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

Last modified June 16, 2009. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    14-3-3 protein theta
Alternative name(s):
    14-3-3 protein tau
    14-3-3 protein T-cell
    Protein HS1
Gene names
Name: YWHAQ
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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. Interacts with PCTK1 By similarity. Interacts with SSH1. Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm.

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.9

Sequence similarities

Belongs to the 14-3-3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADAM22Q9P0K1-12EBI-359854,EBI-1567258
ADAM22Q9P0K1-31EBI-359854,EBI-1567267
ARRB1P494071EBI-359854,EBI-743313
ARRB2P321211EBI-359854,EBI-714559
BRAFP150561EBI-359854,EBI-365980
C22orf9Q6ICG61EBI-359854,EBI-1053969
CALML5Q9NZT11EBI-359854,EBI-1051681
CBWD2Q8IUF11EBI-359854,EBI-359159
DDX6P261961EBI-359854,EBI-351257
DENND4AQ7Z4011EBI-359854,EBI-1046479
EDC3Q96F861EBI-359854,EBI-997311
EML3Q32P441EBI-359854,EBI-1046713
EPB41L2O434911EBI-359854,EBI-1052044
EPB41L3Q9Y2J21EBI-359854,EBI-310986
FSHRP239453EBI-359854,EBI-848239
FUSIP1O754941EBI-359854,EBI-353655
IRS2Q9Y4H21EBI-359854,EBI-1049582
KIF23Q022411EBI-359854,EBI-306852
KIF5BP331761EBI-359854,EBI-355878
KIF5CO602821EBI-359854,EBI-717170
KLC2Q9H0B61EBI-359854,EBI-726994
KLC4Q9NSK01EBI-359854,EBI-949319
LARP1Q6PKG01EBI-359854,EBI-1052114
LUC7L2Q9Y3831EBI-359854,EBI-352851
MAGOHP613261EBI-359854,EBI-299134
MARK3P274481EBI-359854,EBI-707595
MPRIPQ6WCQ11EBI-359854,EBI-1022605
PAK4O960131EBI-359854,EBI-713738
PAK6Q9NQU51EBI-359854,EBI-1053685
PFTK1O949213EBI-359854,EBI-1043945
PI4KBQ9UBF81EBI-359854,EBI-1053214
PNKPQ96T601EBI-359854,EBI-1045072
PPFIBP1Q86W921EBI-359854,EBI-1045582
RABEP1Q152761EBI-359854,EBI-447043
RAF1P040491EBI-359854,EBI-365996
RAI14Q9P0K71EBI-359854,EBI-1023749
RASGRP3Q8IV611EBI-359854,EBI-1047876
SAMD4BQ5PRF91EBI-359854,EBI-1047489
SFRS1Q079551EBI-359854,EBI-398920
SFRS3P841031EBI-359854,EBI-372557
SFRS6Q132471EBI-359854,EBI-745230
SH3BP4Q9P0V31EBI-359854,EBI-1049513
SPIRE1Q08AE81EBI-359854,EBI-1055655
SUV420H1Q4FZB71EBI-359854,EBI-1047962
TJP2Q9UDY21EBI-359854,EBI-1042602
TSC2P498151EBI-359854,EBI-396587
USP8P408181EBI-359854,EBI-1050865

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.6
Modified residue2321Phosphoserine; by CK1 Probable

Experimental info

Sequence conflict1361D → N in AAV38817. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P27348-1 [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: 2015305] [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: 8515476] [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]"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: Eye, Skin and Uterus.
[5]"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 1-18.
Tissue: Platelet.
[6]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, MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Hepatoma.
[7]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.
[8]"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: 9360956] [Abstract]
Cited for: PHOSPHORYLATION AT SER-232, MASS SPECTROMETRY.
[9]"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: 11080204] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"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.
[11]"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: 15159416] [Abstract]
Cited for: INTERACTION WITH SSH1.
[12]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY.
[13]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"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: 7603573] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[16]"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 (2.8 ANGSTROMS) OF 1-234, MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

X56468 mRNA. Translation: CAA39840.1.
X57347 mRNA. Translation: CAA40622.1.
BT020014 mRNA. Translation: AAV38817.1.
BC001197 mRNA. Translation: AAH01197.1.
BC050601 mRNA. Translation: AAH50601.1.
BC056867 mRNA. Translation: AAH56867.1.
BC093019 mRNA. Translation: AAH93019.1.
AF070556 mRNA. Translation: AAC28640.1.
IPIIPI00018146.
PIRS15076.
RefSeqNP_006817.1.
UniGeneHs.74405

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2BTPX-ray2.80A/B1-234[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:27584N.
IntActP27348. 68 interactions.

PTM databases

PhosphoSiteP27348.

2-D gel databases

Cornea-2DPAGEP27348.
OGPP27348.
REPRODUCTION-2DPAGEIPI00018146.

Proteomic databases

PeptideAtlasP27348.
PRIDEP27348.

Genome annotation databases

EnsemblENSG00000134308. Homo sapiens. [Contig view]
GeneID10971.
KEGGhsa:10971.

Organism-specific databases

GeneCardsGC02M009674.
H-InvDBHIX0029798.
HIX0057400.
HGNCHGNC:12854. YWHAQ.
HPACAB010286.
HPA007925.
MIM609009. gene.
PharmGKBPA37443.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP27348.
HOVERGENP27348.
OMAP27348. DTSDKKM.

Enzyme and pathway databases

Pathway_Interaction_DBa6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
foxopathway. FoxO family signaling.
insulin_glucose_pathway. Insulin-mediated glucose transport.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.

Gene expression databases

ArrayExpressP27348.
BgeeP27348.
CleanExHS_YWHAQ.
GermOnlineENSG00000134308. Homo sapiens.

Family and domain databases

InterProIPR000308. 14-3-3.
[Graphical view]
Gene3DG3DSA:1.20.190.20. 14-3-3. 1 hit.
PANTHERPTHR18860. 14-3-3. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
ProDomPD000600. 14-3-3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio41686.
PMAP-CutDBP27348.
SOURCESearch...

Entry information

Entry name1433T_HUMAN
AccessionPrimary (citable) accession number: P27348
Secondary accession number(s): Q567U5, Q5TZU8, Q9UP48
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents