Reviewed, UniProtKB/Swiss-Prot P62258 (1433E_HUMAN)

Names and origin

Protein names

Recommended name:
    14-3-3 protein epsilon
      Short name=14-3-3E

Gene names

Name:

YWHAE

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	255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Heterodimerizes with YWHAZ. Interacts with NDEL1, RGNEF and TIAM2 By similarity. Interacts with HCV core protein. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Weakly interacts with CDKN1B.
Subcellular location	Cytoplasm By similarity. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence similarities	Belongs to the 14-3-3 family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Ref.1 Traceable author statement. Source: ProtInc
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enzyme binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAM22	Q9P0K1-3	1	EBI-356498,EBI-1567267
CDKN1B	P46527	1	EBI-356498,EBI-519280
PFTK1	O94921	3	EBI-356498,EBI-1043945

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 255

255

14-3-3 protein epsilon

PRO_0000058618

Sites

Site

57

1

Interaction with phosphoserine on interacting protein

Site

130

1

Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.11

Modified residue

210

1

Phosphoserine Ref.19

Experimental info

Sequence conflict

106 – 107

2

KH → NY AA sequence Ref.12

Sequence conflict

143

1

E → F AA sequence Ref.12

Sequence conflict

148

1

S → T AA sequence Ref.12

Secondary structure

1

.

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255

Helix Strand Turn

Details...

Helix

4 – 17

14

Helix

20 – 31

12

Helix

39 – 73

35

Helix

76 – 106

31

Helix

108 – 111

4

Helix

115 – 135

21

Helix

138 – 162

25

Helix

168 – 183

16

Helix

188 – 204

17

Helix

205 – 208

4

Turn

211 – 213

3

Helix

214 – 231

18

Sequences

	Sequence		Length	Mass (Da)
	P62258-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 07817CCBD1F75B26	FASTA	255	29,174
	10 20 30 40 50 60 MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW 70 80 90 100 110 120 RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF 130 140 150 160 170 180 YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF 190 200 210 220 230 240 YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE 250 EQNKEALQDV EDENQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"14-3-3 proteins associate with cdc25 phosphatases." Conklin D.S., Galaktionov K., Beach D. Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995) [PubMed: 7644510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region." Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H. Genome Res. 6:735-741(1996) [PubMed: 8858348] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Function of 14-3-3 proteins." Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T. Nature 382:308-308(1996) [PubMed: 8684458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Luk S.C.W., Lee C.Y., Waye M.M.Y. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[5]	"14-3-3 epsilon genomic sequence." Tanigami A., Chong S.S., Ledbetter D.H. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Subthalamic nucleus.
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	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].
[9]	"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: Placenta.
[10]	"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 1-19. Tissue: Platelet.
[11]	Bienvenut W.V. Submitted (MAY-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[12]	"Isolation and partial characterization of the structures of fibroblast activating factor-related proteins from U937 cells." Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W. Immunology 72:350-354(1991) [PubMed: 2026444] [Abstract] Cited for: PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153. Tissue: Histiocytic lymphoma.
[13]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 131-141 AND 154-190, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[14]	"Hepatitis C virus core protein interacts with 14-3-3 protein and activates the kinase Raf-1." Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O. J. Virol. 74:1736-1741(2000) [PubMed: 10644344] [Abstract] Cited for: INTERACTION WITH HCV CORE PROTEIN.
[15]	"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization." Fujita N., Sato S., Katayama K., Tsuruo T. J. Biol. Chem. 277:28706-28713(2002) [PubMed: 12042314] [Abstract] Cited for: INTERACTION WITH CDKN1B, SUBCELLULAR LOCATION.
[16]	"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage." Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y. Nat. Cell Biol. 7:278-285(2005) [PubMed: 15696159] [Abstract] Cited for: INTERACTION WITH ABL1, MASS SPECTROMETRY.
[17]	"Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon." Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y. FEBS Lett. 580:305-310(2006) [PubMed: 16376338] [Abstract] Cited for: INTERACTION WITH YWHAZ.
[18]	"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.
[19]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, MASS SPECTROMETRY. Tissue: Liver.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"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: 17085597] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U20972 mRNA. Translation: AAC50175.1.
U54778 mRNA. Translation: AAC50710.1.
U43399 mRNA. Translation: AAC50625.1.
U43430 mRNA. Translation: AAD00026.1.
U28936 mRNA. Translation: AAA75301.1.
AB017103 Genomic DNA. Translation: BAA32538.1.
AK128785 mRNA. Translation: BAG54733.1.
BT007161 mRNA. Translation: AAP35825.1.
CH471108 Genomic DNA. Translation: EAW90628.1.
BC000179 mRNA. Translation: AAH00179.1.
BC001440 mRNA. Translation: AAH01440.1.

IPI

IPI00000816.

PIR

A61235.
I38947.

RefSeq

NP_006752.1.

UniGene

Hs.513851

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BR9	X-ray	1.75	A	1-233	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P62258. 29 interactions.

2-D gel databases

OGP

P42655.

Proteomic databases

PeptideAtlas

P62258.

PRIDE

P62258.

Genome annotation databases

Ensembl

ENSG00000108953. Homo sapiens. [Contig view]

GeneID

7531.

KEGG

hsa:7531.

Organism-specific databases

GeneCards

GC17M001194.

H-InvDB

HIX0013397.
HIX0013751.
HIX0030006.

HGNC

HGNC:12851. YWHAE.

HPA

CAB016200.
HPA008445.

MIM

605066. gene.

PharmGKB

PA37440.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P62258.

HOVERGEN

P62258.

OMA

P62258. AYQKATD.

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.
igf1_pathway. IGF1 pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.
lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
p75ntrpathway. p75(NTR)-mediated signaling.
telomerasepathway. Regulation of Telomerase.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
tgfbrpathway. TGF-beta receptor signaling.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.

Reactome

REACT_11061. Signalling by NGF.

Gene expression databases

ArrayExpress

P62258.

Bgee

P62258.

CleanEx

HS_YWHAE.

GermOnline

ENSG00000108953. 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]

ProtoNet

Search...

Other Resources

NextBio

29461.

PMAP-CutDB

P62258.

SOURCE

Search...

Entry information

Entry name

1433E_HUMAN

Accession

Primary (citable) accession number: P62258
Secondary accession number(s): B3KY71 , P29360, P42655, Q53XZ5, Q63631, Q7M4R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)