ID 1433B_HUMAN Reviewed; 246 AA. AC P31946; A8K9K2; E1P616; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 247. DE RecName: Full=14-3-3 protein beta/alpha; DE AltName: Full=Protein 1054; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; DE Contains: DE RecName: Full=14-3-3 protein beta/alpha, N-terminally processed; GN Name=YWHAB; 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]. RC TISSUE=Keratinocyte; RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., RA Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has been RT involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Thymus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 1-11; 30-51; 63-73 AND 130-159, INTERACTION WITH PI4KB; RP TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23572552; DOI=10.1128/mbio.00098-13; RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.; RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected RT by enteroviral and kobuviral 3A protein binding."; RL MBio 4:E00098-E00098(2013). RN [7] RP PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Zebisch A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 3-20. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP INTERACTION WITH TESK1. RX PubMed=11555644; DOI=10.1074/jbc.m104620200; RA Toshima J.Y., Toshima J., Watanabe T., Mizuno K.; RT "Binding of 14-3-3beta regulates the kinase activity and subcellular RT localization of testicular protein kinase 1."; RL J. Biol. Chem. 276:43471-43481(2001). RN [10] RP INTERACTION WITH CHLAMYDIA INCG, SUBUNIT (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION (MICROBIAL INFECTION). RX PubMed=11260479; DOI=10.1046/j.1365-2958.2001.02355.x; RA Scidmore M.A., Hackstadt T.; RT "Mammalian 14-3-3beta associates with the Chlamydia trachomatis inclusion RT membrane via its interaction with IncG."; RL Mol. Microbiol. 39:1638-1650(2001). RN [11] RP INTERACTION WITH AANAT. RX PubMed=11427721; DOI=10.1073/pnas.141118798; RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.; RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3- RT binding switch in melatonin synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001). RN [12] RP 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 [13] RP INTERACTION WITH CRTC2. RX PubMed=15454081; DOI=10.1016/j.cell.2004.09.015; RA Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., RA Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., RA Okamoto M., Montminy M.; RT "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive RT coincidence detector."; RL Cell 119:61-74(2004). RN [14] RP INTERACTION WITH YWHAB. RX PubMed=15538381; DOI=10.1038/sj.emboj.7600477; RA Schmidlin M., Lu M., Leuenberger S.A., Stoecklin G., Mallaun M., Gross B., RA Gherzi R., Hess D., Hemmings B.A., Moroni C.; RT "The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by RT protein kinase B."; RL EMBO J. 23:4760-4769(2004). RN [15] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [16] RP INTERACTION WITH ADAM22. RX PubMed=15882968; DOI=10.1016/j.bbrc.2005.03.229; RA Zhu P., Sang Y., Xu H., Zhao J., Xu R., Sun Y., Xu T., Wang X., Chen L., RA Feng H., Li C., Zhao S.; RT "ADAM22 plays an important role in cell adhesion and spreading with the RT assistance of 14-3-3."; RL Biochem. Biophys. Res. Commun. 331:938-946(2005). RN [17] RP INTERACTION WITH ABL1. 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 [18] 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 [19] RP INTERACTION WITH MARK2 AND MARK3. RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200; RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M., RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B., RA Bouwmeester T., Acker-Palmer A.; RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins RT involved in cytoskeletal rearrangements and cell signaling."; RL Mol. Cell. Proteomics 5:2211-2227(2006). RN [20] RP INTERACTION WITH YAP1. RX PubMed=17974916; DOI=10.1101/gad.1602907; RA Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., RA Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., RA Guan K.L.; RT "Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell RT contact inhibition and tissue growth control."; RL Genes Dev. 21:2747-2761(2007). RN [21] RP INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17717073; DOI=10.1210/me.2007-0323; RA Liu Y., Ross J.F., Bodine P.V.N., Billiard J.; RT "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) RT phosphorylation and promotes osteoblast differentiation and bone RT formation."; RL Mol. Endocrinol. 21:3050-3061(2007). RN [22] RP INTERACTION WITH SIRT2. RX PubMed=18249187; DOI=10.1016/j.bbrc.2008.01.114; RA Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y., Lee K.Y.; RT "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of RT p53."; RL Biochem. Biophys. Res. Commun. 368:690-695(2008). RN [23] 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 [24] 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 [25] RP FUNCTION, AND INTERACTION WITH SRPK2. RX PubMed=19592491; DOI=10.1074/jbc.m109.026237; RA Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.; RT "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle RT and cell death in neurons."; RL J. Biol. Chem. 284:24512-24525(2009). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [27] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, AND RP IDENTIFICATION 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 [28] 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 [29] RP FUNCTION, AND INTERACTION WITH AKAP13. RX PubMed=21224381; DOI=10.1074/jbc.m110.185645; RA Cariolato L., Cavin S., Diviani D.; RT "A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling RT complex involved in alpha1-adrenergic receptor-induced p38 activation."; RL J. Biol. Chem. 286:7925-7937(2011). RN [30] RP INTERACTION WITH SOS1. RX PubMed=22827337; DOI=10.1042/bj20120938; RA Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J., RA Roux P.P., Ballif B.A.; RT "RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively RT regulating MAPK activation."; RL Biochem. J. 447:159-166(2012). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, ACETYLATION [LARGE RP SCALE ANALYSIS] AT MET-1 (ISOFORM SHORT), CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND IDENTIFICATION BY MASS RP 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 [33] RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46 (MICROBIAL INFECTION). RX PubMed=23938468; DOI=10.1074/mcp.m113.030866; RA Lin A.E., Greco T.M., Dohner K., Sodeik B., Cristea I.M.; RT "A proteomic perspective of inbuilt viral protein regulation: pUL46 RT tegument protein is targeted for degradation by ICP0 during herpes simplex RT virus type 1 infection."; RL Mol. Cell. Proteomics 12:3237-3252(2013). RN [34] RP INTERACTION WITH MYO1C. RX PubMed=24636949; DOI=10.1016/j.jmb.2014.03.004; RA Stefan Munnich M.H., Manstein D.J.; RT "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: RT implications for Ca(2+)-regulation and 14-3-3 binding."; RL J. Mol. Biol. 426:2070-2081(2014). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY RP 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 [36] 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 [37] RP INTERACTION WITH RIPOR2. RX PubMed=25588844; DOI=10.1242/jcs.161497; RA Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.; RT "Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at RT leading edges polarizes neutrophils."; RL J. Cell Sci. 128:992-1000(2015). RN [38] RP ACETYLATION AT THR-2, AND CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=25489052; DOI=10.1093/hmg/ddu611; RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A., RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H., RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.; RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt- RT acetylation defects."; RL Hum. Mol. Genet. 24:1956-1976(2015). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [40] 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 [41] RP INTERACTION WITH HDAC4. RX PubMed=33537682; DOI=10.1016/j.xhgg.2020.100015; RG DDD Study; RA Wakeling E., McEntagart M., Bruccoleri M., Shaw-Smith C., Stals K.L., RA Wakeling M., Barnicoat A., Beesley C., Hanson-Kahn A.K., Kukolich M., RA Stevenson D.A., Campeau P.M., Ellard S., Elsea S.H., Yang X.J., RA Caswell R.C.; RT "Missense substitutions at a conserved 14-3-3 binding site in HDAC4 cause a RT novel intellectual disability syndrome."; RL HGG Adv. 2:100015-100015(2021). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 protein RT family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). RN [43] RP VARIANT ILE-99. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene RT PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). 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. Negative regulator of CC osteogenesis. Blocks the nuclear translocation of the phosphorylated CC form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on CC cyclin D1 expression resulting in blockage of neuronal apoptosis CC elicited by SRPK2. Negative regulator of signaling cascades that CC mediate activation of MAP kinases via AKAP13. CC {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:19592491, CC ECO:0000269|PubMed:21224381}. CC -!- SUBUNIT: Homodimer (PubMed:17717073). Interacts with SAMSN1 and PRKCE CC (By similarity). Interacts with AKAP13 (PubMed:21224381). Interacts CC with SSH1 and TORC2/CRTC2 (PubMed:15454081, PubMed:15159416). Interacts CC with ABL1; the interaction results in cytoplasmic location of ABL1 and CC inhibition of cABL-mediated apoptosis (PubMed:15696159). Interacts with CC ROR2 (dimer); the interaction results in phosphorylation of YWHAB on CC tyrosine residues (PubMed:17717073). Interacts with GAB2 CC (PubMed:19172738). Interacts with YAP1 (phosphorylated form) CC (PubMed:17974916). Interacts with the phosphorylated (by AKT1) form of CC SRPK2 (PubMed:19592491). Interacts with PKA-phosphorylated AANAT CC (PubMed:11427721). Interacts with MYO1C (PubMed:24636949). Interacts CC with SIRT2 (PubMed:18249187). Interacts with the 'Thr-369' CC phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, CC TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with the 'Ser-1134' CC and 'Ser-1161' phosphorylated form of SOS1 (PubMed:22827337). Interacts CC (via phosphorylated form) with YWHAB; this interaction occurs in a CC protein kinase AKT1-dependent manner (PubMed:15538381). Interacts with CC SLITRK1 (PubMed:19640509). Interacts with SYNPO2 (phosphorylated form); CC YWHAB competes with ACTN2 for interaction with SYNPO2 (By similarity). CC Interacts with RIPOR2 (via phosphorylated form) isoform 2; this CC interaction occurs in a chemokine-dependent manner and does not compete CC for binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2- CC mediated RHOA activity (PubMed:25588844). Interacts with MARK2 and CC MARK3 (PubMed:16959763). Interacts with TESK1; the interaction is CC dependent on the phosphorylation of TESK1 'Ser-437' and inhibits TESK1 CC kinase activity (PubMed:11555644). Interacts with MEFV CC (PubMed:27030597). Interacts with HDAC4 (PubMed:33537682). Interacts CC with ADAM22 (via C-terminus) (PubMed:15882968). CC {ECO:0000250|UniProtKB:Q9CQV8, ECO:0000269|PubMed:11427721, CC ECO:0000269|PubMed:11555644, ECO:0000269|PubMed:15159416, CC ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:15538381, CC ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:15882968, CC ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:17085597, CC ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:17974916, CC ECO:0000269|PubMed:18249187, ECO:0000269|PubMed:19172738, CC ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:19640509, CC ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:22827337, CC ECO:0000269|PubMed:23572552, ECO:0000269|PubMed:24636949, CC ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:26047703, CC ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:33537682}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1 CC protein UL46. {ECO:0000269|PubMed:23938468}. CC -!- SUBUNIT: (Microbial infection) Probably interacts with Chlamydia CC trachomatis protein IncG. {ECO:0000305|PubMed:11260479}. CC -!- INTERACTION: CC P31946; Q9P0K1-3: ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567267; CC P31946; Q12802: AKAP13; NbExp=3; IntAct=EBI-359815, EBI-1373806; CC P31946; Q96B36: AKT1S1; NbExp=3; IntAct=EBI-359815, EBI-720593; CC P31946; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-359815, EBI-25928834; CC P31946; P05067: APP; NbExp=3; IntAct=EBI-359815, EBI-77613; CC P31946; P54253: ATXN1; NbExp=5; IntAct=EBI-359815, EBI-930964; CC P31946; Q92934: BAD; NbExp=5; IntAct=EBI-359815, EBI-700771; CC P31946; P15056: BRAF; NbExp=8; IntAct=EBI-359815, EBI-365980; CC P31946; P22681: CBL; NbExp=4; IntAct=EBI-359815, EBI-518228; CC P31946; O00257: CBX4; NbExp=3; IntAct=EBI-359815, EBI-722425; CC P31946; P30304: CDC25A; NbExp=10; IntAct=EBI-359815, EBI-747671; CC P31946; P30305: CDC25B; NbExp=5; IntAct=EBI-359815, EBI-1051746; CC P31946; P30307: CDC25C; NbExp=6; IntAct=EBI-359815, EBI-974439; CC P31946; O94921: CDK14; NbExp=6; IntAct=EBI-359815, EBI-1043945; CC P31946; Q53ET0: CRTC2; NbExp=4; IntAct=EBI-359815, EBI-1181987; CC P31946; Q9NYF0: DACT1; NbExp=4; IntAct=EBI-359815, EBI-3951744; CC P31946; Q13627-2: DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621; CC P31946; Q9UQC2: GAB2; NbExp=6; IntAct=EBI-359815, EBI-975200; CC P31946; P55040: GEM; NbExp=4; IntAct=EBI-359815, EBI-744104; CC P31946; P56524: HDAC4; NbExp=5; IntAct=EBI-359815, EBI-308629; CC P31946; P42858: HTT; NbExp=11; IntAct=EBI-359815, EBI-466029; CC P31946; Q5S007: LRRK2; NbExp=5; IntAct=EBI-359815, EBI-5323863; CC P31946; Q99759: MAP3K3; NbExp=4; IntAct=EBI-359815, EBI-307281; CC P31946; Q99683: MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263; CC P31946; Q7KZI7: MARK2; NbExp=5; IntAct=EBI-359815, EBI-516560; CC P31946; P27448: MARK3; NbExp=8; IntAct=EBI-359815, EBI-707595; CC P31946; P26045: PTPN3; NbExp=6; IntAct=EBI-359815, EBI-1047946; CC P31946; P04049: RAF1; NbExp=35; IntAct=EBI-359815, EBI-365996; CC P31946; Q96TC7: RMDN3; NbExp=5; IntAct=EBI-359815, EBI-1056589; CC P31946; P61587: RND3; NbExp=2; IntAct=EBI-359815, EBI-1111534; CC P31946; Q96JI7: SPG11; NbExp=2; IntAct=EBI-359815, EBI-2822128; CC P31946; P78362: SRPK2; NbExp=2; IntAct=EBI-359815, EBI-593303; CC P31946; Q8WYL5: SSH1; NbExp=3; IntAct=EBI-359815, EBI-1222387; CC P31946; P49815: TSC2; NbExp=6; IntAct=EBI-359815, EBI-396587; CC P31946; P46937: YAP1; NbExp=7; IntAct=EBI-359815, EBI-1044059; CC P31946; P31946: YWHAB; NbExp=3; IntAct=EBI-359815, EBI-359815; CC P31946; P62258: YWHAE; NbExp=12; IntAct=EBI-359815, EBI-356498; CC P31946; P61981: YWHAG; NbExp=5; IntAct=EBI-359815, EBI-359832; CC P31946; P27348: YWHAQ; NbExp=5; IntAct=EBI-359815, EBI-359854; CC P31946; P67828: CSNK1A1; Xeno; NbExp=3; IntAct=EBI-359815, EBI-7540603; CC P31946; P55041: Gem; Xeno; NbExp=3; IntAct=EBI-359815, EBI-7082069; CC P31946; Q11184: let-756; Xeno; NbExp=2; IntAct=EBI-359815, EBI-3843983; CC P31946; P61588: Rnd3; Xeno; NbExp=5; IntAct=EBI-359815, EBI-6930266; CC P31946; Q91YE8: Synpo2; Xeno; NbExp=3; IntAct=EBI-359815, EBI-7623057; CC P31946; B7UM99: tir; Xeno; NbExp=2; IntAct=EBI-359815, EBI-2504426; CC P31946; P22893: Zfp36; Xeno; NbExp=5; IntAct=EBI-359815, EBI-647803; CC P31946; Q76353; Xeno; NbExp=3; IntAct=EBI-359815, EBI-6248077; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}. CC Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass CC spectrometry in melanosome fractions from stage I to stage IV. CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11260479}. CC Note=(Microbial infection) Upon infection with Chlamydia trachomatis, CC this protein is associated with the pathogen-containing vacuole CC membrane where it colocalizes with IncG. {ECO:0000269|PubMed:11260479}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P31946-1; Sequence=Displayed; CC Name=Short; CC IsoId=P31946-2; Sequence=VSP_018632; CC -!- PTM: The alpha, brain-specific form differs from the beta form in being CC phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type CC catalytic subunit in a sphingosine-dependent fashion. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 14-3-3 family. {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; X57346; CAA40621.1; -; mRNA. DR EMBL; AK292717; BAF85406.1; -; mRNA. DR EMBL; AL008725; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75893.