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 22-SEP-2009, entry version 103. DE RecName: Full=14-3-3 protein theta; DE AltName: Full=14-3-3 protein tau; DE AltName: Full=14-3-3 protein T-cell; DE AltName: Full=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=Placenta, 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 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, RP ACETYLATION AT MET-1, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Hepatoma; RA Bienvenut W.V., Dhillon A.S., Kolch W.; RL Submitted (FEB-2008) 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 PHOSPHORYLATION AT SER-232, AND MASS SPECTROMETRY. RX PubMed=9360956; DOI=10.1074/jbc.272.46.28882; RA Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., RA Morrice N., Moelling K., Aitken A.; RT "14-3-3 is phosphorylated by casein kinase I on residue 233. RT Phosphorylation at this site in vivo regulates Raf/14-3-3 RT interaction."; RL J. Biol. Chem. 272:28882-28888(1997). RN [9] RP TISSUE SPECIFICITY. RX PubMed=11080204; DOI=10.1046/j.1471-4159.2000.0752511.x; 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 [10] RP INTERACTION WITH CDKN1B. RX PubMed=12042314; DOI=10.1074/jbc.M203668200; RA Fujita N., Sato S., Katayama K., Tsuruo T.; RT "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 RT and cytoplasmic localization."; RL J. Biol. Chem. 277:28706-28713(2002). RN [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS RP SPECTROMETRY. RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS RP SPECTROMETRY. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [15] 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). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, MASS SPECTROMETRY, RP INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). 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: Homodimer. Interacts with PCTK1 (By similarity). CC Interacts with SSH1. Interacts with CDKN1B ('Thr-198' CC phosphorylated form); the interaction translocates CDKN1B to the CC cytoplasm. CC -!- INTERACTION: CC Q9P0K1-1:ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567258; CC Q9P0K1-3:ADAM22; NbExp=1; IntAct=EBI-359854, EBI-1567267; CC P49407:ARRB1; NbExp=1; IntAct=EBI-359854, EBI-743313; CC P32121:ARRB2; NbExp=1; IntAct=EBI-359854, EBI-714559; 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 Q32P44:EML3; NbExp=1; IntAct=EBI-359854, EBI-1046713; CC O43491:EPB41L2; NbExp=1; IntAct=EBI-359854, EBI-1052044; CC Q9Y2J2:EPB41L3; NbExp=1; IntAct=EBI-359854, EBI-310986; CC P23945:FSHR; NbExp=3; 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:MPRIP; 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:PI4KB; 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 Q08AE8: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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X56468; CAA39840.1; -; mRNA. DR EMBL; X57347; CAA40622.1; -; mRNA. DR EMBL; BT020014; AAV38817.1; -; 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 IPI; IPI00018146; -. 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 PDBsum; 2BTP; -. DR DIP; DIP:27584N; -. DR IntAct; P27348; 68. DR STRING; P27348; -. DR PhosphoSite; P27348; -. DR Cornea-2DPAGE; P27348; -. DR OGP; P27348; -. DR REPRODUCTION-2DPAGE; IPI00018146; -. DR PeptideAtlas; P27348; -. DR PRIDE; P27348; -. DR Ensembl; ENST00000238081; ENSP00000238081; ENSG00000134308; Homo sapiens. DR Ensembl; ENST00000381844; ENSP00000371267; ENSG00000134308; Homo sapiens. DR GeneID; 10971; -. DR KEGG; hsa:10971; -. DR UCSC; uc002qzw.1; human. DR CTD; 10971; -. DR GeneCards; GC02M009674; -. DR H-InvDB; HIX0029798; -. DR H-InvDB; HIX0057400; -. DR HGNC; HGNC:12854; YWHAQ. DR HPA; CAB010286; -. DR HPA; HPA007925; -. DR MIM; 609009; gene. DR PharmGKB; PA37443; -. DR HOGENOM; P27348; -. DR HOVERGEN; P27348; -. DR OMA; P27348; DTSDKKM. DR Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling. DR Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt. DR Pathway_Interaction_DB; foxopathway; FoxO family signaling. DR Pathway_Interaction_DB; insulin_glucose_pathway; Insulin-mediated glucose transport. DR Pathway_Interaction_DB; p38_mk2pathway; p38 signaling mediated by MAPKAP kinases. DR Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes. DR Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma. DR NextBio; 41686; -. DR PMAP-CutDB; P27348; -. DR ArrayExpress; P27348; -. DR Bgee; P27348; -. DR CleanEx; HS_YWHAQ; -. DR GermOnline; ENSG00000134308; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-d...; IDA: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 PIRSF; PIRSF000868; 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; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Phosphoprotein. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058636. FT SITE 56 56 Interaction with phosphoserine on FT interacting protein. FT SITE 127 127 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 232 232 Phosphoserine; by CK1 (Probable). FT CONFLICT 136 136 D -> N (in Ref. 3; AAV38817). 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 //