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PYM1_MOUSE
ID   PYM1_MOUSE              Reviewed;         203 AA.
AC   Q8CHP5; Q80YD2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804};
DE   AltName: Full=PYM homolog 1 exon junction complex-associated factor {ECO:0000312|MGI:MGI:1925678};
DE   AltName: Full=Protein wibg homolog;
GN   Name=Pym1 {ECO:0000312|MGI:MGI:1925678}; Synonyms=Pym, Wibg;
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] (ISOFORM 1).
RX   PubMed=12438415; DOI=10.1083/jcb.200207128;
RA   Gatfield D., Izaurralde E.;
RT   "REF1/Aly and the additional exon junction complex proteins are dispensable
RT   for nuclear mRNA export.";
RL   J. Cell Biol. 159:579-588(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Key regulator of the exon junction complex (EJC), a
CC       multiprotein complex that associates immediately upstream of the exon-
CC       exon junction on mRNAs and serves as a positional landmark for the
CC       intron exon structure of genes and directs post-transcriptional
CC       processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA
CC       decay (NMD) or translation. Acts as an EJC disassembly factor, allowing
CC       translation-dependent EJC removal and recycling by disrupting mature
CC       EJC from spliced mRNAs. Its association with the 40S ribosomal subunit
CC       probably prevents a translation-independent disassembly of the EJC from
CC       spliced mRNAs, by restricting its activity to mRNAs that have been
CC       translated. Interferes with NMD and enhances translation of spliced
CC       mRNAs, probably by antagonizing EJC functions (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with MAGOH and RBM8A; the
CC       interaction is direct. Associates (eIF2A-like region) with the 40S
CC       ribosomal subunit and the 48S preinitiation complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRP8}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BRP8}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9BRP8}. Note=Shuttles between the nucleus and
CC       the cytoplasm. Nuclear export is mediated by XPO1/CRM1.
CC       {ECO:0000250|UniProtKB:Q9BRP8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CHP5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHP5-2; Sequence=VSP_025431;
CC   -!- DOMAIN: The eIF2A-like region shares sequence similarity with eIF2A and
CC       mediates the interaction with the 40S ribosomal subunit and the 48S
CC       preinitiation complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR   EMBL; AJ459407; CAD30678.1; -; mRNA.
DR   EMBL; BC049647; AAH49647.1; -; mRNA.
DR   CCDS; CCDS48729.1; -. [Q8CHP5-1]
DR   CCDS; CCDS48730.1; -. [Q8CHP5-2]
DR   RefSeq; NP_001164340.1; NM_001170869.2. [Q8CHP5-2]
DR   RefSeq; NP_084376.2; NM_030100.4. [Q8CHP5-1]
DR   AlphaFoldDB; Q8CHP5; -.
DR   SMR; Q8CHP5; -.
DR   BioGRID; 219395; 15.
DR   IntAct; Q8CHP5; 1.
DR   MINT; Q8CHP5; -.
DR   STRING; 10090.ENSMUSP00000129789; -.
DR   iPTMnet; Q8CHP5; -.
DR   PhosphoSitePlus; Q8CHP5; -.
DR   EPD; Q8CHP5; -.
DR   jPOST; Q8CHP5; -.
DR   MaxQB; Q8CHP5; -.
DR   PaxDb; Q8CHP5; -.
DR   PeptideAtlas; Q8CHP5; -.
DR   PRIDE; Q8CHP5; -.
DR   ProteomicsDB; 301854; -. [Q8CHP5-1]
DR   ProteomicsDB; 301855; -. [Q8CHP5-2]
DR   Antibodypedia; 48574; 218 antibodies from 19 providers.
DR   DNASU; 78428; -.
DR   Ensembl; ENSMUST00000065210; ENSMUSP00000067623; ENSMUSG00000064030. [Q8CHP5-2]
DR   Ensembl; ENSMUST00000163377; ENSMUSP00000129789; ENSMUSG00000064030. [Q8CHP5-1]
DR   GeneID; 78428; -.
DR   KEGG; mmu:78428; -.
DR   UCSC; uc007hod.3; mouse. [Q8CHP5-1]
DR   UCSC; uc007hoe.3; mouse. [Q8CHP5-2]
DR   CTD; 84305; -.
DR   MGI; MGI:1925678; Pym1.
DR   VEuPathDB; HostDB:ENSMUSG00000064030; -.
DR   eggNOG; KOG4325; Eukaryota.
DR   GeneTree; ENSGT00730000111107; -.
DR   HOGENOM; CLU_074603_3_0_1; -.
DR   InParanoid; Q8CHP5; -.
DR   OMA; IPGCADS; -.
DR   OrthoDB; 1545729at2759; -.
DR   PhylomeDB; Q8CHP5; -.
DR   TreeFam; TF324615; -.
DR   BioGRID-ORCS; 78428; 3 hits in 40 CRISPR screens.
DR   ChiTaRS; Pym1; mouse.
DR   PRO; PR:Q8CHP5; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8CHP5; protein.
DR   Bgee; ENSMUSG00000064030; Expressed in yolk sac and 64 other tissues.
DR   ExpressionAtlas; Q8CHP5; baseline and differential.
DR   Genevisible; Q8CHP5; MM.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0035145; C:exon-exon junction complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:1903259; P:exon-exon junction complex disassembly; ISO:MGI.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR   InterPro; IPR039333; PYM1.
DR   InterPro; IPR015362; WIBG_mago-bd.
DR   InterPro; IPR036348; WIBG_N_sf.
DR   PANTHER; PTHR22959; PTHR22959; 1.
DR   Pfam; PF09282; Mago-bind; 1.
DR   SMART; SM01273; Mago-bind; 1.
DR   SUPFAM; SSF101931; SSF101931; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..203
FT                   /note="Partner of Y14 and mago"
FT                   /id="PRO_0000287286"
FT   REGION          1..33
FT                   /note="Required for interaction with MAGOH and RBM8A"
FT                   /evidence="ECO:0000250"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..203
FT                   /note="eIF2A-like"
FT                   /evidence="ECO:0000250"
FT   COILED          82..117
FT                   /evidence="ECO:0000255"
FT   COILED          144..203
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRP8"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRP8"
FT   MOD_RES         72
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRP8"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRP8"
FT   VAR_SEQ         1..12
FT                   /note="METASTPEATGT -> MATPYVTDETG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025431"
FT   CONFLICT        159
FT                   /note="K -> N (in Ref. 1; CAD30678)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="R -> P (in Ref. 1; CAD30678)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..180
FT                   /note="SQPSR -> THPTK (in Ref. 1; CAD30678)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22690 MW;  4F41B5278FF42E0E CRC64;
     METASTPEAT GTGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP
     PGLSPEATTP VTPSRPEGGE TGLSKTAKRN LKRKEKRRQQ QEKEAEALSR TLDKVSLGDT
     AQIPSALQGP QATPLAASDP SDSAATTEKA KKIKNLRKKL RQVEELQQRI QAGEVSQPSR
     EQLEKLARRR VLEEELEDLE LGL
 
 
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