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P27348 (1433T_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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 theta
Alternative name(s):
14-3-3 protein T-cell
14-3-3 protein tau
Protein HS1
Gene names
Name:YWHAQ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 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. Negatively regulates the kinase activity of PDPK1. Ref.12

Subunit structure

Homodimer. Interacts with CDK16 By similarity. Interacts with SSH1. Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241' phosphorylated form of PDPK1. Ref.11 Ref.12 Ref.13 Ref.15 Ref.24

Subcellular location

Cytoplasm. Note: In neurons, axonally transported to the nerve terminals.

Tissue specificity

Abundantly expressed in brain, heart and pancreas, and at lower levels in kidney and placenta. Up-regulated in the lumbar spinal cord from patients with sporadic amyotrophic lateral sclerosis (ALS) compared with controls, with highest levels of expression in individuals with predominant lower motor neuron involvement. Ref.10

Post-translational modification

Ser-232 is probably phosphorylated by CK1. Ref.9

Sequence similarities

Belongs to the 14-3-3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24524514-3-3 protein theta
PRO_0000058636

Sites

Site561Interaction with phosphoserine on interacting protein
Site1271Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.19 Ref.22
Modified residue31N6-acetyllysine Ref.19
Modified residue491N6-acetyllysine Ref.19
Modified residue681N6-acetyllysine Ref.19
Modified residue1151N6-acetyllysine Ref.19
Modified residue2321Phosphoserine Ref.9 Ref.17

Experimental info

Sequence conflict1361D → N in AAV38817. Ref.3

Secondary structure

..................... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27348 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 175534325E9E37C4

FASTA24527,764
        10         20         30         40         50         60 
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR 

        70         80         90        100        110        120 
VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK 

       130        140        150        160        170        180 
MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE 

       190        200        210        220        230        240 
ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA 


EGAEN 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of a human protein kinase regulator protein."
Nielsen P.J.
Biochim. Biophys. Acta 1088:425-428(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: T-cell.
[2]"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].
Tissue: Keratinocyte.
[3]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]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].
[5]"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: Placenta, Skin and Uterus.
[6]"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 1-18.
Tissue: Platelet.
[7]Bienvenut W.V., Dhillon A.S., Kolch W.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Hepatoma.
[8]Yu W., Gibbs R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245.
Tissue: Brain.
[9]"14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction."
Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A.
J. Biol. Chem. 272:28882-28888(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal cord."
Malaspina A., Kaushik N., de Belleroche J.
J. Neurochem. 75:2511-2520(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"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.
[12]"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.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSH1.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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 MET-1; LYS-3; LYS-49; LYS-68 AND LYS-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways."
Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., Gamblin S.J.
Nature 376:188-191(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[24]"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 (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56468 mRNA. Translation: CAA39840.1.
X57347 mRNA. Translation: CAA40622.1.
BT020014 mRNA. Translation: AAV38817.1.
CH471053 Genomic DNA. Translation: EAX00977.1.
CH471053 Genomic DNA. Translation: EAX00979.1.
BC050601 mRNA. Translation: AAH50601.1.
BC056867 mRNA. Translation: AAH56867.1.
BC093019 mRNA. Translation: AAH93019.1.
AF070556 mRNA. Translation: AAC28640.1.
CCDSCCDS1666.1.
PIRS15076.
RefSeqNP_006817.1. NM_006826.3.
UniGeneHs.74405.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTPX-ray2.80A/B1-234[»]
ProteinModelPortalP27348.
SMRP27348. Positions 1-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116168. 380 interactions.
DIPDIP-27584N.
IntActP27348. 80 interactions.
MINTMINT-121282.
STRING9606.ENSP00000238081.

PTM databases

PhosphoSiteP27348.

Polymorphism databases

DMDM112690.

2D gel databases

OGPP27348.
REPRODUCTION-2DPAGEIPI00018146.

Proteomic databases

MaxQBP27348.
PaxDbP27348.
PeptideAtlasP27348.
PRIDEP27348.

Protocols and materials databases

DNASU10971.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238081; ENSP00000238081; ENSG00000134308.
ENST00000381844; ENSP00000371267; ENSG00000134308.
GeneID10971.
KEGGhsa:10971.
UCSCuc002qzx.3. human.

Organism-specific databases

CTD10971.
GeneCardsGC02M009724.
H-InvDBHIX0077146.
HGNCHGNC:12854. YWHAQ.
HPACAB010286.
HPA007925.
MIM609009. gene.
neXtProtNX_P27348.
PharmGKBPA37443.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5040.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidP27348.
KOK16197.
OMACELRSIC.
OrthoDBEOG7HHWT3.
PhylomeDBP27348.
TreeFamTF102002.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_578. Apoptosis.
SignaLinkP27348.

Gene expression databases

ArrayExpressP27348.
BgeeP27348.
CleanExHS_YWHAQ.
GenevestigatorP27348.

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

ChiTaRSYWHAQ. human.
EvolutionaryTraceP27348.
GeneWikiYWHAQ.
GenomeRNAi10971.
NextBio41686.
PMAP-CutDBP27348.
PROP27348.
SOURCESearch...

Entry information

Entry name1433T_HUMAN
AccessionPrimary (citable) accession number: P27348
Secondary accession number(s): D6W4Z5 expand/collapse secondary AC list , Q567U5, Q5TZU8, Q9UP48
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 158 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 2

Human chromosome 2: entries, gene names and cross-references to MIM