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SRS1B_DANRE
ID   SRS1B_DANRE             Reviewed;         245 AA.
AC   Q6NYA0; Q502R8; Q6PH14;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Serine/arginine-rich splicing factor 1B;
DE   AltName: Full=Splicing factor, arginine/serine-rich 1;
DE   AltName: Full=Splicing factor, arginine/serine-rich 1B;
GN   Name=srsf1b; Synonyms=sfrs1, sfrs1b;
GN   ORFNames=zgc:111894, zgc:65898, zgc:76897;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 64-245.
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: May play a role in preventing exon skipping, ensuring the
CC       accuracy of splicing and regulating alternative splicing.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07955}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q07955}. Note=In nuclear speckles.
CC       Shuttles between the nucleus and the cytoplasm.
CC       {ECO:0000250|UniProtKB:Q07955}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH56752.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; BC056752; AAH56752.1; ALT_SEQ; mRNA.
DR   EMBL; BC066682; AAH66682.1; -; mRNA.
DR   EMBL; BC095586; AAH95586.1; -; mRNA.
DR   EMBL; AL929224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_956887.2; NM_200593.2.
DR   AlphaFoldDB; Q6NYA0; -.
DR   SMR; Q6NYA0; -.
DR   STRING; 7955.ENSDARP00000102203; -.
DR   PaxDb; Q6NYA0; -.
DR   Ensembl; ENSDART00000143566; ENSDARP00000116886; ENSDARG00000017843.
DR   GeneID; 393565; -.
DR   KEGG; dre:393565; -.
DR   CTD; 393565; -.
DR   ZFIN; ZDB-GENE-040426-1467; srsf1b.
DR   eggNOG; KOG0105; Eukaryota.
DR   GeneTree; ENSGT00940000155585; -.
DR   HOGENOM; CLU_012062_34_0_1; -.
DR   InParanoid; Q6NYA0; -.
DR   OrthoDB; 1321443at2759; -.
DR   PhylomeDB; Q6NYA0; -.
DR   Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DRE-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-DRE-72187; mRNA 3'-end processing.
DR   Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR   PRO; PR:Q6NYA0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 21.
DR   Bgee; ENSDARG00000017843; Expressed in testis and 26 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
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   CDD; cd12597; RRM1_SRSF1; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034520; SRSF1_RRM1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Repeat; RNA-binding.
FT   CHAIN           1..245
FT                   /note="Serine/arginine-rich splicing factor 1B"
FT                   /id="PRO_0000081914"
FT   DOMAIN          15..90
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          120..194
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          89..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..222
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        53
FT                   /note="P -> Q (in Ref. 1; AAH95586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="S -> G (in Ref. 1; AAH95586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244..245
FT                   /note="RT -> PVCFLSSLVCWVFMI (in Ref. 1; AAH95586)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27475 MW;  99F04687D0AEA25F CRC64;
     MSGGVIRGPA GNNDCRIYVG NLPPDIRTKD VEDVFYKYGA IRDIDLKNRR GGPPFAFVEF
     EDPRDAEDAV YGRDGYDYDG YRLRVEFPRS GRGGGRGGGG GGGVGAPRGR YGPPSRRSEY
     RVIVSGLPPS GSWQDLKDHM REAGDVCYAD VFRDGTGVVE FVRKEDMTYA VRKLDNTKFR
     SHEGETAYIR VKVDGPRSPS YGRSRSRSRS RSRSRSNSRS RSYSPRRSRG SPRYSPRHSR
     SRSRT
 
 
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