Full text data of YWHAQ
YWHAQ
[Confidence: high (present in two of the MS resources)]
14-3-3 protein theta (14-3-3 protein T-cell; 14-3-3 protein tau; Protein HS1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
14-3-3 protein theta (14-3-3 protein T-cell; 14-3-3 protein tau; Protein HS1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00018146
IPI00018146 14-3-3 protein tau ctivates tyrosine and tryptophan hydroxylases in the presence of Ca(2+)/calmodulin-dependent protein kinase II, and strongly activates protein kinase C. Is probably a multifunctional regulator of the cell signaling processes mediated by both kinases soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic TAFDEAIAELDTLNEDSYKDSTLIMQLLR found at its expected molecular weight found at molecular weight
IPI00018146 14-3-3 protein tau ctivates tyrosine and tryptophan hydroxylases in the presence of Ca(2+)/calmodulin-dependent protein kinase II, and strongly activates protein kinase C. Is probably a multifunctional regulator of the cell signaling processes mediated by both kinases soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic TAFDEAIAELDTLNEDSYKDSTLIMQLLR found at its expected molecular weight found at molecular weight
UniProt
P27348
ID 1433T_HUMAN Reviewed; 245 AA.
AC P27348; D6W4Z5; Q567U5; Q5TZU8; Q9UP48;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=14-3-3 protein theta;
DE AltName: Full=14-3-3 protein T-cell;
DE AltName: Full=14-3-3 protein tau;
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 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 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-18.
RC TISSUE=Platelet;
RX 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH PDPK1.
RX PubMed=12177059; DOI=10.1074/jbc.M205141200;
RA Sato S., Fujita N., Tsuruo T.;
RT "Regulation of kinase activity of 3-phosphoinositide-dependent protein
RT kinase-1 by binding to 14-3-3.";
RL J. Biol. Chem. 277:39360-39367(2002).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP INTERACTION WITH GAB2.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA Guilhaus M., James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT the Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND
RP LYS-115, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX 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 [24]
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 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.
CC -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity).
CC Interacts with SSH1. Interacts with CDKN1B ('Thr-198'
CC phosphorylated form); the interaction translocates CDKN1B to the
CC cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241'
CC phosphorylated form of PDPK1.
CC -!- INTERACTION:
CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267;
CC P49407:ARRB1; NbExp=3; IntAct=EBI-359854, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559;
CC P22681:CBL; NbExp=6; IntAct=EBI-359854, EBI-518228;
CC O94921:CDK14; NbExp=3; IntAct=EBI-359854, EBI-1043945;
CC P46527:CDKN1B; NbExp=4; IntAct=EBI-359854, EBI-519280;
CC P67828:CSNK1A1 (xeno); NbExp=2; IntAct=EBI-359854, EBI-7540603;
CC P00533:EGFR; NbExp=5; IntAct=EBI-359854, EBI-297353;
CC P23945:FSHR; NbExp=4; IntAct=EBI-359854, EBI-848239;
CC Q14678:KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221;
CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812;
CC Q5S007:LRRK2; NbExp=4; IntAct=EBI-359854, EBI-5323863;
CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359854, EBI-6930266;
CC Q8WYL5:SSH1; NbExp=2; IntAct=EBI-359854, EBI-1222387;
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 -!- PTM: Ser-232 is probably phosphorylated by CK1.
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; CH471053; EAX00977.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00979.1; -; Genomic_DNA.
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; NM_006826.3.
DR RefSeq; XP_005246205.1; XM_005246148.1.
DR UniGene; Hs.74405; -.
DR PDB; 2BTP; X-ray; 2.80 A; A/B=1-234.
DR PDBsum; 2BTP; -.
DR ProteinModelPortal; P27348; -.
DR SMR; P27348; 1-230.
DR DIP; DIP-27584N; -.
DR IntAct; P27348; 75.
DR MINT; MINT-121282; -.
DR STRING; 9606.ENSP00000238081; -.
DR PhosphoSite; P27348; -.
DR DMDM; 112690; -.
DR OGP; P27348; -.
DR REPRODUCTION-2DPAGE; IPI00018146; -.
DR PaxDb; P27348; -.
DR PeptideAtlas; P27348; -.
DR PRIDE; P27348; -.
DR DNASU; 10971; -.
DR Ensembl; ENST00000238081; ENSP00000238081; ENSG00000134308.
DR Ensembl; ENST00000381844; ENSP00000371267; ENSG00000134308.
DR GeneID; 10971; -.
DR KEGG; hsa:10971; -.
DR UCSC; uc002qzx.3; human.
DR CTD; 10971; -.
DR GeneCards; GC02M009724; -.
DR H-InvDB; HIX0077146; -.
DR HGNC; HGNC:12854; YWHAQ.
DR HPA; CAB010286; -.
DR HPA; HPA007925; -.
DR MIM; 609009; gene.
DR neXtProt; NX_P27348; -.
DR PharmGKB; PA37443; -.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P27348; -.
DR KO; K16197; -.
DR OMA; CELRSIC; -.
DR OrthoDB; EOG7HHWT3; -.
DR PhylomeDB; P27348; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; P27348; -.
DR ChiTaRS; YWHAQ; human.
DR EvolutionaryTrace; P27348; -.
DR GeneWiki; YWHAQ; -.
DR GenomeRNAi; 10971; -.
DR NextBio; 41686; -.
DR PMAP-CutDB; P27348; -.
DR PRO; PR:P27348; -.
DR ArrayExpress; P27348; -.
DR Bgee; P27348; -.
DR CleanEx; HS_YWHAQ; -.
DR Genevestigator; P27348; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:BHF-UCL.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
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 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
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 3 3 N6-acetyllysine.
FT MOD_RES 49 49 N6-acetyllysine.
FT MOD_RES 68 68 N6-acetyllysine.
FT MOD_RES 115 115 N6-acetyllysine.
FT MOD_RES 232 232 Phosphoserine.
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
//
ID 1433T_HUMAN Reviewed; 245 AA.
AC P27348; D6W4Z5; Q567U5; Q5TZU8; Q9UP48;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=14-3-3 protein theta;
DE AltName: Full=14-3-3 protein T-cell;
DE AltName: Full=14-3-3 protein tau;
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 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 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-18.
RC TISSUE=Platelet;
RX 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH PDPK1.
RX PubMed=12177059; DOI=10.1074/jbc.M205141200;
RA Sato S., Fujita N., Tsuruo T.;
RT "Regulation of kinase activity of 3-phosphoinositide-dependent protein
RT kinase-1 by binding to 14-3-3.";
RL J. Biol. Chem. 277:39360-39367(2002).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP INTERACTION WITH GAB2.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA Guilhaus M., James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT the Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND
RP LYS-115, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX 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 [24]
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 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.
CC -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity).
CC Interacts with SSH1. Interacts with CDKN1B ('Thr-198'
CC phosphorylated form); the interaction translocates CDKN1B to the
CC cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241'
CC phosphorylated form of PDPK1.
CC -!- INTERACTION:
CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267;
CC P49407:ARRB1; NbExp=3; IntAct=EBI-359854, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559;
CC P22681:CBL; NbExp=6; IntAct=EBI-359854, EBI-518228;
CC O94921:CDK14; NbExp=3; IntAct=EBI-359854, EBI-1043945;
CC P46527:CDKN1B; NbExp=4; IntAct=EBI-359854, EBI-519280;
CC P67828:CSNK1A1 (xeno); NbExp=2; IntAct=EBI-359854, EBI-7540603;
CC P00533:EGFR; NbExp=5; IntAct=EBI-359854, EBI-297353;
CC P23945:FSHR; NbExp=4; IntAct=EBI-359854, EBI-848239;
CC Q14678:KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221;
CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812;
CC Q5S007:LRRK2; NbExp=4; IntAct=EBI-359854, EBI-5323863;
CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359854, EBI-6930266;
CC Q8WYL5:SSH1; NbExp=2; IntAct=EBI-359854, EBI-1222387;
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 -!- PTM: Ser-232 is probably phosphorylated by CK1.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC -----------------------------------------------------------------------
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DR EMBL; X56468; CAA39840.1; -; mRNA.
DR EMBL; X57347; CAA40622.1; -; mRNA.
DR EMBL; BT020014; AAV38817.1; -; mRNA.
