1433T_HUMAN
ID 1433T_HUMAN Reviewed; 245 AA.
AC P27348; D6W4Z5; Q567U5; Q5TZU8; Q9UP48;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 228.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Walbum E.,
RA 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 been
RT 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 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 1-9; 12-55; 61-74; 128-157; 168-193 AND 213-222,
RP INTERACTION WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [8]
RP PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY 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 [9]
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 [10]
RP PHOSPHORYLATION AT SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9360956; DOI=10.1074/jbc.272.46.28882;
RA Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N.,
RA 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 interaction.";
RL J. Biol. Chem. 272:28882-28888(1997).
RN [11]
RP INTERACTION WITH RGS7.
RX PubMed=10862767; DOI=10.1074/jbc.m002905200;
RA Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B.,
RA Schreiber R., Kunzelmann K., Leparc G.G., Kim E., Walz G.;
RT "14-3-3 interacts with regulator of G protein signaling proteins and
RT modulates their activity.";
RL J. Biol. Chem. 275:28167-28172(2000).
RN [12]
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 [13]
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 and
RT cytoplasmic localization.";
RL J. Biol. Chem. 277:28706-28713(2002).
RN [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
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 [17]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP INTERACTION WITH MARK2; MARK3 AND MARK4.
RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200;
RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M.,
RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B.,
RA Bouwmeester T., Acker-Palmer A.;
RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins
RT involved in cytoskeletal rearrangements and cell signaling.";
RL Mol. Cell. Proteomics 5:2211-2227(2006).
RN [19]
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., Guilhaus M.,
RA James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [20]
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [22]
RP INTERACTION WITH SLITRK1.
RX PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
RA Kajiwara Y., Buxbaum J.D., Grice D.E.;
RT "SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-
RT dependent manner.";
RL Biol. Psychiatry 66:918-925(2009).
RN [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-49; LYS-68 AND LYS-115,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [25]
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
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., Buerckstuemmer T.,
RA 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 [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
RN [30]
RP INTERACTION WITH RIPOR2.
RX PubMed=25588844; DOI=10.1242/jcs.161497;
RA Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
RT "Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
RT leading edges polarizes neutrophils.";
RL J. Cell Sci. 128:992-1000(2015).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP INTERACTION WITH MEFV.
RX PubMed=27030597; DOI=10.1126/scitranslmed.aaf1471;
RA Masters S.L., Lagou V., Jeru I., Baker P.J., Van Eyck L., Parry D.A.,
RA Lawless D., De Nardo D., Garcia-Perez J.E., Dagley L.F., Holley C.L.,
RA Dooley J., Moghaddas F., Pasciuto E., Jeandel P.Y., Sciot R., Lyras D.,
RA Webb A.I., Nicholson S.E., De Somer L., van Nieuwenhove E., Ruuth-Praz J.,
RA Copin B., Cochet E., Medlej-Hashim M., Megarbane A., Schroder K., Savic S.,
RA Goris A., Amselem S., Wouters C., Liston A.;
RT "Familial autoinflammation with neutrophilic dermatosis reveals a
RT regulatory mechanism of pyrin activation.";
RL Sci. Transl. Med. 8:332ra45-332ra45(2016).
RN [33]
RP FUNCTION, AND INTERACTION WITH INAVA.
RX PubMed=28436939; DOI=10.1172/jci86282;
RA Yan J., Hedl M., Abraham C.;
RT "An inflammatory bowel disease-risk variant in INAVA decreases pattern
RT recognition receptor-induced outcomes.";
RL J. Clin. Invest. 127:2192-2205(2017).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [35]
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 [36]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS
RP SPECTROMETRY, 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 protein
RT 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 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. Negatively regulates the kinase
CC activity of PDPK1. {ECO:0000269|PubMed:12177059}.
CC -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity). Interacts
CC with RGS7 (phosphorylated form) (PubMed:10862767). Interacts with SSH1.
CC Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction
CC translocates CDKN1B to the cytoplasm. Interacts with GAB2. Interacts
CC with the 'Ser-241' phosphorylated form of PDPK1. Interacts with the
CC 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts
CC with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with
CC SLITRK1 (PubMed:19640509). Interacts with RIPOR2 isoform 2
CC (PubMed:25588844). Interacts with INAVA; the interaction increases upon
CC PRR (pattern recognition receptor) stimulation and is required for
CC cellular signaling pathway activation and cytokine secretion
CC (PubMed:28436939). Interacts with MARK2, MARK3 and MARK4
CC (PubMed:16959763). Interacts with MEFV (PubMed:27030597).
CC {ECO:0000250|UniProtKB:P68254, ECO:0000269|PubMed:10862767,
CC ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:12177059,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:16959763,
CC ECO:0000269|PubMed:17085597, ECO:0000269|PubMed:19172738,
CC ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:23572552,
CC ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:26047703,
CC ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:28436939}.
CC -!- INTERACTION:
CC P27348; Q9P0K1-3: ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267;
CC P27348; P49407: ARRB1; NbExp=3; IntAct=EBI-359854, EBI-743313;
CC P27348; P32121: ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559;
CC P27348; P54253: ATXN1; NbExp=4; IntAct=EBI-359854, EBI-930964;
CC P27348; Q92934: BAD; NbExp=5; IntAct=EBI-359854, EBI-700771;
CC P27348; P22681: CBL; NbExp=6; IntAct=EBI-359854, EBI-518228;
CC P27348; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-359854, EBI-11977221;
CC P27348; P30304: CDC25A; NbExp=3; IntAct=EBI-359854, EBI-747671;
CC P27348; O94921: CDK14; NbExp=3; IntAct=EBI-359854, EBI-1043945;
CC P27348; P00533: EGFR; NbExp=7; IntAct=EBI-359854, EBI-297353;
CC P27348; P23945: FSHR; NbExp=4; IntAct=EBI-359854, EBI-848239;
CC P27348; P56524: HDAC4; NbExp=3; IntAct=EBI-359854, EBI-308629;
CC P27348; Q14678: KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221;
CC P27348; Q14678-2: KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812;
CC P27348; Q5S007: LRRK2; NbExp=10; IntAct=EBI-359854, EBI-5323863;
CC P27348; Q99759: MAP3K3; NbExp=2; IntAct=EBI-359854, EBI-307281;
CC P27348; P04049: RAF1; NbExp=7; IntAct=EBI-359854, EBI-365996;
CC P27348; Q8WYL5: SSH1; NbExp=2; IntAct=EBI-359854, EBI-1222387;
CC P27348; Q8IWZ5: TRIM42; NbExp=4; IntAct=EBI-359854, EBI-5235829;
CC P27348; P31946: YWHAB; NbExp=3; IntAct=EBI-359854, EBI-359815;
CC P27348; P62258: YWHAE; NbExp=7; IntAct=EBI-359854, EBI-356498;
CC P27348; P61981: YWHAG; NbExp=3; IntAct=EBI-359854, EBI-359832;
CC P27348; P27348: YWHAQ; NbExp=2; IntAct=EBI-359854, EBI-359854;
CC P27348; P67828: CSNK1A1; Xeno; NbExp=2; IntAct=EBI-359854, EBI-7540603;
CC P27348; P61588: Rnd3; Xeno; NbExp=2; IntAct=EBI-359854, EBI-6930266;
CC P27348; B7UM99: tir; Xeno; NbExp=6; IntAct=EBI-359854, EBI-2504426;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally transported
CC to the nerve terminals.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and pancreas,
CC and at lower levels in kidney and placenta. Up-regulated in the lumbar
CC spinal cord from patients with sporadic amyotrophic lateral sclerosis
CC (ALS) compared with controls, with highest levels of expression in
CC individuals with predominant lower motor neuron involvement.
CC {ECO:0000269|PubMed:11080204}.
CC -!- PTM: Ser-232 is probably phosphorylated by CK1.
CC {ECO:0000269|PubMed:9360956}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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; 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 CCDS; CCDS1666.1; -.
DR PIR; S15076; S15076.
DR RefSeq; NP_006817.1; NM_006826.3.
DR PDB; 2BTP; X-ray; 2.80 A; A/B=1-234.
DR PDB; 5IQP; X-ray; 2.60 A; A/B=1-245.
DR PDB; 6BCR; X-ray; 1.99 A; A/B/E/F=1-245.
DR PDB; 6BD2; X-ray; 2.90 A; A/B=1-245.
DR PDB; 6BQT; X-ray; 2.80 A; A/B/D/E/G/H/J/K=1-245.
DR PDB; 6KZG; X-ray; 2.00 A; A/B=2-234.
DR PDB; 6KZH; X-ray; 2.65 A; A/B=2-234.
DR PDBsum; 2BTP; -.
DR PDBsum; 5IQP; -.
DR PDBsum; 6BCR; -.
DR PDBsum; 6BD2; -.
DR PDBsum; 6BQT; -.
DR PDBsum; 6KZG; -.
DR PDBsum; 6KZH; -.
DR AlphaFoldDB; P27348; -.
DR SMR; P27348; -.
DR BioGRID; 116168; 882.
DR CORUM; P27348; -.
DR DIP; DIP-27584N; -.
DR ELM; P27348; -.
DR IntAct; P27348; 347.
DR MINT; P27348; -.
DR STRING; 9606.ENSP00000371267; -.
DR BindingDB; P27348; -.
DR ChEMBL; CHEMBL3710408; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; P27348; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P27348; -.
DR MetOSite; P27348; -.
DR PhosphoSitePlus; P27348; -.
DR SwissPalm; P27348; -.
DR BioMuta; YWHAQ; -.
DR DMDM; 112690; -.
DR OGP; P27348; -.
DR REPRODUCTION-2DPAGE; IPI00018146; -.
DR CPTAC; CPTAC-143; -.
DR CPTAC; CPTAC-144; -.
DR EPD; P27348; -.
DR jPOST; P27348; -.
DR MassIVE; P27348; -.
DR MaxQB; P27348; -.
DR PaxDb; P27348; -.
DR PeptideAtlas; P27348; -.
DR PRIDE; P27348; -.
DR ProteomicsDB; 54380; -.
DR TopDownProteomics; P27348; -.
DR Antibodypedia; 1900; 595 antibodies from 46 providers.
DR DNASU; 10971; -.
DR Ensembl; ENST00000238081.8; ENSP00000238081.3; ENSG00000134308.14.
DR Ensembl; ENST00000381844.8; ENSP00000371267.4; ENSG00000134308.14.
DR GeneID; 10971; -.
DR KEGG; hsa:10971; -.
DR MANE-Select; ENST00000238081.8; ENSP00000238081.3; NM_006826.4; NP_006817.1.
DR UCSC; uc002qzx.5; human.
DR CTD; 10971; -.
DR DisGeNET; 10971; -.
DR GeneCards; YWHAQ; -.
DR HGNC; HGNC:12854; YWHAQ.
DR HPA; ENSG00000134308; Low tissue specificity.
DR MIM; 609009; gene.
DR neXtProt; NX_P27348; -.
DR OpenTargets; ENSG00000134308; -.
DR PharmGKB; PA37443; -.
DR VEuPathDB; HostDB:ENSG00000134308; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P27348; -.
DR OMA; FEMATTI; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P27348; -.
DR TreeFam; TF102002; -.
DR PathwayCommons; P27348; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-HSA-9614399; Regulation of localization of FOXO transcription factors.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SignaLink; P27348; -.
DR SIGNOR; P27348; -.
DR BioGRID-ORCS; 10971; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; YWHAQ; human.
DR EvolutionaryTrace; P27348; -.
DR GeneWiki; YWHAQ; -.
DR GenomeRNAi; 10971; -.
DR Pharos; P27348; Tchem.
DR PRO; PR:P27348; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P27348; protein.
DR Bgee; ENSG00000134308; Expressed in sperm and 212 other tissues.
DR ExpressionAtlas; P27348; baseline and differential.
DR Genevisible; P27348; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR CDD; cd10023; 14-3-3_theta; 1.
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 InterPro; IPR042584; 14-3-3_theta.
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; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nitration; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..245
FT /note="14-3-3 protein theta"
FT /id="PRO_0000058636"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT SITE 127
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 82
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68254"
FT MOD_RES 104
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9360956,
FT ECO:0007744|PubMed:18669648"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 136
FT /note="D -> N (in Ref. 3; AAV38817)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 38..68
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 136..159
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:6BCR"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:6BCR"
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
