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PYM_CULQU
ID   PYM_CULQU               Reviewed;         238 AA.
AC   B0WII7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804};
DE   AltName: Full=Protein wibg homolog;
GN   Name=Pym {ECO:0000250|UniProtKB:P82804}; Synonyms=wibg;
GN   ORFNames=CPIJ006916;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB;
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulator of the exon junction complex (EJC), a multiprotein
CC       complex that associates immediately upstream of the exon-exon junction
CC       on mRNAs and serves as a positional landmarks for the intron exon
CC       structure of genes and directs post-transcriptional processes in the
CC       cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or
CC       translation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with mago and tsu/Y14; the
CC       interaction is direct. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is
CC       mediated by emb/Crm1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR   EMBL; DS231949; EDS28510.1; -; Genomic_DNA.
DR   RefSeq; XP_001848521.1; XM_001848469.1.
DR   AlphaFoldDB; B0WII7; -.
DR   SMR; B0WII7; -.
DR   STRING; 7176.CPIJ006916-PA; -.
DR   GeneID; 6038803; -.
DR   KEGG; cqu:CpipJ_CPIJ006916; -.
DR   VEuPathDB; VectorBase:CPIJ006916; -.
DR   VEuPathDB; VectorBase:CQUJHB006611; -.
DR   eggNOG; KOG4325; Eukaryota.
DR   HOGENOM; CLU_074603_3_0_1; -.
DR   InParanoid; B0WII7; -.
DR   OMA; MAKLESW; -.
DR   OrthoDB; 1363113at2759; -.
DR   PhylomeDB; B0WII7; -.
DR   Proteomes; UP000002320; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035145; C:exon-exon junction complex; ISS:UniProtKB.
DR   GO; GO:1903259; P:exon-exon junction complex disassembly; IEA:InterPro.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; 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   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..238
FT                   /note="Partner of Y14 and mago"
FT                   /id="PRO_0000378162"
FT   REGION          1..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          176..233
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  26934 MW;  E06B49C605F99E7B CRC64;
     MTTYATDSQG KFIPATQRPD GTWRKPRRVR DGYVPQEEVP LYESKGKLFA QKPSLPPGLP
     PEMAQKAREK REKEQRKAAA RPAQNPVPGL LILHEDNKAN QRQAKPANAK PKKKAVELPD
     VLLEQKQKEE QKAASRQQAQ DQRNSKQQQS QNQSKPLDDV TKAVQDLQLG TASGADGHSD
     LSKKLRKLRK KIREIEVIEE RLRASDGPRP DKDQIEKAKR KAEILKEIEE LERGGGHK
 
 
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