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 27-MAR-2024, entry version 212. 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 INTERACTION WITH ADAM22. RX PubMed=12589811; DOI=10.1016/s0006-291x(03)00056-1; RA Zhu P., Sun Y., Xu R., Sang Y., Zhao J., Liu G., Cai L., Li C., Zhao S.; RT "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell RT adhesion and spreading."; RL Biochem. Biophys. Res. Commun. 301:991-999(2003). RN [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] 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 [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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 [47] RP FUNCTION, AND INTERACTION WITH TRIM25 AND EPSTEIN-BARR VIRUS PROTEIN BPLF1 RP (MICROBIAL INFECTION). RX PubMed=29357390; DOI=10.1371/journal.ppat.1006852; RA Gupta S., Ylae-Anttila P., Callegari S., Tsai M.H., Delecluse H.J., RA Masucci M.G.; RT "Herpesvirus deconjugases inhibit the IFN response by promoting TRIM25 RT autoubiquitination and functional inactivation of the RIG-I signalosome."; RL PLoS Pathog. 14:e1006852-e1006852(2018). RN [48] RP FUNCTION, AND INTERACTION WITH TRIM25 AND EPSTEIN-BARR VIRUS PROTEIN BPLF1 RP (MICROBIAL INFECTION). RX PubMed=31710640; DOI=10.1371/journal.ppat.1008146; RA Gupta S., Ylae-Anttila P., Sandalova T., Sun R., Achour A., Masucci M.G.; RT "14-3-3 scaffold proteins mediate the inactivation of trim25 and inhibition RT of the type I interferon response by herpesvirus deconjugases."; RL PLoS Pathog. 15:e1008146-e1008146(2019). RN [49] RP FUNCTION. RX PubMed=35662396; DOI=10.1016/j.molcel.2022.05.009; RA Zhang Z., Chen C., Yang F., Zeng Y.X., Sun P., Liu P., Li X.; RT "Itaconate is a lysosomal inducer that promotes antibacterial innate RT immunity."; RL Mol. Cell 0:0-0(2022). RN [50] 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 [51] 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 [52] 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 [53] 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 [54] 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 CC (PubMed:14578935, PubMed:15071501, PubMed:15644438, PubMed:16376338, CC PubMed:16959763, PubMed:31024343, PubMed:9360956). Binds to a large CC number of partners, usually by recognition of a phosphoserine or CC phosphothreonine motif (PubMed:35662396). Binding generally results in CC the modulation of the activity of the binding partner CC (PubMed:35662396). Promotes cytosolic retention and inactivation of CC TFEB transcription factor by binding to phosphorylated TFEB CC (PubMed:35662396). Induces ARHGEF7 activity on RAC1 as well as CC lamellipodia and membrane ruffle formation (PubMed:16959763). In CC neurons, regulates spine maturation through the modulation of ARHGEF7 CC activity (By similarity). {ECO:0000250|UniProtKB:O55043, CC ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15071501, CC ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:16376338, CC ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:31024343, CC ECO:0000269|PubMed:35662396, 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 (PubMed:12865427, PubMed:16376338). Heterodimerizes with YWHAE CC (PubMed:16376338). Homo- and heterodimerization is inhibited by CC phosphorylation on Ser-58 (PubMed:16376338). Interacts with FOXO4, CC NOXA1, SSH1 and ARHGEF2. Interacts with Pseudomonas aeruginosa exoS CC (unphosphorylated form). Interacts with BAX; the interaction occurs in CC the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation CC releases BAX to mitochondria. Interacts with phosphorylated RAF1; the CC interaction is inhibited when YWHAZ is phosphorylated on Thr-232 CC (PubMed:31024343). Interacts with BRAF (PubMed:31024343). Interacts CC with TP53; the interaction enhances p53 transcriptional activity. The CC Ser-58 phosphorylated form inhibits this interaction and p53 CC transcriptional activity. Interacts with ABL1 (phosphorylated form); CC the interaction retains ABL1 in the cytoplasm. Interacts with PKA- CC phosphorylated AANAT; the interaction modulates AANAT enzymatic CC activity by increasing affinity for arylalkylamines and acetyl-CoA and CC protecting the enzyme from dephosphorylation and proteasomal CC degradation. It may also prevent thiol-dependent inactivation. CC Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates CC dimerization. Interacts with GAB2 and TLK2. Interacts with the 'Thr- CC 369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with CC PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with ZFP36L1 CC (via phosphorylated form); this interaction occurs in a p38 MAPK- and CC AKT-signaling pathways (By similarity). Interacts with SLITRK1 CC (PubMed:19640509). Interacts with AK5, LDB1, MADD, MARK3, PDE1A and CC SMARCB1 (PubMed:16959763). Interacts with MEFV (PubMed:27030597). CC Interacts with ADAM22 (via C-terminus) (PubMed:12589811). CC {ECO:0000250|UniProtKB:P63101, ECO:0000250|UniProtKB:Q9ES28, CC ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:11336675, CC ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:11956222, CC ECO:0000269|PubMed:12589811, ECO:0000269|PubMed:12865427, CC ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:14970201, CC ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15159416, CC ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:15660133, CC ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:16114898, CC ECO:0000269|PubMed:16246723, ECO:0000269|PubMed:16376338, CC ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:17235285, CC ECO:0000269|PubMed:17913709, ECO:0000269|PubMed:19172738, CC ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:23572552, CC ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:27030597, CC ECO:0000269|PubMed:31024343, ECO:0000269|PubMed:9360956}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus CC protein BPLF1 and TRIM25; leading to inhibition of the type-I IFN CC response. {ECO:0000269|PubMed:29357390, ECO:0000269|PubMed:31710640}. 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=3; IntAct=EBI-347088, EBI-1373806; CC P63104; P10398: ARAF; NbExp=8; IntAct=EBI-347088, EBI-365961; CC P63104; Q5T5U3: ARHGAP21; NbExp=4; IntAct=EBI-347088, EBI-1642518; CC P63104; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-347088, EBI-1057448; CC P63104; Q92974: ARHGEF2; NbExp=5; 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=9; IntAct=EBI-347088, EBI-700771; CC P63104; Q9UQB8: BAIAP2; NbExp=5; IntAct=EBI-347088, EBI-525456; CC P63104; P15056: BRAF; NbExp=10; IntAct=EBI-347088, EBI-365980; CC P63104; P62158: CALM3; NbExp=2; IntAct=EBI-347088, EBI-397435; CC P63104; P22681: CBL; NbExp=3; IntAct=EBI-347088, EBI-518228; 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=4; IntAct=EBI-347088, EBI-624648; CC P63104; Q07002: CDK18; NbExp=3; IntAct=EBI-347088, EBI-746238; CC P63104; Q5SW79: CEP170; NbExp=3; IntAct=EBI-347088, EBI-1104799; CC P63104; P23528: CFL1; NbExp=3; IntAct=EBI-347088, EBI-352733; CC P63104; Q9P2M7: CGN; NbExp=4; IntAct=EBI-347088, EBI-79537; CC P63104; P31327: CPS1; NbExp=2; IntAct=EBI-347088, EBI-536811; CC P63104; Q7Z401: DENND4A; NbExp=5; 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=4; IntAct=EBI-347088, EBI-1108782; CC P63104; O43524: FOXO3; NbExp=4; 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=7; 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=5; IntAct=EBI-347088, EBI-1049582; CC P63104; O43896: KIF1C; NbExp=3; IntAct=EBI-347088, EBI-1644048; CC P63104; Q02241: KIF23; NbExp=8; IntAct=EBI-347088, EBI-306852; CC P63104; P33176: KIF5B; NbExp=3; IntAct=EBI-347088, EBI-355878; CC P63104; Q9H0B6: KLC2; NbExp=4; IntAct=EBI-347088, EBI-726994; CC P63104; Q6P597: KLC3; NbExp=2; IntAct=EBI-347088, EBI-1643885; CC P63104; Q6PKG0: LARP1; NbExp=3; IntAct=EBI-347088, EBI-1052114; CC P63104; Q9UHB6: LIMA1; NbExp=2; IntAct=EBI-347088, EBI-351479; CC P63104; P02545: LMNA; NbExp=2; IntAct=EBI-347088, EBI-351935; CC P63104; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-347088, EBI-739832; CC P63104; P42704: LRPPRC; NbExp=2; IntAct=EBI-347088, EBI-1050853; CC P63104; Q5S007: LRRK2; NbExp=11; IntAct=EBI-347088, EBI-5323863; CC P63104; Q9NYL2: MAP3K20; NbExp=6; IntAct=EBI-347088, EBI-602273; CC P63104; Q99759: MAP3K3; NbExp=4; 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=9; IntAct=EBI-347088, EBI-516560; CC P63104; P27448: MARK3; NbExp=14; IntAct=EBI-347088, EBI-707595; CC P63104; O15151: MDM4; NbExp=2; IntAct=EBI-347088, EBI-398437; CC P63104; Q6WCQ1: MPRIP; NbExp=3; IntAct=EBI-347088, EBI-1022605; CC P63104; O75592: MYCBP2; NbExp=3; 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=6; IntAct=EBI-347088, EBI-713738; CC P63104; Q8TEW0: PARD3; NbExp=8; IntAct=EBI-347088, EBI-81968; CC P63104; Q15154: PCM1; NbExp=2; IntAct=EBI-347088, EBI-741421; CC P63104; O60825: PFKFB2; NbExp=4; IntAct=EBI-347088, EBI-764425; CC P63104; O00750: PIK3C2B; NbExp=3; IntAct=EBI-347088, EBI-641107; CC P63104; Q86W92: PPFIBP1; NbExp=3; IntAct=EBI-347088, EBI-1045582; 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=30; 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; Q6R327: RICTOR; NbExp=3; IntAct=EBI-347088, EBI-1387196; 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=6; 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=7; IntAct=EBI-347088, EBI-1181460; CC P63104; O60292: SIPA1L3; NbExp=3; IntAct=EBI-347088, EBI-2559690; CC P63104; O94875: SORBS2; NbExp=4; IntAct=EBI-347088, EBI-311323; CC P63104; Q96JI7: SPG11; NbExp=2; IntAct=EBI-347088, EBI-2822128; CC P63104; Q7Z6B7: SRGAP1; NbExp=2; IntAct=EBI-347088, EBI-2481729; CC P63104; O75044: SRGAP2; NbExp=4; 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=3; 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=5; IntAct=EBI-347088, EBI-77642; CC P63104; P49815: TSC2; NbExp=8; IntAct=EBI-347088, EBI-396587; CC P63104; P40818: USP8; NbExp=3; IntAct=EBI-347088, EBI-1050865; CC P63104; P55072: VCP; NbExp=2; IntAct=EBI-347088, EBI-355164; CC P63104; P08670: VIM; NbExp=3; IntAct=EBI-347088, EBI-353844; CC P63104; P30291: WEE1; NbExp=4; IntAct=EBI-347088, EBI-914695; CC P63104; O14980: XPO1; NbExp=2; IntAct=EBI-347088, EBI-355867; CC P63104; P46937: YAP1; NbExp=10; IntAct=EBI-347088, EBI-1044059; CC P63104; P62258: YWHAE; NbExp=14; 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. {ECO:0000269|PubMed:17081065}. 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 (Probable). Phosphorylation on Ser-184 by MAPK8; CC promotes dissociation of BAX and translocation of BAX to mitochondria CC (PubMed:15071501, PubMed:15696159). Phosphorylation on Thr-232; CC inhibits binding of RAF1 (PubMed:9360956). Phosphorylated on Ser-58 by CC PKA and protein kinase C delta type catalytic subunit in a sphingosine- CC dependent fashion (PubMed:11956222, PubMed:12865427, PubMed:15883165, CC PubMed:16376338). Phosphorylation on Ser-58 by PKA; disrupts CC homodimerization and heterodimerization with YHAE and TP53 CC (PubMed:11956222, PubMed:12865427, PubMed:15883165, PubMed:16376338). CC {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, ECO:0000305}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7ZIT; X-ray; 1.79 A; A/B=1-230. DR PDB; 8A9G; X-ray; 1.96 A; A/B=1-230. DR PDB; 8AH2; X-ray; 2.90 A; A/C=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 PDBsum; 7ZIT; -. DR PDBsum; 8A9G; -. DR PDBsum; 8AH2; -. DR AlphaFoldDB; P63104; -. DR BMRB; P63104; -. DR EMDB; EMD-20551; -. DR EMDB; EMD-23813; -. DR EMDB; EMD-23814; -. DR EMDB; EMD-23815; -. DR SASBDB; P63104; -. DR SMR; P63104; -. DR BioGRID; 113366; 1230. DR ComplexPortal; CPX-1147; FOXO3-YWHAZ complex. DR CORUM; P63104; -. DR DIP; DIP-563N; -. DR ELM; P63104; -. DR IntAct; P63104; 917. 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 GlyCosmos; P63104; 1 site, 1 glycan. 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 EPD; P63104; -. DR jPOST; P63104; -. DR MassIVE; P63104; -. DR MaxQB; P63104; -. DR PaxDb; 9606-ENSP00000379287; -. DR PeptideAtlas; P63104; -. DR PRIDE; P63104; -. DR ProteomicsDB; 57477; -. DR Pumba; P63104; -. DR TopDownProteomics; P63104-1; -. [P63104-1] DR Antibodypedia; 3905; 1188 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 AGR; HGNC:12855; -. DR CTD; 7534; -. DR DisGeNET; 7534; -. DR GeneCards; YWHAZ; -. DR HGNC; HGNC:12855; YWHAZ. DR HPA; ENSG00000164924; Low tissue specificity. DR MalaCards; YWHAZ; -. DR MIM; 601288; gene. DR neXtProt; NX_P63104; -. DR OpenTargets; ENSG00000164924; -. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR PharmGKB; PA37444; -. DR VEuPathDB; HostDB:ENSG00000164924; -. DR eggNOG; KOG0841; Eukaryota. DR GeneTree; ENSGT01090000260040; -. DR InParanoid; P63104; -. DR OMA; YDEMVNE; -. DR OrthoDB; 920089at2759; -. 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-9735871; SARS-CoV-1 targets host intracellular signalling and regulatory pathways. 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; 169 hits in 1093 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 215 other cell types or tissues. DR ExpressionAtlas; P63104; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:UniProt. 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: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:0050815; F:phosphoserine residue binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0140311; F:protein sequestering activity; IDA: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:0042149; P:cellular response to glucose starvation; IDA:UniProt. DR GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB. DR GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc. DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProt. DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:UniProt. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProt. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB. 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:0007165; P:signal transduction; IMP:UniProtKB. DR CDD; cd10022; 14-3-3_beta_zeta; 1. DR Gene3D; 1.20.190.20; 14-3-3 domain; 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; 14-3-3 PROTEIN; 1. DR PANTHER; PTHR18860:SF7; 14-3-3 PROTEIN ZETA_DELTA; 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; 14-3-3 protein; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. DR UCD-2DPAGE; P63104; -. DR Genevisible; P63104; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Disease variant; Host-virus interaction; KW Phosphoprotein; 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|UniProtKB:P63103" FT SITE 127 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P63103" 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; uncertain 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; uncertain 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; uncertain 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; uncertain significance; gain-of-function mutation FT in signal transduction; changed regulation of ERK1 and ERK2 FT cascade; increased interaction with BRAF; increased FT interaction with RAF1; loss of phosphorylation by CK1 at FT 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 FT ABL1-mediated apoptosis. No loss of interaction with BAX FT under 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 //