P31946 (1433B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
14-3-3 protein beta/alpha

Alternative name(s):
Protein 1054
Protein kinase C inhibitor protein 1
Short name=KCIP-1

Cleaved into the following chain:

1. 14-3-3 protein beta/alpha, N-terminally processed

Gene names

Name:

YWHAB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. 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. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Ref.13 Ref.15
Subunit structure	Homodimer. Interacts with SAMSN1 and KRPCE By similarity. Interacts with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis. Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated form). Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts with PKA-phosphorylated AANAT. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19
Subcellular location	Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.11
Post-translational modification	The alpha, brain-specific form differs from the beta form in being phosphorylated By similarity. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion By similarity. Ref.13 Isoform Short contains a N-acetylmethionine at position 1 By similarity.
Sequence similarities	Belongs to the 14-3-3 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Traceable author statement. Source: Reactome Ras protein signal transduction Traceable author statement. Source: Reactome activation of MAPKK activity Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome cytoplasmic sequestering of protein Inferred from direct assay PubMed 10869435. Source: BHF-UCL epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome hippo signaling cascade Traceable author statement. Source: Reactome insulin receptor signaling pathway Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of protein dephosphorylation Inferred from direct assay PubMed 17255105. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome protein heterooligomerization Inferred from electronic annotation. Source: Compara protein targeting Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay PubMed 12963375. Source: UniProtKB transcriptional repressor complex Inferred from electronic annotation. Source: Compara
Molecular_function	transcription corepressor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q76353	3	EBI-359815,EBI-6248077	From a different organism.
ADAM22	Q9P0K1-3	2	EBI-359815,EBI-1567267
CBX4	O00257	2	EBI-359815,EBI-722425
CDC25A	P30304	8	EBI-359815,EBI-747671
CDK14	O94921	5	EBI-359815,EBI-1043945
DACT1	Q9NYF0	4	EBI-359815,EBI-3951744
DYRK1A	Q13627-2	3	EBI-359815,EBI-1053621
let-756	Q11184	2	EBI-359815,EBI-3843983	From a different organism.
LRRK2	Q5S007	3	EBI-359815,EBI-5323863
MAP3K5	Q99683	3	EBI-359815,EBI-476263
MARK2	Q7KZI7	2	EBI-359815,EBI-516560
MARK3	P27448	2	EBI-359815,EBI-707595
RAF1	P04049	10	EBI-359815,EBI-365996

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Long (identifier: P31946-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P31946-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: Missing.

Note: Contains a N-acetylmethionine at position 1 (By similarity).

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 246

246

14-3-3 protein beta/alpha

PRO_0000367900

Initiator methionine

1

1

Removed; alternate Ref.6

Chain

2 – 246

245

14-3-3 protein beta/alpha, N-terminally processed

PRO_0000000003

Sites

Site

58

1

Interaction with phosphoserine on interacting protein By similarity

Site

129

1

Interaction with phosphoserine on interacting protein By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate Ref.6

Modified residue

2

1

N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed Ref.6

Modified residue

60

1

Phosphoserine By similarity

Modified residue

70

1

N6-acetyllysine Ref.17

Modified residue

117

1

N6-acetyllysine Ref.17

Modified residue

186

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 2

2

Missing in isoform Short.

VSP_018632

Natural variant

99

1

V → I Found in a renal cell carcinoma sample; somatic mutation. Ref.20

VAR_064762

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

246

Helix Strand Turn

Details...

Helix

5 – 17

13

Helix

21 – 33

13

Helix

40 – 69

30

Helix

75 – 105

31

Helix

107 – 110

4

Helix

114 – 133

20

Helix

139 – 161

23

Helix

167 – 182

16

Helix

187 – 202

16

Helix

203 – 207

5

Turn

210 – 212

3

Helix

213 – 232

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6BE1A9BF97468017	FASTA	246	28,082
	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
	Isoform Short [UniParc]. Checksum: CE0A59BF8C33FE2F	FASTA	244	27,850
	10 20 30 40 50 60 MDKSELVQKA KLAEQAERYD DMAAAMKAVT EQGHELSNEE RNLLSVAYKN VVGARRSSWR 70 80 90 100 110 120 VISSIEQKTE RNEKKQQMGK EYREKIEAEL QDICNDVLEL LDKYLIPNAT QPESKVFYLK 130 140 150 160 170 180 MKGDYFRYLS EVASGDNKQT TVSNSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE 190 200 210 220 230 240 ILNSPEKACS LAKTAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG EGEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E. J. Mol. Biol. 231:982-998(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Thymus.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." 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. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[6]	Bienvenut W.V., Zebisch A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: 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, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-20. Tissue: Platelet.
[8]	"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis." Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C. Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AANAT.
[9]	"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector." 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. Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CRTC2.
[10]	"A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia." 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. J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SSH1.
[11]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." 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. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[12]	"Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control." Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L. Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YAP1.
[13]	"Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation." Liu Y., Ross J.F., Bodine P.V.N., Billiard J. Mol. Endocrinol. 21:3050-3061(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, MASS SPECTROMETRY.
[14]	"Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein." Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J. EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GAB2.
[15]	"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons." Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K. J. Biol. Chem. 284:24512-24525(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRPK2.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, MASS SPECTROMETRY.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Structural basis for protein-protein interactions in the 14-3-3 protein family." Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M. Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
[20]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ILE-99.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57346 mRNA. Translation: CAA40621.1.
AK292717 mRNA. Translation: BAF85406.1.
AL008725 Genomic DNA. Translation: CAA15497.1.
CH471077 Genomic DNA. Translation: EAW75893.1.
CH471077 Genomic DNA. Translation: EAW75894.1.
CH471077 Genomic DNA. Translation: EAW75896.1.
BC001359 mRNA. Translation: AAH01359.1.

IPI

IPI00216318.
IPI00759832.

PIR

S34755.

RefSeq

NP_003395.1. NM_003404.3.
NP_647539.1. NM_139323.2.

UniGene

Hs.643544.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BQ0	X-ray	2.50	A/B	1-239	[»]
2C23	X-ray	2.65	A	1-239	[»]
4DNK	X-ray	2.20	A/B	1-246	[»]

ProteinModelPortal

P31946.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-743N.

IntAct

P31946. 54 interactions.

MINT

MINT-99570.

STRING

9606.ENSP00000300161.

PTM databases

PhosphoSite

P31946.

Polymorphism databases

DMDM

1345590.

2D gel databases

OGP

P31946.

REPRODUCTION-2DPAGE

IPI00216318.

Proteomic databases

PaxDb

P31946.

PRIDE

P31946.

Protocols and materials databases

DNASU

7529.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353703; ENSP00000300161; ENSG00000166913.
ENST00000372839; ENSP00000361930; ENSG00000166913.

GeneID

7529.

KEGG

hsa:7529.

UCSC

uc002xmt.3. human.

Organism-specific databases

CTD

7529.

GeneCards

GC20P043515.

HGNC

HGNC:12849. YWHAB.

HPA

CAB003759.
HPA007925.
HPA011212.

MIM

601289. gene.

neXtProt

NX_P31946.

PharmGKB

PA37438.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5040.

HOGENOM

HOG000240379.

HOVERGEN

HBG050423.

InParanoid

P31946.

KO

K16197.

OMA

CNDVLXT.

OrthoDB

EOG4N30PR.

PhylomeDB

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_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_21257. Metabolism of RNA.
REACT_578. Apoptosis.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P31946.

Bgee

P31946.

CleanEx

HS_YWHAB.

Genevestigator

P31946.

GermOnline

ENSG00000166913. Homo sapiens.

Family and domain databases

Gene3D

1.20.190.20. 1 hit.

InterPro

IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]

PANTHER

PTHR18860. PTHR18860. 1 hit.

Pfam

PF00244. 14-3-3. 1 hit.
[Graphical view]

PIRSF

PIRSF000868. 14-3-3. 1 hit.

PRINTS

PR00305. 1433ZETA.

SMART

SM00101. 14_3_3. 1 hit.
[Graphical view]

SUPFAM

SSF48445. 14-3-3. 1 hit.

PROSITE

PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

YWHAB. human.

EvolutionaryTrace

P31946.

GenomeRNAi

7529.

NextBio

29453.

SOURCE

Search...

Entry information

Entry name

1433B_HUMAN

Accession

Primary (citable) accession number: P31946
Secondary accession number(s): A8K9K2, E1P616

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.