Details for: THRAP3

Gene ID: 9967

Symbol: THRAP3

Ensembl ID: ENSG00000054118

Description: thyroid hormone receptor associated protein 3

Associated with

Other Information

Genular Protein ID: 510248252

Symbol: TR150_HUMAN

Name: Thyroid hormone receptor-associated protein 3

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10198638

Title: Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.

PubMed ID: 10198638

DOI: 10.1016/s1097-2765(00)80463-3

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

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: 14654843

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

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15144186

Title: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.

PubMed ID: 15144186

DOI: 10.1021/ac035352d

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17095540

Title: Protein composition of human mRNPs spliced in vitro and differential requirements for mRNP protein recruitment.

PubMed ID: 17095540

DOI: 10.1261/rna.336807

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18794151

Title: Regulation of cyclin D1 RNA stability by SNIP1.

PubMed ID: 18794151

DOI: 10.1158/0008-5472.can-08-1217

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

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: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

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: 20932480

Title: Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing.

PubMed ID: 20932480

DOI: 10.1016/j.molcel.2010.09.013

PubMed ID: 20123736

Title: TRAP150 activates pre-mRNA splicing and promotes nuclear mRNA degradation.

PubMed ID: 20123736

DOI: 10.1093/nar/gkq017

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: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22424773

Title: Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.

PubMed ID: 22424773

DOI: 10.1016/j.molcel.2012.01.026

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: 24100041

Title: Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle.

PubMed ID: 24100041

DOI: 10.1074/jbc.m113.500397

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24055347

Title: Proteome-wide identification of poly(ADP-Ribosyl)ation targets in different genotoxic stress responses.

PubMed ID: 24055347

DOI: 10.1016/j.molcel.2013.08.026

PubMed ID: 23525231

Title: THRAP3 interacts with HELZ2 and plays a novel role in adipocyte differentiation.

PubMed ID: 23525231

DOI: 10.1210/me.2012-1332

PubMed ID: 24043798

Title: A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the basic transcriptional machinery.

PubMed ID: 24043798

DOI: 10.1073/pnas.1305980110

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: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

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

Sequence Information:

  • Length: 955
  • Mass: 108666
  • Checksum: 01131D2479B8C0F4
  • Sequence:
  • MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR SRSYSPAHNR 
    ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP 
    RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK 
    KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS 
    ELSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG 
    QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE EQKTENGKDK 
    EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE KPFRGSQSPK RYKLRDDFEK 
    KMADFHKEEM DDQDKDKAKG RKESEFDDEP KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG 
    KEKQRKTEEL EEESFPERSK KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK 
    TSESRDKLGA KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS 
    NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL HERFTKYLKR 
    GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR EPGYKAEGKY KDDPVDLRLD 
    IERRKKHKER DLKRGKSRES VDSRDSSHSR ERSAEKTEKT HKGSKKQKKH RRARDRSRSS 
    SSSSQSSHSY KAEEYTEETE EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG 
    RGWGRGNYSG NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG 
    RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI QPTTE

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.