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

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14-3-3 protein epsilon

Short name=14-3-3E
Gene names
Name:YWHAE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceEvidence 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.25 Ref.30

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 processHost-virus interaction
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

hippo signaling

Traceable author statement. Source: Reactome

hippocampus development

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Traceable author statement Ref.1. Source: ProtInc

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

membrane repolarization during cardiac muscle cell action potential

Inferred by curator PubMed 11953308. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of peptidyl-serine dephosphorylation

Inferred from direct assay PubMed 11953308. Source: BHF-UCL

neuron migration

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

regulation of heart rate by cardiac conduction

Inferred by curator PubMed 11953308. Source: BHF-UCL

regulation of heart rate by hormone

Non-traceable author statement PubMed 11953308. Source: BHF-UCL

regulation of membrane repolarization

Inferred from direct assay PubMed 11953308. Source: BHF-UCL

regulation of potassium ion transmembrane transporter activity

Inferred from direct assay PubMed 11953308. Source: BHF-UCL

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProtKB

kinesin complex

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionMHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

enzyme binding

Inferred from physical interaction PubMed 10788521. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction PubMed 10869435. Source: BHF-UCL

ion channel binding

Inferred from physical interaction PubMed 11953308. Source: BHF-UCL

phosphoprotein binding

Inferred from physical interaction PubMed 10869435. Source: BHF-UCL

phosphoserine binding

Inferred from physical interaction PubMed 10869435. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

potassium channel regulator activity

Inferred from direct assay PubMed 11953308. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 1266503Ref.18Ref.22. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 11953308. Source: BHF-UCL

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25525514-3-3 protein epsilon
PRO_0000058618

Sites

Site571Interaction with phosphoserine on interacting protein
Site1301Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12 Ref.24
Modified residue501N6-acetyllysine Ref.26
Modified residue691N6-acetyllysine Ref.26
Modified residue1181N6-acetyllysine Ref.26
Modified residue1231N6-acetyllysine Ref.26
Modified residue2101Phosphoserine Ref.27 Ref.29

Natural variations

Alternative sequence1 – 2222Missing in isoform SV.
VSP_040621

Experimental info

Sequence conflict106 – 1072KH → NY AA sequence Ref.13
Sequence conflict1431E → F AA sequence Ref.13
Sequence conflict1481S → T AA sequence Ref.13

Secondary structure

....................... 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 07817CCBD1F75B26

FASTA25529,174
        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 

« Hide

Isoform SV [UniParc].

Checksum: 20302F1E0AB73C8A
Show »

FASTA23326,504

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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].
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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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].
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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, IDENTIFICATION BY 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.
CCDSCCDS11001.1. [P62258-1]
PIRA61235.
I38947.
RefSeqNP_006752.1. NM_006761.4. [P62258-1]
UniGeneHs.513851.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BR9X-ray1.75A1-233[»]
3UALX-ray1.80A1-232[»]
3UBWX-ray1.90A1-234[»]
ProteinModelPortalP62258.
SMRP62258. Positions 3-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113363. 316 interactions.
DIPDIP-36676N.
IntActP62258. 147 interactions.
MINTMINT-4998623.
STRING9606.ENSP00000264335.

PTM databases

PhosphoSiteP62258.

Polymorphism databases

DMDM51702210.

2D gel databases

OGPP42655.
UCD-2DPAGEP62258.

Proteomic databases

MaxQBP62258.
PaxDbP62258.
PeptideAtlasP62258.
PRIDEP62258.

Protocols and materials databases

DNASU7531.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264335; ENSP00000264335; ENSG00000108953. [P62258-1]
ENST00000571732; ENSP00000461762; ENSG00000108953. [P62258-2]
GeneID7531.
KEGGhsa:7531.
UCSCuc002fsj.3. human. [P62258-1]

Organism-specific databases

CTD7531.
GeneCardsGC17M001148.
H-InvDBHIX0013751.
HIX0030006.
HGNCHGNC:12851. YWHAE.
HPACAB016200.
CAB021109.
CAB047350.
HPA008445.
MIM605066. gene.
neXtProtNX_P62258.
Orphanet217385. 17p13.3 microduplication syndrome.
261257. Distal 17p13.3 microdeletion syndrome.
531. Miller-Dieker syndrome.
PharmGKBPA37440.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5040.
HOVERGENHBG050423.
InParanoidP62258.
KOK06630.
OMAMQESDKP.
OrthoDBEOG7HHWT3.
PhylomeDBP62258.
TreeFamTF102003.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_578. Apoptosis.
SignaLinkP62258.

Gene expression databases

ArrayExpressP62258.
BgeeP62258.
CleanExHS_YWHAE.
GenevestigatorP62258.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSYWHAE. human.
EvolutionaryTraceP62258.
GeneWikiYWHAE.
GenomeRNAi7531.
NextBio29461.
PMAP-CutDBP62258.
PROP62258.
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Entry information

Entry name1433E_HUMAN
AccessionPrimary (citable) accession number: P62258
Secondary accession number(s): B3KY71 expand/collapse secondary AC list , 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: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM