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1433Z_CHICK
ID   1433Z_CHICK             Reviewed;         245 AA.
AC   Q5ZKC9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=14-3-3 protein zeta;
GN   Name=YWHAZ; ORFNames=RCJMB04_11l21;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds to a
CC       large number of partners, usually by recognition of a phosphoserine or
CC       phosphothreonine motif. Binding generally results in the modulation of
CC       the activity of the binding partner (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; AJ720155; CAG31814.1; -; mRNA.
DR   RefSeq; NP_001026514.1; NM_001031343.1.
DR   AlphaFoldDB; Q5ZKC9; -.
DR   SMR; Q5ZKC9; -.
DR   BioGRID; 685627; 3.
DR   IntAct; Q5ZKC9; 1.
DR   STRING; 9031.ENSGALP00000028746; -.
DR   PaxDb; Q5ZKC9; -.
DR   PRIDE; Q5ZKC9; -.
DR   Ensembl; ENSGALT00000059383; ENSGALP00000049152; ENSGALG00000031387.
DR   Ensembl; ENSGALT00000077278; ENSGALP00000048283; ENSGALG00000031387.
DR   Ensembl; ENSGALT00000084548; ENSGALP00000061526; ENSGALG00000031387.
DR   Ensembl; ENSGALT00000086950; ENSGALP00000064772; ENSGALG00000031387.
DR   GeneID; 425619; -.
DR   KEGG; gga:425619; -.
DR   CTD; 7534; -.
DR   VEuPathDB; HostDB:geneid_425619; -.
DR   eggNOG; KOG0841; Eukaryota.
DR   GeneTree; ENSGT01050000244817; -.
DR   HOGENOM; CLU_058290_1_0_1; -.
DR   InParanoid; Q5ZKC9; -.
DR   OMA; ERVCQDV; -.
DR   OrthoDB; 1176818at2759; -.
DR   PhylomeDB; Q5ZKC9; -.
DR   TreeFam; TF102003; -.
DR   Reactome; R-GGA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-GGA-392517; Rap1 signalling.
DR   Reactome; R-GGA-430116; GP1b-IX-V activation signalling.
DR   Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-GGA-9614399; Regulation of localization of FOXO transcription factors.
DR   PRO; PR:Q5ZKC9; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000031387; Expressed in brain and 13 other tissues.
DR   ExpressionAtlas; Q5ZKC9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0051683; P:establishment of Golgi localization; IEA:Ensembl.
DR   GO; GO:0090168; P:Golgi reassembly; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR   GO; GO:0010941; P:regulation of cell death; IEA:Ensembl.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0090128; P:regulation of synapse maturation; IEA:Ensembl.
DR   GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
DR   GO; GO:0035148; P:tube formation; IEA:Ensembl.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR036815; 14-3-3_dom_sf.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; SSF48445; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..245
FT                   /note="14-3-3 protein zeta"
FT                   /id="PRO_0000058632"
FT   SITE            56
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000250"
FT   SITE            127
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  27775 MW;  F2A813EE4B23B42D CRC64;
     MDKNELVQKA KLAEQAERYD DMASCMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
     VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK
     MKGDYYRYLA EVAAGDDKKG IVEQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
     EGGEN
 
 
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