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PYM1_DANRE
ID   PYM1_DANRE              Reviewed;         194 AA.
AC   Q6PH11; Q6NVC8;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804};
DE   AltName: Full=PYM homolog 1 exon junction complex-associated factor {ECO:0000250|UniProtKB:Q9BRP8};
DE   AltName: Full=Protein wibg homolog;
GN   Name=pym1 {ECO:0000250|UniProtKB:Q9BRP8}; Synonyms=pym, wibg;
GN   ORFNames=zgc:65891;
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 Testis;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR   EMBL; BC056755; AAH56755.1; -; mRNA.
DR   EMBL; BC068187; AAH68187.1; -; mRNA.
DR   EMBL; BC100118; AAI00119.1; -; mRNA.
DR   RefSeq; NP_956888.2; NM_200594.2.
DR   AlphaFoldDB; Q6PH11; -.
DR   SMR; Q6PH11; -.
DR   STRING; 7955.ENSDARP00000067667; -.
DR   PaxDb; Q6PH11; -.
DR   Ensembl; ENSDART00000167361; ENSDARP00000136874; ENSDARG00000046024.
DR   GeneID; 393566; -.
DR   KEGG; dre:393566; -.
DR   CTD; 84305; -.
DR   ZFIN; ZDB-GENE-040426-1464; pym1.
DR   eggNOG; KOG4325; Eukaryota.
DR   GeneTree; ENSGT00730000111107; -.
DR   InParanoid; Q6PH11; -.
DR   OrthoDB; 1545729at2759; -.
DR   PhylomeDB; Q6PH11; -.
DR   TreeFam; TF324615; -.
DR   PRO; PR:Q6PH11; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000046024; Expressed in mature ovarian follicle and 21 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0035145; C:exon-exon junction complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; Translation regulation.
FT   CHAIN           1..194
FT                   /note="Partner of Y14 and mago"
FT                   /id="PRO_0000287287"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          137..192
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        64..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        102
FT                   /note="S -> P (in Ref. 1; AAH68187)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22066 MW;  B3010A21866CC700 CRC64;
     MATPYVTDES GKYIAATQRP DGSWRKPRRV RDGYVPQEEV PVYENKFVKF FKSKPELPPG
     VCVETPPQTQ TQPSDAAGLS RTAKRNMKRK EKRRQQGQET KSEPELQPEP ELQPEPEPQG
     LSQQMQQLEL SASQGPGAAD SARRLKNLRK KLRQVEELQQ RVLSGELKPS QEQLDKLGRA
     QALREELQQL EAHS
 
 
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