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14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) (KCIP-1)

 1433Z_HUMAN             Reviewed;         245 AA.
P63104; A8K1N0; B7Z465; P29213; P29312; Q32P43; Q5XJ08; Q6GPI2;
Q6IN74; Q6NUR9; Q6P3U9; Q86V33;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
05-DEC-2018, entry version 179.
RecName: Full=14-3-3 protein zeta/delta;
AltName: Full=Protein kinase C inhibitor protein 1;
Short=KCIP-1;
Name=YWHAZ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=1577711;
Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.;
"Cloning and expression of a human 14-3-3 protein mediating
phospholipolysis. Identification of an arachidonoyl-enzyme
intermediate during catalysis.";
J. Biol. Chem. 267:8707-8710(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=9512661; DOI=10.1016/S0167-4781(97)00171-1;
Seluja G.A., Pietromonaco S.F., Elias L.;
"Two unique 5' untranslated regions in mRNAs encoding human 14-3-3
zeta: differential expression in hemopoietic cells.";
Biochim. Biophys. Acta 1395:281-287(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hippocampus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Colon, Eye, Melanoma, PNS, Skin, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-18.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
PROTEIN SEQUENCE OF 1-9; 12-49; 57-74; 84-103; 128-158 AND 194-222,
INTERACTION WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=23572552; DOI=10.1128/mBio.00098-13;
Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
DeRisi J.L.;
"ACBD3 interaction with TBC1 domain 22 protein is differentially
affected by enteroviral and kobuviral 3A protein binding.";
MBio 4:E00098-E00098(2013).
[8]
PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND
213-222, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma, and Platelet;
Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.;
Submitted (NOV-2005) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 92-103; 140-157; 194-212 AND 223-245, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, AND FUNCTION.
PubMed=9360956; DOI=10.1074/jbc.272.46.28882;
Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y.,
Morrice N., Moelling K., Aitken A.;
"14-3-3 is phosphorylated by casein kinase I on residue 233.
Phosphorylation at this site in vivo regulates Raf/14-3-3
interaction.";
J. Biol. Chem. 272:28882-28888(1997).
[11]
INTERACTION WITH TLK2.
PubMed=10455159; DOI=10.1074/jbc.274.35.24865;
Zhang S., Xing H., Muslin A.J.;
"Nuclear localization of protein kinase U-alpha is regulated by 14-3-
3.";
J. Biol. Chem. 274:24865-24872(1999).
[12]
INTERACTION WITH AANAT.
PubMed=11427721; DOI=10.1073/pnas.141118798;
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
3-3-binding switch in melatonin synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
[13]
PHOSPHORYLATION AT SER-58, AND INTERACTION WITH AKT1.
PubMed=11956222; DOI=10.1074/jbc.M203167200;
Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.;
"Identification of 14-3-3zeta as a protein kinase B/Akt substrate.";
J. Biol. Chem. 277:21639-21642(2002).
[14]
PHOSPHORYLATION AT SER-58, AND DIMERIZATION.
PubMed=12865427; DOI=10.1074/jbc.M304689200;
Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.;
"The dimeric versus monomeric status of 14-3-3zeta is controlled by
phosphorylation of Ser58 at the dimer interface.";
J. Biol. Chem. 278:36323-36327(2003).
[15]
INTERACTION WITH AANAT, AND FUNCTION.
PubMed=14578935; DOI=10.1038/nsb1005;
Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.;
"Cellular stabilization of the melatonin rhythm enzyme induced by
nonhydrolyzable phosphonate incorporation.";
Nat. Struct. Biol. 10:1054-1057(2003).
[16]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[17]
PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, AND
MUTAGENESIS OF SER-184.
PubMed=15071501; DOI=10.1038/sj.emboj.7600194;
Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S.,
Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.;
"JNK promotes Bax translocation to mitochondria through
phosphorylation of 14-3-3 proteins.";
EMBO J. 23:1889-1899(2004).
[18]
INTERACTION WITH SSH1.
PubMed=15159416; DOI=10.1083/jcb.200401136;
Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
"A pathway of neuregulin-induced activation of cofilin-phosphatase
Slingshot and cofilin in lamellipodia.";
J. Cell Biol. 165:465-471(2004).
[19]
INTERACTION WITH MLLT7.
PubMed=16114898; DOI=10.1021/bi050618r;
Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J.,
Boura E., Obsil T.;
"14-3-3 protein interacts with nuclear localization sequence of
forkhead transcription factor FoxO4.";
Biochemistry 44:11608-11617(2005).
[20]
INTERACTION WITH SSH1.
PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N.,
Sarcevic B., Sampath R., Bamburg J.R., Bernard O.;
"Interplay between components of a novel LIM kinase-slingshot
phosphatase complex regulates cofilin.";
EMBO J. 24:473-486(2005).
[21]
PHOSPHORYLATION AT SER-58, AND MUTAGENESIS OF SER-58.
PubMed=15883165; DOI=10.1074/jbc.M409081200;
Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.;
"Sphingosine activates protein kinase A type II by a novel cAMP-
independent mechanism.";
J. Biol. Chem. 280:26011-26017(2005).
[22]
INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY,
PHOSPHORYLATION AT SER-184, AND MUTAGENESIS OF SER-184.
PubMed=15696159; DOI=10.1038/ncb1228;
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
c-Abl in the apoptotic response to DNA damage.";
Nat. Cell Biol. 7:278-285(2005).
[23]
INTERACTION WITH AANAT, AND FUNCTION.
PubMed=15644438; DOI=10.1073/pnas.0406871102;
Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.;
"Melatonin synthesis: 14-3-3-dependent activation and inhibition of
arylalkylamine N-acetyltransferase mediated by phosphoserine-205.";
Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND
YWHAE, FUNCTION, AND MUTAGENESIS OF SER-58.
PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024;
Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.;
"Protein kinase A phosphorylates and regulates dimerization of 14-3-3
epsilon.";
FEBS Lett. 580:305-310(2006).
[26]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[27]
INTERACTION WITH NOXA1, AND MUTAGENESIS OF LYS-49.
PubMed=17913709; DOI=10.1074/jbc.M704754200;
Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
"Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1
and 14-3-3 binding.";
J. Biol. Chem. 282:34787-34800(2007).
[28]
INTERACTION WITH ARHGEF2.
PubMed=14970201; DOI=10.1074/jbc.M400084200;
Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P.,
Bokoch G.M.;
"p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to
GEF-H1, a microtubule-localized Rho exchange factor.";
J. Biol. Chem. 279:18392-18400(2004).
[29]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[32]
INTERACTION WITH SLITRK1.
PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
Kajiwara Y., Buxbaum J.D., Grice D.E.;
"SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a
phosphorylation-dependent manner.";
Biol. Psychiatry 66:918-925(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-68, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND THR-232, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[42]
INTERACTION WITH DAPK2.
PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
"Suppression of death-associated protein kinase 2 by interaction with
14-3-3 proteins.";
Biochem. Biophys. Res. Commun. 464:70-75(2015).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[44]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=10488331; DOI=10.1016/S1097-2765(00)80363-9;
Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C.,
Smerdon S.J., Gamblin S.J., Yaffe M.B.;
"Structural analysis of 14-3-3 phosphopeptide complexes identifies a
dual role for the nuclear export signal of 14-3-3 in ligand binding.";
Mol. Cell 4:153-166(1999).
[45]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
PubMed=11336675; DOI=10.1016/S0092-8674(01)00316-6;
Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.;
"Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase
complex. a role for scaffolding in enzyme regulation.";
Cell 105:257-267(2001).
[46]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3
PHOSPHOPEPTIDE.
PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032;
Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B.,
Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W.,
Clayton A.L., Endicott J.A., Mahadevan L.C.;
"Molecular basis for the recognition of phosphorylated and
phosphoacetylated histone h3 by 14-3-3.";
Mol. Cell 20:199-211(2005).
[47]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-230 IN COMPLEX WITH
PSEUDOMONAS AERUGINOSA EXOS.
PubMed=17235285; DOI=10.1038/sj.emboj.7601530;
Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H.,
Palmer R.H., Francis M.S., Hauser A.R., Wittinghofer A., Hallberg B.;
"Phosphorylation-independent interaction between 14-3-3 and exoenzyme
S: from structure to pathogenesis.";
EMBO J. 26:902-913(2007).
-!- FUNCTION: Adapter protein implicated in the regulation of a large
spectrum of both general and specialized signaling pathways. Binds
to a large number of partners, usually by recognition of a
phosphoserine or phosphothreonine motif. Binding generally results
in the modulation of the activity of the binding partner.
{ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15071501,
ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:16376338,
ECO:0000269|PubMed:9360956}.
-!- SUBUNIT: Interacts with CDK16 and BSPRY (By similarity). Interacts
with WEE1 (C-terminal). Interacts with SAMSN1 (By similarity).
Interacts with MLF1 (phosphorylated form); the interaction retains
it in the cytoplasm (By similarity). Interacts with Thr-
phosphorylated ITGB2 (By similarity). Interacts with BCL2L11 (By
similarity). Homodimer. Heterodimerizes with YWHAE. Homo- and
hetero-dimerization is inhibited by phosphorylation on Ser-58.
Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with
Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts
with BAX; the interaction occurs in the cytoplasm. Under stress
conditions, MAPK8-mediated phosphorylation releases BAX to
mitochondria. Interacts with phosphorylated RAF1; the interaction
is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts
with TP53; the interaction enhances p53 transcriptional activity.
The Ser-58 phosphorylated form inhibits this interaction and p53
transcriptional activity. Interacts with ABL1 (phosphorylated
form); the interaction retains ABL1 in the cytoplasm. Interacts
with PKA-phosphorylated AANAT; the interaction modulates AANAT
enzymatic activity by increasing affinity for arylalkylamines and
acetyl-CoA and protecting the enzyme from dephosphorylation and
proteasomal degradation. It may also prevent thiol-dependent
inactivation. Interacts with AKT1; the interaction phosphorylates
YWHAZ and modulates dimerization. Interacts with GAB2 and TLK2.
Interacts with the 'Thr-369' phosphorylated form of DAPK2
(PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B
(PubMed:23572552). Interacts with ZFP36L1 (via phosphorylated
form); this interaction occurs in a p38 MAPK- and AKT-signaling
pathways (By similarity). Interacts with SLITRK1
(PubMed:19640509). {ECO:0000250|UniProtKB:P63101,
ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:11336675,
ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:11956222,
ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:14970201,
ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15159416,
ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:15660133,
ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:16114898,
ECO:0000269|PubMed:16246723, ECO:0000269|PubMed:16376338,
ECO:0000269|PubMed:17235285, ECO:0000269|PubMed:17913709,
ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19640509,
ECO:0000269|PubMed:23572552, ECO:0000269|PubMed:26047703,
ECO:0000269|PubMed:9360956}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-347088, EBI-347088;
Q29495:AANAT (xeno); NbExp=3; IntAct=EBI-347088, EBI-446413;
P00519:ABL1; NbExp=3; IntAct=EBI-347088, EBI-375543;
P60709:ACTB; NbExp=3; IntAct=EBI-347088, EBI-353944;
Q9P0K1:ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567236;
Q9P0K1-3:ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567267;
P10398:ARAF; NbExp=5; IntAct=EBI-347088, EBI-365961;
Q92974:ARHGEF2; NbExp=2; IntAct=EBI-347088, EBI-302405;
P25705:ATP5F1A; NbExp=3; IntAct=EBI-347088, EBI-351437;
P06576:ATP5F1B; NbExp=2; IntAct=EBI-347088, EBI-356231;
Q92934:BAD; NbExp=5; IntAct=EBI-347088, EBI-700771;
Q61337:Bad (xeno); NbExp=3; IntAct=EBI-347088, EBI-400328;
P15056:BRAF; NbExp=4; IntAct=EBI-347088, EBI-365980;
P62158:CALM3; NbExp=2; IntAct=EBI-347088, EBI-397435;
O00257-3:CBX4; NbExp=2; IntAct=EBI-347088, EBI-4392727;
P30304:CDC25A; NbExp=2; IntAct=EBI-347088, EBI-747671;
P30305:CDC25B; NbExp=5; IntAct=EBI-347088, EBI-1051746;
Q00537:CDK17; NbExp=2; IntAct=EBI-347088, EBI-624648;
Q07002:CDK18; NbExp=2; IntAct=EBI-347088, EBI-746238;
P23528:CFL1; NbExp=3; IntAct=EBI-347088, EBI-352733;
P31327:CPS1; NbExp=2; IntAct=EBI-347088, EBI-536811;
P67828:CSNK1A1 (xeno); NbExp=4; IntAct=EBI-347088, EBI-7540603;
P68104:EEF1A1; NbExp=2; IntAct=EBI-347088, EBI-352162;
P00533:EGFR; NbExp=5; IntAct=EBI-347088, EBI-297353;
P06733:ENO1; NbExp=2; IntAct=EBI-347088, EBI-353877;
O43524:FOXO3; NbExp=2; IntAct=EBI-347088, EBI-1644164;
Q16658:FSCN1; NbExp=3; IntAct=EBI-347088, EBI-351076;
P30793:GCH1; NbExp=4; IntAct=EBI-347088, EBI-958183;
P49841:GSK3B; NbExp=4; IntAct=EBI-347088, EBI-373586;
P54256-2:Hap1 (xeno); NbExp=4; IntAct=EBI-347088, EBI-994554;
P56524:HDAC4; NbExp=5; IntAct=EBI-347088, EBI-308629;
Q9UQL6:HDAC5; NbExp=2; IntAct=EBI-347088, EBI-715576;
Q8WUI4:HDAC7; NbExp=3; IntAct=EBI-347088, EBI-1048378;
P0C0S8:HIST1H2AM; NbExp=2; IntAct=EBI-347088, EBI-1390628;
P68431:HIST1H3D; NbExp=3; IntAct=EBI-347088, EBI-79722;
P62805:HIST2H4B; NbExp=3; IntAct=EBI-347088, EBI-302023;
P07910:HNRNPC; NbExp=2; IntAct=EBI-347088, EBI-357966;
P04792:HSPB1; NbExp=4; IntAct=EBI-347088, EBI-352682;
Q9Y4H2:IRS2; NbExp=2; IntAct=EBI-347088, EBI-1049582;
Q02241:KIF23; NbExp=5; IntAct=EBI-347088, EBI-306852;
P02545:LMNA; NbExp=2; IntAct=EBI-347088, EBI-351935;
Q5S007:LRRK2; NbExp=9; IntAct=EBI-347088, EBI-5323863;
Q9NYL2:MAP3K20; NbExp=4; IntAct=EBI-347088, EBI-602273;
Q99683:MAP3K5; NbExp=4; IntAct=EBI-347088, EBI-476263;
P10636:MAPT; NbExp=8; IntAct=EBI-347088, EBI-366182;
P10636-3:MAPT; NbExp=9; IntAct=EBI-347088, EBI-7145070;
P29172:MAPT (xeno); NbExp=2; IntAct=EBI-347088, EBI-7291149;
Q7KZI7:MARK2; NbExp=6; IntAct=EBI-347088, EBI-516560;
P27448:MARK3; NbExp=10; IntAct=EBI-347088, EBI-707595;
O75592:MYCBP2; NbExp=2; IntAct=EBI-347088, EBI-1043774;
P19338:NCL; NbExp=2; IntAct=EBI-347088, EBI-346967;
P06748:NPM1; NbExp=2; IntAct=EBI-347088, EBI-78579;
Q8TEW0:PARD3; NbExp=4; IntAct=EBI-347088, EBI-81968;
Q02156:PRKCE; NbExp=5; IntAct=EBI-347088, EBI-706254;
P16471:PRLR; NbExp=3; IntAct=EBI-347088, EBI-476182;
O14744:PRMT5; NbExp=2; IntAct=EBI-347088, EBI-351098;
P26045:PTPN3; NbExp=3; IntAct=EBI-347088, EBI-1047946;
P04049:RAF1; NbExp=13; IntAct=EBI-347088, EBI-365996;
Q8NFH8-2:REPS2; NbExp=2; IntAct=EBI-347088, EBI-8029141;
P61587:RND3; NbExp=11; IntAct=EBI-347088, EBI-1111534;
P61588:Rnd3 (xeno); NbExp=3; IntAct=EBI-347088, EBI-6930266;
P23396:RPS3; NbExp=2; IntAct=EBI-347088, EBI-351193;
P31947:SFN; NbExp=2; IntAct=EBI-347088, EBI-476295;
P57059:SIK1; NbExp=4; IntAct=EBI-347088, EBI-1181640;
Q9Y2K2:SIK3; NbExp=5; IntAct=EBI-347088, EBI-1181460;
O94875:SORBS2; NbExp=2; IntAct=EBI-347088, EBI-311323;
Q15831:STK11; NbExp=6; IntAct=EBI-347088, EBI-306838;
O00506:STK25; NbExp=2; IntAct=EBI-347088, EBI-618295;
P36897:TGFBR1; NbExp=4; IntAct=EBI-347088, EBI-1027557;
P04637:TP53; NbExp=2; IntAct=EBI-347088, EBI-366083;
Q13625:TP53BP2; NbExp=2; IntAct=EBI-347088, EBI-77642;
P49815:TSC2; NbExp=7; IntAct=EBI-347088, EBI-396587;
P55072:VCP; NbExp=2; IntAct=EBI-347088, EBI-355164;
P08670:VIM; NbExp=2; IntAct=EBI-347088, EBI-353844;
P30291:WEE1; NbExp=3; IntAct=EBI-347088, EBI-914695;
O14980:XPO1; NbExp=2; IntAct=EBI-347088, EBI-355867;
P46937:YAP1; NbExp=8; IntAct=EBI-347088, EBI-1044059;
P62258:YWHAE; NbExp=6; IntAct=EBI-347088, EBI-356498;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=Located to stage I
to stage IV melanosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P63104-1; Sequence=Displayed;
Name=2;
IsoId=P63104-2; Sequence=VSP_047505;
Note=No experimental confirmation available.;
-!- PTM: The delta, brain-specific form differs from the zeta form in
being phosphorylated (By similarity). Phosphorylation on Ser-184
by MAPK8; promotes dissociation of BAX and translocation of BAX to
mitochondria. Phosphorylation on Thr-232; inhibits binding of
RAF1. Phosphorylated on Ser-58 by PKA and protein kinase C delta
type catalytic subunit in a sphingosine-dependent fashion.
Phosphorylation on Ser-58 by PKA; disrupts homodimerization and
heterodimerization with YHAE and TP53. {ECO:0000250,
ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427,
ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159,
ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338,
ECO:0000269|PubMed:9360956}.
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
-!- CAUTION: Was originally thought to have phospholipase A2 activity.
{ECO:0000305|PubMed:1577711}.
-!- SEQUENCE CAUTION:
Sequence=AAH51814.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH73141.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M86400; AAA36446.1; -; mRNA.
EMBL; U28964; AAC52052.1; -; mRNA.
EMBL; AK289945; BAF82634.1; -; mRNA.
EMBL; AK296902; BAH12451.1; -; mRNA.
EMBL; CH471060; EAW91823.1; -; Genomic_DNA.
EMBL; BC003623; AAH03623.3; -; mRNA.
EMBL; BC051814; AAH51814.1; ALT_INIT; mRNA.
EMBL; BC063824; AAH63824.2; -; mRNA.
EMBL; BC068456; AAH68456.2; -; mRNA.
EMBL; BC072426; AAH72426.2; -; mRNA.
EMBL; BC073141; AAH73141.1; ALT_INIT; mRNA.
EMBL; BC083508; AAH83508.2; -; mRNA.
EMBL; BC099904; AAH99904.1; -; mRNA.
EMBL; BC101483; AAI01484.1; -; mRNA.
EMBL; BC108281; AAI08282.1; -; mRNA.
EMBL; BC111951; AAI11952.1; -; mRNA.
CCDS; CCDS6290.1; -. [P63104-1]
PIR; A38246; PSHUAM.
RefSeq; NP_001129171.1; NM_001135699.1. [P63104-1]
RefSeq; NP_001129172.1; NM_001135700.1. [P63104-1]
RefSeq; NP_001129173.1; NM_001135701.1. [P63104-1]
RefSeq; NP_001129174.1; NM_001135702.1. [P63104-1]
RefSeq; NP_003397.1; NM_003406.3. [P63104-1]
RefSeq; NP_663723.1; NM_145690.2. [P63104-1]
RefSeq; XP_005251118.1; XM_005251061.3. [P63104-1]
RefSeq; XP_005251120.1; XM_005251063.3. [P63104-1]
RefSeq; XP_016869299.1; XM_017013810.1. [P63104-1]
RefSeq; XP_016869300.1; XM_017013811.1. [P63104-1]
UniGene; Hs.492407; -.
PDB; 1IB1; X-ray; 2.70 A; A/B/C/D=1-245.
PDB; 1QJA; X-ray; 2.00 A; A/B=1-245.
PDB; 1QJB; X-ray; 2.00 A; A/B=1-245.
PDB; 2C1J; X-ray; 2.60 A; A/B=1-245.
PDB; 2C1N; X-ray; 2.00 A; A/B=1-245.
PDB; 2O02; X-ray; 1.50 A; A/B=1-230.
PDB; 2WH0; X-ray; 2.25 A; A/B/C/D=1-245.
PDB; 3CU8; X-ray; 2.40 A; A/B=1-245.
PDB; 3NKX; X-ray; 2.40 A; A/B=1-245.
PDB; 3RDH; X-ray; 2.39 A; A/B/C/D=1-245.
PDB; 4BG6; X-ray; 2.30 A; A/B=1-245.
PDB; 4FJ3; X-ray; 1.95 A; A/B=1-230.
PDB; 4HKC; X-ray; 2.20 A; A=1-245.
PDB; 4IHL; X-ray; 2.20 A; A/B=1-230.
PDB; 4N7G; X-ray; 2.25 A; A=1-230.
PDB; 4N7Y; X-ray; 2.16 A; A/B=1-230.
PDB; 4N84; X-ray; 2.50 A; A/B=1-230.
PDB; 4WRQ; X-ray; 2.41 A; A/B=1-245.
PDB; 4ZDR; X-ray; 2.90 A; A/B=1-230.
PDB; 5D2D; X-ray; 2.10 A; A/B=1-230.
PDB; 5D3F; X-ray; 2.74 A; A/B=1-230.
PDB; 5EWZ; X-ray; 2.34 A; A/B=1-230.
PDB; 5EXA; X-ray; 1.95 A; A/B=1-230.
PDB; 5J31; X-ray; 2.40 A; A/B=1-230.
PDB; 5JM4; X-ray; 2.34 A; A/B=1-229.
PDB; 5M35; X-ray; 2.38 A; A/B=2-230.
PDB; 5M36; X-ray; 2.45 A; A/B=2-230.
PDB; 5M37; X-ray; 2.35 A; A/B=1-230.
PDB; 5NAS; X-ray; 2.08 A; A/B=1-230.
PDB; 5ULO; X-ray; 2.14 A; A/B=1-245.
PDB; 5WXN; X-ray; 2.93 A; A/B=1-245.
PDB; 5XY9; X-ray; 2.30 A; A/B=1-245.
PDB; 6EJL; X-ray; 2.38 A; A/B=1-230.
PDB; 6EWW; X-ray; 2.68 A; A/B/C/D=1-230.
PDB; 6F08; X-ray; 1.90 A; A/B/I/J=1-230.
PDB; 6F09; X-ray; 1.59 A; P/Q/R/S=1-230.
PDB; 6FN9; X-ray; 2.27 A; A/B=1-230.
PDB; 6FNA; X-ray; 2.12 A; A/B=1-230.
PDB; 6FNB; X-ray; 2.30 A; A/B=1-230.
PDB; 6FNC; X-ray; 2.12 A; A/B=1-230.
PDBsum; 1IB1; -.
PDBsum; 1QJA; -.
PDBsum; 1QJB; -.
PDBsum; 2C1J; -.
PDBsum; 2C1N; -.
PDBsum; 2O02; -.
PDBsum; 2WH0; -.
PDBsum; 3CU8; -.
PDBsum; 3NKX; -.
PDBsum; 3RDH; -.
PDBsum; 4BG6; -.
PDBsum; 4FJ3; -.
PDBsum; 4HKC; -.
PDBsum; 4IHL; -.
PDBsum; 4N7G; -.
PDBsum; 4N7Y; -.
PDBsum; 4N84; -.
PDBsum; 4WRQ; -.
PDBsum; 4ZDR; -.
PDBsum; 5D2D; -.
PDBsum; 5D3F; -.
PDBsum; 5EWZ; -.
PDBsum; 5EXA; -.
PDBsum; 5J31; -.
PDBsum; 5JM4; -.
PDBsum; 5M35; -.
PDBsum; 5M36; -.
PDBsum; 5M37; -.
PDBsum; 5NAS; -.
PDBsum; 5ULO; -.
PDBsum; 5WXN; -.
PDBsum; 5XY9; -.
PDBsum; 6EJL; -.
PDBsum; 6EWW; -.
PDBsum; 6F08; -.
PDBsum; 6F09; -.
PDBsum; 6FN9; -.
PDBsum; 6FNA; -.
PDBsum; 6FNB; -.
PDBsum; 6FNC; -.
ProteinModelPortal; P63104; -.
SMR; P63104; -.
BioGrid; 113366; 405.
ComplexPortal; CPX-1147; FOXO3-YWHAZ complex.
CORUM; P63104; -.
DIP; DIP-563N; -.
ELM; P63104; -.
IntAct; P63104; 585.
MINT; P63104; -.
STRING; 9606.ENSP00000309503; -.
MoonDB; P63104; Predicted.
TCDB; 8.A.98.1.2; the 14-3-3 protein (14-3-3) family.
iPTMnet; P63104; -.
PhosphoSitePlus; P63104; -.
SwissPalm; P63104; -.
BioMuta; YWHAZ; -.
DMDM; 52000887; -.
DOSAC-COBS-2DPAGE; P63104; -.
OGP; P63104; -.
UCD-2DPAGE; P63104; -.
EPD; P63104; -.
MaxQB; P63104; -.
PaxDb; P63104; -.
PeptideAtlas; P63104; -.
PRIDE; P63104; -.
TopDownProteomics; P63104-1; -. [P63104-1]
DNASU; 7534; -.
Ensembl; ENST00000353245; ENSP00000309503; ENSG00000164924. [P63104-1]
Ensembl; ENST00000395951; ENSP00000379281; ENSG00000164924. [P63104-1]
Ensembl; ENST00000395953; ENSP00000379283; ENSG00000164924. [P63104-1]
Ensembl; ENST00000395956; ENSP00000379286; ENSG00000164924. [P63104-1]
Ensembl; ENST00000395957; ENSP00000379287; ENSG00000164924. [P63104-1]
Ensembl; ENST00000395958; ENSP00000379288; ENSG00000164924. [P63104-1]
Ensembl; ENST00000419477; ENSP00000395114; ENSG00000164924. [P63104-1]
Ensembl; ENST00000457309; ENSP00000398599; ENSG00000164924. [P63104-1]
Ensembl; ENST00000522542; ENSP00000430072; ENSG00000164924. [P63104-2]
GeneID; 7534; -.
KEGG; hsa:7534; -.
UCSC; uc003yjv.3; human. [P63104-1]
CTD; 7534; -.
DisGeNET; 7534; -.
EuPathDB; HostDB:ENSG00000164924.17; -.
GeneCards; YWHAZ; -.
HGNC; HGNC:12855; YWHAZ.
HPA; CAB005065; -.
MIM; 601288; gene.
neXtProt; NX_P63104; -.
OpenTargets; ENSG00000164924; -.
PharmGKB; PA37444; -.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00940000153153; -.
HOGENOM; HOG000240379; -.
HOVERGEN; HBG050423; -.
InParanoid; P63104; -.
KO; K16197; -.
PhylomeDB; P63104; -.
TreeFam; TF102003; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-392517; Rap1 signalling.
Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
SignaLink; P63104; -.
SIGNOR; P63104; -.
ChiTaRS; YWHAZ; human.
EvolutionaryTrace; P63104; -.
GeneWiki; YWHAZ; -.
GenomeRNAi; 7534; -.
PRO; PR:P63104; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164924; Expressed in 234 organ(s), highest expression level in frontal cortex.
ExpressionAtlas; P63104; baseline and differential.
Genevisible; P63104; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IPI:SynGO-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0090128; P:regulation of synapse maturation; IDA:SynGO.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Phosphoprotein;
Reference proteome.
CHAIN 1 245 14-3-3 protein zeta/delta.
/FTId=PRO_0000058627.
SITE 56 56 Interaction with phosphoserine on
interacting protein. {ECO:0000250}.
SITE 127 127 Interaction with phosphoserine on
interacting protein. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 58 58 Phosphoserine; by PKA and PKB/AKT1.
{ECO:0000269|PubMed:11956222,
ECO:0000269|PubMed:12865427,
ECO:0000269|PubMed:15883165,
ECO:0000269|PubMed:16376338}.
MOD_RES 68 68 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 184 184 Phosphoserine; by MAPK8.
{ECO:0000269|PubMed:15071501,
ECO:0000269|PubMed:15696159}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000250|UniProtKB:P63102}.
MOD_RES 232 232 Phosphothreonine; by CK1.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:9360956}.
VAR_SEQ 1 98 MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEER
NLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREY
REKIETELRDICNDVL -> MSQPCRKLWRHNYETSSCIEF
LK (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047505.
MUTAGEN 49 49 K->E: Loss of interaction with NOXA1.
{ECO:0000269|PubMed:17913709}.
MUTAGEN 58 58 S->A: Loss of sphingosine-activated PKA
phosphorylation. Promotes
homodimerization and heterodimerization
with YWHAE. Enhanced transcriptional
activity of P53.
{ECO:0000269|PubMed:15883165,
ECO:0000269|PubMed:16376338}.
MUTAGEN 58 58 S->E: Loss of homodimerization. Reduced
dimerization with YWHAE. Significantly
reduced interaction with P53. No
enhancement of P53 transcriptional
activity. {ECO:0000269|PubMed:15883165,
ECO:0000269|PubMed:16376338}.
MUTAGEN 184 184 S->A: On DNA damage, loss of MAPK8-
mediated phosphorylation. Loss of binding
ABL1. Attenuates ABL1-mediated apoptosis.
No loss of interaction with BAX under
stress conditions. Inhibits translocation
of BAX to mitochondria.
{ECO:0000269|PubMed:15071501,
ECO:0000269|PubMed:15696159}.
CONFLICT 22 22 M -> V (in Ref. 5; AAH68456).
{ECO:0000305}.
CONFLICT 136 136 D -> G (in Ref. 3; BAH12451).
{ECO:0000305}.
HELIX 3 15 {ECO:0000244|PDB:2O02}.
HELIX 19 31 {ECO:0000244|PDB:2O02}.
HELIX 38 67 {ECO:0000244|PDB:2O02}.
TURN 69 71 {ECO:0000244|PDB:2O02}.
HELIX 76 103 {ECO:0000244|PDB:2O02}.
HELIX 105 108 {ECO:0000244|PDB:2O02}.
HELIX 112 131 {ECO:0000244|PDB:2O02}.
HELIX 135 159 {ECO:0000244|PDB:2O02}.
HELIX 165 180 {ECO:0000244|PDB:2O02}.
HELIX 185 200 {ECO:0000244|PDB:2O02}.
HELIX 201 205 {ECO:0000244|PDB:2O02}.
TURN 208 210 {ECO:0000244|PDB:2O02}.
HELIX 211 228 {ECO:0000244|PDB:2O02}.
SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64;
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
EGGEN


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