1433G_HUMAN
ID 1433G_HUMAN Reviewed; 247 AA.
AC P61981; O70457; P35214; Q6FH52; Q9UDP2; Q9UN99;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=14-3-3 protein gamma;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
DE Contains:
DE RecName: Full=14-3-3 protein gamma, N-terminally processed;
GN Name=YWHAG;
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], PHOSPHORYLATION, AND INTERACTION WITH RAF1.
RC TISSUE=Vascular smooth muscle;
RX PubMed=10433554; DOI=10.1089/104454999315105;
RA Autieri M.V., Carbone C.J.;
RT "14-3-3gamma interacts with and is phosphorylated by multiple protein
RT kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells.";
RL DNA Cell Biol. 18:555-564(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=10486217; DOI=10.1006/geno.1999.5887;
RA Horie M., Suzuki M., Takahashi E., Tanigami A.;
RT "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene
RT (YWHAG) to 7q11.23.";
RL Genomics 60:241-243(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrial tumor;
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 1-10; 29-50; 62-77; 133-198 AND 228-247, INTERACTION
RP WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS 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 [7]
RP PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, PHOSPHORYLATION AT
RP THR-145, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 2-12.
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 [9]
RP PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP INTERACTION WITH AANAT.
RX PubMed=11427721; DOI=10.1073/pnas.141118798;
RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [12]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=14534293; DOI=10.1074/jbc.m309039200;
RA Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R.,
RA Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J.,
RA Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E.;
RT "Proteomics-based target identification: bengamides as a new class of
RT methionine aminopeptidase inhibitors.";
RL J. Biol. Chem. 278:52964-52971(2003).
RN [13]
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 [14]
RP INTERACTION WITH CRTC2.
RX PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
RA Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
RA Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
RA Okamoto M., Montminy M.;
RT "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
RT coincidence detector.";
RL Cell 119:61-74(2004).
RN [15]
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 [16]
RP INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15696159; DOI=10.1038/ncb1228;
RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-
RT Abl in the apoptotic response to DNA damage.";
RL Nat. Cell Biol. 7:278-285(2005).
RN [17]
RP FUNCTION IN TP53 ACTIVATION, AND INTERACTION WITH MDM4.
RX PubMed=16511572; DOI=10.1038/sj.emboj.7601010;
RA Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.;
RT "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1,
RT resulting in p53 activation.";
RL EMBO J. 25:1207-1218(2006).
RN [18]
RP INTERACTION WITH MARK2 AND MARK3.
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 SIRT2.
RX PubMed=18249187; DOI=10.1016/j.bbrc.2008.01.114;
RA Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y., Lee K.Y.;
RT "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of
RT p53.";
RL Biochem. Biophys. Res. Commun. 368:690-695(2008).
RN [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234 AND SER-235, AND
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 [28]
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 [29]
RP IDENTIFICATION BY MASS 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 [30]
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 [31]
RP INTERACTION WITH LRRK2.
RX PubMed=28202711; DOI=10.1042/bcj20161078;
RA Stevers L.M., de Vries R.M., Doveston R.G., Milroy L.G., Brunsveld L.,
RA Ottmann C.;
RT "Structural interface between LRRK2 and 14-3-3 protein.";
RL Biochem. J. 474:1273-1287(2017).
RN [32]
RP INTERACTION WITH ENDOG; TSC2 AND PIK3C3.
RX PubMed=33473107; DOI=10.1038/s41467-020-20780-2;
RA Wang W., Li J., Tan J., Wang M., Yang J., Zhang Z.M., Li C.,
RA Basnakian A.G., Tang H.W., Perrimon N., Zhou Q.;
RT "Endonuclease G promotes autophagy by suppressing mTOR signaling and
RT activating the DNA damage response.";
RL Nat. Commun. 12:476-476(2021).
RN [33]
RP INVOLVEMENT IN DEE56, VARIANTS DEE56 ALA-15; GLU-129 AND CYS-132, AND
RP VARIANTS GLN-50 AND SER-133.
