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RBY1B_MOUSE
ID   RBY1B_MOUSE             Reviewed;         380 AA.
AC   Q60990; E9Q2F9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=RNA-binding motif protein, Y chromosome, family 1 member B;
DE   AltName: Full=RNA-binding motif protein 1;
GN   Name=Rbmy1b; Synonyms=Gm3376, Rbm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=8817321; DOI=10.1093/hmg/5.7.869;
RA   Elliott D.J., Ma K., Kerr S.M., Thakrar R., Speed R., Chandley A.C.,
RA   Cooke H.;
RT   "An RBM homologue maps to the mouse Y chromosome and is expressed in germ
RT   cells.";
RL   Hum. Mol. Genet. 5:869-874(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12356914; DOI=10.1242/jcs.00111;
RA   Turner J.M.A., Mahadevaiah S.K., Elliott D.J., Garchon H.-J., Pehrson J.R.,
RA   Jaenisch R., Burgoyne P.S.;
RT   "Meiotic sex chromosome inactivation in male mice with targeted disruptions
RT   of Xist.";
RL   J. Cell Sci. 115:4097-4105(2002).
RN   [4]
RP   OVEREXPRESSION.
RX   PubMed=15051956; DOI=10.1159/000076821;
RA   Szot M., Grigoriev V., Mahadevaiah S.K., Ojarikre O.A., Toure A.,
RA   von Glasenapp E., Rattigan A., Turner J.M.A., Elliott D.J., Burgoyne P.S.;
RT   "Does Rbmy have a role in sperm development in mice?";
RL   Cytogenet. Genome Res. 103:330-336(2003).
RN   [5]
RP   ERRATUM OF PUBMED:15051956.
RA   Szot M., Grigoriev V., Mahadevaiah S.K., Ojarikre O.A., Toure A.,
RA   von Glasenapp E., Rattigan A., Turner J.M.A., Elliott D.J., Burgoyne P.S.;
RL   Cytogenet. Genome Res. 105:160-160(2004).
CC   -!- FUNCTION: RNA-binding protein which may be involved in spermatogenesis.
CC       Required for sperm development, possibly by participating in pre-mRNA
CC       splicing in the testis.
CC   -!- SUBUNIT: Interacts with splicing factor proteins SFRS3/SRP20,
CC       TRA2B/SFRS10, KHDRBS1/SAM68 and KHDRBS3.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8817321}.
CC   -!- DEVELOPMENTAL STAGE: Only expressed in spermatogonia and early
CC       spermatocytes, suggesting that expression is inactivated in the XY body
CC       during meiosis. {ECO:0000269|PubMed:12356914,
CC       ECO:0000269|PubMed:8817321}.
CC   -!- MISCELLANEOUS: The RBMY1 proteins are encoded by repeated regions of
CC       the Y chromosome. The exact number of functional copies is unclear and
CC       may vary between individuals, and some of them may represent
CC       pseudogenes.
CC   -!- MISCELLANEOUS: Overexpression of Rbmy proteins in mice carrying the
CC       Y(d1) deletion that removes most of the multi-copy Rbmy gene cluster
CC       does not have any effect and fails to reduce the frequency of abnormal
CC       sperm. These results raize the question of the role of Rbmy proteins in
CC       sperm development.
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DR   EMBL; U36929; AAB81555.1; -; mRNA.
DR   EMBL; AC163691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS85842.1; -.
DR   RefSeq; NP_001257441.1; NM_001270512.1.
DR   AlphaFoldDB; Q60990; -.
DR   SMR; Q60990; -.
DR   STRING; 10090.ENSMUSP00000141183; -.
DR   PaxDb; Q60990; -.
DR   PRIDE; Q60990; -.
DR   Ensembl; ENSMUST00000180202; ENSMUSP00000136808; ENSMUSG00000096520.
DR   Ensembl; ENSMUST00000186140; ENSMUSP00000141183; ENSMUSG00000096520.
DR   GeneID; 100041505; -.
DR   KEGG; mmu:100041505; -.
DR   MGI; MGI:3781554; Gm3376.
DR   VEuPathDB; HostDB:ENSMUSG00000096520; -.
DR   eggNOG; ENOG502QS9N; Eukaryota.
DR   GeneTree; ENSGT00940000163524; -.
DR   HOGENOM; CLU_042286_0_0_1; -.
DR   InParanoid; Q60990; -.
DR   OMA; HESYTIS; -.
DR   OrthoDB; 1579773at2759; -.
DR   PhylomeDB; Q60990; -.
DR   TreeFam; TF331833; -.
DR   BioGRID-ORCS; 100041505; 0 hits in 28 CRISPR screens.
DR   PRO; PR:Q60990; -.
DR   Proteomes; UP000000589; Chromosome Y.
DR   RNAct; Q60990; protein.
DR   Bgee; ENSMUSG00000096520; Expressed in spermatid and 6 other tissues.
DR   Genevisible; Q60990; MM.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
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; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..380
FT                   /note="RNA-binding motif protein, Y chromosome, family 1
FT                   member B"
FT                   /id="PRO_0000341541"
FT   DOMAIN          8..86
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          82..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        235
FT                   /note="H -> R (in Ref. 1; AAB81555)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="E -> Q (in Ref. 1; AAB81555)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="S -> N (in Ref. 1; AAB81555)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  43143 MW;  972820C72C476208 CRC64;
     MAETDQPGKI FIGGLNIKTR QKTLQEIFGR FGPVARVILM RDRETKKSRG FAFLTFRRPA
     DAKNAVKEMN GVILDGKRIK VKQARRPSSL ESGSKKRPPS FSRTRGASRI LKCGRGGRSR
     ARSGPSCEGN LGGDRYTPNF NVSSSGRHFA VKRNPSSKRD GPPSKRSATS AQTRSNTGLR
     GREPHRREIS RNMPRGEPAS SRRDEYPLPR DYGQSSNDRK YESTSRGYCD YGNYHSREES
     ASKVFSDHAG YLGGRDRDFS EYLSGNSYRD TYRSYGRFHE APSARGGNNR YDDYSNSQDG
     YGGRGEPYIS NRSNIYSSDY ERSGRQEVLP PPIDREYFDR EGRQERGHSP KDGLYSASRE
     SYSSNTKIWG IPWRSWRKQI
 
 
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