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EBI Dbfetch

ID   1433T_RAT               Reviewed;         245 AA.
AC   P68255; P35216;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-APR-2014, entry version 85.
DE   RecName: Full=14-3-3 protein theta;
DE   AltName: Full=14-3-3 protein tau;
GN   Name=Ywhaq;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=7984035; DOI=10.1016/0169-328X(94)90285-2;
RA   Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.,
RA   Inoue Y.;
RT   "Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14-
RT   3-3 protein and differential distributions of their mRNAs in the
RT   brain.";
RL   Brain Res. Mol. Brain Res. 25:113-121(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 4-9; 12-18; 28-49; 61-68; 84-115; 128-157; 159-167
RP   AND 194-222, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC       Negatively regulates the kinase activity of PDPK1 (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with CDK16.
CC       Interacts with CDKN1B ('Thr-198' phosphorylated form); the
CC       interaction translocates CDKN1B to the cytoplasm. Interacts with
CC       SSH1 (By similarity). Interacts with GAB2 (By similarity).
CC       Interacts with the 'Ser-241' phosphorylated form of PDPK1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; D17614; BAA04533.1; -; mRNA.
DR   EMBL; BC062409; AAH62409.1; -; mRNA.
DR   PIR; I52647; S59927.
DR   RefSeq; NP_037185.1; NM_013053.1.
DR   UniGene; Rn.2502; -.
DR   ProteinModelPortal; P68255; -.
DR   SMR; P68255; 1-230.
DR   BioGrid; 247608; 3.
DR   DIP; DIP-947N; -.
DR   IntAct; P68255; 4.
DR   MINT; MINT-203396; -.
DR   PhosphoSite; P68255; -.
DR   PaxDb; P68255; -.
DR   PRIDE; P68255; -.
DR   Ensembl; ENSRNOT00000011501; ENSRNOP00000011501; ENSRNOG00000008104.
DR   GeneID; 25577; -.
DR   KEGG; rno:25577; -.
DR   CTD; 10971; -.
DR   RGD; 3979; Ywhaq.
DR   eggNOG; COG5040; -.
DR   GeneTree; ENSGT00730000110424; -.
DR   HOGENOM; HOG000240379; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P68255; -.
DR   KO; K16197; -.
DR   OMA; CELRSIC; -.
DR   OrthoDB; EOG7HHWT3; -.
DR   PhylomeDB; P68255; -.
DR   TreeFam; TF102002; -.
DR   NextBio; 607215; -.
DR   PRO; PR:P68255; -.
DR   Genevestigator; P68255; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IDA:RGD.
DR   GO; GO:0071889; F:14-3-3 protein binding; IPI:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR   Gene3D; 1.20.190.20; -; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
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   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1    245       14-3-3 protein theta.
FT                                /FTId=PRO_0000058640.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        127    127       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES     115    115       N6-acetyllysine (By similarity).
FT   MOD_RES     232    232       Phosphoserine; by CK1 (Probable).
SQ   SEQUENCE   245 AA;  27778 MW;  E30471260E8B366E CRC64;
     MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
     VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
     MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
     EGAEN
//


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