RX PubMed=28777935; DOI=10.1016/j.ajhg.2017.07.004;
RG Epilepsy Genomics Study;
RG Deciphering Developmental Disorders Study;
RA Guella I., McKenzie M.B., Evans D.M., Buerki S.E., Toyota E.B.,
RA Van Allen M.I., Suri M., Elmslie F., Simon M.E.H., van Gassen K.L.I.,
RA Heron D., Keren B., Nava C., Connolly M.B., Demos M., Farrer M.J.;
RT "De novo mutations in YWHAG cause early-onset epilepsy.";
RL Am. J. Hum. Genet. 101:300-310(2017).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), 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. {ECO:0000269|PubMed:16511572}.
CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 (By similarity). Interacts
CC with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated
CC form); the interaction retains it in the cytoplasm. Interacts with
CC GAB2. Interacts with MDM4 (phosphorylated); negatively regulates MDM4
CC activity toward TP53. Interacts with PKA-phosphorylated AANAT and
CC SIRT2.Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B
CC (PubMed:23572552). Interacts with SLITRK1 (PubMed:19640509). Interacts
CC with LRRK2; this interaction is dependent on LRRK2 phosphorylation
CC (PubMed:28202711). Interacts with MARK2 and MARK3 (PubMed:16959763).
CC Interacts with MEFV (PubMed:27030597). Interacts with ENDOG, TSC2 and
CC PIK3C3; interaction with ENDOG weakens its interaction with TSC2 and
CC PIK3C3 (PubMed:33473107). {ECO:0000250, ECO:0000250|UniProtKB:P61982,
CC ECO:0000269|PubMed:10433554, ECO:0000269|PubMed:11427721,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15454081,
CC ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:16511572,
CC ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:17085597,
CC ECO:0000269|PubMed:18249187, ECO:0000269|PubMed:19172738,
CC ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:23572552,
CC ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:27030597,
CC ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:33473107}.
CC -!- INTERACTION:
CC P61981; P00519: ABL1; NbExp=4; IntAct=EBI-359832, EBI-375543;
CC P61981; Q15027: ACAP1; NbExp=3; IntAct=EBI-359832, EBI-751746;
CC P61981; Q9NPJ3: ACOT13; NbExp=3; IntAct=EBI-359832, EBI-1045357;
CC P61981; Q8IWZ3-3: ANKHD1; NbExp=3; IntAct=EBI-359832, EBI-25833200;
CC P61981; O43307: ARHGEF9; NbExp=3; IntAct=EBI-359832, EBI-3447299;
CC P61981; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-359832, EBI-5280499;
CC P61981; Q9Y576: ASB1; NbExp=3; IntAct=EBI-359832, EBI-2323092;
CC P61981; Q14032: BAAT; NbExp=3; IntAct=EBI-359832, EBI-8994378;
CC P61981; Q92934: BAD; NbExp=4; IntAct=EBI-359832, EBI-700771;
CC P61981; Q13072: BAGE; NbExp=3; IntAct=EBI-359832, EBI-25884811;
CC P61981; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-359832, EBI-11524452;
CC P61981; Q6PH81: C16orf87; NbExp=3; IntAct=EBI-359832, EBI-6598617;
CC P61981; Q96HJ3-2: CCDC34; NbExp=3; IntAct=EBI-359832, EBI-17641690;
CC P61981; Q96A33: CCDC47; NbExp=3; IntAct=EBI-359832, EBI-720151;
CC P61981; Q96LY2-2: CCDC74B; NbExp=3; IntAct=EBI-359832, EBI-17967022;
CC P61981; Q9GZT6: CCDC90B; NbExp=3; IntAct=EBI-359832, EBI-713148;
CC P61981; P30305: CDC25B; NbExp=3; IntAct=EBI-359832, EBI-1051746;
CC P61981; Q9HC77: CENPJ; NbExp=3; IntAct=EBI-359832, EBI-946194;
CC P61981; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-359832, EBI-1210604;
CC P61981; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-359832, EBI-742887;
CC P61981; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-359832, EBI-743375;
CC P61981; O14757: CHEK1; NbExp=7; IntAct=EBI-359832, EBI-974488;
CC P61981; Q99828: CIB1; NbExp=3; IntAct=EBI-359832, EBI-372594;
CC P61981; P15169: CPN1; NbExp=3; IntAct=EBI-359832, EBI-2116369;
CC P61981; P43234: CTSO; NbExp=3; IntAct=EBI-359832, EBI-2874283;
CC P61981; O95424: DEXI; NbExp=3; IntAct=EBI-359832, EBI-724515;
CC P61981; O43598: DNPH1; NbExp=3; IntAct=EBI-359832, EBI-748674;
CC P61981; P21728: DRD1; NbExp=3; IntAct=EBI-359832, EBI-6624459;
CC P61981; P60228: EIF3E; NbExp=3; IntAct=EBI-359832, EBI-347740;
CC P61981; Q96J88-3: EPSTI1; NbExp=3; IntAct=EBI-359832, EBI-25885343;
CC P61981; Q9NYF3: FAM53C; NbExp=6; IntAct=EBI-359832, EBI-1644252;
CC P61981; Q8IVH2-2: FOXP4; NbExp=3; IntAct=EBI-359832, EBI-25885364;
CC P61981; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-359832, EBI-13213391;
CC P61981; O14926: FSCN2; NbExp=3; IntAct=EBI-359832, EBI-21017948;
CC P61981; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-359832, EBI-618189;
CC P61981; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-359832, EBI-9088619;
CC P61981; P19440-3: GGT1; NbExp=3; IntAct=EBI-359832, EBI-21558069;
CC P61981; O95837: GNA14; NbExp=3; IntAct=EBI-359832, EBI-7951023;
CC P61981; Q96F32: GNB5; NbExp=3; IntAct=EBI-359832, EBI-25902214;
CC P61981; O43292-2: GPAA1; NbExp=3; IntAct=EBI-359832, EBI-25884370;
CC P61981; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-359832, EBI-11959863;
CC P61981; Q9UJ42: GPR160; NbExp=3; IntAct=EBI-359832, EBI-25885139;
CC P61981; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-359832, EBI-473189;
CC P61981; Q13322-4: GRB10; NbExp=3; IntAct=EBI-359832, EBI-12353035;
CC P61981; P62805: H4C9; NbExp=3; IntAct=EBI-359832, EBI-302023;
CC P61981; O00165: HAX1; NbExp=3; IntAct=EBI-359832, EBI-357001;
CC P61981; Q8N7T0: hCG_1820408; NbExp=3; IntAct=EBI-359832, EBI-25858908;
CC P61981; P56524: HDAC4; NbExp=8; IntAct=EBI-359832, EBI-308629;
CC P61981; Q5T1R4: HIVEP3; NbExp=2; IntAct=EBI-359832, EBI-28989979;
CC P61981; P52597: HNRNPF; NbExp=3; IntAct=EBI-359832, EBI-352986;
CC P61981; Q92826: HOXB13; NbExp=3; IntAct=EBI-359832, EBI-11317274;
CC P61981; P09017: HOXC4; NbExp=3; IntAct=EBI-359832, EBI-3923226;
CC P61981; Q03933-2: HSF2; NbExp=3; IntAct=EBI-359832, EBI-10223348;
CC P61981; Q02363: ID2; NbExp=3; IntAct=EBI-359832, EBI-713450;
CC P61981; Q96FT9-2: IFT43; NbExp=3; IntAct=EBI-359832, EBI-11944538;
CC P61981; P78318: IGBP1; NbExp=3; IntAct=EBI-359832, EBI-1055954;
CC P61981; P17936: IGFBP3; NbExp=3; IntAct=EBI-359832, EBI-715709;
CC P61981; P26951: IL3RA; NbExp=3; IntAct=EBI-359832, EBI-1757512;
CC P61981; Q14678-2: KANK1; NbExp=3; IntAct=EBI-359832, EBI-6173812;
CC P61981; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-359832, EBI-743960;
CC P61981; Q02241: KIF23; NbExp=3; IntAct=EBI-359832, EBI-306852;
CC P61981; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-359832, EBI-750750;
CC P61981; Q5JUW0-3: KRBOX4; NbExp=3; IntAct=EBI-359832, EBI-12893625;
CC P61981; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-359832, EBI-9996449;
CC P61981; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-359832, EBI-25835523;
CC P61981; Q9Y234: LIPT1; NbExp=3; IntAct=EBI-359832, EBI-727376;
CC P61981; Q5S007: LRRK2; NbExp=26; IntAct=EBI-359832, EBI-5323863;
CC P61981; P51884: LUM; NbExp=3; IntAct=EBI-359832, EBI-725780;
CC P61981; Q96GV9: MACIR; NbExp=4; IntAct=EBI-359832, EBI-2350695;
CC P61981; Q9H213: MAGEH1; NbExp=3; IntAct=EBI-359832, EBI-473834;
CC P61981; Q99759: MAP3K3; NbExp=3; IntAct=EBI-359832, EBI-307281;
CC P61981; P80192: MAP3K9; NbExp=3; IntAct=EBI-359832, EBI-3951604;
CC P61981; Q15759: MAPK11; NbExp=3; IntAct=EBI-359832, EBI-298304;
CC P61981; Q7KZI7: MARK2; NbExp=4; IntAct=EBI-359832, EBI-516560;
CC P61981; P27448: MARK3; NbExp=4; IntAct=EBI-359832, EBI-707595;
CC P61981; O15151: MDM4; NbExp=7; IntAct=EBI-359832, EBI-398437;
CC P61981; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-359832, EBI-13288755;
CC P61981; Q9H8H3: METTL7A; NbExp=3; IntAct=EBI-359832, EBI-1390168;
CC P61981; P41218: MNDA; NbExp=3; IntAct=EBI-359832, EBI-2829677;
CC P61981; Q8N983-3: MRPL43; NbExp=3; IntAct=EBI-359832, EBI-11109389;
CC P61981; Q16718: NDUFA5; NbExp=3; IntAct=EBI-359832, EBI-746417;
CC P61981; P49821: NDUFV1; NbExp=3; IntAct=EBI-359832, EBI-748312;
CC P61981; I6L9F6: NEFL; NbExp=3; IntAct=EBI-359832, EBI-10178578;
CC P61981; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-359832, EBI-2859639;
CC P61981; Q2M1J6: OXA1L; NbExp=3; IntAct=EBI-359832, EBI-9978021;
CC P61981; Q16342: PDCD2; NbExp=3; IntAct=EBI-359832, EBI-359462;
CC P61981; Q9BRX2: PELO; NbExp=3; IntAct=EBI-359832, EBI-1043580;
CC P61981; Q9Y6X2: PIAS3; NbExp=3; IntAct=EBI-359832, EBI-2803703;
CC P61981; Q86T03: PIP4P1; NbExp=3; IntAct=EBI-359832, EBI-6164623;
CC P61981; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-359832, EBI-10694821;
CC P61981; Q9UNA4: POLI; NbExp=3; IntAct=EBI-359832, EBI-741774;
CC P61981; P07225: PROS1; NbExp=3; IntAct=EBI-359832, EBI-2803380;
CC P61981; P26045: PTPN3; NbExp=5; IntAct=EBI-359832, EBI-1047946;
CC P61981; Q3YEC7-3: RABL6; NbExp=3; IntAct=EBI-359832, EBI-25885259;
CC P61981; P04049: RAF1; NbExp=6; IntAct=EBI-359832, EBI-365996;
CC P61981; Q96I51: RCC1L; NbExp=3; IntAct=EBI-359832, EBI-2117080;
CC P61981; O94844: RHOBTB1; NbExp=3; IntAct=EBI-359832, EBI-6426999;
CC P61981; Q9UJD0: RIMS3; NbExp=4; IntAct=EBI-359832, EBI-3909436;
CC P61981; Q9NWS8-3: RMND1; NbExp=3; IntAct=EBI-359832, EBI-25884400;
CC P61981; Q9Y508: RNF114; NbExp=3; IntAct=EBI-359832, EBI-723587;
CC P61981; Q9ULK6-3: RNF150; NbExp=3; IntAct=EBI-359832, EBI-23640835;
CC P61981; P62913-2: RPL11; NbExp=3; IntAct=EBI-359832, EBI-11027771;
CC P61981; P18077: RPL35A; NbExp=3; IntAct=EBI-359832, EBI-353383;
CC P61981; Q99643: SDHC; NbExp=3; IntAct=EBI-359832, EBI-1224539;
CC P61981; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-359832, EBI-745901;
CC P61981; Q01105-2: SET; NbExp=3; IntAct=EBI-359832, EBI-7481343;
CC P61981; P31947: SFN; NbExp=2; IntAct=EBI-359832, EBI-476295;
CC P61981; Q13573: SNW1; NbExp=3; IntAct=EBI-359832, EBI-632715;
CC P61981; Q9Y5X0: SNX10; NbExp=3; IntAct=EBI-359832, EBI-10329478;
CC P61981; Q8WV41: SNX33; NbExp=3; IntAct=EBI-359832, EBI-2481535;
CC P61981; P56693: SOX10; NbExp=3; IntAct=EBI-359832, EBI-1167533;
CC P61981; Q9BRW5: SP2; NbExp=3; IntAct=EBI-359832, EBI-25868254;
CC P61981; Q13586: STIM1; NbExp=3; IntAct=EBI-359832, EBI-448878;
CC P61981; Q13033-2: STRN3; NbExp=3; IntAct=EBI-359832, EBI-1053876;
CC P61981; O43761: SYNGR3; NbExp=3; IntAct=EBI-359832, EBI-11321949;
CC P61981; P15884: TCF4; NbExp=3; IntAct=EBI-359832, EBI-533224;
CC P61981; Q92481: TFAP2B; NbExp=3; IntAct=EBI-359832, EBI-725275;
CC P61981; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-359832, EBI-717399;
CC P61981; Q3YBM2: TMEM176B; NbExp=3; IntAct=EBI-359832, EBI-2821479;
CC P61981; Q969K7: TMEM54; NbExp=3; IntAct=EBI-359832, EBI-3922833;
CC P61981; P04637: TP53; NbExp=5; IntAct=EBI-359832, EBI-366083;
CC P61981; P51580: TPMT; NbExp=3; IntAct=EBI-359832, EBI-25902017;
CC P61981; Q9UJA5: TRMT6; NbExp=3; IntAct=EBI-359832, EBI-934061;
CC P61981; Q99598: TSNAX; NbExp=3; IntAct=EBI-359832, EBI-742638;
CC P61981; Q8NB14: USP38; NbExp=3; IntAct=EBI-359832, EBI-2512509;
CC P61981; Q15836: VAMP3; NbExp=3; IntAct=EBI-359832, EBI-722343;
CC P61981; O95498: VNN2; NbExp=3; IntAct=EBI-359832, EBI-21494555;
CC P61981; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-359832, EBI-12040603;
CC P61981; P31946: YWHAB; NbExp=3; IntAct=EBI-359832, EBI-359815;
CC P61981; P62258: YWHAE; NbExp=7; IntAct=EBI-359832, EBI-356498;
CC P61981; P61981: YWHAG; NbExp=3; IntAct=EBI-359832, EBI-359832;
CC P61981; P27348: YWHAQ; NbExp=3; IntAct=EBI-359832, EBI-359854;
CC P61981; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-359832, EBI-14104088;
CC P61981; Q9BQ24: ZFYVE21; NbExp=3; IntAct=EBI-359832, EBI-2849569;
CC P61981; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-359832, EBI-2602314;
CC P61981; Q14202: ZMYM3; NbExp=3; IntAct=EBI-359832, EBI-2556139;
CC P61981; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-359832, EBI-25835471;
CC P61981; Q9UL40: ZNF346; NbExp=3; IntAct=EBI-359832, EBI-2462313;
CC P61981; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-359832, EBI-12010736;
CC P61981; O15535: ZSCAN9; NbExp=3; IntAct=EBI-359832, EBI-751531;
CC P61981; Q9HBH6; NbExp=3; IntAct=EBI-359832, EBI-25901704;
CC P61981; P67828: CSNK1A1; Xeno; NbExp=3; IntAct=EBI-359832, EBI-7540603;
CC P61981; P61014: Pln; Xeno; NbExp=3; IntAct=EBI-359832, EBI-10148373;
CC P61981; P61588: Rnd3; Xeno; NbExp=2; IntAct=EBI-359832, EBI-6930266;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle, and
CC heart. {ECO:0000269|PubMed:10486217}.
CC -!- PTM: Phosphorylated by various PKC isozymes.
CC {ECO:0000269|PubMed:10433554, ECO:0000269|Ref.7}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 56 (DEE56)
CC [MIM:617665]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE56 is an autosomal dominant condition.
CC {ECO:0000269|PubMed:28777935}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; AF142498; AAD48408.1; -; mRNA.
DR EMBL; AB024334; BAA85184.1; -; mRNA.
DR EMBL; CR541904; CAG46702.1; -; mRNA.
DR EMBL; CR541925; CAG46723.1; -; mRNA.
DR EMBL; AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020963; AAH20963.1; -; mRNA.
DR CCDS; CCDS5584.1; -.
DR RefSeq; NP_036611.2; NM_012479.3.
DR PDB; 2B05; X-ray; 2.55 A; A/B/C/D/E/F=2-247.
DR PDB; 3UZD; X-ray; 1.86 A; A=1-247.
DR PDB; 4E2E; X-ray; 2.25 A; A=1-247.
DR PDB; 4J6S; X-ray; 3.08 A; A/B/C/D=1-247.
DR PDB; 4O46; X-ray; 2.90 A; A/B/C/D/E/F=1-247.
DR PDB; 5D3E; X-ray; 2.75 A; A/B/E/F/I/J=1-238.
DR PDB; 6A5S; X-ray; 2.10 A; A/B/D/G=1-247.
DR PDB; 6BYJ; X-ray; 2.90 A; A/B/C/D/E/F=2-241.
DR PDB; 6BYL; X-ray; 3.35 A; A/B/C/D/E/F=2-241.
DR PDB; 6BZD; X-ray; 2.67 A; A/B/C/D=2-247.
DR PDB; 6FEL; X-ray; 2.84 A; A/B/C/D=1-234.
DR PDB; 6GKF; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-234.
DR PDB; 6GKG; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-234.
DR PDB; 6S9K; X-ray; 1.60 A; A=1-234.
DR PDB; 6SAD; X-ray; 2.75 A; A/B=1-234.
DR PDB; 6Y4K; X-ray; 3.00 A; A/B=1-234.
DR PDB; 6Y6B; X-ray; 3.08 A; A/B=1-234.
DR PDB; 6ZBT; X-ray; 1.80 A; A/B/C/D=1-234.
DR PDB; 6ZC9; X-ray; 1.90 A; A/B/C/D=1-234.
DR PDB; 7A6R; X-ray; 2.70 A; A/B/C/D=1-234.
DR PDB; 7A6Y; X-ray; 2.50 A; A/B/C/D=1-234.
DR PDBsum; 2B05; -.
DR PDBsum; 3UZD; -.
DR PDBsum; 4E2E; -.
DR PDBsum; 4J6S; -.
DR PDBsum; 4O46; -.
DR PDBsum; 5D3E; -.
DR PDBsum; 6A5S; -.
DR PDBsum; 6BYJ; -.
DR PDBsum; 6BYL; -.
DR PDBsum; 6BZD; -.
DR PDBsum; 6FEL; -.
DR PDBsum; 6GKF; -.
DR PDBsum; 6GKG; -.
DR PDBsum; 6S9K; -.
DR PDBsum; 6SAD; -.
DR PDBsum; 6Y4K; -.
DR PDBsum; 6Y6B; -.
DR PDBsum; 6ZBT; -.
DR PDBsum; 6ZC9; -.
DR PDBsum; 7A6R; -.
DR PDBsum; 7A6Y; -.
DR AlphaFoldDB; P61981; -.
DR SMR; P61981; -.
DR BioGRID; 113364; 780.
DR CORUM; P61981; -.
DR DIP; DIP-33406N; -.
DR ELM; P61981; -.
DR IntAct; P61981; 674.
DR MINT; P61981; -.
DR STRING; 9606.ENSP00000306330; -.
DR BindingDB; P61981; -.
DR ChEMBL; CHEMBL1293296; -.
DR GlyGen; P61981; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61981; -.
DR MetOSite; P61981; -.
DR PhosphoSitePlus; P61981; -.
DR SwissPalm; P61981; -.
DR BioMuta; YWHAG; -.
DR DMDM; 48428721; -.
DR REPRODUCTION-2DPAGE; IPI00220642; -.
DR CPTAC; CPTAC-450; -.
DR CPTAC; CPTAC-451; -.
DR EPD; P61981; -.
DR jPOST; P61981; -.
DR MassIVE; P61981; -.
DR MaxQB; P61981; -.
DR PaxDb; P61981; -.
DR PeptideAtlas; P61981; -.
DR PRIDE; P61981; -.
DR ProteomicsDB; 57355; -.
DR TopDownProteomics; P61981; -.
DR Antibodypedia; 4339; 574 antibodies from 41 providers.
DR DNASU; 7532; -.
DR Ensembl; ENST00000307630.5; ENSP00000306330.3; ENSG00000170027.7.
DR GeneID; 7532; -.
DR KEGG; hsa:7532; -.
DR MANE-Select; ENST00000307630.5; ENSP00000306330.3; NM_012479.4; NP_036611.2.
DR UCSC; uc011kgj.2; human.
DR CTD; 7532; -.
DR DisGeNET; 7532; -.
DR GeneCards; YWHAG; -.
DR HGNC; HGNC:12852; YWHAG.
DR HPA; ENSG00000170027; Tissue enhanced (brain, skeletal muscle).
DR MalaCards; YWHAG; -.
DR MIM; 605356; gene.
DR MIM; 617665; phenotype.
DR neXtProt; NX_P61981; -.
DR OpenTargets; ENSG00000170027; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA37441; -.
DR VEuPathDB; HostDB:ENSG00000170027; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P61981; -.
DR OMA; MANTERD; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P61981; -.
DR TreeFam; TF102003; -.
DR PathwayCommons; P61981; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body 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-8854518; AURKA Activation by TPX2.
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; P61981; -.
DR SIGNOR; P61981; -.
DR BioGRID-ORCS; 7532; 27 hits in 1083 CRISPR screens.
DR ChiTaRS; YWHAG; human.
DR EvolutionaryTrace; P61981; -.
DR GeneWiki; YWHAG; -.
DR GenomeRNAi; 7532; -.
DR Pharos; P61981; Tchem.
DR PRO; PR:P61981; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P61981; protein.
DR Bgee; ENSG00000170027; Expressed in lateral nuclear group of thalamus and 191 other tissues.
DR Genevisible; P61981; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 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 Disease variant; Epilepsy; Phosphoprotein; Reference proteome.
FT CHAIN 1..247
FT /note="14-3-3 protein gamma"
FT /id="PRO_0000367907"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7,
FT ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330"
FT CHAIN 2..247
FT /note="14-3-3 protein gamma, N-terminally processed"
FT /id="PRO_0000058606"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT SITE 132
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT MOD_RES 1
FT /note="N-acetylmethionine; in 14-3-3 protein gamma;
FT alternate; partial"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 2
FT /note="N-acetylvaline; in 14-3-3 protein gamma, N-
FT terminally processed; partial"
FT /evidence="ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7,
FT ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="N-acetylvaline; partial"
FT /evidence="ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7,
FT ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 15
FT /note="E -> A (in DEE56; unknown pathological significance;
FT dbSNP:rs1554618767)"
FT /evidence="ECO:0000269|PubMed:28777935"
FT /id="VAR_080224"
FT VARIANT 50
FT /note="K -> Q (found in an individual with autism; unknown
FT pathological significance; dbSNP:rs1554616652)"
FT /evidence="ECO:0000269|PubMed:28777935"
FT /id="VAR_080225"
FT VARIANT 129
FT /note="D -> E (in DEE56; dbSNP:rs1554616630)"
FT /evidence="ECO:0000269|PubMed:28777935"
FT /id="VAR_080226"
FT VARIANT 132
FT /note="R -> C (in DEE56; dbSNP:rs1554616628)"
FT /evidence="ECO:0000269|PubMed:28777935"
FT /id="VAR_080227"
FT VARIANT 133
FT /note="Y -> S (probable disease-associated variant found in
FT an individual with neurodevelopmental disorder;
FT dbSNP:rs1554616627)"
FT /evidence="ECO:0000269|PubMed:28777935"
FT /id="VAR_080228"
FT CONFLICT 4
FT /note="R -> P (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="R -> G (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="Missing (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="I -> V (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> V (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="I -> Y (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..122
FT /note="SKVF -> RKDL (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="AT -> GD (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..158
FT /note="AH -> R (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..202
FT /note="AFD -> EFE (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="D -> E (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="D -> DH (in Ref. 1; AAD48408)"
FT /evidence="ECO:0000305"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:6S9K"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6ZBT"
FT HELIX 39..69
FT /evidence="ECO:0007829|PDB:6S9K"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:6SAD"
FT HELIX 77..106
FT /evidence="ECO:0007829|PDB:6S9K"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 117..137
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 140..164
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6S9K"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:6S9K"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6BYL"
SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64;
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW
RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK
VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS
VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD
DGGEGNN
