ID   1433B_HUMAN             Reviewed;         246 AA.
AC   P31946;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-APR-2008, entry version 95.
DE   14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1)
DE   (KCIP-1) (Protein 1054).
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   MEDLINE=93294871; 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 GENOMIC DNA].
RX   MEDLINE=21638749; 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   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 3-20.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; 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   [5]
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   [6]
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   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. 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.
CC   -!- SUBUNIT: Homodimer. Interacts with SSH1 and TORC2/CRTC2.
CC   -!- INTERACTION:
CC       Q9P0K1-1:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567258;
CC       Q9P0K1-3:ADAM22; NbExp=1; IntAct=EBI-359815, EBI-1567267;
CC       Q12802:AKAP13; NbExp=1; IntAct=EBI-359815, EBI-1373806;
CC       O43521:BCL2L11; NbExp=1; IntAct=EBI-359815, EBI-526406;
CC       P15056:BRAF; NbExp=1; IntAct=EBI-359815, EBI-365980;
CC       P46527:CDKN1B; NbExp=1; IntAct=EBI-359815, EBI-519280;
CC       Q9P2M7:CGN; NbExp=1; IntAct=EBI-359815, EBI-79537;
CC       P68400:CSNK2A1; NbExp=1; IntAct=EBI-359815, EBI-347804;
CC       Q7Z401:DENND4A; NbExp=1; IntAct=EBI-359815, EBI-1046479;
CC       Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621;
CC       Q96F86:EDC3; NbExp=1; IntAct=EBI-359815, EBI-997311;
CC       Q9Y2J2:EPB41L3; NbExp=1; IntAct=EBI-359815, EBI-310986;
CC       Q96TC7:FAM82C; NbExp=1; IntAct=EBI-359815, EBI-1056589;
CC       Q9Y4H2:IRS2; NbExp=1; IntAct=EBI-359815, EBI-1049582;
CC       Q02241:KIF23; NbExp=1; IntAct=EBI-359815, EBI-306852;
CC       P33176:KIF5B; NbExp=1; IntAct=EBI-359815, EBI-355878;
CC       Q07866:KLC1; NbExp=1; IntAct=EBI-359815, EBI-721019;
CC       Q6PKG0:LARP1; NbExp=1; IntAct=EBI-359815, EBI-1052114;
CC       P27448:MARK3; NbExp=1; IntAct=EBI-359815, EBI-707595;
CC       Q6WCQ1:MRIP; NbExp=1; IntAct=EBI-359815, EBI-1022605;
CC       Q9Y2A7:NCKAP1; NbExp=1; IntAct=EBI-359815, EBI-389845;
CC       Q9H4L5:OSBPL3; NbExp=1; IntAct=EBI-359815, EBI-1051317;
CC       Q8TEW0:PARD3; NbExp=1; IntAct=EBI-359815, EBI-81968;
CC       O94921:PFTK1; NbExp=5; IntAct=EBI-359815, EBI-1043945;
CC       Q9UBF8:PIK4CB; NbExp=1; IntAct=EBI-359815, EBI-1053214;
CC       Q9UJ41:RABGEF1; NbExp=1; IntAct=EBI-359815, EBI-913954;
CC       Q9H0H5:RACGAP1; NbExp=1; IntAct=EBI-359815, EBI-717233;
CC       P04049:RAF1; NbExp=4; IntAct=EBI-359815, EBI-365996;
CC       Q9P0K7:RAI14; NbExp=1; IntAct=EBI-359815, EBI-1023749;
CC       Q5PRF9:SAMD4B; NbExp=1; IntAct=EBI-359815, EBI-1047489;
CC       Q9Y6M7:SLC4A7; NbExp=1; IntAct=EBI-359815, EBI-1044546;
CC       Q9UQ35:SRRM2; NbExp=1; IntAct=EBI-359815, EBI-1050142;
CC       Q9UDY2:TJP2; NbExp=1; IntAct=EBI-359815, EBI-1042602;
CC       P40818:USP8; NbExp=1; IntAct=EBI-359815, EBI-1050865;
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: Isoform alpha differs from isoform beta in being
CC       phosphorylated (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; AL008725; CAA15497.1; -; Genomic_DNA.
DR   EMBL; BC001359; AAH01359.1; -; mRNA.
DR   PIR; S34755; S34755.
DR   RefSeq; NP_003395.1; -.
DR   RefSeq; NP_647539.1; -.
DR   UniGene; Hs.651212; -.
DR   PDB; 2BQ0; X-ray; 2.50 A; A/B=1-239.
DR   PDB; 2C23; X-ray; 2.65 A; A=1-239.
DR   PDBsum; 2BQ0; -.
DR   PDBsum; 2C23; -.
DR   DIP; DIP:743N; -.
DR   IntAct; P31946; -.
DR   PhosphoSite; P31946; -.
DR   Cornea-2DPAGE; P31946; -.
DR   OGP; P31946; -.
DR   REPRODUCTION-2DPAGE; IPI00216318; -.
DR   Ensembl; ENSG00000166913; Homo sapiens.
DR   GeneID; 7529; -.
DR   KEGG; hsa:7529; -.
DR   H-InvDB; HIX0015846; -.
DR   HGNC; HGNC:12849; YWHAB.
DR   HPA; CAB003759; -.
DR   MIM; 601289; gene.
DR   PharmGKB; PA37438; -.
DR   Reactome; REACT_578; Apoptosis.
DR   ArrayExpress; P31946; -.
DR   CleanEx; HS_YWHAB; -.
DR   GermOnline; ENSG00000166913; Homo sapiens.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR000308; 14-3-3.
DR   Gene3D; G3DSA:1.20.190.20; 14-3-3; 1.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   ProDom; PD000600; 14-3-3; 1.
DR   SMART; SM00101; 14_3_3; 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; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    246       14-3-3 protein beta/alpha.
FT                                /FTId=PRO_0000000003.
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   VAR_SEQ       1      2       Missing (in isoform Short).
FT                                /FTId=VSP_018632.
FT   HELIX         5     17
FT   HELIX        21     32
FT   HELIX        40     67
FT   HELIX        75    105
FT   HELIX       107    110
FT   HELIX       114    133
FT   HELIX       138    161
FT   HELIX       167    182
FT   HELIX       187    202
FT   HELIX       203    207
FT   TURN        210    212
FT   HELIX       213    231
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
//