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Q04917 (1433F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14-3-3 protein eta
Alternative name(s):
Protein AS1
Gene names
Name:YWHAH
Synonyms:YWHA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Negatively regulates the kinase activity of PDPK1. Ref.13

Subunit structure

Homodimer By similarity. Interacts with many nuclear hormone receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with ARHGEF28 and CDK16 By similarity. Weakly interacts with CDKN1B. Interacts with GAB2. Interacts with KCNK18 in a phosphorylation-dependent manner. Interacts with SAMSN1 By similarity. Interacts with the 'Ser-241' phosphorylated form of PDPK1. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19

Tissue specificity

Expressed mainly in the brain and present in other tissues albeit at lower levels.

Post-translational modification

Phosphorylated on Ser-59 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion By similarity.

Sequence similarities

Belongs to the 14-3-3 family.

Ontologies

Keywords
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

glucocorticoid catabolic process

Inferred from direct assay PubMed 15790729. Source: UniProtKB

glucocorticoid receptor signaling pathway

Inferred from direct assay PubMed 15790729. Source: UniProtKB

intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

membrane depolarization during action potential

Inferred from direct assay PubMed 16728661. Source: BHF-UCL

membrane organization

Traceable author statement. Source: Reactome

negative regulation of dendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15790729. Source: UniProtKB

regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sodium ion transmembrane transporter activity

Inferred from direct assay PubMed 16728661. Source: BHF-UCL

regulation of sodium ion transport

Inferred from direct assay PubMed 16728661. Source: BHF-UCL

regulation of synaptic plasticity

Inferred from sequence or structural similarity. Source: UniProtKB

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProtKB

intercalated disc

Inferred by curator PubMed 16728661. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 16728661. Source: BHF-UCL

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 17255105. Source: BHF-UCL

glucocorticoid receptor binding

Inferred from physical interaction PubMed 9079630. Source: UniProtKB

insulin-like growth factor receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

ion channel binding

Inferred from physical interaction PubMed 11953308PubMed 16728661. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 18397886Ref.16. Source: UniProtKB

protein domain specific binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterodimerization activity

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

sodium channel regulator activity

Inferred from direct assay PubMed 16728661. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10 Ref.11
Chain2 – 24624514-3-3 protein eta
PRO_0000058623

Sites

Site571Interaction with phosphoserine on interacting protein
Site1321Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue21N-acetylglycine Ref.11
Modified residue251Phosphoserine Ref.17
Modified residue591Phosphoserine By similarity

Experimental info

Sequence conflict1441N → T in CAA40620. Ref.9
Sequence conflict1571A → G in AAA35483. Ref.1
Sequence conflict2371Q → L in AAA35483. Ref.1

Secondary structure

...................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04917 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D70FBC100C45D6E5

FASTA24628,219
        10         20         30         40         50         60 
MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW 

        70         80         90        100        110        120 
RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK 

       130        140        150        160        170        180 
VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS 

       190        200        210        220        230        240 
VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE 


EAGEGN 

« Hide

References

« Hide 'large scale' references
[1]"The human and bovine 14-3-3 eta protein mRNAs are highly conserved in both their translated and untranslated regions."
Swanson K.D., Dhar M.S., Joshi J.G.
Biochim. Biophys. Acta 1216:145-148(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"cDNA cloning and chromosome assignment of the gene for human brain 14-3-3 protein eta chain."
Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y., Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.
J. Neurosci. Res. 31:600-605(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[3]Leffers H., Tommerup N., Celis J.E.
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The effect on methamphetamine on the mRNA level for 14.3.3 eta chain in the human cultured cells."
Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R., Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.
Mol. Neurobiol. 11:223-230(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Structural organization and chromosomal assignment of the human 14-3-3 eta chain gene (YWHAH)."
Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y., Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.
Genomics 36:63-69(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Lymph.
[9]"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] OF 27-225.
Tissue: Keratinocyte.
[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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10.
Tissue: Platelet.
[11]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10; 29-50; 62-69; 126-132; 144-155; 163-172 AND 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[12]"Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140."
Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.
Mol. Endocrinol. 15:501-511(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA.
[13]"Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3."
Sato S., Fujita N., Tsuruo T.
J. Biol. Chem. 277:39360-39367(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PDPK1.
[14]"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization."
Fujita N., Sato S., Tsuruo T.
J. Biol. Chem. 278:49254-49260(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDKN1B.
[15]"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.
[16]"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.
[17]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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 (2.15 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20422 mRNA. Translation: AAA35483.1.
X80536 Genomic DNA. Translation: CAA56676.1.
X78138 mRNA. Translation: CAA55017.1.
X57345 mRNA. Translation: CAA40620.1.
D78577 Genomic DNA. Translation: BAA11418.1.
S80794 mRNA. Translation: AAB36036.1.
CR456612 mRNA. Translation: CAG30498.1.
Z82248 Genomic DNA. Translation: CAB05112.1.
BC003047 mRNA. Translation: AAH03047.1.
CCDSCCDS13901.1.
PIRS34756.
S38509.
S38532.
RefSeqNP_003396.1. NM_003405.3.
UniGeneHs.226755.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C63X-ray2.15A/B/C/D2-246[»]
2C74X-ray2.70A/B2-246[»]
ProteinModelPortalQ04917.
SMRQ04917. Positions 3-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113365. 121 interactions.
DIPDIP-27566N.
IntActQ04917. 144 interactions.
MINTMINT-124456.
STRING9606.ENSP00000248975.

PTM databases

PhosphoSiteQ04917.

Polymorphism databases

DMDM1345593.

Proteomic databases

MaxQBQ04917.
PaxDbQ04917.
PeptideAtlasQ04917.
PRIDEQ04917.

Protocols and materials databases

DNASU7533.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248975; ENSP00000248975; ENSG00000128245.
GeneID7533.
KEGGhsa:7533.
UCSCuc003alz.3. human.

Organism-specific databases

CTD7533.
GeneCardsGC22P032340.
HGNCHGNC:12853. YWHAH.
HPACAB025918.
MIM113508. gene.
neXtProtNX_Q04917.
PharmGKBPA37442.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5040.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidQ04917.
KOK16198.
OMAESSEAAY.
OrthoDBEOG7HHWT3.
PhylomeDBQ04917.
TreeFamTF102003.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_578. Apoptosis.
SignaLinkQ04917.

Gene expression databases

ArrayExpressQ04917.
BgeeQ04917.
CleanExHS_YWHAH.
GenevestigatorQ04917.

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

ChiTaRSYWHAH. human.
EvolutionaryTraceQ04917.
GeneWikiYWHAH.
GenomeRNAi7533.
NextBio29471.
PROQ04917.
SOURCESearch...

Entry information

Entry name1433F_HUMAN
AccessionPrimary (citable) accession number: Q04917
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 161 of the entry and version 4 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 22

Human chromosome 22: entries, gene names and cross-references to MIM