ID   1433T_HUMAN             Reviewed;         245 AA.
AC   P27348; Q567U5; Q5TZU8; Q9UP48;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-DEC-2007, entry version 82.
DE   14-3-3 protein theta (14-3-3 protein tau) (14-3-3 protein T-cell)
DE   (Protein HS1).
GN   Name=YWHAQ;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RX   MEDLINE=91198149; PubMed=2015305; DOI=10.1016/0167-4781(91)90136-A;
RA   Nielsen P.J.;
RT   "Primary structure of a human protein kinase regulator protein.";
RL   Biochim. Biophys. Acta 1088:425-428(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Keratinocyte;
RX   MEDLINE=93294871; PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
RA   Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
RA   Walbum E., Vandekerckhove J., Celis J.E.;
RT   "Molecular cloning and expression of the transformation sensitive
RT   epithelial marker stratifin. A member of a protein family that has
RT   been involved in the protein kinase C signalling pathway.";
RL   J. Mol. Biol. 231:982-998(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Skin, and Uterus;
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   [5]
RP   PROTEIN SEQUENCE OF 1-18.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [6]
RP   PROTEIN SEQUENCE OF 42-49; 61-68 AND 159-167, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (MAR-2005) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245.
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=11080204;
RA   Malaspina A., Kaushik N., de Belleroche J.;
RT   "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal
RT   cord.";
RL   J. Neurochem. 75:2511-2520(2000).
RN   [9]
RP   INTERACTION WITH SSH1.
RX   PubMed=15159416; DOI=10.1083/jcb.200401136;
RA   Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA   Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT   "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT   Slingshot and cofilin in lamellipodia.";
RL   J. Cell Biol. 165:465-471(2004).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   MEDLINE=95327195; PubMed=7603573; DOI=10.1038/376188a0;
RA   Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A.,
RA   Gamblin S.J.;
RT   "Structure of a 14-3-3 protein and implications for coordination of
RT   multiple signalling pathways.";
RL   Nature 376:188-191(1995).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. 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   -!- SUBUNIT: Interacts with PCTK1 (By similarity). Homodimer.
CC       Interacts with SSH1.
CC   -!- INTERACTION:
CC       Q6ZW60:-; NbExp=1; IntAct=EBI-359854, EBI-1047240;
CC       P15056:BRAF; NbExp=1; IntAct=EBI-359854, EBI-365980;
CC       Q6ICG6:C22orf9; NbExp=1; IntAct=EBI-359854, EBI-1053969;
CC       Q9NZT1:CALML5; NbExp=1; IntAct=EBI-359854, EBI-1051681;
CC       Q8IUF1:CBWD2; NbExp=1; IntAct=EBI-359854, EBI-359159;
CC       P26196:DDX6; NbExp=1; IntAct=EBI-359854, EBI-351257;
CC       Q7Z401:DENND4A; NbExp=1; IntAct=EBI-359854, EBI-1046479;
CC       Q96F86:EDC3; NbExp=1; IntAct=EBI-359854, EBI-997311;
CC       O43491:EPB41L2; NbExp=1; IntAct=EBI-359854, EBI-1052044;
CC       Q9Y2J2:EPB41L3; NbExp=1; IntAct=EBI-359854, EBI-310986;
CC       P23945:FSHR; NbExp=1; IntAct=EBI-359854, EBI-848239;
CC       O75494:FUSIP1; NbExp=1; IntAct=EBI-359854, EBI-353655;
CC       Q9Y4H2:IRS2; NbExp=1; IntAct=EBI-359854, EBI-1049582;
CC       Q02241:KIF23; NbExp=1; IntAct=EBI-359854, EBI-306852;
CC       P33176:KIF5B; NbExp=1; IntAct=EBI-359854, EBI-355878;
CC       O60282:KIF5C; NbExp=1; IntAct=EBI-359854, EBI-717170;
CC       Q9H0B6:KLC2; NbExp=1; IntAct=EBI-359854, EBI-726994;
CC       Q9NSK0:KLC4; NbExp=1; IntAct=EBI-359854, EBI-949319;
CC       Q6PKG0:LARP1; NbExp=1; IntAct=EBI-359854, EBI-1052114;
CC       Q9Y383:LUC7L2; NbExp=1; IntAct=EBI-359854, EBI-352851;
CC       P61326:MAGOH; NbExp=1; IntAct=EBI-359854, EBI-299134;
CC       P27448:MARK3; NbExp=1; IntAct=EBI-359854, EBI-707595;
CC       Q6WCQ1:MRIP; NbExp=1; IntAct=EBI-359854, EBI-1022605;
CC       O96013:PAK4; NbExp=1; IntAct=EBI-359854, EBI-713738;
CC       Q9NQU5:PAK6; NbExp=1; IntAct=EBI-359854, EBI-1053685;
CC       O94921:PFTK1; NbExp=3; IntAct=EBI-359854, EBI-1043945;
CC       Q9UBF8:PIK4CB; NbExp=1; IntAct=EBI-359854, EBI-1053214;
CC       Q96T60:PNKP; NbExp=1; IntAct=EBI-359854, EBI-1045072;
CC       Q86W92:PPFIBP1; NbExp=1; IntAct=EBI-359854, EBI-1045582;
CC       Q15276:RABEP1; NbExp=1; IntAct=EBI-359854, EBI-447043;
CC       P04049:RAF1; NbExp=1; IntAct=EBI-359854, EBI-365996;
CC       Q9P0K7:RAI14; NbExp=1; IntAct=EBI-359854, EBI-1023749;
CC       Q8IV61:RASGRP3; NbExp=1; IntAct=EBI-359854, EBI-1047876;
CC       Q5PRF9:SAMD4B; NbExp=1; IntAct=EBI-359854, EBI-1047489;
CC       Q07955:SFRS1; NbExp=1; IntAct=EBI-359854, EBI-398920;
CC       P84103:SFRS3; NbExp=1; IntAct=EBI-359854, EBI-372557;
CC       Q13247:SFRS6; NbExp=1; IntAct=EBI-359854, EBI-745230;
CC       Q9P0V3:SH3BP4; NbExp=1; IntAct=EBI-359854, EBI-1049513;
CC       Q9ULT4:SPIRE1; NbExp=1; IntAct=EBI-359854, EBI-1055655;
CC       Q4FZB7:SUV420H1; NbExp=1; IntAct=EBI-359854, EBI-1047962;
CC       Q9UDY2:TJP2; NbExp=1; IntAct=EBI-359854, EBI-1042602;
CC       P49815:TSC2; NbExp=1; IntAct=EBI-359854, EBI-396587;
CC       P40818:USP8; NbExp=1; IntAct=EBI-359854, EBI-1050865;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally
CC       transported to the nerve terminals.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and
CC       pancreas, and at lower levels in kidney and placenta. Up-regulated
CC       in the lumbar spinal cord from patients with sporadic amyotrophic
CC       lateral sclerosis (ALS) compared with controls, with highest
CC       levels of expression in individuals with predominant lower motor
CC       neuron involvement.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; X56468; CAA39840.1; -; mRNA.
DR   EMBL; X57347; CAA40622.1; -; mRNA.
DR   EMBL; BT020014; AAV38817.1; -; mRNA.
DR   EMBL; BC001197; AAH01197.1; -; mRNA.
DR   EMBL; BC050601; AAH50601.1; -; mRNA.
DR   EMBL; BC056867; AAH56867.1; -; mRNA.
DR   EMBL; BC093019; AAH93019.1; -; mRNA.
DR   EMBL; AF070556; AAC28640.1; -; mRNA.
DR   PIR; S15076; S15076.
DR   RefSeq; NP_006817.1; -.
DR   UniGene; Hs.74405; -.
DR   PDB; 2BTP; X-ray; 2.80 A; A/B=1-234.
DR   DIP; DIP:27584N; -.
DR   IntAct; P27348; -.
DR   Cornea-2DPAGE; P27348; HUMAN.
DR   OGP; P27348; -.
DR   REPRODUCTION-2DPAGE; P27348; HUMAN.
DR   PeptideAtlas; P27348; -.
DR   Ensembl; ENSG00000134308; Homo sapiens.
DR   GeneID; 10971; -.
DR   KEGG; hsa:10971; -.
DR   H-InvDB; HIX0029798; -.
DR   H-InvDB; HIX0057400; -.
DR   HGNC; HGNC:12854; YWHAQ.
DR   MIM; 609009; gene.
DR   PharmGKB; PA37443; -.
DR   LinkHub; P27348; -.
DR   ArrayExpress; P27348; -.
DR   CleanEx; HS_YWHAQ; -.
DR   GermOnline; ENSG00000134308; Homo sapiens.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR000308; 14-3-3.
DR   Gene3D; G3DSA:1.20.190.20; 14-3-3; 1.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   ProDom; PD000600; 14-3-3; 1.
DR   SMART; SM00101; 14_3_3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing.
FT   CHAIN         1    245       14-3-3 protein theta.
FT                                /FTId=PRO_0000058636.
FT   CONFLICT    136    136       D -> N (in Ref. 3).
FT   HELIX         3     15
FT   HELIX        19     31
FT   HELIX        38     68
FT   HELIX        75    103
FT   TURN        104    108
FT   HELIX       112    132
FT   HELIX       135    159
FT   HELIX       165    180
FT   HELIX       185    201
FT   TURN        202    205
FT   HELIX       208    227
SQ   SEQUENCE   245 AA;  27764 MW;  175534325E9E37C4 CRC64;
     MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
     VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
     MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
     EGAEN
//