Full text data of YWHAG
YWHAG
[Confidence: high (present in two of the MS resources)]
14-3-3 protein gamma (Protein kinase C inhibitor protein 1; KCIP-1; 14-3-3 protein gamma, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
14-3-3 protein gamma (Protein kinase C inhibitor protein 1; KCIP-1; 14-3-3 protein gamma, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00220642
IPI00220642 14-3-3 protein gamma Protein kinase C inhibitor protein-1, actin binding, insulin-like growth factor receptor binding, protein binding, protein homodimerization activity, protein kinase C binding, cytoskeleton organization soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic TAFDDAIAELDTLNEDSYKDSTLIMQLLR found at its expected molecular weight found at molecular weight
IPI00220642 14-3-3 protein gamma Protein kinase C inhibitor protein-1, actin binding, insulin-like growth factor receptor binding, protein binding, protein homodimerization activity, protein kinase C binding, cytoskeleton organization soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic TAFDDAIAELDTLNEDSYKDSTLIMQLLR found at its expected molecular weight found at molecular weight
UniProt
P61981
ID 1433G_HUMAN Reviewed; 247 AA.
AC P61981; O70457; P35214; Q6FH52; Q9UDP2; Q9UN99;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 116.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH
RP 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
RT 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
RT gene (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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2,
RP PHOSPHORYLATION AT THR-145, AND 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 [7]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
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 MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, AND 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 [10]
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-
RT 3-3-binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [11]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS
RP 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 [12]
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 [13]
RP INTERACTION WITH SSH1.
RX PubMed=15159416; DOI=10.1083/jcb.200401136;
RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT Slingshot and cofilin in lamellipodia.";
RL J. Cell Biol. 165:465-471(2004).
RN [14]
RP INTERACTION WITH ABL1, AND 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
RT c-Abl in the apoptotic response to DNA damage.";
RL Nat. Cell Biol. 7:278-285(2005).
RN [15]
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
RT Chk1, resulting in p53 activation.";
RL EMBO J. 25:1207-1218(2006).
RN [16]
RP INTERACTION WITH GAB2.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA Guilhaus M., James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT the Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), MASS SPECTROMETRY, INTERACTION
RP WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT "Structural basis for protein-protein interactions in the 14-3-3
RT protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds
CC to a large number of partners, usually by recognition of a
CC phosphoserine or phosphothreonine motif. Binding generally results
CC in the modulation of the activity of the binding partner.
CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 (By similarity).
CC Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1
CC (phosphorylated form); the interaction retains it in the
CC cytoplasm. Interacts with GAB2. Interacts with MDM4
CC (phosphorylated); negatively regulates MDM4 activity toward TP53.
CC Interacts with PKA-phosphorylated AANAT.
CC -!- INTERACTION:
CC O14757:CHEK1; NbExp=7; IntAct=EBI-359832, EBI-974488;
CC P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359832, EBI-7540603;
CC P56524:HDAC4; NbExp=3; IntAct=EBI-359832, EBI-308629;
CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359832, EBI-6173812;
CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-359832, EBI-5323863;
CC Q7KZI7:MARK2; NbExp=2; IntAct=EBI-359832, EBI-516560;
CC P27448:MARK3; NbExp=2; IntAct=EBI-359832, EBI-707595;
CC O15151:MDM4; NbExp=7; IntAct=EBI-359832, EBI-398437;
CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359832, EBI-6930266;
CC P04637:TP53; NbExp=5; IntAct=EBI-359832, EBI-366083;
CC P62258:YWHAE; NbExp=4; IntAct=EBI-359832, EBI-356498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle,
CC and heart.
CC -!- PTM: Phosphorylated by various PKC isozymes.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
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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 RefSeq; NP_036611.2; NM_012479.3.
DR UniGene; Hs.744840; -.
DR PDB; 2B05; X-ray; 2.55 A; A/B/C/D/E/F=2-246.
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=2-247.
DR PDBsum; 2B05; -.
DR PDBsum; 3UZD; -.
DR PDBsum; 4E2E; -.
DR PDBsum; 4J6S; -.
DR ProteinModelPortal; P61981; -.
DR SMR; P61981; 1-235.
DR IntAct; P61981; 96.
DR MINT; MINT-248956; -.
DR STRING; 9606.ENSP00000306330; -.
DR BindingDB; P61981; -.
DR ChEMBL; CHEMBL1293296; -.
DR PhosphoSite; P61981; -.
DR DMDM; 48428721; -.
DR REPRODUCTION-2DPAGE; IPI00220642; -.
DR PaxDb; P61981; -.
DR PeptideAtlas; P61981; -.
DR PRIDE; P61981; -.
DR DNASU; 7532; -.
DR Ensembl; ENST00000307630; ENSP00000306330; ENSG00000170027.
DR GeneID; 7532; -.
DR KEGG; hsa:7532; -.
DR UCSC; uc011kgj.1; human.
DR CTD; 7532; -.
DR GeneCards; GC07M075956; -.
DR HGNC; HGNC:12852; YWHAG.
DR HPA; CAB013274; -.
DR HPA; CAB018389; -.
DR HPA; HPA026918; -.
DR MIM; 605356; gene.
DR neXtProt; NX_P61981; -.
DR PharmGKB; PA37441; -.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P61981; -.
DR KO; K16198; -.
DR OMA; CSETQHE; -.
DR OrthoDB; EOG7HHWT3; -.
DR PhylomeDB; P61981; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; P61981; -.
DR ChiTaRS; YWHAG; human.
DR EvolutionaryTrace; P61981; -.
DR GeneWiki; YWHAG; -.
DR GenomeRNAi; 7532; -.
DR NextBio; 29467; -.
DR PRO; PR:P61981; -.
DR ArrayExpress; P61981; -.
DR Bgee; P61981; -.
DR CleanEx; HS_YWHAG; -.
DR Genevestigator; P61981; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
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:0045664; P:regulation of neuron differentiation; IMP: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; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1 247 14-3-3 protein gamma.
FT /FTId=PRO_0000367907.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 247 14-3-3 protein gamma, N-terminally
FT processed.
FT /FTId=PRO_0000058606.
FT SITE 57 57 Interaction with phosphoserine on
FT interacting protein.
FT SITE 132 132 Interaction with phosphoserine on
FT interacting protein.
FT MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein
FT gamma; alternate; partial.
FT MOD_RES 2 2 N-acetylvaline; in 14-3-3 protein gamma,
FT N-terminally processed; partial.
FT MOD_RES 2 2 N-acetylvaline; partial.
FT MOD_RES 145 145 Phosphothreonine.
FT CONFLICT 4 4 R -> P (in Ref. 1; AAD48408).
FT CONFLICT 19 19 R -> G (in Ref. 1; AAD48408).
FT CONFLICT 78 78 Missing (in Ref. 1; AAD48408).
FT CONFLICT 89 89 I -> V (in Ref. 1; AAD48408).
FT CONFLICT 104 104 L -> V (in Ref. 1; AAD48408).
FT CONFLICT 109 109 I -> Y (in Ref. 1; AAD48408).
FT CONFLICT 119 122 SKVF -> RKDL (in Ref. 1; AAD48408).
FT CONFLICT 144 145 AT -> GD (in Ref. 1; AAD48408).
FT CONFLICT 157 158 AH -> R (in Ref. 1; AAD48408).
FT CONFLICT 200 202 AFD -> EFE (in Ref. 1; AAD48408).
FT CONFLICT 214 214 D -> E (in Ref. 1; AAD48408).
FT CONFLICT 240 240 D -> DH (in Ref. 1; AAD48408).
FT HELIX 4 16
FT HELIX 20 31
FT HELIX 39 70
FT HELIX 79 106
FT HELIX 108 111
FT HELIX 117 137
FT HELIX 140 164
FT HELIX 170 185
FT HELIX 190 206
FT HELIX 207 210
FT TURN 213 215
FT HELIX 216 233
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
//
ID 1433G_HUMAN Reviewed; 247 AA.
AC P61981; O70457; P35214; Q6FH52; Q9UDP2; Q9UN99;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 116.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH
RP 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
RT 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
RT gene (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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2,
RP PHOSPHORYLATION AT THR-145, AND 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 [7]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
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 MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, AND 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 [10]
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-
RT 3-3-binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [11]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS
RP 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 [12]
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 [13]
RP INTERACTION WITH SSH1.
RX PubMed=15159416; DOI=10.1083/jcb.200401136;
RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT Slingshot and cofilin in lamellipodia.";
RL J. Cell Biol. 165:465-471(2004).
RN [14]
RP INTERACTION WITH ABL1, AND 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
RT c-Abl in the apoptotic response to DNA damage.";
RL Nat. Cell Biol. 7:278-285(2005).
RN [15]
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
RT Chk1, resulting in p53 activation.";
RL EMBO J. 25:1207-1218(2006).
RN [16]
RP INTERACTION WITH GAB2.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
RA Guilhaus M., James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT the Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), MASS SPECTROMETRY, INTERACTION
RP WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT "Structural basis for protein-protein interactions in the 14-3-3
RT protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds
CC to a large number of partners, usually by recognition of a
CC phosphoserine or phosphothreonine motif. Binding generally results
CC in the modulation of the activity of the binding partner.
CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 (By similarity).
CC Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1
CC (phosphorylated form); the interaction retains it in the
CC cytoplasm. Interacts with GAB2. Interacts with MDM4
CC (phosphorylated); negatively regulates MDM4 activity toward TP53.
CC Interacts with PKA-phosphorylated AANAT.
CC -!- INTERACTION:
CC O14757:CHEK1; NbExp=7; IntAct=EBI-359832, EBI-974488;
CC P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359832, EBI-7540603;
CC P56524:HDAC4; NbExp=3; IntAct=EBI-359832, EBI-308629;
CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359832, EBI-6173812;
CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-359832, EBI-5323863;
CC Q7KZI7:MARK2; NbExp=2; IntAct=EBI-359832, EBI-516560;
CC P27448:MARK3; NbExp=2; IntAct=EBI-359832, EBI-707595;
CC O15151:MDM4; NbExp=7; IntAct=EBI-359832, EBI-398437;
CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359832, EBI-6930266;
CC P04637:TP53; NbExp=5; IntAct=EBI-359832, EBI-366083;
CC P62258:YWHAE; NbExp=4; IntAct=EBI-359832, EBI-356498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle,
CC and heart.
CC -!- PTM: Phosphorylated by various PKC isozymes.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC -----------------------------------------------------------------------
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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 RefSeq; NP_036611.2; NM_012479.3.
DR UniGene; Hs.744840; -.
DR PDB; 2B05; X-ray; 2.55 A; A/B/C/D/E/F=2-246.
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=2-247.
DR PDBsum; 2B05; -.
DR PDBsum; 3UZD; -.
DR PDBsum; 4E2E; -.
DR PDBsum; 4J6S; -.
DR ProteinModelPortal; P61981; -.
DR SMR; P61981; 1-235.
DR IntAct; P61981; 96.
DR MINT; MINT-248956; -.
DR STRING; 9606.ENSP00000306330; -.
DR BindingDB; P61981; -.
DR ChEMBL; CHEMBL1293296; -.
DR PhosphoSite; P61981; -.
DR DMDM; 48428721; -.
DR REPRODUCTION-2DPAGE; IPI00220642; -.
DR PaxDb; P61981; -.
DR PeptideAtlas; P61981; -.
DR PRIDE; P61981; -.
DR DNASU; 7532; -.
DR Ensembl; ENST00000307630; ENSP00000306330; ENSG00000170027.
DR GeneID; 7532; -.
DR KEGG; hsa:7532; -.
DR UCSC; uc011kgj.1; human.
DR CTD; 7532; -.
DR GeneCards; GC07M075956; -.
DR HGNC; HGNC:12852; YWHAG.
DR HPA; CAB013274; -.
DR HPA; CAB018389; -.
DR HPA; HPA026918; -.
DR MIM; 605356; gene.
DR neXtProt; NX_P61981; -.
DR PharmGKB; PA37441; -.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P61981; -.
DR KO; K16198; -.
DR OMA; CSETQHE; -.
DR OrthoDB; EOG7HHWT3; -.
DR PhylomeDB; P61981; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; P61981; -.
DR ChiTaRS; YWHAG; human.
DR EvolutionaryTrace; P61981; -.
DR GeneWiki; YWHAG; -.
DR GenomeRNAi; 7532; -.
DR NextBio; 29467; -.
DR PRO; PR:P61981; -.
DR ArrayExpress; P61981; -.
DR Bgee; P61981; -.
DR CleanEx; HS_YWHAG; -.
DR Genevestigator; P61981; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
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:0045664; P:regulation of neuron differentiation; IMP: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; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1 247 14-3-3 protein gamma.
FT /FTId=PRO_0000367907.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 247 14-3-3 protein gamma, N-terminally
FT processed.
FT /FTId=PRO_0000058606.
FT SITE 57 57 Interaction with phosphoserine on
FT interacting protein.
FT SITE 132 132 Interaction with phosphoserine on
FT interacting protein.
FT MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein
FT gamma; alternate; partial.
FT MOD_RES 2 2 N-acetylvaline; in 14-3-3 protein gamma,
FT N-terminally processed; partial.
FT MOD_RES 2 2 N-acetylvaline; partial.
FT MOD_RES 145 145 Phosphothreonine.
FT CONFLICT 4 4 R -> P (in Ref. 1; AAD48408).
FT CONFLICT 19 19 R -> G (in Ref. 1; AAD48408).
FT CONFLICT 78 78 Missing (in Ref. 1; AAD48408).
FT CONFLICT 89 89 I -> V (in Ref. 1; AAD48408).
FT CONFLICT 104 104 L -> V (in Ref. 1; AAD48408).
FT CONFLICT 109 109 I -> Y (in Ref. 1; AAD48408).
FT CONFLICT 119 122 SKVF -> RKDL (in Ref. 1; AAD48408).
FT CONFLICT 144 145 AT -> GD (in Ref. 1; AAD48408).
FT CONFLICT 157 158 AH -> R (in Ref. 1; AAD48408).
FT CONFLICT 200 202 AFD -> EFE (in Ref. 1; AAD48408).
FT CONFLICT 214 214 D -> E (in Ref. 1; AAD48408).
FT CONFLICT 240 240 D -> DH (in Ref. 1; AAD48408).
FT HELIX 4 16
FT HELIX 20 31
FT HELIX 39 70
FT HELIX 79 106
FT HELIX 108 111
FT HELIX 117 137
FT HELIX 140 164
FT HELIX 170 185
FT HELIX 190 206
FT HELIX 207 210
FT TURN 213 215
FT HELIX 216 233
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
//
MIM
605356
*RECORD*
*FIELD* NO
605356
*FIELD* TI
*605356 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN,
GAMMA ISOFORM; YWHAG
read more;;14-3-3-GAMMA
*FIELD* TX
DESCRIPTION
Members of the 14-3-3 protein family, such as YWHAG, play an important
role in signal transduction leading to mitosis and cellular
proliferation (Morrison, 1994). For background information on 14-3-3
proteins, see 113508.
CLONING
Using PCR primers based on the rat 14-3-3-gamma (YWHAG) sequence to
screen human vascular smooth muscle cells (VSMC), Autieri and Carbone
(1999) isolated a cDNA encoding YWHAG. The deduced 246-amino acid
protein, which shares 98% sequence identity with the rat sequence, has
preserved 14-3-3 family signature motifs, a predicted annexin motif, and
several potential phosphorylation sites but not the CDK2 (116953)
phosphorylation motif. By EST database searching, Horie et al. (1999)
also obtained a cDNA encoding YWHAG, which they found to be 100%
identical to the 247-amino acid rat sequence. Northern blot analysis
revealed ubiquitous expression of a 3.8-kb YWHAG transcript that is
relatively strong in brain, skeletal muscle, and heart but weak in
peripheral blood leukocytes. By SDS-PAGE and autoradiographic analysis,
Autieri and Carbone (1999) found that YWHAG is expressed and
phosphorylated by activation with platelet-derived growth factor
(190040) and other activators of several isoforms of protein kinase C
(PKC; e.g., 176960). Inhibitors of PKC block YWHAG phosphorylation.
Western blot analysis showed that YWHAG interacts with PKC and with RAF1
(164760).
GENE FUNCTION
Autieri et al. (1995, 1996) found that YWHAG is upregulated in injured
rat carotid arteries and that YWHAG mRNA is upregulated in
cytokine-stimulated human VSMC.
MAPPING
By fluorescence in situ hybridization, Horie et al. (1999) mapped the
YWHAG gene to chromosome 7q11.23. By radiation hybrid analysis, they
mapped the gene 2.33 cR telomeric to D7S1870, at the most telomeric end
of the common deletion region of Williams-Beuren syndrome (194050).
ANIMAL MODEL
Komoike et al. (2010) found that knockdown of Ywhag1 in zebrafish
resulted in reduced brain size and increased diameter of the heart tube
with increased cardiac arrhythmia. Two unrelated human patients with
interstitial deletions at chromosome 7q11.23 (613729) including the
YWHAG gene had severe infantile seizures and hypertrophic
cardiomyopathy, which Komoike et al. (2010) postulated may have resulted
from haploinsufficiency of YWHAG.
*FIELD* RF
1. Autieri, M. V.; Carbone, C. J.: 14-3-3-Gamma interacts with and
is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated
human vascular smooth muscle cells. DNA Cell Biol. 18: 555-564,
1999.
2. Autieri, M. V.; Feuerstein, G. Z.; Yue, T.-L.; Ohlstein, E. H.;
Douglas, S. A.: Use of differential display to identify differentially
expressed mRNAs induced by rat carotid artery balloon angioplasty. Lab.
Invest. 72: 656-661, 1995.
3. Autieri, M. V.; Haines, D. S.; Romanic, A. M.; Ohlstein, E. H.
: Expression of 14-3-3-gamma in injured arteries and growth factor-
and cytokine-stimulated human vascular smooth muscle cells. Cell
Growth Diff. 7: 1453-1460, 1996.
4. Horie, M.; Suzuki, M.; Takahashi, E.; Tanigami, A.: Cloning, expression,
and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23. Genomics 60:
241-243, 1999.
5. Komoike, Y.; Fujii, K.; Nishimura, A.; Hiraki, Y.; Hayashidani,
M.; Shimojima, K.; Nishizawa, T.; Higashi, K.; Yasukawa, K.; Saitsu,
H.; Miyake, N.; Mizuguchi, T.; Matsumoto, N.; Osawa, M.; Kohno, Y.;
Higashinakagawa, T.; Yamamoto, T.: Zebrafish gene knockdowns imply
roles for human YWHAG in infantile spasms and cardiomegaly. Genesis 48:
233-243, 2010.
6. Morrison, D.: 14-3-3: modulators of signaling proteins? Science 266:
56-57, 1994.
*FIELD* CN
Cassandra L. Kniffin - updated: 3/24/2011
*FIELD* CD
Paul J. Converse: 10/23/2000
*FIELD* ED
wwang: 05/04/2011
ckniffin: 3/24/2011
alopez: 7/17/2009
terry: 1/18/2001
carol: 10/23/2000
*RECORD*
*FIELD* NO
605356
*FIELD* TI
*605356 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN,
GAMMA ISOFORM; YWHAG
read more;;14-3-3-GAMMA
*FIELD* TX
DESCRIPTION
Members of the 14-3-3 protein family, such as YWHAG, play an important
role in signal transduction leading to mitosis and cellular
proliferation (Morrison, 1994). For background information on 14-3-3
proteins, see 113508.
CLONING
Using PCR primers based on the rat 14-3-3-gamma (YWHAG) sequence to
screen human vascular smooth muscle cells (VSMC), Autieri and Carbone
(1999) isolated a cDNA encoding YWHAG. The deduced 246-amino acid
protein, which shares 98% sequence identity with the rat sequence, has
preserved 14-3-3 family signature motifs, a predicted annexin motif, and
several potential phosphorylation sites but not the CDK2 (116953)
phosphorylation motif. By EST database searching, Horie et al. (1999)
also obtained a cDNA encoding YWHAG, which they found to be 100%
identical to the 247-amino acid rat sequence. Northern blot analysis
revealed ubiquitous expression of a 3.8-kb YWHAG transcript that is
relatively strong in brain, skeletal muscle, and heart but weak in
peripheral blood leukocytes. By SDS-PAGE and autoradiographic analysis,
Autieri and Carbone (1999) found that YWHAG is expressed and
phosphorylated by activation with platelet-derived growth factor
(190040) and other activators of several isoforms of protein kinase C
(PKC; e.g., 176960). Inhibitors of PKC block YWHAG phosphorylation.
Western blot analysis showed that YWHAG interacts with PKC and with RAF1
(164760).
GENE FUNCTION
Autieri et al. (1995, 1996) found that YWHAG is upregulated in injured
rat carotid arteries and that YWHAG mRNA is upregulated in
cytokine-stimulated human VSMC.
MAPPING
By fluorescence in situ hybridization, Horie et al. (1999) mapped the
YWHAG gene to chromosome 7q11.23. By radiation hybrid analysis, they
mapped the gene 2.33 cR telomeric to D7S1870, at the most telomeric end
of the common deletion region of Williams-Beuren syndrome (194050).
ANIMAL MODEL
Komoike et al. (2010) found that knockdown of Ywhag1 in zebrafish
resulted in reduced brain size and increased diameter of the heart tube
with increased cardiac arrhythmia. Two unrelated human patients with
interstitial deletions at chromosome 7q11.23 (613729) including the
YWHAG gene had severe infantile seizures and hypertrophic
cardiomyopathy, which Komoike et al. (2010) postulated may have resulted
from haploinsufficiency of YWHAG.
*FIELD* RF
1. Autieri, M. V.; Carbone, C. J.: 14-3-3-Gamma interacts with and
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*FIELD* CN
Cassandra L. Kniffin - updated: 3/24/2011
*FIELD* CD
Paul J. Converse: 10/23/2000
*FIELD* ED
wwang: 05/04/2011
ckniffin: 3/24/2011
alopez: 7/17/2009
terry: 1/18/2001
carol: 10/23/2000