1433B_HUMAN
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 03-AUG-2022, entry version 238.
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 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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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). {ECO:0000250|UniProtKB:Q9CQV8,
CC ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:11555644,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15454081,
CC ECO:0000269|PubMed:15538381, ECO:0000269|PubMed:15696159,
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}.
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; 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=4; IntAct=EBI-359815, EBI-930964;
CC P31946; Q92934: BAD; NbExp=4; IntAct=EBI-359815, EBI-700771;
CC P31946; P15056: BRAF; NbExp=6; IntAct=EBI-359815, EBI-365980;
CC P31946; P22681: CBL; NbExp=3; IntAct=EBI-359815, EBI-518228;
CC P31946; O00257: CBX4; NbExp=2; 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=5; IntAct=EBI-359815, EBI-974439;
CC P31946; O94921: CDK14; NbExp=5; IntAct=EBI-359815, EBI-1043945;
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=4; IntAct=EBI-359815, EBI-975200;
CC P31946; P55040: GEM; NbExp=4; IntAct=EBI-359815, EBI-744104;
CC P31946; P56524: HDAC4; NbExp=3; 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=2; IntAct=EBI-359815, EBI-307281;
CC P31946; Q99683: MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263;
CC P31946; Q7KZI7: MARK2; NbExp=4; IntAct=EBI-359815, EBI-516560;
CC P31946; P27448: MARK3; NbExp=5; IntAct=EBI-359815, EBI-707595;
CC P31946; P26045: PTPN3; NbExp=5; IntAct=EBI-359815, EBI-1047946;
CC P31946; P04049: RAF1; NbExp=21; 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; 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=4; IntAct=EBI-359815, EBI-396587;
CC P31946; P46937: YAP1; NbExp=6; IntAct=EBI-359815, EBI-1044059;
CC P31946; P31946: YWHAB; NbExp=3; IntAct=EBI-359815, EBI-359815;
CC P31946; P62258: YWHAE; NbExp=6; IntAct=EBI-359815, EBI-356498;
CC P31946; P61981: YWHAG; NbExp=3; IntAct=EBI-359815, EBI-359832;
CC P31946; P27348: YWHAQ; NbExp=3; 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}.
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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. [P31946-1]
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 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 AlphaFoldDB; P31946; -.
DR SASBDB; P31946; -.
DR SMR; P31946; -.
DR BioGRID; 113361; 770.
DR CORUM; P31946; -.
DR DIP; DIP-743N; -.
DR ELM; P31946; -.
DR IntAct; P31946; 472.
DR MINT; P31946; -.
DR STRING; 9606.ENSP00000361930; -.
DR BindingDB; P31946; -.
DR ChEMBL; CHEMBL3710403; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
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; P31946; -.
DR PeptideAtlas; P31946; -.
DR PRIDE; P31946; -.
DR ProteomicsDB; 54816; -.
DR ProteomicsDB; 54817; -. [P31946-2]
DR TopDownProteomics; P31946-1; -. [P31946-1]
DR TopDownProteomics; P31946-2; -. [P31946-2]
DR Antibodypedia; 1906; 727 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 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; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P31946; -.
DR OMA; KGCQLAR; -.
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-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SignaLink; P31946; -.
DR SIGNOR; P31946; -.
DR BioGRID-ORCS; 7529; 18 hits in 1077 CRISPR screens.
DR ChiTaRS; YWHAB; human.
DR EvolutionaryTrace; P31946; -.
DR GeneWiki; YWHAB; -.
DR GenomeRNAi; 7529; -.
DR Pharos; P31946; Tchem.
DR PRO; PR:P31946; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P31946; protein.
DR Bgee; ENSG00000166913; Expressed in endothelial cell and 212 other tissues.
DR ExpressionAtlas; P31946; baseline and differential.
DR Genevisible; P31946; HS.
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:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 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; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative 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:5N10"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:5N10"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6GN0"
FT HELIX 40..70
FT /evidence="ECO:0007829|PDB:5N10"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 78..105
FT /evidence="ECO:0007829|PDB:5N10"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 114..134
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 137..161
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:5N10"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5N10"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:5N10"
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
