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RB24B_XENLA
ID   RB24B_XENLA             Reviewed;         224 AA.
AC   Q9I8B3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=RNA-binding protein 24-B {ECO:0000305};
DE   AltName: Full=MTR-1a;
DE   AltName: Full=RNA-binding motif protein 24-B;
GN   Name=rbm24-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RA   Jasper H., Rupp R.A.;
RT   "MTG-1, an evolutionary conserved RNA binding protein involved in
RT   myogenesis.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=20338237; DOI=10.1016/j.mod.2010.03.002;
RA   Li H.Y., Bourdelas A., Carron C., Shi D.L.;
RT   "The RNA-binding protein Seb4/RBM24 is a direct target of MyoD and is
RT   required for myogenesis during Xenopus early development.";
RL   Mech. Dev. 127:281-291(2010).
CC   -!- FUNCTION: Multifunctional RNA-binding protein involved in the
CC       regulation of pre-mRNA splicing, mRNA stability and mRNA translation
CC       important for cell fate decision and differentiation. Plays a major
CC       role in pre-mRNA alternative splicing regulation. Mediates
CC       preferentially muscle-specific exon inclusion in numerous mRNAs
CC       important for striated cardiac and skeletal muscle cell
CC       differentiation. Binds to intronic splicing enhancer (ISE) composed of
CC       stretches of GU-rich motifs localized in flanking intron of exon that
CC       will be included by alternative splicing. Involved in embryonic stem
CC       cell (ESC) transition to cardiac cell differentiation by promoting pre-
CC       mRNA alternative splicing events of several pluripotency and/or
CC       differentiation genes. Plays a role in the regulation of mRNA stability
CC       and mRNA translation to which it is bound (By similarity). Involved in
CC       myogenic differentiation by regulating myog levels (PubMed:20338237).
CC       Binds to a huge amount of mRNAs. Required for embryonic heart
CC       development, sarcomer and M-band formation in striated muscles (By
CC       similarity). {ECO:0000250|UniProtKB:D3Z4I3,
CC       ECO:0000250|UniProtKB:Q9BX46, ECO:0000269|PubMed:20338237}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:D3Z4I3}.
CC   -!- INDUCTION: Up-regulated by the myogenic factor myoD during
CC       gastrulation. {ECO:0000269|PubMed:20338237}.
CC   -!- DOMAIN: The RRM domain is necessary for mRNA stability and mRNA
CC       translation regulation. {ECO:0000250|UniProtKB:Q9BX46}.
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DR   EMBL; AJ271404; CAB96420.1; -; mRNA.
DR   EMBL; BC044956; AAH44956.1; -; mRNA.
DR   RefSeq; NP_001079578.1; NM_001086109.1.
DR   AlphaFoldDB; Q9I8B3; -.
DR   SMR; Q9I8B3; -.
DR   DNASU; 379265; -.
DR   GeneID; 379265; -.
DR   KEGG; xla:379265; -.
DR   CTD; 379265; -.
DR   Xenbase; XB-GENE-6256347; rbm24.S.
DR   OMA; FAFGMPQ; -.
DR   OrthoDB; 1579773at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 379265; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:1990715; F:mRNA CDS binding; ISS:UniProtKB.
DR   GO; GO:0097157; F:pre-mRNA intronic binding; ISS:UniProtKB.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR   GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR   GO; GO:1902811; P:positive regulation of skeletal muscle fiber differentiation; ISS:UniProtKB.
DR   GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR   GO; GO:0010830; P:regulation of myotube differentiation; ISS: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; 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   Cytoplasm; Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; RNA-binding; Translation regulation.
FT   CHAIN           1..224
FT                   /note="RNA-binding protein 24-B"
FT                   /id="PRO_0000273374"
FT   DOMAIN          11..88
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   224 AA;  24076 MW;  170DE6886309160D CRC64;
     MHTTQKDTTY TKIFVGGLPY HTTDSSLRKY FEVFGDIEEA VVITDRQTGK SRGYGFVTMA
     DRAAAERACK DPNPIIDGRK ANVNLAYLGA KPRIMQPGFA FGVQQIHPAL VQRPYGIPAH
     YVYPQAYVQQ GLVIPHVQQT AAASTSPYID YTSAAYAQYA AAAAAAYDQY PYAASPATTG
     YVTAAGYGYA VPQPLTAATP GTAAAAAAAF AQYQPQQLQA DRMQ
 
 
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