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

Names and origin

Protein names

Recommended name:
    14-3-3 protein beta/alpha
Alternative name(s):
    Protein kinase C inhibitor protein 1
      Short name=KCIP-1
    Protein 1054

Gene names

Name:

YWHAB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 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.
Subunit structure	Homodimer. Interacts with SSH1 and TORC2/CRTC2.
Subcellular location	Cytoplasm. Melanosome. Note= Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Post-translational modification	Isoform alpha differs from isoform beta in being phosphorylated By similarity. 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
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Ras protein signal transduction Inferred from Experiment. Source: Reactome activation of pro-apoptotic gene products Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	protein domain specific binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAM22	Q9P0K1-1	2	EBI-359815,EBI-1567258
ADAM22	Q9P0K1-3	1	EBI-359815,EBI-1567267
AKAP13	Q12802	1	EBI-359815,EBI-1373806
BCL2L11	O43521	1	EBI-359815,EBI-526406
BRAF	P15056	1	EBI-359815,EBI-365980
CDKN1B	P46527	1	EBI-359815,EBI-519280
CGN	Q9P2M7	1	EBI-359815,EBI-79537
CSNK2A1	P68400	1	EBI-359815,EBI-347804
DENND4A	Q7Z401	1	EBI-359815,EBI-1046479
DYRK1A	Q13627-2	3	EBI-359815,EBI-1053621
EDC3	Q96F86	1	EBI-359815,EBI-997311
EPB41L3	Q9Y2J2	1	EBI-359815,EBI-310986
FAM82C	Q96TC7	1	EBI-359815,EBI-1056589
IRS2	Q9Y4H2	1	EBI-359815,EBI-1049582
KIF23	Q02241	1	EBI-359815,EBI-306852
KIF5B	P33176	1	EBI-359815,EBI-355878
KLC1	Q07866	1	EBI-359815,EBI-721019
LARP1	Q6PKG0	1	EBI-359815,EBI-1052114
MARK3	P27448	1	EBI-359815,EBI-707595
MRIP	Q6WCQ1	1	EBI-359815,EBI-1022605
NCKAP1	Q9Y2A7	1	EBI-359815,EBI-389845
OSBPL3	Q9H4L5	1	EBI-359815,EBI-1051317
PARD3	Q8TEW0	1	EBI-359815,EBI-81968
PFTK1	O94921	5	EBI-359815,EBI-1043945
PIK4CB	Q9UBF8	1	EBI-359815,EBI-1053214
RABGEF1	Q9UJ41	1	EBI-359815,EBI-913954
RACGAP1	Q9H0H5	1	EBI-359815,EBI-717233
RAF1	P04049	4	EBI-359815,EBI-365996
RAI14	Q9P0K7	1	EBI-359815,EBI-1023749
SAMD4B	Q5PRF9	1	EBI-359815,EBI-1047489
SLC4A7	Q9Y6M7	1	EBI-359815,EBI-1044546
SRRM2	Q9UQ35	1	EBI-359815,EBI-1050142
TJP2	Q9UDY2	1	EBI-359815,EBI-1042602
USP8	P40818	1	EBI-359815,EBI-1050865

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.

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 246

245

14-3-3 protein beta/alpha

Amino acid modifications

Modified residue

2

1

N-acetylthreonine By similarity

Modified residue

186

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 2

2

Missing in isoform Short.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

246

Helix Strand Turn

Details...

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

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		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: 8515476] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte.
[2]	"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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[4]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-20. Tissue: Platelet.
[5]	"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: 15454081] [Abstract] Cited for: INTERACTION WITH CRTC2.
[6]	"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: 15159416] [Abstract] Cited for: INTERACTION WITH SSH1.
[7]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X57346 mRNA. Translation: CAA40621.1.
AL008725 Genomic DNA. Translation: CAA15497.1.
BC001359 mRNA. Translation: AAH01359.1.

PIR

S34755.

RefSeq

NP_003395.1.
NP_647539.1.

UniGene

Hs.651212

3D structure databases

PDBMSD

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:743N.

IntAct

P31946.

PTM databases

PhosphoSite

P31946.

2-D gel databases

Cornea-2DPAGE

P31946.

OGP

P31946.

REPRODUCTION-2DPAGE

IPI00216318.

Genome annotation databases

Ensembl

ENSG00000166913. Homo sapiens. [Contig view]

GeneID

7529.

KEGG

hsa:7529.

Organism-specific databases

H-InvDB

HIX0015846.

HGNC

HGNC:12849. YWHAB.

HPA

CAB003759.
HPA011212.

MIM

601289. gene.

PharmGKB

PA37438.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P31946.

HOVERGEN

P31946.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P31946.

CleanEx

HS_YWHAB.

GermOnline

ENSG00000166913. Homo sapiens.

Family and domain databases

InterPro

IPR000308. 14-3-3.
[Graphical view]

Gene3D

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

PANTHER

PTHR18860. 14-3-3. 1 hit.

Pfam

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

PIRSF

PIRSF000868. 14-3-3. 1 hit.

PRINTS

PR00305. 1433ZETA.

ProDom

PD000600. 14-3-3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

PROSITE

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

BLOCKS

Search...

Other Resources

SOURCE

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ProtoNet

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Entry information

Entry name

1433B_HUMAN

Accession

Primary (citable) accession number: P31946

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)