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RBM22_PONAB
ID   RBM22_PONAB             Reviewed;         420 AA.
AC   Q5RAY5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Pre-mRNA-splicing factor RBM22;
DE   AltName: Full=RNA-binding motif protein 22;
GN   Name=RBM22;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC       spliceosome. Involved in the first step of pre-mRNA splicing. Binds
CC       directly to the internal stem-loop (ISL) domain of the U6 snRNA and to
CC       the pre-mRNA intron near the 5' splice site during the activation and
CC       catalytic phases of the spliceosome cycle. Involved in both
CC       translocations of the nuclear SLU7 to the cytoplasm and the cytosolic
CC       calcium-binding protein PDCD6 to the nucleus upon cellular stress
CC       responses. {ECO:0000250|UniProtKB:Q9NW64}.
CC   -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC       complexes. Component of the postcatalytic spliceosome P complex.
CC       Interacts with PDCD6; the interaction induces translocation of PDCD6 in
CC       the cytoplasm. Interacts with PPIL1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NW64}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NW64}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9NW64}. Note=Nearly exclusively nuclear.
CC       Translocated from the nucleus to the cytoplasm after heat shock cell
CC       treatment. May be shuttling between the nucleus and the cytosol.
CC       {ECO:0000250|UniProtKB:Q9NW64}.
CC   -!- DOMAIN: The C-terminal RRM domain and the zinc finger motif are
CC       necessary for RNA-binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SLT11 family. {ECO:0000305}.
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DR   EMBL; CR858876; CAH91075.1; -; mRNA.
DR   RefSeq; NP_001125624.1; NM_001132152.1.
DR   AlphaFoldDB; Q5RAY5; -.
DR   SMR; Q5RAY5; -.
DR   STRING; 9601.ENSPPYP00000017855; -.
DR   GeneID; 100172542; -.
DR   KEGG; pon:100172542; -.
DR   CTD; 55696; -.
DR   eggNOG; KOG0153; Eukaryota.
DR   InParanoid; Q5RAY5; -.
DR   OrthoDB; 1272857at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR   GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039171; Cwc2/Slt11.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR14089; PTHR14089; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Spliceosome; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   CHAIN           2..420
FT                   /note="Pre-mRNA-splicing factor RBM22"
FT                   /id="PRO_0000250550"
FT   DOMAIN          232..305
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         159..186
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          303..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..398
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   CROSSLNK        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   CROSSLNK        149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT   CROSSLNK        290
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NW64"
SQ   SEQUENCE   420 AA;  46864 MW;  B172FB3FC9D9DB66 CRC64;
     MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRVTKEK YGKECKICAR PFTVFRWCPG
     VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSFKDDMPKS DVNKEYYTQN
     MEREISNSDG TRPVGMLGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP
     YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG
     DTITETDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV
     KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV
     VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP
 
 
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