Full text data of YWHAB
YWHAB
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
14-3-3 protein beta/alpha (Protein 1054; Protein kinase C inhibitor protein 1; KCIP-1; 14-3-3 protein beta/alpha, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
14-3-3 protein beta/alpha (Protein 1054; Protein kinase C inhibitor protein 1; KCIP-1; 14-3-3 protein beta/alpha, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P31946
ID 1433B_HUMAN Reviewed; 246 AA.
AC P31946; A8K9K2; E1P616;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 160.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Walbum E., 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
RT been 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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 MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
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-
RT 3-3-binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 [12]
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.,
RA Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G.,
RA Lai Z.C., Guan K.L.;
RT "Inactivation of YAP oncoprotein by the Hippo pathway is involved in
RT cell contact inhibition and tissue growth control.";
RL Genes Dev. 21:2747-2761(2007).
RN [13]
RP INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND
RP 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-
RT 3(beta) phosphorylation and promotes osteoblast differentiation and
RT bone formation.";
RL Mol. Endocrinol. 21:3050-3061(2007).
RN [14]
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.,
RA Guilhaus M., James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT the Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [15]
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
RT cycle and cell death in neurons.";
RL J. Biol. Chem. 284:24512-24525(2009).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [18]
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.,
RA Buerckstuemmer T., 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, AND MASS
RP SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, MASS SPECTROMETRY,
RP 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
RT protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
RN [21]
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.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene 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
CC to a large number of partners, usually by recognition of a
CC phosphoserine or phosphothreonine motif. Binding generally results
CC in the modulation of the activity of the binding partner. Negative
CC regulator of osteogenesis. Blocks the nuclear translocation of the
CC phosphorylated form (by AKT1) of SRPK2 and antagonizes its
CC stimulatory effect on cyclin D1 expression resulting in blockage
CC of neuronal apoptosis elicited by SRPK2.
CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 and PRKCE (By
CC similarity). Interacts with SSH1 and TORC2/CRTC2. Interacts with
CC ABL1; the interaction results in cytoplasmic location of ABL1 and
CC inhibition of cABL-mediated apoptosis. Interacts with ROR2
CC (dimer); the interaction results in phosphorylation of YWHAB on
CC tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated
CC form). Interacts with the phosphorylated (by AKT1) form of SRPK2.
CC Interacts with PKA-phosphorylated AANAT.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=3; IntAct=EBI-359815, EBI-6248077;
CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567267;
CC P15056:BRAF; NbExp=3; IntAct=EBI-359815, EBI-365980;
CC P22681:CBL; NbExp=3; IntAct=EBI-359815, EBI-518228;
CC O00257:CBX4; NbExp=2; IntAct=EBI-359815, EBI-722425;
CC P30304:CDC25A; NbExp=8; IntAct=EBI-359815, EBI-747671;
CC P30305:CDC25B; NbExp=4; IntAct=EBI-359815, EBI-1051746;
CC O94921:CDK14; NbExp=5; IntAct=EBI-359815, EBI-1043945;
CC P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7540603;
CC Q9NYF0:DACT1; NbExp=4; IntAct=EBI-359815, EBI-3951744;
CC Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621;
CC Q9UQC2:GAB2; NbExp=4; IntAct=EBI-359815, EBI-975200;
CC P55040:GEM; NbExp=3; IntAct=EBI-359815, EBI-744104;
CC P55041:Gem (xeno); NbExp=3; IntAct=EBI-359815, EBI-7082069;
CC P56524:HDAC4; NbExp=3; IntAct=EBI-359815, EBI-308629;
CC P08069:IGF1R; NbExp=3; IntAct=EBI-359815, EBI-475981;
CC Q11184:let-756 (xeno); NbExp=2; IntAct=EBI-359815, EBI-3843983;
CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-359815, EBI-5323863;
CC Q99683:MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263;
CC Q7KZI7:MARK2; NbExp=3; IntAct=EBI-359815, EBI-516560;
CC P27448:MARK3; NbExp=4; IntAct=EBI-359815, EBI-707595;
CC P04049:RAF1; NbExp=17; IntAct=EBI-359815, EBI-365996;
CC P61587:RND3; NbExp=2; IntAct=EBI-359815, EBI-1111534;
CC P61588:Rnd3 (xeno); NbExp=5; IntAct=EBI-359815, EBI-6930266;
CC P78362:SRPK2; NbExp=2; IntAct=EBI-359815, EBI-593303;
CC Q8WYL5:SSH1; NbExp=3; IntAct=EBI-359815, EBI-1222387;
CC Q91YE8:Synpo2 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7623057;
CC P49815:TSC2; NbExp=5; IntAct=EBI-359815, EBI-396587;
CC P46937:YAP1; NbExp=4; IntAct=EBI-359815, EBI-1044059;
CC P62258:YWHAE; NbExp=3; IntAct=EBI-359815, EBI-356498;
CC P22893:Zfp36 (xeno); NbExp=5; IntAct=EBI-359815, EBI-647803;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by
CC mass spectrometry in melanosome fractions from stage I to stage
CC IV.
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 Note=Contains a N-acetylmethionine at position 1 (By
CC similarity);
CC -!- PTM: The alpha, brain-specific form differs from the beta form in
CC being phosphorylated (By similarity). Phosphorylated on Ser-60 by
CC protein kinase C delta type catalytic subunit in a sphingosine-
CC dependent fashion (By similarity).
CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR EMBL; X57346; CAA40621.1; -; mRNA.
DR EMBL; AK292717; BAF85406.1; -; mRNA.
DR EMBL; AL008725; CAA15497.1; -; 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 PIR; S34755; S34755.
DR RefSeq; NP_003395.1; NM_003404.4.
DR RefSeq; NP_647539.1; NM_139323.3.
DR UniGene; Hs.643544; -.
DR PDB; 2BQ0; X-ray; 2.50 A; A/B=1-239.
DR PDB; 2C23; X-ray; 2.65 A; A=1-239.
DR PDB; 4DNK; X-ray; 2.20 A; A/B=1-246.
DR PDBsum; 2BQ0; -.
DR PDBsum; 2C23; -.
DR PDBsum; 4DNK; -.
DR ProteinModelPortal; P31946; -.
DR SMR; P31946; 1-234.
DR DIP; DIP-743N; -.
DR IntAct; P31946; 240.
DR MINT; MINT-99570; -.
DR STRING; 9606.ENSP00000300161; -.
DR PhosphoSite; P31946; -.
DR DMDM; 1345590; -.
DR OGP; P31946; -.
DR REPRODUCTION-2DPAGE; IPI00216318; -.
DR PaxDb; P31946; -.
DR PRIDE; P31946; -.
DR DNASU; 7529; -.
DR Ensembl; ENST00000353703; ENSP00000300161; ENSG00000166913.
DR Ensembl; ENST00000372839; ENSP00000361930; ENSG00000166913.
DR GeneID; 7529; -.
DR KEGG; hsa:7529; -.
DR UCSC; uc002xmt.3; human.
DR CTD; 7529; -.
DR GeneCards; GC20P043515; -.
DR HGNC; HGNC:12849; YWHAB.
DR HPA; CAB003759; -.
DR HPA; HPA007925; -.
DR HPA; HPA011212; -.
DR MIM; 601289; gene.
DR neXtProt; NX_P31946; -.
DR PharmGKB; PA37438; -.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P31946; -.
DR KO; K16197; -.
DR OMA; MGREYRE; -.
DR OrthoDB; EOG7HHWT3; -.
DR PhylomeDB; P31946; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; P31946; -.
DR ChiTaRS; YWHAB; human.
DR EvolutionaryTrace; P31946; -.
DR GeneWiki; YWHAB; -.
DR GenomeRNAi; 7529; -.
DR NextBio; 29453; -.
DR PRO; PR:P31946; -.
DR ArrayExpress; P31946; -.
DR Bgee; P31946; -.
DR CleanEx; HS_YWHAB; -.
DR Genevestigator; P31946; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:BHF-UCL.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0035329; P:hippo signaling cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nitration; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 246 14-3-3 protein beta/alpha.
FT /FTId=PRO_0000367900.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 246 14-3-3 protein beta/alpha, N-terminally
FT processed.
FT /FTId=PRO_0000000003.
FT SITE 58 58 Interaction with phosphoserine on
FT interacting protein (By similarity).
FT SITE 129 129 Interaction with phosphoserine on
FT interacting protein (By similarity).
FT MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein
FT beta/alpha; alternate.
FT MOD_RES 2 2 N-acetylthreonine; in 14-3-3 protein
FT beta/alpha, N-terminally processed.
FT MOD_RES 60 60 Phosphoserine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine.
FT MOD_RES 84 84 Nitrated tyrosine (By similarity).
FT MOD_RES 106 106 Nitrated tyrosine (By similarity).
FT MOD_RES 117 117 N6-acetyllysine.
FT MOD_RES 186 186 Phosphoserine (By similarity).
FT VAR_SEQ 1 2 Missing (in isoform Short).
FT /FTId=VSP_018632.
FT VARIANT 99 99 V -> I (found in a renal cell carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_064762.
FT HELIX 5 17
FT HELIX 21 33
FT HELIX 40 69
FT HELIX 75 105
FT HELIX 107 110
FT HELIX 114 133
FT HELIX 139 161
FT HELIX 167 182
FT HELIX 187 202
FT HELIX 203 207
FT TURN 210 212
FT HELIX 213 232
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
//
ID 1433B_HUMAN Reviewed; 246 AA.
AC P31946; A8K9K2; E1P616;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 160.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Walbum E., 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
RT been 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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 MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
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-
RT 3-3-binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 [12]
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.,
RA Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G.,
RA Lai Z.C., Guan K.L.;
RT "Inactivation of YAP oncoprotein by the Hippo pathway is involved in
RT cell contact inhibition and tissue growth control.";
RL Genes Dev. 21:2747-2761(2007).
RN [13]
RP INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND
RP 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-
RT 3(beta) phosphorylation and promotes osteoblast differentiation and
RT bone formation.";
RL Mol. Endocrinol. 21:3050-3061(2007).
RN [14]
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.,
RA Guilhaus M., James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT the Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [15]
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
RT cycle and cell death in neurons.";
RL J. Biol. Chem. 284:24512-24525(2009).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [18]
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.,
RA Buerckstuemmer T., 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, AND MASS
RP SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, MASS SPECTROMETRY,
RP 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
RT protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
RN [21]
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.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene 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
CC to a large number of partners, usually by recognition of a
CC phosphoserine or phosphothreonine motif. Binding generally results
CC in the modulation of the activity of the binding partner. Negative
CC regulator of osteogenesis. Blocks the nuclear translocation of the
CC phosphorylated form (by AKT1) of SRPK2 and antagonizes its
CC stimulatory effect on cyclin D1 expression resulting in blockage
CC of neuronal apoptosis elicited by SRPK2.
CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 and PRKCE (By
CC similarity). Interacts with SSH1 and TORC2/CRTC2. Interacts with
CC ABL1; the interaction results in cytoplasmic location of ABL1 and
CC inhibition of cABL-mediated apoptosis. Interacts with ROR2
CC (dimer); the interaction results in phosphorylation of YWHAB on
CC tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated
CC form). Interacts with the phosphorylated (by AKT1) form of SRPK2.
CC Interacts with PKA-phosphorylated AANAT.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=3; IntAct=EBI-359815, EBI-6248077;
CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567267;
CC P15056:BRAF; NbExp=3; IntAct=EBI-359815, EBI-365980;
CC P22681:CBL; NbExp=3; IntAct=EBI-359815, EBI-518228;
CC O00257:CBX4; NbExp=2; IntAct=EBI-359815, EBI-722425;
CC P30304:CDC25A; NbExp=8; IntAct=EBI-359815, EBI-747671;
CC P30305:CDC25B; NbExp=4; IntAct=EBI-359815, EBI-1051746;
CC O94921:CDK14; NbExp=5; IntAct=EBI-359815, EBI-1043945;
CC P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7540603;
CC Q9NYF0:DACT1; NbExp=4; IntAct=EBI-359815, EBI-3951744;
CC Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621;
CC Q9UQC2:GAB2; NbExp=4; IntAct=EBI-359815, EBI-975200;
CC P55040:GEM; NbExp=3; IntAct=EBI-359815, EBI-744104;
CC P55041:Gem (xeno); NbExp=3; IntAct=EBI-359815, EBI-7082069;
CC P56524:HDAC4; NbExp=3; IntAct=EBI-359815, EBI-308629;
CC P08069:IGF1R; NbExp=3; IntAct=EBI-359815, EBI-475981;
CC Q11184:let-756 (xeno); NbExp=2; IntAct=EBI-359815, EBI-3843983;
CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-359815, EBI-5323863;
CC Q99683:MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263;
CC Q7KZI7:MARK2; NbExp=3; IntAct=EBI-359815, EBI-516560;
CC P27448:MARK3; NbExp=4; IntAct=EBI-359815, EBI-707595;
CC P04049:RAF1; NbExp=17; IntAct=EBI-359815, EBI-365996;
CC P61587:RND3; NbExp=2; IntAct=EBI-359815, EBI-1111534;
CC P61588:Rnd3 (xeno); NbExp=5; IntAct=EBI-359815, EBI-6930266;
CC P78362:SRPK2; NbExp=2; IntAct=EBI-359815, EBI-593303;
CC Q8WYL5:SSH1; NbExp=3; IntAct=EBI-359815, EBI-1222387;
CC Q91YE8:Synpo2 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7623057;
CC P49815:TSC2; NbExp=5; IntAct=EBI-359815, EBI-396587;
CC P46937:YAP1; NbExp=4; IntAct=EBI-359815, EBI-1044059;
CC P62258:YWHAE; NbExp=3; IntAct=EBI-359815, EBI-356498;
CC P22893:Zfp36 (xeno); NbExp=5; IntAct=EBI-359815, EBI-647803;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by
CC mass spectrometry in melanosome fractions from stage I to stage
CC IV.
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 Note=Contains a N-acetylmethionine at position 1 (By
CC similarity);
CC -!- PTM: The alpha, brain-specific form differs from the beta form in
CC being phosphorylated (By similarity). Phosphorylated on Ser-60 by
CC protein kinase C delta type catalytic subunit in a sphingosine-
CC dependent fashion (By similarity).
CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR EMBL; X57346; CAA40621.1; -; mRNA.
DR EMBL; AK292717; BAF85406.1; -; mRNA.
DR EMBL; AL008725; CAA15497.1; -; 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 PIR; S34755; S34755.
DR RefSeq; NP_003395.1; NM_003404.4.
DR RefSeq; NP_647539.1; NM_139323.3.
DR UniGene; Hs.643544; -.
DR PDB; 2BQ0; X-ray; 2.50 A; A/B=1-239.
DR PDB; 2C23; X-ray; 2.65 A; A=1-239.
DR PDB; 4DNK; X-ray; 2.20 A; A/B=1-246.
DR PDBsum; 2BQ0; -.
DR PDBsum; 2C23; -.
DR PDBsum; 4DNK; -.
DR ProteinModelPortal; P31946; -.
DR SMR; P31946; 1-234.
DR DIP; DIP-743N; -.
DR IntAct; P31946; 240.
DR MINT; MINT-99570; -.
DR STRING; 9606.ENSP00000300161; -.
DR PhosphoSite; P31946; -.
DR DMDM; 1345590; -.
DR OGP; P31946; -.
DR REPRODUCTION-2DPAGE; IPI00216318; -.
DR PaxDb; P31946; -.
DR PRIDE; P31946; -.
DR DNASU; 7529; -.
DR Ensembl; ENST00000353703; ENSP00000300161; ENSG00000166913.
DR Ensembl; ENST00000372839; ENSP00000361930; ENSG00000166913.
DR GeneID; 7529; -.
DR KEGG; hsa:7529; -.
DR UCSC; uc002xmt.3; human.
DR CTD; 7529; -.
DR GeneCards; GC20P043515; -.
DR HGNC; HGNC:12849; YWHAB.
DR HPA; CAB003759; -.
DR HPA; HPA007925; -.
DR HPA; HPA011212; -.
DR MIM; 601289; gene.
DR neXtProt; NX_P31946; -.
DR PharmGKB; PA37438; -.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P31946; -.
DR KO; K16197; -.
DR OMA; MGREYRE; -.
DR OrthoDB; EOG7HHWT3; -.
DR PhylomeDB; P31946; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; P31946; -.
DR ChiTaRS; YWHAB; human.
DR EvolutionaryTrace; P31946; -.
DR GeneWiki; YWHAB; -.
DR GenomeRNAi; 7529; -.
DR NextBio; 29453; -.
DR PRO; PR:P31946; -.
DR ArrayExpress; P31946; -.
DR Bgee; P31946; -.
DR CleanEx; HS_YWHAB; -.
DR Genevestigator; P31946; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:BHF-UCL.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0035329; P:hippo signaling cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nitration; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 246 14-3-3 protein beta/alpha.
FT /FTId=PRO_0000367900.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 246 14-3-3 protein beta/alpha, N-terminally
FT processed.
FT /FTId=PRO_0000000003.
FT SITE 58 58 Interaction with phosphoserine on
FT interacting protein (By similarity).
FT SITE 129 129 Interaction with phosphoserine on
FT interacting protein (By similarity).
FT MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein
FT beta/alpha; alternate.
FT MOD_RES 2 2 N-acetylthreonine; in 14-3-3 protein
FT beta/alpha, N-terminally processed.
FT MOD_RES 60 60 Phosphoserine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine.
FT MOD_RES 84 84 Nitrated tyrosine (By similarity).
FT MOD_RES 106 106 Nitrated tyrosine (By similarity).
FT MOD_RES 117 117 N6-acetyllysine.
FT MOD_RES 186 186 Phosphoserine (By similarity).
FT VAR_SEQ 1 2 Missing (in isoform Short).
FT /FTId=VSP_018632.
FT VARIANT 99 99 V -> I (found in a renal cell carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_064762.
FT HELIX 5 17
FT HELIX 21 33
FT HELIX 40 69
FT HELIX 75 105
FT HELIX 107 110
FT HELIX 114 133
FT HELIX 139 161
FT HELIX 167 182
FT HELIX 187 202
FT HELIX 203 207
FT TURN 210 212
FT HELIX 213 232
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
//
MIM
601289
*RECORD*
*FIELD* NO
601289
*FIELD* TI
*601289 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN,
BETA ISOFORM; YWHAB
read more;;BRAIN PROTEIN 14-3-3, BETA ISOFORM;;
14-3-3-BETA
*FIELD* TX
CLONING
The highly conserved 14-3-3 proteins are found in both plants and
mammals; see YWHAH (113508) and YWHAZ (601288). Some have been shown to
be involved in the activation of c-Raf (164760) by their participation
in the protein kinase C signaling pathway (see 176960). Leffers et al.
(1993) reported the cloning of 14-3-3 beta.
GENE FUNCTION
The 14-3-3 family of proteins mediates signal transduction by binding to
phosphoserine-containing proteins. Using phosphoserine-oriented peptide
libraries to probe all mammalian and yeast 14-3-3s, Yaffe et al. (1997)
identified 2 different binding motifs, RSXpSXP and RXY/FXpSXP, present
in nearly all known 14-3-3 binding proteins. The crystal structure of
YWHAZ complexed with the phosphoserine motif in polyoma middle-T was
determined to 2.6-angstrom resolution. The authors showed that the
14-3-3 dimer binds tightly to single molecules containing tandem repeats
of phosphoserine motifs, implicating bidentate association as a
signaling mechanism with molecules such as Raf, BAD (603167), and Cbl.
Using 2-hybrid experiments, Han et al. (1997) demonstrated interaction
between murine Ywhab and the RAS-binding domain of RIN1 (605965).
Shumway et al. (2003) found that 14-3-3-beta interacts with the TSC1
(605284)-TSC2 (191092) dimer. The interaction required phosphorylation
of TSC2 at ser1210. Binding of 14-3-3-beta to TSC2 did not alter the
interaction between TSC1 and TSC2, but it reduced the ability of the
complex to inhibit phosphorylation of ribosomal protein S6 kinase
(608938), impairing the ability of the complex to inhibit cell growth.
MAPPING
Tommerup and Leffers (1996) mapped the YWHAB gene to 20q13.1 by
fluorescence in situ hybridization.
*FIELD* RF
1. Han, L. Wong, D.; Dhaka, A.; Afar, D.; White, M.; Xie, W.; Herschman,
H.; Witte, O.: Colicelli, J.: Protein binding and signaling properties
of RIN1 suggest a unique effector function. Proc. Nat. Acad. Sci. 94:
4954-4959, 1997.
2. Leffers, H.; Madsen, P.; Rasmussen, H. H.; Honore, B.; Andersen,
A. H.; Walbum, E.; Vandekerckhove, J.; Celis, J. E.: Molecular cloning
and expression of the transformation sensitive epithelial marker stratifin:
a member of a protein family that has been involved in the protein
kinase C signalling pathway. J. Molec. Biol. 231: 982-998, 1993.
3. Shumway, S. D.; Li, Y.; Xiong, Y.: 14-3-3-beta binds to and negatively
regulates the tuberous sclerosis complex 2 (TSC2) tumor suppressor
gene product, tuberin. J. Biol. Chem. 278: 2089-2092, 2003.
4. Tommerup, N.; Leffers, H.: Assignment of the human genes encoding
14-3-3 eta (YWHAH) to 22q12, 14-3-3 zeta (YWHAZ) to 2p25.1-p25.2,
and 14-3-3 beta (YWHAB) to 20q13.1 by in situ hybridization. Genomics 33:
149-150, 1996.
5. Yaffe, M. B.; Rittinger, K.; Volinia, S.; Caron, P. R.; Aitken,
A.; Leffers, H.; Gamblin, S. J.; Smerdon, S. J.; Cantley, L. C.:
The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91:
961-971, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 2/27/2003
Dawn Watkins-Chow - updated: 5/25/2001
Stylianos E. Antonarakis - updated: 2/20/1998
*FIELD* CD
Alan F. Scott: 6/3/1996
*FIELD* ED
mgross: 09/23/2004
mgross: 2/27/2003
carol: 5/25/2001
mcapotos: 6/23/2000
terry: 11/13/1998
alopez: 10/20/1998
terry: 6/1/1998
dholmes: 2/20/1998
jenny: 4/8/1997
terry: 6/3/1996
mark: 6/3/1996
*RECORD*
*FIELD* NO
601289
*FIELD* TI
*601289 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN,
BETA ISOFORM; YWHAB
read more;;BRAIN PROTEIN 14-3-3, BETA ISOFORM;;
14-3-3-BETA
*FIELD* TX
CLONING
The highly conserved 14-3-3 proteins are found in both plants and
mammals; see YWHAH (113508) and YWHAZ (601288). Some have been shown to
be involved in the activation of c-Raf (164760) by their participation
in the protein kinase C signaling pathway (see 176960). Leffers et al.
(1993) reported the cloning of 14-3-3 beta.
GENE FUNCTION
The 14-3-3 family of proteins mediates signal transduction by binding to
phosphoserine-containing proteins. Using phosphoserine-oriented peptide
libraries to probe all mammalian and yeast 14-3-3s, Yaffe et al. (1997)
identified 2 different binding motifs, RSXpSXP and RXY/FXpSXP, present
in nearly all known 14-3-3 binding proteins. The crystal structure of
YWHAZ complexed with the phosphoserine motif in polyoma middle-T was
determined to 2.6-angstrom resolution. The authors showed that the
14-3-3 dimer binds tightly to single molecules containing tandem repeats
of phosphoserine motifs, implicating bidentate association as a
signaling mechanism with molecules such as Raf, BAD (603167), and Cbl.
Using 2-hybrid experiments, Han et al. (1997) demonstrated interaction
between murine Ywhab and the RAS-binding domain of RIN1 (605965).
Shumway et al. (2003) found that 14-3-3-beta interacts with the TSC1
(605284)-TSC2 (191092) dimer. The interaction required phosphorylation
of TSC2 at ser1210. Binding of 14-3-3-beta to TSC2 did not alter the
interaction between TSC1 and TSC2, but it reduced the ability of the
complex to inhibit phosphorylation of ribosomal protein S6 kinase
(608938), impairing the ability of the complex to inhibit cell growth.
MAPPING
Tommerup and Leffers (1996) mapped the YWHAB gene to 20q13.1 by
fluorescence in situ hybridization.
*FIELD* RF
1. Han, L. Wong, D.; Dhaka, A.; Afar, D.; White, M.; Xie, W.; Herschman,
H.; Witte, O.: Colicelli, J.: Protein binding and signaling properties
of RIN1 suggest a unique effector function. Proc. Nat. Acad. Sci. 94:
4954-4959, 1997.
2. Leffers, H.; Madsen, P.; Rasmussen, H. H.; Honore, B.; Andersen,
A. H.; Walbum, E.; Vandekerckhove, J.; Celis, J. E.: Molecular cloning
and expression of the transformation sensitive epithelial marker stratifin:
a member of a protein family that has been involved in the protein
kinase C signalling pathway. J. Molec. Biol. 231: 982-998, 1993.
3. Shumway, S. D.; Li, Y.; Xiong, Y.: 14-3-3-beta binds to and negatively
regulates the tuberous sclerosis complex 2 (TSC2) tumor suppressor
gene product, tuberin. J. Biol. Chem. 278: 2089-2092, 2003.
4. Tommerup, N.; Leffers, H.: Assignment of the human genes encoding
14-3-3 eta (YWHAH) to 22q12, 14-3-3 zeta (YWHAZ) to 2p25.1-p25.2,
and 14-3-3 beta (YWHAB) to 20q13.1 by in situ hybridization. Genomics 33:
149-150, 1996.
5. Yaffe, M. B.; Rittinger, K.; Volinia, S.; Caron, P. R.; Aitken,
A.; Leffers, H.; Gamblin, S. J.; Smerdon, S. J.; Cantley, L. C.:
The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91:
961-971, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 2/27/2003
Dawn Watkins-Chow - updated: 5/25/2001
Stylianos E. Antonarakis - updated: 2/20/1998
*FIELD* CD
Alan F. Scott: 6/3/1996
*FIELD* ED
mgross: 09/23/2004
mgross: 2/27/2003
carol: 5/25/2001
mcapotos: 6/23/2000
terry: 11/13/1998
alopez: 10/20/1998
terry: 6/1/1998
dholmes: 2/20/1998
jenny: 4/8/1997
terry: 6/3/1996
mark: 6/3/1996