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

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) [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	255 AA.
Sequence status	Complete.
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.
Subunit structure	Homodimer. Heterodimerizes with YWHAZ. Interacts with NDEL1, ARHGEF28 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. Interacts with GAB2. Interacts with phosphorylated GRB10. Interacts with PKA-phosphorylated AANAT. Interacts with the phosphorylated (by AKT1) form of SRPK2. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.29
Subcellular location	Cytoplasm By similarity. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.17 Ref.21
Sequence similarities	Belongs to the 14-3-3 family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cellular membrane organization Traceable author statement. Source: Reactome cerebral cortex development Inferred from electronic annotation. Source: Compara hippo signaling cascade Traceable author statement. Source: Reactome hippocampus development Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway Traceable author statement. Source: Reactome negative regulation of protein dephosphorylation Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Traceable author statement. Source: Reactome protein targeting Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	axon part Inferred from electronic annotation. Source: Compara cytoplasmic vesicle membrane Traceable author statement. Source: Reactome cytosol Traceable author statement. Source: Reactome kinesin complex Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX4	O00257-3	2	EBI-356498,EBI-4392727
CDK14	O94921	3	EBI-356498,EBI-1043945
FBXO4	Q9UKT5	5	EBI-356498,EBI-960409
KANK1	Q14678-2	3	EBI-356498,EBI-6173812
LRRK2	Q5S007	3	EBI-356498,EBI-5323863
YWHAG	P61981	4	EBI-356498,EBI-359832

Alternative products

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

Isoform 1 (identifier: P62258-1)

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 SV (identifier: P62258-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.

Note: Unable to dimerize with YWHAZ.

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.12

Modified residue

50

1

N6-acetyllysine Ref.25

Modified residue

69

1

N6-acetyllysine Ref.25

Modified residue

118

1

N6-acetyllysine Ref.25

Modified residue

123

1

N6-acetyllysine Ref.25

Modified residue

210

1

Phosphoserine Ref.26 Ref.28

Natural variations

Alternative sequence

1 – 22

22

Missing in isoform SV.

VSP_040621

Experimental info

Sequence conflict

106 – 107

2

KH → NY AA sequence Ref.13

Sequence conflict

143

1

E → F AA sequence Ref.13

Sequence conflict

148

1

S → T AA sequence Ref.13

Secondary structure

1

.

.

.

.

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.

.

.

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.

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.

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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)
	Isoform 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
	Isoform SV [UniParc]. Checksum: 20302F1E0AB73C8A	FASTA	233	26,504
	10 20 30 40 50 60 MVESMKKVAG MDVELTVEER NLLSVAYKNV IGARRASWRI ISSIEQKEEN KGGEDKLKMI 70 80 90 100 110 120 REYRQMVETE LKLICCDILD VLDKHLIPAA NTGESKVFYY KMKGDYHRYL AEFATGNDRK 130 140 150 160 170 180 EAAENSLVAY KAASDIAMTE LPPTHPIRLG LALNFSVFYY EILNSPDRAC RLAKAAFDDA 190 200 210 220 230 IAELDTLSEE SYKDSTLIMQ LLRDNLTLWT SDMQGDGEEQ NKEALQDVED ENQ

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Functional identification of a novel 14-3-3 epsilon splicing variant suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-induced apoptosis." Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L. Biochem. Biophys. Res. Commun. 396:401-406(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), ALTERNATIVE SPLICING. Tissue: Brain.
[5]	"Sequence determination of human epsilon 14-3-3 protein." 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] (ISOFORM 1). Tissue: Heart.
[6]	"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].
[7]	"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] (ISOFORMS 1 AND SV). Tissue: Caudate nucleus, Heart and Subthalamic nucleus.
[8]	"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] (ISOFORM 1).
[9]	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].
[10]	"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] (ISOFORM 1). Tissue: Placenta.
[11]	"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 1-19. Tissue: Platelet.
[12]	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.
[13]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153. Tissue: Histiocytic lymphoma.
[14]	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.
[15]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCV CORE PROTEIN.
[16]	"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.
[17]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDKN1B, SUBCELLULAR LOCATION.
[18]	"Phosphorylation of grb10 regulates its interaction with 14-3-3." Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J. J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB10.
[19]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABL1, MASS SPECTROMETRY.
[20]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YWHAZ.
[21]	"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.
[22]	"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.
[23]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[24]	"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: INTERACTION WITH SRPK2.
[25]	"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-50; LYS-69; LYS-118 AND LYS-123, MASS SPECTROMETRY.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, MASS SPECTROMETRY.
[29]	"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 (1.75 ANGSTROMS) OF 1-233, MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
AY883089 mRNA. Translation: AAX68683.1.
AK128785 mRNA. Translation: BAG54733.1.
AK295260 mRNA. Translation: BAG58249.1.
AK316185 mRNA. Translation: BAH14556.1.
BT007161 mRNA. Translation: AAP35825.1.
CH471108 Genomic DNA. Translation: EAW90628.1.
CH471108 Genomic DNA. Translation: EAW90629.1.
BC000179 mRNA. Translation: AAH00179.1.
BC001440 mRNA. Translation: AAH01440.1.

IPI

IPI00000816.
IPI00974544.

PIR

A61235.
I38947.

RefSeq

NP_006752.1. NM_006761.4.

UniGene

Hs.513851.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BR9	X-ray	1.75	A	1-233	[»]
3UAL	X-ray	1.80	A	1-232	[»]
3UBW	X-ray	1.90	A	1-234	[»]

ProteinModelPortal

P62258.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36676N.

IntAct

P62258. 99 interactions.

MINT

MINT-4998623.

STRING

9606.ENSP00000264335.

PTM databases

PhosphoSite

P62258.

Polymorphism databases

DMDM

51702210.

2D gel databases

OGP

P42655.

UCD-2DPAGE

P62258.

Proteomic databases

PaxDb

P62258.

PeptideAtlas

P62258.

PRIDE

P62258.

Protocols and materials databases

DNASU

7531.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264335; ENSP00000264335; ENSG00000108953.
ENST00000571732; ENSP00000461762; ENSG00000108953.

GeneID

7531.

KEGG

hsa:7531.

UCSC

uc002fsj.3. human.

Organism-specific databases

CTD

7531.

GeneCards

GC17M001247.

H-InvDB

HIX0013751.
HIX0030006.

HGNC

HGNC:12851. YWHAE.

HPA

CAB016200.
CAB021109.
CAB047350.
HPA008445.

MIM

605066. gene.

neXtProt

NX_P62258.

Orphanet

217385. 17p13.3 microduplication syndrome.
261257. Distal 17p13.3 microdeletion syndrome.
531. Miller-Dieker syndrome.

PharmGKB

PA37440.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5040.

HOVERGEN

HBG050423.

InParanoid

P62258.

KO

K06630.

OMA

KESALIM.

OrthoDB

EOG4HHP34.

PhylomeDB

P62258.

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_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.

SignaLink

P62258.

Gene expression databases

ArrayExpress

P62258.

Bgee

P62258.

CleanEx

HS_YWHAE.

Genevestigator

P62258.

GermOnline

ENSG00000108953. 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

YWHAE. human.

EvolutionaryTrace

P62258.

GenomeRNAi

7531.

NextBio

29461.

PMAP-CutDB

P62258.

SOURCE

Search...

Entry information

Entry name

1433E_HUMAN

Accession

Primary (citable) accession number: P62258
Secondary accession number(s): B3KY71 , D3DTH5, P29360, P42655, Q4VJB6, Q53XZ5, Q63631, Q7M4R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 111 of the entry and version 1 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.