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P27348

- 1433T_HUMAN

UniProt

P27348 - 1433T_HUMAN

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Protein
14-3-3 protein theta
Gene
YWHAQ
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 PDPK1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Interaction with phosphoserine on interacting protein
Sitei127 – 1271Interaction with phosphoserine on interacting protein

GO - Molecular functioni

  1. protein N-terminus binding Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. intrinsic apoptotic signaling pathway Source: Reactome
  3. membrane organization Source: Reactome
  4. negative regulation of transcription, DNA-templated Source: BHF-UCL
  5. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  6. protein targeting Source: Ensembl
  7. small GTPase mediated signal transduction Source: Ensembl
  8. substantia nigra development Source: UniProt
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
SignaLinkiP27348.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein theta
Alternative name(s):
14-3-3 protein T-cell
14-3-3 protein tau
Protein HS1
Gene namesi
Name:YWHAQ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12854. YWHAQ.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoplasmic vesicle membrane Source: Reactome
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24524514-3-3 protein theta
PRO_0000058636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei49 – 491N6-acetyllysine1 Publication
Modified residuei68 – 681N6-acetyllysine1 Publication
Modified residuei115 – 1151N6-acetyllysine1 Publication
Modified residuei232 – 2321Phosphoserine2 Publications

Post-translational modificationi

Ser-232 is probably phosphorylated by CK1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP27348.
PaxDbiP27348.
PeptideAtlasiP27348.
PRIDEiP27348.

2D gel databases

OGPiP27348.
REPRODUCTION-2DPAGEIPI00018146.

PTM databases

PhosphoSiteiP27348.

Miscellaneous databases

PMAP-CutDBP27348.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiP27348.
BgeeiP27348.
CleanExiHS_YWHAQ.
GenevestigatoriP27348.

Organism-specific databases

HPAiCAB010286.
HPA007925.

Interactioni

Subunit structurei

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 PDPK1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM22Q9P0K1-32EBI-359854,EBI-1567267
ARRB1P494073EBI-359854,EBI-743313
ARRB2P321213EBI-359854,EBI-714559
CBLP226816EBI-359854,EBI-518228
CDK14O949213EBI-359854,EBI-1043945
CDKN1BP465274EBI-359854,EBI-519280
CSNK1A1P678282EBI-359854,EBI-7540603From a different organism.
EGFRP005335EBI-359854,EBI-297353
FSHRP239454EBI-359854,EBI-848239
KANK1Q146782EBI-359854,EBI-2556221
KANK1Q14678-23EBI-359854,EBI-6173812
LRRK2Q5S0077EBI-359854,EBI-5323863
Rnd3P615882EBI-359854,EBI-6930266From a different organism.
SSH1Q8WYL52EBI-359854,EBI-1222387

Protein-protein interaction databases

BioGridi116168. 374 interactions.
DIPiDIP-27584N.
IntActiP27348. 81 interactions.
MINTiMINT-121282.
STRINGi9606.ENSP00000238081.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513
Helixi19 – 3113
Helixi38 – 6831
Helixi75 – 10329
Turni104 – 1085
Helixi112 – 13221
Helixi135 – 15925
Helixi165 – 18016
Helixi185 – 20117
Turni202 – 2054
Helixi208 – 22720

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTPX-ray2.80A/B1-234[»]
ProteinModelPortaliP27348.
SMRiP27348. Positions 1-230.

Miscellaneous databases

EvolutionaryTraceiP27348.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.

Phylogenomic databases

eggNOGiCOG5040.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP27348.
KOiK16197.
OMAiCELRSIC.
OrthoDBiEOG7HHWT3.
PhylomeDBiP27348.
TreeFamiTF102002.

Family and domain databases

Gene3Di1.20.190.20. 1 hit.
InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27348-1 [UniParc]FASTAAdd to Basket

« Hide

MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN    50
VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL 100
LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ 150
EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI 200
AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN 245
Length:245
Mass (Da):27,764
Last modified:August 1, 1992 - v1
Checksum:i175534325E9E37C4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361D → N in AAV38817. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1666.1.
PIRiS15076.
RefSeqiNP_006817.1. NM_006826.3.
UniGeneiHs.74405.

Genome annotation databases

EnsembliENST00000238081; ENSP00000238081; ENSG00000134308.
ENST00000381844; ENSP00000371267; ENSG00000134308.
GeneIDi10971.
KEGGihsa:10971.
UCSCiuc002qzx.3. human.

Polymorphism databases

DMDMi112690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1666.1.
PIRi S15076.
RefSeqi NP_006817.1. NM_006826.3.
UniGenei Hs.74405.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BTP X-ray 2.80 A/B 1-234 [» ]
ProteinModelPortali P27348.
SMRi P27348. Positions 1-230.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116168. 374 interactions.
DIPi DIP-27584N.
IntActi P27348. 81 interactions.
MINTi MINT-121282.
STRINGi 9606.ENSP00000238081.

PTM databases

PhosphoSitei P27348.

Polymorphism databases

DMDMi 112690.

2D gel databases

OGPi P27348.
REPRODUCTION-2DPAGE IPI00018146.

Proteomic databases

MaxQBi P27348.
PaxDbi P27348.
PeptideAtlasi P27348.
PRIDEi P27348.

Protocols and materials databases

DNASUi 10971.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000238081 ; ENSP00000238081 ; ENSG00000134308 .
ENST00000381844 ; ENSP00000371267 ; ENSG00000134308 .
GeneIDi 10971.
KEGGi hsa:10971.
UCSCi uc002qzx.3. human.

Organism-specific databases

CTDi 10971.
GeneCardsi GC02M009724.
H-InvDB HIX0077146.
HGNCi HGNC:12854. YWHAQ.
HPAi CAB010286.
HPA007925.
MIMi 609009. gene.
neXtProti NX_P27348.
PharmGKBi PA37443.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5040.
HOGENOMi HOG000240379.
HOVERGENi HBG050423.
InParanoidi P27348.
KOi K16197.
OMAi CELRSIC.
OrthoDBi EOG7HHWT3.
PhylomeDBi P27348.
TreeFami TF102002.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
SignaLinki P27348.

Miscellaneous databases

ChiTaRSi YWHAQ. human.
EvolutionaryTracei P27348.
GeneWikii YWHAQ.
GenomeRNAii 10971.
NextBioi 41686.
PMAP-CutDB P27348.
PROi P27348.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27348.
Bgeei P27348.
CleanExi HS_YWHAQ.
Genevestigatori P27348.

Family and domain databases

Gene3Di 1.20.190.20. 1 hit.
InterProi IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view ]
PANTHERi PTHR18860. PTHR18860. 1 hit.
Pfami PF00244. 14-3-3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000868. 14-3-3. 1 hit.
PRINTSi PR00305. 1433ZETA.
SMARTi SM00101. 14_3_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48445. SSF48445. 1 hit.
PROSITEi PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

Entry informationi

Entry namei1433T_HUMAN
AccessioniPrimary (citable) accession number: P27348
Secondary accession number(s): D6W4Z5
, Q567U5, Q5TZU8, Q9UP48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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