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75894.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75896.1; -; Genomic_DNA. DR EMBL; BC001359; AAH01359.1; -; mRNA. DR CCDS; CCDS13339.1; -. [P31946-1] DR PIR; S34755; S34755. DR RefSeq; NP_003395.1; NM_003404.4. [P31946-1] DR RefSeq; NP_647539.1; NM_139323.3. [P31946-1] DR RefSeq; XP_016883528.1; XM_017028039.1. DR PDB; 2BQ0; X-ray; 2.50 A; A/B=2-239. DR PDB; 2C23; X-ray; 2.65 A; A=2-239. DR PDB; 4DNK; X-ray; 2.20 A; A/B=1-246. DR PDB; 5N10; X-ray; 1.60 A; A/B=1-246. DR PDB; 6A5Q; X-ray; 2.00 A; A/B/C=1-246. DR PDB; 6BYK; X-ray; 3.00 A; A/B/C/D=3-232. DR PDB; 6GN0; X-ray; 3.24 A; A/B/C/D=1-239. DR PDB; 6GN8; X-ray; 2.34 A; A/B=1-234. DR PDB; 6GNJ; X-ray; 3.24 A; A/B=1-234. DR PDB; 6GNK; X-ray; 2.55 A; A/B=1-234. DR PDB; 6GNN; X-ray; 3.79 A; A=1-239. DR PDB; 6HEP; X-ray; 1.86 A; A/B/C/D=1-232. DR PDB; 8DP5; EM; 3.10 A; C=1-246. DR PDB; 8EQ8; X-ray; 1.50 A; A/B=1-239. DR PDB; 8EQH; X-ray; 1.90 A; A/B=1-239. DR PDBsum; 2BQ0; -. DR PDBsum; 2C23; -. DR PDBsum; 4DNK; -. DR PDBsum; 5N10; -. DR PDBsum; 6A5Q; -. DR PDBsum; 6BYK; -. DR PDBsum; 6GN0; -. DR PDBsum; 6GN8; -. DR PDBsum; 6GNJ; -. DR PDBsum; 6GNK; -. DR PDBsum; 6GNN; -. DR PDBsum; 6HEP; -. DR PDBsum; 8DP5; -. DR PDBsum; 8EQ8; -. DR PDBsum; 8EQH; -. DR AlphaFoldDB; P31946; -. DR EMDB; EMD-27630; -. DR SASBDB; P31946; -. DR SMR; P31946; -. DR BioGRID; 113361; 1076. DR CORUM; P31946; -. DR DIP; DIP-743N; -. DR ELM; P31946; -. DR IntAct; P31946; 651. DR MINT; P31946; -. DR STRING; 9606.ENSP00000361930; -. DR BindingDB; P31946; -. DR ChEMBL; CHEMBL3710403; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyGen; P31946; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P31946; -. DR MetOSite; P31946; -. DR PhosphoSitePlus; P31946; -. DR SwissPalm; P31946; -. DR BioMuta; YWHAB; -. DR DMDM; 1345590; -. DR OGP; P31946; -. DR REPRODUCTION-2DPAGE; IPI00216318; -. DR CPTAC; CPTAC-142; -. DR EPD; P31946; -. DR jPOST; P31946; -. DR MassIVE; P31946; -. DR MaxQB; P31946; -. DR PaxDb; 9606-ENSP00000361930; -. DR PeptideAtlas; P31946; -. DR PRIDE; P31946; -. DR ProteomicsDB; 54816; -. DR ProteomicsDB; 54817; -. [P31946-2] DR Pumba; P31946; -. DR TopDownProteomics; P31946-1; -. [P31946-1] DR TopDownProteomics; P31946-2; -. [P31946-2] DR Antibodypedia; 1906; 847 antibodies from 46 providers. DR CPTC; P31946; 3 antibodies. DR DNASU; 7529; -. DR Ensembl; ENST00000353703.9; ENSP00000300161.4; ENSG00000166913.13. [P31946-1] DR Ensembl; ENST00000372839.7; ENSP00000361930.3; ENSG00000166913.13. [P31946-1] DR GeneID; 7529; -. DR KEGG; hsa:7529; -. DR MANE-Select; ENST00000353703.9; ENSP00000300161.4; NM_139323.4; NP_647539.1. DR AGR; HGNC:12849; -. DR CTD; 7529; -. DR DisGeNET; 7529; -. DR GeneCards; YWHAB; -. DR HGNC; HGNC:12849; YWHAB. DR HPA; ENSG00000166913; Low tissue specificity. DR MIM; 601289; gene. DR neXtProt; NX_P31946; -. DR OpenTargets; ENSG00000166913; -. DR PharmGKB; PA37438; -. DR VEuPathDB; HostDB:ENSG00000166913; -. DR eggNOG; KOG0841; Eukaryota. DR GeneTree; ENSGT01090000260040; -. DR HOGENOM; CLU_058290_1_0_1; -. DR InParanoid; P31946; -. DR OMA; EQHVTII; -. DR OrthoDB; 920089at2759; -. DR PhylomeDB; P31946; -. DR TreeFam; TF102003; -. DR PathwayCommons; P31946; -. 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-165159; MTOR signalling. DR Reactome; R-HSA-166208; mTORC1-mediated signalling. DR Reactome; R-HSA-170968; Frs2-mediated activation. DR Reactome; R-HSA-170984; ARMS-mediated activation. DR Reactome; R-HSA-2028269; Signaling by Hippo. DR Reactome; R-HSA-392517; Rap1 signalling. DR Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA. DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA. DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-5673000; RAF activation. DR Reactome; R-HSA-5674135; MAP2K and MAPK activation. DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway. DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants. DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF. DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR Reactome; R-HSA-9614399; Regulation of localization of FOXO transcription factors. DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants. DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants. DR Reactome; R-HSA-9726840; SHOC2 M1731 mutant abolishes MRAS complex function. DR Reactome; R-HSA-9726842; Gain-of-function MRAS complexes activate RAF signaling. 