DR EMBL; CH471053; EAX00977.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00979.1; -; Genomic_DNA.
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; NM_006826.3.
DR RefSeq; XP_005246205.1; XM_005246148.1.
DR UniGene; Hs.74405; -.
DR PDB; 2BTP; X-ray; 2.80 A; A/B=1-234.
DR PDBsum; 2BTP; -.
DR ProteinModelPortal; P27348; -.
DR SMR; P27348; 1-230.
DR DIP; DIP-27584N; -.
DR IntAct; P27348; 75.
DR MINT; MINT-121282; -.
DR STRING; 9606.ENSP00000238081; -.
DR PhosphoSite; P27348; -.
DR DMDM; 112690; -.
DR OGP; P27348; -.
DR REPRODUCTION-2DPAGE; IPI00018146; -.
DR PaxDb; P27348; -.
DR PeptideAtlas; P27348; -.
DR PRIDE; P27348; -.
DR DNASU; 10971; -.
DR Ensembl; ENST00000238081; ENSP00000238081; ENSG00000134308.
DR Ensembl; ENST00000381844; ENSP00000371267; ENSG00000134308.
DR GeneID; 10971; -.
DR KEGG; hsa:10971; -.
DR UCSC; uc002qzx.3; human.
DR CTD; 10971; -.
DR GeneCards; GC02M009724; -.
DR H-InvDB; HIX0077146; -.
DR HGNC; HGNC:12854; YWHAQ.
DR HPA; CAB010286; -.
DR HPA; HPA007925; -.
DR MIM; 609009; gene.
DR neXtProt; NX_P27348; -.
DR PharmGKB; PA37443; -.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P27348; -.
DR KO; K16197; -.
DR OMA; CELRSIC; -.
DR OrthoDB; EOG7HHWT3; -.
DR PhylomeDB; P27348; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; P27348; -.
DR ChiTaRS; YWHAQ; human.
DR EvolutionaryTrace; P27348; -.
DR GeneWiki; YWHAQ; -.
DR GenomeRNAi; 10971; -.
DR NextBio; 41686; -.
DR PMAP-CutDB; P27348; -.
DR PRO; PR:P27348; -.
DR ArrayExpress; P27348; -.
DR Bgee; P27348; -.
DR CleanEx; HS_YWHAQ; -.
DR Genevestigator; P27348; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:BHF-UCL.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
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 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
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 3 3 N6-acetyllysine.
FT MOD_RES 49 49 N6-acetyllysine.
FT MOD_RES 68 68 N6-acetyllysine.
FT MOD_RES 115 115 N6-acetyllysine.
FT MOD_RES 232 232 Phosphoserine.
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
//
MIM
609009
*RECORD*
*FIELD* NO
609009
*FIELD* TI
*609009 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN,
THETA ISOFORM; YWHAQ
read more;;14-3-3 PROTEIN, T-CELL;;
14-3-3-THETA;;
14-3-3-TAU;;
HS1
*FIELD* TX
DESCRIPTION
YWHAQ is a member of the 14-3-3 family of signaling proteins involved in
apoptosis and cell proliferation (Malaspina et al., 2000).
CLONING
By screening a Jurkat human T-cell cDNA library with a probe coding for
an uncharacterized nuclear protein, Nielsen (1991) cloned YWHAQ. The
deduced 245-amino acid protein has a calculated molecular mass of 28 kD
and shares 72% amino acid identity with bovine brain 14-3-3-eta
(113508). Northern blot analysis of Jurkat and HeLa cells showed strong
bands at 1.9 and 2.1 kb, and a weaker band at 1.7 kb. Strongest
expression was in brain, followed by lung, kidney, liver, and spleen.
By sequencing cDNAs encoding related acidic human keratinocyte proteins,
Leffers et al. (1993) cloned YWHAQ, which they designated HS1. The YWHAQ
protein shares significant similarity with stratifin (601290). It showed
an apparent molecular mass of 31.1 kD by 2-dimensional gel
electrophoresis. Expression of YWHAQ was abundant in transformed amnion
epithelia cells and fetal ear fibroblasts. Northern blot analysis
detected high expression in all cell types and tissues analyzed. The
authors identified 3 YWHAQ transcripts resulting from the utilization of
different polyadenylation sites.
By screening a spinal cord cDNA library for cDNAs encoding
trinucleotide- and tandem repeat-containing proteins, Malaspina et al.
(2000) cloned YWHAQ. The 5-prime UTR immediately before the start codon
of the YWHAQ transcript contains a homogeneous 6-bp (CCCCGG)3 tandem
repeat. Northern blot analysis detected a 2-kb transcript abundantly
expressed in brain, heart, and pancreas, with lower expression in kidney
and placenta. Spinal cord mRNA showed transcripts of about 1.8 and 2.2
kb. Malaspina et al. (2000) found that YWHAQ was consistently
upregulated in spinal cord of amyotrophic lateral sclerosis (105400)
patients. Expression was highest in 2 individuals with the most
consistent clinical picture of lower motor neuron involvement.
Watanabe et al. (1994) isolated the rat theta isoform of 14-3-3 from rat
brain. The deduced 245-amino acid protein shares high sequence homology
with other 14-3-3 subtypes. The theta mRNA was detected in gray matter
of the cerebellar cortex and hippocampus and in white matter.
BIOCHEMICAL FEATURES
Xiao et al. (1995) determined the crystal structure of the human T-cell
YWHAQ dimer at 2.6-angstrom resolution. Each monomer is composed of an
unusual arrangement of 9 antiparallel alpha helices organized as 2
structural domains. The dimer creates a large, negatively charged
channel approximately 35 angstroms broad, 35 angstroms wide, and 20
angstroms deep. Overall, invariant residues line the interior of the
channel, whereas more variable residues are distributed on the outer
surface. At the base of the channel is a 16-residue segment implicated
in the binding of 14-3-3 to protein kinase C (see 176960).
MAPPING
By analyzing human-rodent hybrids, Malaspina et al. (2000) mapped the
YWHAQ gene to chromosome 2. They identified a pseudogene on chromosome
22.
*FIELD* RF
1. Leffers, H.; Madsen, P.; Rasmussen, H. H.; Honore, B.; Andersen,
A. H.; Walbum, E.; Vandekerckhove, J.; Celis, J. E.: Molecular cloning
and expression of the transformation sensitive epithelial marker stratifin. J.
Molec. Biol. 231: 982-998, 1993.
2. Malaspina, A.; Kaushik, N.; de Belleroche, J.: A 14-3-3 mRNA is
up-regulated in amyotrophic lateral sclerosis spinal cord. J. Neurochem. 75:
2511-2520, 2000.
3. Nielsen, P. J.: Primary structure of a human protein kinase regulator
protein. Biochim. Biophys. Acta 1088: 425-428, 1991.
4. Watanabe, M.; Isobe, T.; Ichimura, T.; Kuwano, R.; Takahashi, Y.;
Kondo, H.; Inoue, Y.: Molecular cloning of rat cDNAs for the zeta
and theta subtypes of 14-3-3 protein and differential distributions
of their mRNAs in the brain. Molec. Brain Res. 25: 113-121, 1994.
5. Xiao, B.; Smerdon, S. J.; Jones, D. H.; Dodson, G. G.; Soneji,
Y.; Aitken, A.; Gamblin, S. J.: Structure of 14-3-3 protein and implications
for coordination of multiple signalling pathways. Nature 376: 188-191,
1995.
*FIELD* CD
Patricia A. Hartz: 11/2/2004
*FIELD* ED
tkritzer: 02/22/2005
ckniffin: 2/7/2005
mgross: 11/2/2004
*RECORD*
*FIELD* NO
609009
*FIELD* TI
*609009 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN,
THETA ISOFORM; YWHAQ
read more;;14-3-3 PROTEIN, T-CELL;;
14-3-3-THETA;;
14-3-3-TAU;;
HS1
*FIELD* TX
DESCRIPTION
YWHAQ is a member of the 14-3-3 family of signaling proteins involved in
apoptosis and cell proliferation (Malaspina et al., 2000).
CLONING
By screening a Jurkat human T-cell cDNA library with a probe coding for
an uncharacterized nuclear protein, Nielsen (1991) cloned YWHAQ. The
deduced 245-amino acid protein has a calculated molecular mass of 28 kD
and shares 72% amino acid identity with bovine brain 14-3-3-eta
(113508). Northern blot analysis of Jurkat and HeLa cells showed strong
bands at 1.9 and 2.1 kb, and a weaker band at 1.7 kb. Strongest
expression was in brain, followed by lung, kidney, liver, and spleen.
By sequencing cDNAs encoding related acidic human keratinocyte proteins,
Leffers et al. (1993) cloned YWHAQ, which they designated HS1. The YWHAQ
protein shares significant similarity with stratifin (601290). It showed
an apparent molecular mass of 31.1 kD by 2-dimensional gel
electrophoresis. Expression of YWHAQ was abundant in transformed amnion
epithelia cells and fetal ear fibroblasts. Northern blot analysis
detected high expression in all cell types and tissues analyzed. The
authors identified 3 YWHAQ transcripts resulting from the utilization of
different polyadenylation sites.
By screening a spinal cord cDNA library for cDNAs encoding
trinucleotide- and tandem repeat-containing proteins, Malaspina et al.
(2000) cloned YWHAQ. The 5-prime UTR immediately before the start codon
of the YWHAQ transcript contains a homogeneous 6-bp (CCCCGG)3 tandem
repeat. Northern blot analysis detected a 2-kb transcript abundantly
expressed in brain, heart, and pancreas, with lower expression in kidney
and placenta. Spinal cord mRNA showed transcripts of about 1.8 and 2.2
kb. Malaspina et al. (2000) found that YWHAQ was consistently
upregulated in spinal cord of amyotrophic lateral sclerosis (105400)
patients. Expression was highest in 2 individuals with the most
consistent clinical picture of lower motor neuron involvement.
Watanabe et al. (1994) isolated the rat theta isoform of 14-3-3 from rat
brain. The deduced 245-amino acid protein shares high sequence homology
with other 14-3-3 subtypes. The theta mRNA was detected in gray matter
of the cerebellar cortex and hippocampus and in white matter.
BIOCHEMICAL FEATURES
Xiao et al. (1995) determined the crystal structure of the human T-cell
YWHAQ dimer at 2.6-angstrom resolution. Each monomer is composed of an
unusual arrangement of 9 antiparallel alpha helices organized as 2
structural domains. The dimer creates a large, negatively charged
channel approximately 35 angstroms broad, 35 angstroms wide, and 20
angstroms deep. Overall, invariant residues line the interior of the
channel, whereas more variable residues are distributed on the outer
surface. At the base of the channel is a 16-residue segment implicated
in the binding of 14-3-3 to protein kinase C (see 176960).
MAPPING
By analyzing human-rodent hybrids, Malaspina et al. (2000) mapped the
YWHAQ gene to chromosome 2. They identified a pseudogene on chromosome
22.
*FIELD* RF
1. Leffers, H.; Madsen, P.; Rasmussen, H. H.; Honore, B.; Andersen,
A. H.; Walbum, E.; Vandekerckhove, J.; Celis, J. E.: Molecular cloning
and expression of the transformation sensitive epithelial marker stratifin. J.
Molec. Biol. 231: 982-998, 1993.
2. Malaspina, A.; Kaushik, N.; de Belleroche, J.: A 14-3-3 mRNA is
up-regulated in amyotrophic lateral sclerosis spinal cord. J. Neurochem. 75:
2511-2520, 2000.
3. Nielsen, P. J.: Primary structure of a human protein kinase regulator
protein. Biochim. Biophys. Acta 1088: 425-428, 1991.
4. Watanabe, M.; Isobe, T.; Ichimura, T.; Kuwano, R.; Takahashi, Y.;
Kondo, H.; Inoue, Y.: Molecular cloning of rat cDNAs for the zeta
and theta subtypes of 14-3-3 protein and differential distributions
of their mRNAs in the brain. Molec. Brain Res. 25: 113-121, 1994.
5. Xiao, B.; Smerdon, S. J.; Jones, D. H.; Dodson, G. G.; Soneji,
Y.; Aitken, A.; Gamblin, S. J.: Structure of 14-3-3 protein and implications
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*FIELD* CD
Patricia A. Hartz: 11/2/2004
*FIELD* ED
tkritzer: 02/22/2005
ckniffin: 2/7/2005
mgross: 11/2/2004