1433Z_HUMAN
ID 1433Z_HUMAN Reviewed; 245 AA.
AC P63104; A8K1N0; B7Z465; P29213; P29312; Q32P43; Q5XJ08; Q6GPI2; Q6IN74;
AC Q6NUR9; Q6P3U9; Q86V33;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=14-3-3 protein zeta/delta;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
GN Name=YWHAZ;
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] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1577711; DOI=10.1016/s0021-9258(19)50334-9;
RA Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.;
RT "Cloning and expression of a human 14-3-3 protein mediating
RT phospholipolysis. Identification of an arachidonoyl-enzyme intermediate
RT during catalysis.";
RL J. Biol. Chem. 267:8707-8710(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9512661; DOI=10.1016/s0167-4781(97)00171-1;
RA Seluja G.A., Pietromonaco S.F., Elias L.;
RT "Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 zeta:
RT differential expression in hemopoietic cells.";
RL Biochim. Biophys. Acta 1395:281-287(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Colon, Eye, Melanoma, PNS, Skin, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-18.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 1-9; 12-49; 57-74; 84-103; 128-158 AND 194-222,
RP INTERACTION WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [8]
RP PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND 213-222,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Platelet;
RA Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 92-103; 140-157; 194-212 AND 223-245, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, AND FUNCTION.
RX PubMed=9360956; DOI=10.1074/jbc.272.46.28882;
RA Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N.,
RA Moelling K., Aitken A.;
RT "14-3-3 is phosphorylated by casein kinase I on residue 233.
RT Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.";
RL J. Biol. Chem. 272:28882-28888(1997).
RN [11]
RP INTERACTION WITH TLK2.
RX PubMed=10455159; DOI=10.1074/jbc.274.35.24865;
RA Zhang S., Xing H., Muslin A.J.;
RT "Nuclear localization of protein kinase U-alpha is regulated by 14-3-3.";
RL J. Biol. Chem. 274:24865-24872(1999).
RN [12]
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 [13]
RP PHOSPHORYLATION AT SER-58, AND INTERACTION WITH AKT1.
RX PubMed=11956222; DOI=10.1074/jbc.m203167200;
RA Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.;
RT "Identification of 14-3-3zeta as a protein kinase B/Akt substrate.";
RL J. Biol. Chem. 277:21639-21642(2002).
RN [14]
RP PHOSPHORYLATION AT SER-58, AND DIMERIZATION.
RX PubMed=12865427; DOI=10.1074/jbc.m304689200;
RA Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.;
RT "The dimeric versus monomeric status of 14-3-3zeta is controlled by
RT phosphorylation of Ser58 at the dimer interface.";
RL J. Biol. Chem. 278:36323-36327(2003).
RN [15]
RP INTERACTION WITH AANAT, AND FUNCTION.
RX PubMed=14578935; DOI=10.1038/nsb1005;
RA Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.;
RT "Cellular stabilization of the melatonin rhythm enzyme induced by
RT nonhydrolyzable phosphonate incorporation.";
RL Nat. Struct. Biol. 10:1054-1057(2003).
RN [16]
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 [17]
RP PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, AND MUTAGENESIS
RP OF SER-184.
RX PubMed=15071501; DOI=10.1038/sj.emboj.7600194;
RA Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., Tsujimoto Y.,
RA Yoshioka K., Masuyama N., Gotoh Y.;
RT "JNK promotes Bax translocation to mitochondria through phosphorylation of
RT 14-3-3 proteins.";
RL EMBO J. 23:1889-1899(2004).
RN [18]
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 [19]
RP INTERACTION WITH MLLT7.
RX PubMed=16114898; DOI=10.1021/bi050618r;
RA Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J.,
RA Boura E., Obsil T.;
RT "14-3-3 protein interacts with nuclear localization sequence of forkhead
RT transcription factor FoxO4.";
RL Biochemistry 44:11608-11617(2005).
RN [20]
RP INTERACTION WITH SSH1.
RX PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B.,
RA Sampath R., Bamburg J.R., Bernard O.;
RT "Interplay between components of a novel LIM kinase-slingshot phosphatase
RT complex regulates cofilin.";
RL EMBO J. 24:473-486(2005).
RN [21]
RP PHOSPHORYLATION AT SER-58, AND MUTAGENESIS OF SER-58.
RX PubMed=15883165; DOI=10.1074/jbc.m409081200;
RA Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.;
RT "Sphingosine activates protein kinase A type II by a novel cAMP-independent
RT mechanism.";
RL J. Biol. Chem. 280:26011-26017(2005).
RN [22]
RP INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION
RP AT SER-184, AND MUTAGENESIS OF SER-184.
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 [23]
RP INTERACTION WITH AANAT, AND FUNCTION.
RX PubMed=15644438; DOI=10.1073/pnas.0406871102;
RA Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.;
RT "Melatonin synthesis: 14-3-3-dependent activation and inhibition of
RT arylalkylamine N-acetyltransferase mediated by phosphoserine-205.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [25]
RP PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND YWHAE,
RP FUNCTION, AND MUTAGENESIS OF SER-58.
RX PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024;
RA Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.;
RT "Protein kinase A phosphorylates and regulates dimerization of 14-3-3
RT epsilon.";
RL FEBS Lett. 580:305-310(2006).
RN [26]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [27]
RP FUNCTION, INTERACTION WITH AK5; LDB1; MADD; MARK3; PDE1A AND SMARCB1, AND
RP MUTAGENESIS OF 56-ARG--ARG-60.
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 [28]
RP INTERACTION WITH NOXA1, AND MUTAGENESIS OF LYS-49.
RX PubMed=17913709; DOI=10.1074/jbc.m704754200;
RA Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
RT "Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 and
RT 14-3-3 binding.";
RL J. Biol. Chem. 282:34787-34800(2007).
RN [29]
RP INTERACTION WITH ARHGEF2.
RX PubMed=14970201; DOI=10.1074/jbc.m400084200;
RA Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P.,
RA Bokoch G.M.;
RT "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-
RT H1, a microtubule-localized Rho exchange factor.";
RL J. Biol. Chem. 279:18392-18400(2004).
RN [30]
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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [33]
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP 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 [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-68, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND THR-232, AND
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 [37]
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 [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [41]
RP IDENTIFICATION BY 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 [42]
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 [43]
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 [44]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [45]
RP INTERACTION WITH MEFV.
RX PubMed=27030597; DOI=10.1126/scitranslmed.aaf1471;
RA Masters S.L., Lagou V., Jeru I., Baker P.J., Van Eyck L., Parry D.A.,
RA Lawless D., De Nardo D., Garcia-Perez J.E., Dagley L.F., Holley C.L.,
RA Dooley J., Moghaddas F., Pasciuto E., Jeandel P.Y., Sciot R., Lyras D.,
RA Webb A.I., Nicholson S.E., De Somer L., van Nieuwenhove E., Ruuth-Praz J.,
RA Copin B., Cochet E., Medlej-Hashim M., Megarbane A., Schroder K., Savic S.,
RA Goris A., Amselem S., Wouters C., Liston A.;
RT "Familial autoinflammation with neutrophilic dermatosis reveals a
RT regulatory mechanism of pyrin activation.";
RL Sci. Transl. Med. 8:332ra45-332ra45(2016).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10488331; DOI=10.1016/s1097-2765(00)80363-9;
RA Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., Smerdon S.J.,
RA Gamblin S.J., Yaffe M.B.;
RT "Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual
RT role for the nuclear export signal of 14-3-3 in ligand binding.";
RL Mol. Cell 4:153-166(1999).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
RX PubMed=11336675; DOI=10.1016/s0092-8674(01)00316-6;
RA Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.;
RT "Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex.
RT a role for scaffolding in enzyme regulation.";
RL Cell 105:257-267(2001).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3
RP PHOSPHOPEPTIDE.
RX PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032;
RA Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B.,
RA Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W.,
RA Clayton A.L., Endicott J.A., Mahadevan L.C.;
RT "Molecular basis for the recognition of phosphorylated and
RT phosphoacetylated histone h3 by 14-3-3.";
RL Mol. Cell 20:199-211(2005).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-230 IN COMPLEX WITH PSEUDOMONAS
RP AERUGINOSA EXOS.
RX PubMed=17235285; DOI=10.1038/sj.emboj.7601530;
RA Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H., Palmer R.H.,
RA Francis M.S., Hauser A.R., Wittinghofer A., Hallberg B.;
RT "Phosphorylation-independent interaction between 14-3-3 and exoenzyme S:
RT from structure to pathogenesis.";
RL EMBO J. 26:902-913(2007).
RN [50]
RP VARIANTS 14-GLU--ASN-245 DEL; ARG-53; LEU-145 AND TRP-230, CHARACTERIZATION
RP OF VARIANT TRP-230, FUNCTION, INTERACTION WITH BRAF AND RAF1,
RP PHOSPHORYLATION AT THR-232 BY CK1, AND MUTAGENESIS OF THR-232.
RX PubMed=31024343; DOI=10.3389/fphys.2019.00388;
RA Popov I.K., Hiatt S.M., Whalen S., Keren B., Ruivenkamp C.,
RA van Haeringen A., Chen M.J., Cooper G.M., Korf B.R., Chang C.;
RT "A YWHAZ variant associated with cardiofaciocutaneous syndrome activates
RT the RAF-ERK pathway.";
RL Front. Physiol. 10:388-388(2019).
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. Induces ARHGEF7 activity on RAC1
CC as well as lamellipodia and membrane ruffle formation
CC (PubMed:16959763). In neurons, regulates spine maturation through the
CC modulation of ARHGEF7 activity (By similarity).
CC {ECO:0000250|UniProtKB:O55043, ECO:0000269|PubMed:14578935,
CC ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15644438,
CC ECO:0000269|PubMed:16376338, ECO:0000269|PubMed:16959763,
CC ECO:0000269|PubMed:31024343, ECO:0000269|PubMed:9360956}.
CC -!- SUBUNIT: Interacts with CDK16 and BSPRY (By similarity). Interacts with
CC WEE1 (C-terminal). Interacts with SAMSN1 (By similarity). Interacts
CC with MLF1 (phosphorylated form); the interaction retains it in the
CC cytoplasm (By similarity). Interacts with Thr-phosphorylated ITGB2 (By
CC similarity). Interacts with BCL2L11 (By similarity). Homodimer.
CC Heterodimerizes with YWHAE. Homo- and heterodimerization is inhibited
CC by phosphorylation on Ser-58. Interacts with FOXO4, NOXA1, SSH1 and
CC ARHGEF2. Interacts with Pseudomonas aeruginosa exoS (unphosphorylated
CC form). Interacts with BAX; the interaction occurs in the cytoplasm.
CC Under stress conditions, MAPK8-mediated phosphorylation releases BAX to
CC mitochondria. Interacts with phosphorylated RAF1; the interaction is
CC inhibited when YWHAZ is phosphorylated on Thr-232 (PubMed:31024343).
CC Interacts with BRAF (PubMed:31024343). Interacts with TP53; the
CC interaction enhances p53 transcriptional activity. The Ser-58
CC phosphorylated form inhibits this interaction and p53 transcriptional
CC activity. Interacts with ABL1 (phosphorylated form); the interaction
CC retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT;
CC the interaction modulates AANAT enzymatic activity by increasing
CC affinity for arylalkylamines and acetyl-CoA and protecting the enzyme
CC from dephosphorylation and proteasomal degradation. It may also prevent
CC thiol-dependent inactivation. Interacts with AKT1; the interaction
CC phosphorylates YWHAZ and modulates dimerization. Interacts with GAB2
CC and TLK2. Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B
CC (PubMed:23572552). Interacts with ZFP36L1 (via phosphorylated form);
CC this interaction occurs in a p38 MAPK- and AKT-signaling pathways (By
CC similarity). Interacts with SLITRK1 (PubMed:19640509). Interacts with
CC AK5, LDB1, MADD, MARK3, PDE1A and SMARCB1 (PubMed:16959763). Interacts
CC with MEFV (PubMed:27030597). {ECO:0000250|UniProtKB:P63101,
CC ECO:0000250|UniProtKB:Q9ES28, ECO:0000269|PubMed:10455159,
CC ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11427721,
CC ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:14578935,
CC ECO:0000269|PubMed:14970201, ECO:0000269|PubMed:15071501,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15644438,
CC ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15696159,
CC ECO:0000269|PubMed:16114898, ECO:0000269|PubMed:16246723,
CC ECO:0000269|PubMed:16376338, ECO:0000269|PubMed:16959763,
CC ECO:0000269|PubMed:17235285, ECO:0000269|PubMed:17913709,
CC ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19640509,
CC ECO:0000269|PubMed:23572552, ECO:0000269|PubMed:26047703,
CC ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:31024343,
CC ECO:0000269|PubMed:9360956}.
CC -!- INTERACTION:
CC P63104; P00519: ABL1; NbExp=3; IntAct=EBI-347088, EBI-375543;
CC P63104; P60709: ACTB; NbExp=3; IntAct=EBI-347088, EBI-353944;
CC P63104; Q9P0K1: ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567236;
CC P63104; Q9P0K1-3: ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567267;
CC P63104; Q12802: AKAP13; NbExp=2; IntAct=EBI-347088, EBI-1373806;
CC P63104; P10398: ARAF; NbExp=7; IntAct=EBI-347088, EBI-365961;
CC P63104; Q5T5U3: ARHGAP21; NbExp=2; IntAct=EBI-347088, EBI-1642518;
CC P63104; Q5VV41: ARHGEF16; NbExp=2; IntAct=EBI-347088, EBI-1057448;
CC P63104; Q92974: ARHGEF2; NbExp=3; IntAct=EBI-347088, EBI-302405;
CC P63104; P25705: ATP5F1A; NbExp=3; IntAct=EBI-347088, EBI-351437;
CC P63104; P06576: ATP5F1B; NbExp=2; IntAct=EBI-347088, EBI-356231;
CC P63104; P54253: ATXN1; NbExp=8; IntAct=EBI-347088, EBI-930964;
CC P63104; Q92934: BAD; NbExp=8; IntAct=EBI-347088, EBI-700771;
CC P63104; Q9UQB8: BAIAP2; NbExp=3; IntAct=EBI-347088, EBI-525456;
CC P63104; P15056: BRAF; NbExp=9; IntAct=EBI-347088, EBI-365980;
CC P63104; P62158: CALM3; NbExp=2; IntAct=EBI-347088, EBI-397435;
CC P63104; O00257-3: CBX4; NbExp=2; IntAct=EBI-347088, EBI-4392727;
CC P63104; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-347088, EBI-947308;
CC P63104; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-347088, EBI-11977221;
CC P63104; P30304: CDC25A; NbExp=2; IntAct=EBI-347088, EBI-747671;
CC P63104; P30305: CDC25B; NbExp=7; IntAct=EBI-347088, EBI-1051746;
CC P63104; P30307: CDC25C; NbExp=2; IntAct=EBI-347088, EBI-974439;
CC P63104; Q00537: CDK17; NbExp=3; IntAct=EBI-347088, EBI-624648;
CC P63104; Q07002: CDK18; NbExp=2; IntAct=EBI-347088, EBI-746238;
CC P63104; P23528: CFL1; NbExp=3; IntAct=EBI-347088, EBI-352733;
CC P63104; Q9P2M7: CGN; NbExp=3; IntAct=EBI-347088, EBI-79537;
CC P63104; P31327: CPS1; NbExp=2; IntAct=EBI-347088, EBI-536811;
CC P63104; Q7Z401: DENND4A; NbExp=2; IntAct=EBI-347088, EBI-1046479;
CC P63104; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-347088, EBI-529989;
CC P63104; P68104: EEF1A1; NbExp=2; IntAct=EBI-347088, EBI-352162;
CC P63104; P00533: EGFR; NbExp=6; IntAct=EBI-347088, EBI-297353;
CC P63104; P06733: ENO1; NbExp=2; IntAct=EBI-347088, EBI-353877;
CC P63104; Q12778: FOXO1; NbExp=3; IntAct=EBI-347088, EBI-1108782;
CC P63104; O43524: FOXO3; NbExp=3; IntAct=EBI-347088, EBI-1644164;
CC P63104; Q16658: FSCN1; NbExp=3; IntAct=EBI-347088, EBI-351076;
CC P63104; P30793: GCH1; NbExp=4; IntAct=EBI-347088, EBI-958183;
CC P63104; Q9Y4H4: GPSM3; NbExp=5; IntAct=EBI-347088, EBI-347538;
CC P63104; P49841: GSK3B; NbExp=4; IntAct=EBI-347088, EBI-373586;
CC P63104; P0C0S8: H2AC17; NbExp=2; IntAct=EBI-347088, EBI-1390628;
CC P63104; P68431: H3C12; NbExp=3; IntAct=EBI-347088, EBI-79722;
CC P63104; P62805: H4C9; NbExp=3; IntAct=EBI-347088, EBI-302023;
CC P63104; P56524: HDAC4; NbExp=6; IntAct=EBI-347088, EBI-308629;
CC P63104; Q9UQL6: HDAC5; NbExp=3; IntAct=EBI-347088, EBI-715576;
CC P63104; Q8WUI4: HDAC7; NbExp=4; IntAct=EBI-347088, EBI-1048378;
CC P63104; Q9Y4D8: HECTD4; NbExp=2; IntAct=EBI-347088, EBI-7195436;
CC P63104; P07910: HNRNPC; NbExp=2; IntAct=EBI-347088, EBI-357966;
CC P63104; P04792: HSPB1; NbExp=4; IntAct=EBI-347088, EBI-352682;
CC P63104; Q9Y4H2: IRS2; NbExp=3; IntAct=EBI-347088, EBI-1049582;
CC P63104; Q02241: KIF23; NbExp=6; IntAct=EBI-347088, EBI-306852;
CC P63104; P33176: KIF5B; NbExp=2; IntAct=EBI-347088, EBI-355878;
CC P63104; Q9H0B6: KLC2; NbExp=2; IntAct=EBI-347088, EBI-726994;
CC P63104; Q6P597: KLC3; NbExp=2; IntAct=EBI-347088, EBI-1643885;
CC P63104; P02545: LMNA; NbExp=2; IntAct=EBI-347088, EBI-351935;
CC P63104; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-347088, EBI-739832;
CC P63104; Q5S007: LRRK2; NbExp=11; IntAct=EBI-347088, EBI-5323863;
CC P63104; Q9NYL2: MAP3K20; NbExp=5; IntAct=EBI-347088, EBI-602273;
CC P63104; Q99759: MAP3K3; NbExp=2; IntAct=EBI-347088, EBI-307281;
CC P63104; Q99683: MAP3K5; NbExp=4; IntAct=EBI-347088, EBI-476263;
CC P63104; P10636: MAPT; NbExp=8; IntAct=EBI-347088, EBI-366182;
CC P63104; P10636-2: MAPT; NbExp=2; IntAct=EBI-347088, EBI-7796412;
CC P63104; P10636-3: MAPT; NbExp=9; IntAct=EBI-347088, EBI-7145070;
CC P63104; Q7KZI7: MARK2; NbExp=8; IntAct=EBI-347088, EBI-516560;
CC P63104; P27448: MARK3; NbExp=12; IntAct=EBI-347088, EBI-707595;
CC P63104; O15151: MDM4; NbExp=2; IntAct=EBI-347088, EBI-398437;
CC P63104; Q6WCQ1: MPRIP; NbExp=2; IntAct=EBI-347088, EBI-1022605;
CC P63104; O75592: MYCBP2; NbExp=2; IntAct=EBI-347088, EBI-1043774;
CC P63104; O95544: NADK; NbExp=2; IntAct=EBI-347088, EBI-743949;
CC P63104; P19338: NCL; NbExp=2; IntAct=EBI-347088, EBI-346967;
CC P63104; P06748: NPM1; NbExp=2; IntAct=EBI-347088, EBI-78579;
CC P63104; O96013: PAK4; NbExp=5; IntAct=EBI-347088, EBI-713738;
CC P63104; Q8TEW0: PARD3; NbExp=5; IntAct=EBI-347088, EBI-81968;
CC P63104; O60825: PFKFB2; NbExp=2; IntAct=EBI-347088, EBI-764425;
CC P63104; O00750: PIK3C2B; NbExp=2; IntAct=EBI-347088, EBI-641107;
CC P63104; O95685: PPP1R3D; NbExp=3; IntAct=EBI-347088, EBI-1045661;
CC P63104; Q02156: PRKCE; NbExp=7; IntAct=EBI-347088, EBI-706254;
CC P63104; P16471: PRLR; NbExp=3; IntAct=EBI-347088, EBI-476182;
CC P63104; O14744: PRMT5; NbExp=2; IntAct=EBI-347088, EBI-351098;
CC P63104; P26045: PTPN3; NbExp=5; IntAct=EBI-347088, EBI-1047946;
CC P63104; P04049: RAF1; NbExp=16; IntAct=EBI-347088, EBI-365996;
CC P63104; Q9P0K7: RAI14; NbExp=2; IntAct=EBI-347088, EBI-1023749;
CC P63104; Q8NFH8: REPS2; NbExp=2; IntAct=EBI-347088, EBI-7067016;
CC P63104; P61587: RND3; NbExp=11; IntAct=EBI-347088, EBI-1111534;
CC P63104; P23396: RPS3; NbExp=2; IntAct=EBI-347088, EBI-351193;
CC P63104; Q5PRF9: SAMD4B; NbExp=2; IntAct=EBI-347088, EBI-1047489;
CC P63104; P31947: SFN; NbExp=3; IntAct=EBI-347088, EBI-476295;
CC P63104; Q7L8J4: SH3BP5L; NbExp=2; IntAct=EBI-347088, EBI-747389;
CC P63104; P57059: SIK1; NbExp=5; IntAct=EBI-347088, EBI-1181640;
CC P63104; Q9Y2K2: SIK3; NbExp=5; IntAct=EBI-347088, EBI-1181460;
CC P63104; O60292: SIPA1L3; NbExp=2; IntAct=EBI-347088, EBI-2559690;
CC P63104; O94875: SORBS2; NbExp=2; IntAct=EBI-347088, EBI-311323;
CC P63104; Q7Z6B7: SRGAP1; NbExp=2; IntAct=EBI-347088, EBI-2481729;
CC P63104; O75044: SRGAP2; NbExp=2; IntAct=EBI-347088, EBI-1051034;
CC P63104; Q15831: STK11; NbExp=6; IntAct=EBI-347088, EBI-306838;
CC P63104; O00506: STK25; NbExp=2; IntAct=EBI-347088, EBI-618295;
CC P63104; O60343: TBC1D4; NbExp=2; IntAct=EBI-347088, EBI-522028;
CC P63104; P36897: TGFBR1; NbExp=4; IntAct=EBI-347088, EBI-1027557;
CC P63104; P04637: TP53; NbExp=2; IntAct=EBI-347088, EBI-366083;
CC P63104; Q13625: TP53BP2; NbExp=3; IntAct=EBI-347088, EBI-77642;
CC P63104; P49815: TSC2; NbExp=7; IntAct=EBI-347088, EBI-396587;
CC P63104; P40818: USP8; NbExp=2; IntAct=EBI-347088, EBI-1050865;
CC P63104; P55072: VCP; NbExp=2; IntAct=EBI-347088, EBI-355164;
CC P63104; P08670: VIM; NbExp=2; IntAct=EBI-347088, EBI-353844;
CC P63104; P30291: WEE1; NbExp=3; IntAct=EBI-347088, EBI-914695;
CC P63104; O14980: XPO1; NbExp=2; IntAct=EBI-347088, EBI-355867;
CC P63104; P46937: YAP1; NbExp=9; IntAct=EBI-347088, EBI-1044059;
CC P63104; P62258: YWHAE; NbExp=9; IntAct=EBI-347088, EBI-356498;
CC P63104; P63104: YWHAZ; NbExp=3; IntAct=EBI-347088, EBI-347088;
CC P63104; Q29495: AANAT; Xeno; NbExp=3; IntAct=EBI-347088, EBI-446413;
CC P63104; Q61337: Bad; Xeno; NbExp=3; IntAct=EBI-347088, EBI-400328;
CC P63104; P67828: CSNK1A1; Xeno; NbExp=4; IntAct=EBI-347088, EBI-7540603;
CC P63104; P54256-2: Hap1; Xeno; NbExp=4; IntAct=EBI-347088, EBI-994554;
CC P63104; P29172: MAPT; Xeno; NbExp=2; IntAct=EBI-347088, EBI-7291149;
CC P63104; P61588: Rnd3; Xeno; NbExp=3; IntAct=EBI-347088, EBI-6930266;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}.
CC Melanosome {ECO:0000269|PubMed:17081065}. Note=Located to stage I to
CC stage IV melanosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63104-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63104-2; Sequence=VSP_047505;
CC -!- PTM: The delta, brain-specific form differs from the zeta form in being
CC phosphorylated (By similarity). Phosphorylation on Ser-184 by MAPK8;
CC promotes dissociation of BAX and translocation of BAX to mitochondria.
CC Phosphorylation on Thr-232; inhibits binding of RAF1. Phosphorylated on
CC Ser-58 by PKA and protein kinase C delta type catalytic subunit in a
CC sphingosine-dependent fashion. Phosphorylation on Ser-58 by PKA;
CC disrupts homodimerization and heterodimerization with YHAE and TP53.
CC {ECO:0000250, ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427,
CC ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159,
CC ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338,
CC ECO:0000269|PubMed:9360956}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have phospholipase A2 activity.
CC {ECO:0000305|PubMed:1577711}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51814.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH73141.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M86400; AAA36446.1; -; mRNA.
DR EMBL; U28964; AAC52052.1; -; mRNA.
DR EMBL; AK289945; BAF82634.1; -; mRNA.
DR EMBL; AK296902; BAH12451.1; -; mRNA.
DR EMBL; CH471060; EAW91823.1; -; Genomic_DNA.
DR EMBL; BC003623; AAH03623.3; -; mRNA.
DR EMBL; BC051814; AAH51814.1; ALT_INIT; mRNA.
DR EMBL; BC063824; AAH63824.2; -; mRNA.
DR EMBL; BC068456; AAH68456.2; -; mRNA.
DR EMBL; BC072426; AAH72426.2; -; mRNA.
DR EMBL; BC073141; AAH73141.1; ALT_INIT; mRNA.
DR EMBL; BC083508; AAH83508.2; -; mRNA.
DR EMBL; BC099904; AAH99904.1; -; mRNA.
DR EMBL; BC101483; AAI01484.1; -; mRNA.
DR EMBL; BC108281; AAI08282.1; -; mRNA.
DR EMBL; BC111951; AAI11952.1; -; mRNA.
DR CCDS; CCDS6290.1; -. [P63104-1]
DR PIR; A38246; PSHUAM.
DR RefSeq; NP_001129171.1; NM_001135699.1. [P63104-1]
DR RefSeq; NP_001129172.1; NM_001135700.1. [P63104-1]
DR RefSeq; NP_001129173.1; NM_001135701.1. [P63104-1]
DR RefSeq; NP_001129174.1; NM_001135702.1. [P63104-1]
DR RefSeq; NP_003397.1; NM_003406.3. [P63104-1]
DR RefSeq; NP_663723.1; NM_145690.2. [P63104-1]
DR RefSeq; XP_005251118.1; XM_005251061.3. [P63104-1]
DR RefSeq; XP_005251120.1; XM_005251063.3. [P63104-1]
DR RefSeq; XP_016869299.1; XM_017013810.1. [P63104-1]
DR RefSeq; XP_016869300.1; XM_017013811.1. [P63104-1]
DR PDB; 1IB1; X-ray; 2.70 A; A/B/C/D=1-245.
DR PDB; 1QJA; X-ray; 2.00 A; A/B=1-245.
DR PDB; 1QJB; X-ray; 2.00 A; A/B=1-245.
DR PDB; 2C1J; X-ray; 2.60 A; A/B=1-245.
DR PDB; 2C1N; X-ray; 2.00 A; A/B=1-245.
DR PDB; 2O02; X-ray; 1.50 A; A/B=1-230.
DR PDB; 2WH0; X-ray; 2.25 A; A/B/C/D=1-245.
DR PDB; 3CU8; X-ray; 2.40 A; A/B=1-245.
DR PDB; 3NKX; X-ray; 2.40 A; A/B=1-245.
DR PDB; 3RDH; X-ray; 2.39 A; A/B/C/D=1-245.
DR PDB; 4BG6; X-ray; 2.30 A; A/B=1-245.
DR PDB; 4FJ3; X-ray; 1.95 A; A/B=1-230.
DR PDB; 4HKC; X-ray; 2.20 A; A=1-245.
DR PDB; 4IHL; X-ray; 2.20 A; A/B=1-230.
DR PDB; 4N7G; X-ray; 2.25 A; A=1-230.
DR PDB; 4N7Y; X-ray; 2.16 A; A/B=1-230.
DR PDB; 4N84; X-ray; 2.50 A; A/B=1-230.
DR PDB; 4WRQ; X-ray; 2.41 A; A/B=1-245.
DR PDB; 4ZDR; X-ray; 2.90 A; A/B=1-230.
DR PDB; 5D2D; X-ray; 2.10 A; A/B=1-230.
DR PDB; 5D3F; X-ray; 2.74 A; A/B=1-230.
DR PDB; 5EWZ; X-ray; 2.34 A; A/B=1-230.
DR PDB; 5EXA; X-ray; 1.95 A; A/B=1-230.
DR PDB; 5J31; X-ray; 2.40 A; A/B=1-230.
DR PDB; 5JM4; X-ray; 2.34 A; A/B=1-229.
DR PDB; 5M35; X-ray; 2.38 A; A/B=2-230.
DR PDB; 5M36; X-ray; 2.45 A; A/B=2-230.
DR PDB; 5M37; X-ray; 2.35 A; A/B=1-230.
DR PDB; 5NAS; X-ray; 2.08 A; A/B=1-230.
DR PDB; 5ULO; X-ray; 2.14 A; A/B=1-245.
DR PDB; 5WXN; X-ray; 2.93 A; A/B=1-245.
DR PDB; 5XY9; X-ray; 2.30 A; A/B=1-245.
DR PDB; 6EF5; X-ray; 2.44 A; A/B/C/D=1-245.
DR PDB; 6EJL; X-ray; 2.38 A; A/B=1-230.
DR PDB; 6EWW; X-ray; 2.68 A; A/B/C/D=1-230.
DR PDB; 6F08; X-ray; 1.90 A; A/B/I/J=1-230.
DR PDB; 6F09; X-ray; 1.59 A; P/Q/R/S=1-230.
DR PDB; 6FN9; X-ray; 2.27 A; A/B=1-230.
DR PDB; 6FNA; X-ray; 2.12 A; A/B=1-230.
DR PDB; 6FNB; X-ray; 2.30 A; A/B=1-230.
DR PDB; 6FNC; X-ray; 2.12 A; A/B=1-230.
DR PDB; 6Q0K; EM; 6.80 A; X/Y=1-245.
DR PDB; 6RLZ; X-ray; 3.70 A; A/B=1-230.
DR PDB; 6U2H; X-ray; 2.50 A; A/B=1-230.
DR PDB; 6XAG; X-ray; 3.30 A; A/B=1-230.
DR PDB; 6YMO; X-ray; 2.02 A; A/B=1-230.
DR PDB; 6YO8; X-ray; 2.09 A; A/B/C/D=1-230.
DR PDB; 6YOS; X-ray; 2.75 A; A/B=1-230.
DR PDB; 6ZFD; X-ray; 1.90 A; A/B=1-229.
DR PDB; 6ZFG; X-ray; 1.85 A; A/B=1-229.
DR PDB; 7D8H; X-ray; 2.42 A; A=1-245.
DR PDB; 7D8P; X-ray; 2.00 A; A/B=1-245.
DR PDB; 7D9V; X-ray; 2.21 A; A/B=1-245.
DR PDB; 7MFD; EM; 3.66 A; C/D=1-245.
DR PDB; 7MFE; EM; 4.07 A; B/C=1-245.
DR PDB; 7MFF; EM; 3.89 A; C/D=1-245.
DR PDB; 7Q16; X-ray; 2.36 A; A=1-229.
DR PDBsum; 1IB1; -.
DR PDBsum; 1QJA; -.
DR PDBsum; 1QJB; -.
DR PDBsum; 2C1J; -.
DR PDBsum; 2C1N; -.
DR PDBsum; 2O02; -.
DR PDBsum; 2WH0; -.
DR PDBsum; 3CU8; -.
DR PDBsum; 3NKX; -.
DR PDBsum; 3RDH; -.
DR PDBsum; 4BG6; -.
DR PDBsum; 4FJ3; -.
DR PDBsum; 4HKC; -.
DR PDBsum; 4IHL; -.
DR PDBsum; 4N7G; -.
DR PDBsum; 4N7Y; -.
DR PDBsum; 4N84; -.
DR PDBsum; 4WRQ; -.
DR PDBsum; 4ZDR; -.
DR PDBsum; 5D2D; -.
DR PDBsum; 5D3F; -.
DR PDBsum; 5EWZ; -.
DR PDBsum; 5EXA; -.
DR PDBsum; 5J31; -.
DR PDBsum; 5JM4; -.
DR PDBsum; 5M35; -.
DR PDBsum; 5M36; -.
DR PDBsum; 5M37; -.
DR PDBsum; 5NAS; -.
DR PDBsum; 5ULO; -.
DR PDBsum; 5WXN; -.
DR PDBsum; 5XY9; -.
DR PDBsum; 6EF5; -.
DR PDBsum; 6EJL; -.
DR PDBsum; 6EWW; -.
DR PDBsum; 6F08; -.
DR PDBsum; 6F09; -.
DR PDBsum; 6FN9; -.
DR PDBsum; 6FNA; -.
DR PDBsum; 6FNB; -.
DR PDBsum; 6FNC; -.
DR PDBsum; 6Q0K; -.
DR PDBsum; 6RLZ; -.
DR PDBsum; 6U2H; -.
DR PDBsum; 6XAG; -.
DR PDBsum; 6YMO; -.
DR PDBsum; 6YO8; -.
DR PDBsum; 6YOS; -.
DR PDBsum; 6ZFD; -.
DR PDBsum; 6ZFG; -.
DR PDBsum; 7D8H; -.
DR PDBsum; 7D8P; -.
DR PDBsum; 7D9V; -.
DR PDBsum; 7MFD; -.
DR PDBsum; 7MFE; -.
DR PDBsum; 7MFF; -.
DR PDBsum; 7Q16; -.
DR AlphaFoldDB; P63104; -.
DR BMRB; P63104; -.
DR SASBDB; P63104; -.
DR SMR; P63104; -.
DR BioGRID; 113366; 797.
DR ComplexPortal; CPX-1147; FOXO3-YWHAZ complex.
DR CORUM; P63104; -.
DR DIP; DIP-563N; -.
DR ELM; P63104; -.
DR IntAct; P63104; 722.
DR MINT; P63104; -.
DR STRING; 9606.ENSP00000379287; -.
DR BindingDB; P63104; -.
DR ChEMBL; CHEMBL4105899; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR MoonDB; P63104; Predicted.
DR TCDB; 8.A.98.1.2; the 14-3-3 protein (14-3-3) family.
DR GlyGen; P63104; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P63104; -.
DR MetOSite; P63104; -.
DR PhosphoSitePlus; P63104; -.
DR SwissPalm; P63104; -.
DR BioMuta; YWHAZ; -.
DR DMDM; 52000887; -.
DR DOSAC-COBS-2DPAGE; P63104; -.
DR OGP; P63104; -.
DR UCD-2DPAGE; P63104; -.
DR EPD; P63104; -.
DR jPOST; P63104; -.
DR MassIVE; P63104; -.
DR MaxQB; P63104; -.
DR PaxDb; P63104; -.
DR PeptideAtlas; P63104; -.
DR PRIDE; P63104; -.
DR ProteomicsDB; 57477; -.
DR TopDownProteomics; P63104-1; -. [P63104-1]
DR Antibodypedia; 3905; 1027 antibodies from 43 providers.
DR DNASU; 7534; -.
DR Ensembl; ENST00000353245.7; ENSP00000309503.3; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000395951.7; ENSP00000379281.3; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000395953.6; ENSP00000379283.2; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000395956.7; ENSP00000379286.3; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000395957.6; ENSP00000379287.2; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000395958.6; ENSP00000379288.2; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000419477.6; ENSP00000395114.2; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000457309.2; ENSP00000398599.1; ENSG00000164924.18. [P63104-1]
DR Ensembl; ENST00000522542.5; ENSP00000430072.1; ENSG00000164924.18. [P63104-2]
DR GeneID; 7534; -.
DR KEGG; hsa:7534; -.
DR MANE-Select; ENST00000395958.6; ENSP00000379288.2; NM_145690.3; NP_663723.1.
DR UCSC; uc003yjv.3; human. [P63104-1]
DR CTD; 7534; -.
DR DisGeNET; 7534; -.
DR GeneCards; YWHAZ; -.
DR HGNC; HGNC:12855; YWHAZ.
DR HPA; ENSG00000164924; Low tissue specificity.
DR MIM; 601288; gene.
DR neXtProt; NX_P63104; -.
DR OpenTargets; ENSG00000164924; -.
DR PharmGKB; PA37444; -.
DR VEuPathDB; HostDB:ENSG00000164924; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR InParanoid; P63104; -.
DR OMA; ERVCQDV; -.
DR PhylomeDB; P63104; -.
DR TreeFam; TF102003; -.
DR PathwayCommons; P63104; -.
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-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-392517; Rap1 signalling.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
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-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9614399; Regulation of localization of FOXO transcription factors.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SignaLink; P63104; -.
DR SIGNOR; P63104; -.
DR BioGRID-ORCS; 7534; 164 hits in 1031 CRISPR screens.
DR ChiTaRS; YWHAZ; human.
DR EvolutionaryTrace; P63104; -.
DR GeneWiki; YWHAZ; -.
DR GenomeRNAi; 7534; -.
DR Pharos; P63104; Tchem.
DR PRO; PR:P63104; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P63104; protein.
DR Bgee; ENSG00000164924; Expressed in oral epithelium and 213 other tissues.
DR ExpressionAtlas; P63104; baseline and differential.
DR Genevisible; P63104; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:SynGO-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
DR GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; IDA:SynGO.
DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
DR GO; GO:0035148; P:tube formation; IEA:Ensembl.
DR Gene3D; 1.20.190.20; -; 1.
DR IDEAL; IID00061; -.
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; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..245
FT /note="14-3-3 protein zeta/delta"
FT /id="PRO_0000058627"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 58
FT /note="Phosphoserine; by PKA and PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:11956222,
FT ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165,
FT ECO:0000269|PubMed:16376338"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 184
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:15071501,
FT ECO:0000269|PubMed:15696159"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63102"
FT MOD_RES 232
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000269|PubMed:31024343,
FT ECO:0000269|PubMed:9360956, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..98
FT /note="MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVV
FT GARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVL -> MSQPCRKLW
FT RHNYETSSCIEFLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047505"
FT VARIANT 14..245
FT /note="Missing (found in a patient with a
FT neurodevelopmental disorder; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31024343"
FT /id="VAR_082640"
FT VARIANT 53
FT /note="G -> R (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:31024343"
FT /id="VAR_082641"
FT VARIANT 145
FT /note="S -> L (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:31024343"
FT /id="VAR_082642"
FT VARIANT 230
FT /note="S -> W (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance; gain-of-
FT function mutation in signal transduction; changed
FT regulation of ERK1 and ERK2 cascade; increased interaction
FT with BRAF; increased interaction with RAF1; loss of
FT phosphorylation by CK1 at Thr-232)"
FT /evidence="ECO:0000269|PubMed:31024343"
FT /id="VAR_082643"
FT MUTAGEN 49
FT /note="K->E: Loss of interaction with NOXA1."
FT /evidence="ECO:0000269|PubMed:17913709"
FT MUTAGEN 56..60
FT /note="RSSWR->ASSWA: Abolishes lamellipodia formation and
FT induces filopodia formation."
FT /evidence="ECO:0000269|PubMed:16959763"
FT MUTAGEN 58
FT /note="S->A: Loss of sphingosine-activated PKA
FT phosphorylation. Promotes homodimerization and
FT heterodimerization with YWHAE. Enhanced transcriptional
FT activity of P53."
FT /evidence="ECO:0000269|PubMed:15883165,
FT ECO:0000269|PubMed:16376338"
FT MUTAGEN 58
FT /note="S->E: Loss of homodimerization. Reduced dimerization
FT with YWHAE. Significantly reduced interaction with P53. No
FT enhancement of P53 transcriptional activity."
FT /evidence="ECO:0000269|PubMed:15883165,
FT ECO:0000269|PubMed:16376338"
FT MUTAGEN 184
FT /note="S->A: On DNA damage, loss of MAPK8-mediated
FT phosphorylation. Loss of binding ABL1. Attenuates ABL1-
FT mediated apoptosis. No loss of interaction with BAX under
FT stress conditions. Inhibits translocation of BAX to
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:15071501,
FT ECO:0000269|PubMed:15696159"
FT MUTAGEN 232
FT /note="T->A: Loss of phosphorylation by CK1."
FT /evidence="ECO:0000269|PubMed:31024343"
FT CONFLICT 22
FT /note="M -> V (in Ref. 5; AAH68456)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="D -> G (in Ref. 3; BAH12451)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 38..67
FT /evidence="ECO:0007829|PDB:2O02"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 112..131
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 135..159
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2O02"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2O02"
FT HELIX 211..228
FT /evidence="ECO:0007829|PDB:2O02"
SQ 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