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; P31946; -. DR SIGNOR; P31946; -. DR BioGRID-ORCS; 7529; 19 hits in 1156 CRISPR screens. DR ChiTaRS; YWHAB; human. DR EvolutionaryTrace; P31946; -. DR GeneWiki; YWHAB; -. DR GenomeRNAi; 7529; -. DR Pharos; P31946; Tbio. DR PRO; PR:P31946; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P31946; Protein. DR Bgee; ENSG00000166913; Expressed in endothelial cell and 214 other cell types or tissues. DR ExpressionAtlas; P31946; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL. DR GO; GO:0050815; F:phosphoserine residue binding; IPI:BHF-UCL. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB. DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:BHF-UCL. DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:BHF-UCL. DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:BHF-UCL. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd10022; 14-3-3_beta_zeta; 1. DR Gene3D; 1.20.190.20; 14-3-3 domain; 1. DR IDEAL; IID00038; -. 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:SF28; 14-3-3 PROTEIN BETA_ALPHA; 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 Genevisible; P31946; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Cytoplasm; KW Direct protein sequencing; Host-virus interaction; Isopeptide bond; KW Membrane; Nitration; Phosphoprotein; Reference proteome; Ubl conjugation; KW Vacuole. FT CHAIN 1..246 FT /note="14-3-3 protein beta/alpha" FT /id="PRO_0000367900" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..246 FT /note="14-3-3 protein beta/alpha, N-terminally processed" FT /id="PRO_0000000003" FT SITE 58 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250" FT SITE 129 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine; in 14-3-3 protein beta/alpha; FT alternate" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="N-acetylthreonine; in 14-3-3 protein beta/alpha, N- FT terminally processed" FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 5 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 51 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P27348" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV8" FT MOD_RES 70 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 84 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV8" FT MOD_RES 106 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV8" FT MOD_RES 117 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 186 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68251" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 51 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P27348" FT VAR_SEQ 1..2 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000305" FT /id="VSP_018632" FT VARIANT 99 FT /note="V -> I (found in a renal cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064762" FT HELIX 5..17 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 21..32 FT /evidence="ECO:0007829|PDB:8EQ8" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:6GN0" FT HELIX 40..70 FT /evidence="ECO:0007829|PDB:8EQ8" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:5N10" FT HELIX 76..105 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 114..134 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 138..161 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 167..182 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 187..202 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 203..207 FT /evidence="ECO:0007829|PDB:8EQ8" FT TURN 210..213 FT /evidence="ECO:0007829|PDB:8EQ8" FT HELIX 214..231 FT /evidence="ECO:0007829|PDB:8EQ8" FT MOD_RES P31946-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 246 AA; 28082 MW; 6BE1A9BF97468017 CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN //