A49418.
DR AlphaFoldDB; P0DJD4; -.
DR SMR; P0DJD4; -.
DR iPTMnet; P0DJD4; -.
DR PhosphoSitePlus; P0DJD4; -.
DR BioMuta; HGNC:9914; -.
DR DMDM; 378522970; -.
DR jPOST; P0DJD4; -.
DR MassIVE; P0DJD4; -.
DR PRIDE; P0DJD4; -.
DR GeneCards; RBMY1C; -.
DR HGNC; HGNC:9914; RBMY1C.
DR MIM; 400006; gene.
DR neXtProt; NX_P0DJD4; -.
DR InParanoid; P0DJD4; -.
DR PathwayCommons; P0DJD4; -.
DR Pharos; P0DJD4; Tdark.
DR PRO; PR:P0DJD4; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P0DJD4; protein.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Activator; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..496
FT /note="RNA-binding motif protein, Y chromosome, family 1
FT member C"
FT /id="PRO_0000415665"
FT DOMAIN 8..85
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 80..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 83..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"
SQ SEQUENCE 496 AA; 55784 MW; F912A0248CE0282E CRC64;
MVEADHPGKL FIGGLNRETN EKMLKAVFGK HGPISEVLLI KDRTSKSRGF AFITFENPAD
AKNAAKDMNG KSLHGKAIKV EQAQKPSFQS 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
