[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Keratinocyte; DOI=10.1006/jmbi.1993.1346; PubMed=8515476 [NCBI, ExPASy, EBI, Israel, Japan] 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. Mol. Biol. 231:982-998(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan] Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; "The DNA sequence and comparative analysis of human chromosome 20."; Nature 414:865-871(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND MASS SPECTROMETRY. TISSUE=Colon carcinoma; Bienvenut W.V., Zebisch A., Kolch W.; Submitted (DEC-2008) to UniProtKB.
[5]	PROTEIN SEQUENCE OF 3-20. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[6]	INTERACTION WITH CRTC2. DOI=10.1016/j.cell.2004.09.015; PubMed=15454081 [NCBI, ExPASy, EBI, Israel, Japan] Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.; "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."; Cell 119:61-74(2004).
[7]	INTERACTION WITH SSH1. DOI=10.1083/jcb.200401136; PubMed=15159416 [NCBI, ExPASy, EBI, Israel, Japan] Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."; J. Cell Biol. 165:465-471(2004).
[8]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan] Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."; J. Proteome Res. 5:3135-3144(2006).
[9]	INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND MASS SPECTROMETRY. DOI=10.1210/me.2007-0323; PubMed=17717073 [NCBI, ExPASy, EBI, Israel, Japan] Liu Y., Ross J.F., Bodine P.V.N., Billiard J.; "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation."; Mol. Endocrinol. 21:3050-3061(2007).
[10]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[11]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. DOI=10.1073/pnas.0605779103; PubMed=17085597 [NCBI, ExPASy, EBI, Israel, Japan] Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; "Structural basis for protein-protein interactions in the 14-3-3 protein family."; Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).

Comments

FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathway. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis.
SUBUNIT: Homodimer. Interacts with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhition of cABL-mediated apoptosis. Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues.
INTERACTION:
Q9P0K1-1:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567258;
Q9P0K1-3:ADAM22; NbExp=1; IntAct=EBI-359815, EBI-1567267;
Q12802:AKAP13; NbExp=1; IntAct=EBI-359815, EBI-1373806;
O43521:BCL2L11; NbExp=1; IntAct=EBI-359815, EBI-526406;
P15056:BRAF; NbExp=1; IntAct=EBI-359815, EBI-365980;
P46527:CDKN1B; NbExp=1; IntAct=EBI-359815, EBI-519280;
Q9P2M7:CGN; NbExp=1; IntAct=EBI-359815, EBI-79537;
P68400:CSNK2A1; NbExp=1; IntAct=EBI-359815, EBI-347804;
Q7Z401:DENND4A; NbExp=1; IntAct=EBI-359815, EBI-1046479;
Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621;
Q96F86:EDC3; NbExp=1; IntAct=EBI-359815, EBI-997311;
Q9Y2J2:EPB41L3; NbExp=1; IntAct=EBI-359815, EBI-310986;
Q96TC7:FAM82A2; NbExp=1; IntAct=EBI-359815, EBI-1056589;
O94915:FRYL; NbExp=1; IntAct=EBI-359815, EBI-1104821;
Q9Y4H2:IRS2; NbExp=1; IntAct=EBI-359815, EBI-1049582;
Q02241:KIF23; NbExp=1; IntAct=EBI-359815, EBI-306852;
P33176:KIF5B; NbExp=1; IntAct=EBI-359815, EBI-355878;
Q07866:KLC1; NbExp=1; IntAct=EBI-359815, EBI-721019;
Q6PKG0:LARP1; NbExp=1; IntAct=EBI-359815, EBI-1052114;
P27448:MARK3; NbExp=1; IntAct=EBI-359815, EBI-707595;
Q6WCQ1:MPRIP; NbExp=1; IntAct=EBI-359815, EBI-1022605;
Q9Y2A7:NCKAP1; NbExp=1; IntAct=EBI-359815, EBI-389845;
Q9H4L5:OSBPL3; NbExp=1; IntAct=EBI-359815, EBI-1051317;
Q8TEW0:PARD3; NbExp=1; IntAct=EBI-359815, EBI-81968;
O94921:PFTK1; NbExp=5; IntAct=EBI-359815, EBI-1043945;
Q9UBF8:PI4KB; NbExp=1; IntAct=EBI-359815, EBI-1053214;
Q9UJ41:RABGEF1; NbExp=1; IntAct=EBI-359815, EBI-913954;
Q9H0H5:RACGAP1; NbExp=1; IntAct=EBI-359815, EBI-717233;
P04049:RAF1; NbExp=4; IntAct=EBI-359815, EBI-365996;
Q9P0K7:RAI14; NbExp=1; IntAct=EBI-359815, EBI-1023749;
Q5PRF9:SAMD4B; NbExp=1; IntAct=EBI-359815, EBI-1047489;
Q9Y6M7:SLC4A7; NbExp=1; IntAct=EBI-359815, EBI-1044546;
Q9UQ35:SRRM2; NbExp=1; IntAct=EBI-359815, EBI-1050142;
Q9UDY2:TJP2; NbExp=1; IntAct=EBI-359815, EBI-1042602;
P40818:USP8; NbExp=1; IntAct=EBI-359815, EBI-1050865;
SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.

Name	Long
Isoform ID	P31946-1
This is the isoform sequence displayed in this entry.

Name	Short
Isoform ID	P31946-2
Note: Contains a N-acetylmethionine at position 1 (By similarity).
Features which should be applied to build the isoform sequence: VSP_018632.

PTM: The alpha, brain-specific form differs from the beta form in being phosphorylated (By similarity).
PTM: Isoform Short contains a N-acetylmethionine at position 1 (By similarity).
SIMILARITY: Belongs to the 14-3-3 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X57346; CAA40621.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL008725; CAA15497.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001359; AAH01359.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00216318; -.
IPI00759832; -.

PIR

S34755; S34755.

RefSeq

NP_003395.1; -.
NP_647539.1; -.

UniGene

Hs.643544

3D structure databases

PDB

2BQ0; X-ray; 2.50 A; A/B=1-239.	[ExPASy / RCSB / EBI]
2C23; X-ray; 2.65 A; A=1-239.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2BQ0; -.
2C23; -.

ModBase

P31946.

Protein-protein interaction databases

DIP

DIP:743N; -.

IntAct

P31946; 98.

PTM databases

PhosphoSite

P31946; -.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
foxopathway; FoxO family signaling.
insulin_glucose_pathway; Insulin-mediated glucose transport.
p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classii_pathway; Signaling events mediated by HDAC Class II.
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.

Reactome

REACT_11061; Signalling by NGF.
REACT_498; Signaling by Insulin receptor.
REACT_578; Apoptosis.
REACT_9417; Signaling by EGFR.

2D gel databases

Cornea-2DPAGE

P31946; -.

OGP

P31946; -.

REPRODUCTION-2DPAGE

IPI00216318; -.

Organism-specific databases

GC20P042947; -.

HIX0015846; -.

HGNC:12849; YWHAB.

CAB003759; -.
HPA007925; -.
HPA011212; -.

MIM

601289; gene. [NCBI / EBI]

PharmGKB

PA37438; -.

Gene expression databases

P31946; -.

P31946; -.

HS_YWHAB; -.

ENSG00000166913; Homo sapiens.

Ontologies

GO:0005813;	Cellular component: centrosome (inferred from direct assay from HPA).
GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0042470;	Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0019899;	Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0019904;	Molecular function: protein domain specific binding (inferred from physical interaction from UniProtKB).
GO:0008633;	Biological process: activation of pro-apoptotic gene products (inferred from experiment from Reactome).
GO:0035308;	Biological process: negative regulation of protein amino acid dephosphorylation (inferred from direct assay from UniProtKB).
GO:0043085;	Biological process: positive regulation of catalytic activity (inferred from direct assay from UniProtKB).
GO:0007265;	Biological process: Ras protein signal transduction (inferred from experiment from Reactome).
QuickGo view.

Family and domain databases

InterPro

IPR000308; 14-3-3.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.190.20; 14-3-3; 1.

PANTHER

PTHR18860; 14-3-3; 1.

Pfam

PF00244; 14-3-3; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000868; 14-3-3; 1.

PRINTS

PR00305; 1433ZETA.

ProDom

PD000600; 14-3-3; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00101; 14_3_3; 1.
SMART graphical view of domain structure.

PROSITE

PS00796; 1433_1; 1.
PS00797; 1433_2; 1.

Proteomic databases

PRIDE

P31946; -.

Genome annotation databases

Ensembl

ENSG00000166913; Homo sapiens. [Contig view]

GeneID

7529; -.

KEGG

hsa:7529; -.

Phylogenomic databases

HOGENOM

P31946; -.

HOVERGEN

P31946; -.

OMA

P31946; KESALIM.

Other

29453; -.

YWHAB; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Alternative initiation; Cytoplasm; Direct protein sequencing; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 246`	`246`	`14-3-3 protein beta/alpha.`	`PRO_0000367900`
`INIT_MET`	`1 1`		`Removed; alternate.`
`CHAIN`	`2 246`	`245`	`14-3-3 protein beta/alpha, N-terminally processed.`	`PRO_0000000003`
`SITE`	`58 58`	`1`	`Interaction with phosphoserine on interacting protein (By similarity).`
`SITE`	`129 129`	`1`	`Interaction with phosphoserine on interacting protein (By similarity).`
`MOD_RES`	`1 1`		`N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate.`
`MOD_RES`	`2 2`		`N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed.`
`MOD_RES`	`186 186`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`1 2`		`Missing (in isoform Short).`	`VSP_018632`
`HELIX`	`5 17`	`13`
`HELIX`	`21 32`	`12`
`HELIX`	`40 67`	`28`
`HELIX`	`75 105`	`31`
`HELIX`	`107 110`	`4`
`HELIX`	`114 133`	`20`
`HELIX`	`138 161`	`24`
`HELIX`	`167 182`	`16`
`HELIX`	`187 202`	`16`
`HELIX`	`203 207`	`5`
`TURN`	`210 212`	`3`
`HELIX`	`213 231`	`19`

Sequence information

Length: 246 AA [This is the length of the unprocessed precursor]

Molecular weight: 28082 Da [This is the MW of the unprocessed precursor]

CRC64: 6BE1A9BF97468017 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS 

        70         80         90        100        110        120 
WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY 

       130        140        150        160        170        180 
LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY 

       190        200        210        220        230        240 
YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD 


AGEGEN

P31946 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools