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Database: UniProt
Entry: P61981
LinkDB: P61981
Original site: P61981 
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   17-JUN-2020, entry version 177.
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 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   [31]
RP   INVOLVEMENT IN EIEE56, VARIANTS EIEE56 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   [32]
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       {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:28202711}.
CC   -!- INTERACTION:
CC       P61981; P00519: ABL1; NbExp=4; IntAct=EBI-359832, EBI-375543;
CC       P61981; Q92934: BAD; NbExp=4; IntAct=EBI-359832, EBI-700771;
CC       P61981; P30305: CDC25B; NbExp=3; IntAct=EBI-359832, EBI-1051746;
CC       P61981; Q9HC77: CENPJ; NbExp=3; IntAct=EBI-359832, EBI-946194;
CC       P61981; O14757: CHEK1; NbExp=7; IntAct=EBI-359832, EBI-974488;
CC       P61981; Q9NYF3: FAM53C; NbExp=6; IntAct=EBI-359832, EBI-1644252;
CC       P61981; P56524: HDAC4; NbExp=8; IntAct=EBI-359832, EBI-308629;
CC       P61981; Q14678-2: KANK1; NbExp=3; IntAct=EBI-359832, EBI-6173812;
CC       P61981; Q02241: KIF23; NbExp=3; IntAct=EBI-359832, EBI-306852;
CC       P61981; Q5S007: LRRK2; NbExp=26; IntAct=EBI-359832, EBI-5323863;
CC       P61981; Q99759: MAP3K3; NbExp=2; IntAct=EBI-359832, EBI-307281;
CC       P61981; Q7KZI7: MARK2; NbExp=3; IntAct=EBI-359832, EBI-516560;
CC       P61981; P27448: MARK3; NbExp=3; IntAct=EBI-359832, EBI-707595;
CC       P61981; O15151: MDM4; NbExp=7; IntAct=EBI-359832, EBI-398437;
CC       P61981; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-359832, EBI-2859639;
CC       P61981; P26045: PTPN3; NbExp=4; IntAct=EBI-359832, EBI-1047946;
CC       P61981; P04049: RAF1; NbExp=5; IntAct=EBI-359832, EBI-365996;
CC       P61981; P31947: SFN; NbExp=2; IntAct=EBI-359832, EBI-476295;
CC       P61981; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-359832, EBI-717399;
CC       P61981; P04637: TP53; NbExp=5; IntAct=EBI-359832, EBI-366083;
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; P67828: CSNK1A1; Xeno; NbExp=3; IntAct=EBI-359832, EBI-7540603;
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: Epileptic encephalopathy, early infantile, 56 (EIEE56)
CC       [MIM:617665]: A form of epileptic encephalopathy, a heterogeneous group
CC       of severe childhood onset epilepsies characterized by refractory
CC       seizures, neurodevelopmental impairment, and poor prognosis.
CC       Development is normal prior to seizure onset, after which cognitive and
CC       motor delays become apparent. EIEE56 is an autosomal dominant
CC       condition. {ECO:0000269|PubMed:28777935}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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   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   SMR; P61981; -.
DR   BioGRID; 113364; 381.
DR   CORUM; P61981; -.
DR   DIP; DIP-33406N; -.
DR   ELM; P61981; -.
DR   IntAct; P61981; 492.
DR   MINT; P61981; -.
DR   STRING; 9606.ENSP00000306330; -.
DR   BindingDB; P61981; -.
DR   ChEMBL; CHEMBL1293296; -.
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; 536 antibodies.
DR   DNASU; 7532; -.
DR   Ensembl; ENST00000307630; ENSP00000306330; ENSG00000170027.
DR   GeneID; 7532; -.
DR   KEGG; hsa:7532; -.
DR   UCSC; uc011kgj.2; human.
DR   CTD; 7532; -.
DR   DisGeNET; 7532; -.
DR   EuPathDB; HostDB:ENSG00000170027.6; -.
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; Undetermined early-onset epileptic encephalopathy.
DR   PharmGKB; PA37441; -.
DR   eggNOG; KOG0841; Eukaryota.
DR   eggNOG; COG5040; LUCA.
DR   GeneTree; ENSGT00990000203523; -.
DR   HOGENOM; CLU_058290_0_0_1; -.
DR   InParanoid; P61981; -.
DR   KO; K16198; -.
DR   OMA; IKNCGET; -.
DR   OrthoDB; 1176818at2759; -.
DR   PhylomeDB; P61981; -.
DR   TreeFam; TF102003; -.
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   SignaLink; P61981; -.
DR   SIGNOR; P61981; -.
DR   BioGRID-ORCS; 7532; 13 hits in 791 CRISPR screens.
DR   ChiTaRS; YWHAG; human.
DR   EvolutionaryTrace; P61981; -.
DR   GeneWiki; YWHAG; -.
DR   GenomeRNAi; 7532; -.
DR   Pharos; P61981; Tbio.
DR   PRO; PR:P61981; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P61981; protein.
DR   Bgee; ENSG00000170027; Expressed in lateral nuclear group of thalamus and 209 other tissues.
DR   Genevisible; P61981; HS.
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:0005739; C:mitochondrion; IEA:GOC.
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:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0061024; P:membrane organization; TAS:Reactome.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB.
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:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
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   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 mutation; 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:0000244|PubMed:19413330,
FT                   ECO:0000269|PubMed:12665801, ECO:0000269|PubMed:14534293,
FT                   ECO:0000269|Ref.7, ECO:0000269|Ref.9"
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:0000244|PubMed:19413330,
FT                   ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7,
FT                   ECO:0000269|Ref.9"
FT   MOD_RES         2
FT                   /note="N-acetylvaline; partial"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7,
FT                   ECO:0000269|Ref.9"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PubMed:24275569"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   VARIANT         15
FT                   /note="E -> A (in EIEE56; unknown pathological
FT                   significance; 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 EIEE56; dbSNP:rs1554616630)"
FT                   /evidence="ECO:0000269|PubMed:28777935"
FT                   /id="VAR_080226"
FT   VARIANT         132
FT                   /note="R -> C (in EIEE56; 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:0000244|PDB:6S9K"
FT   HELIX           20..31
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   TURN            32..34
FT                   /evidence="ECO:0000244|PDB:6FEL"
FT   HELIX           39..69
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   TURN            71..74
FT                   /evidence="ECO:0000244|PDB:6SAD"
FT   HELIX           77..106
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   TURN            107..111
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           117..137
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           140..164
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           170..185
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           190..206
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           207..210
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   TURN            213..215
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           216..233
FT                   /evidence="ECO:0000244|PDB:6S9K"
FT   HELIX           237..240
FT                   /evidence="ECO:0000244|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
//
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