Details for: YWHAQ

Gene ID: 10971

Symbol: YWHAQ

Ensembl ID: ENSG00000134308

Description: tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta

Associated with

Other Information

Genular Protein ID: 336810968

Symbol: 1433T_HUMAN

Name: 14-3-3 protein theta

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 2015305

Title: Primary structure of a human protein kinase regulator protein.

PubMed ID: 2015305

DOI: 10.1016/0167-4781(91)90136-a

PubMed ID: 8515476

Title: 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.

PubMed ID: 8515476

DOI: 10.1006/jmbi.1993.1346

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 12665801

Title: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.

PubMed ID: 12665801

DOI: 10.1038/nbt810

PubMed ID: 23572552

Title: ACBD3 interaction with TBC1 domain 22 protein is differentially affected by enteroviral and kobuviral 3A protein binding.

PubMed ID: 23572552

DOI: 10.1128/mbio.00098-13

PubMed ID: 9360956

Title: 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.

PubMed ID: 9360956

DOI: 10.1074/jbc.272.46.28882

PubMed ID: 10862767

Title: 14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity.

PubMed ID: 10862767

DOI: 10.1074/jbc.m002905200

PubMed ID: 11080204

Title: A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal cord.

PubMed ID: 11080204

DOI: 10.1046/j.1471-4159.2000.0752511.x

PubMed ID: 12042314

Title: Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization.

PubMed ID: 12042314

DOI: 10.1074/jbc.m203668200

PubMed ID: 12177059

Title: Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.

PubMed ID: 12177059

DOI: 10.1074/jbc.m205141200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15159416

Title: A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia.

PubMed ID: 15159416

DOI: 10.1083/jcb.200401136

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16959763

Title: Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling.

PubMed ID: 16959763

DOI: 10.1074/mcp.m600147-mcp200

PubMed ID: 19172738

Title: Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein.

PubMed ID: 19172738

DOI: 10.1038/emboj.2008.159

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19640509

Title: SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-dependent manner.

PubMed ID: 19640509

DOI: 10.1016/j.biopsych.2009.05.033

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26047703

Title: Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins.

PubMed ID: 26047703

DOI: 10.1016/j.bbrc.2015.05.105

PubMed ID: 25588844

Title: Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at leading edges polarizes neutrophils.

PubMed ID: 25588844

DOI: 10.1242/jcs.161497

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27030597

Title: Familial autoinflammation with neutrophilic dermatosis reveals a regulatory mechanism of pyrin activation.

PubMed ID: 27030597

DOI: 10.1126/scitranslmed.aaf1471

PubMed ID: 28436939

Title: An inflammatory bowel disease-risk variant in INAVA decreases pattern recognition receptor-induced outcomes.

PubMed ID: 28436939

DOI: 10.1172/jci86282

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 7603573

Title: Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways.

PubMed ID: 7603573

DOI: 10.1038/376188a0

PubMed ID: 17085597

Title: Structural basis for protein-protein interactions in the 14-3-3 protein family.

PubMed ID: 17085597

DOI: 10.1073/pnas.0605779103

Sequence Information:

  • Length: 245
  • Mass: 27764
  • Checksum: 175534325E9E37C4
  • Sequence:
  • MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR 
    VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK 
    MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE 
    ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA 
    EGAEN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.