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Q9Y2W1 (TR150_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid hormone receptor-associated protein 3
Alternative name(s):
Thyroid hormone receptor-associated protein complex 150 kDa component
Short name=Trap150
Gene names
Name:THRAP3
Synonyms:TRAP150
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length955 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Ref.21 Ref.22 Ref.26 Ref.29

Subunit structure

Associated with the large multiprotein complex TRAP (Mediator complex-like). Interacts with SFPQ; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an ESS1 exonic splicing silencer element-containing RNA. Interacts with NXF1. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes. Interacts with HELZ2 and PPARG. Ref.1 Ref.10 Ref.12 Ref.21 Ref.22 Ref.29

Subcellular location

Nucleus Ref.22 Ref.29.

Tissue specificity

Ubiquitous. Ref.1

Post-translational modification

ADP-ribosylation during genotoxic stress promotes accumulation in nuclear speckles.

Sequence caution

The sequence AAH37554.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Receptor
   PTMAcetylation
ADP-ribosylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

androgen receptor signaling pathway

Inferred from direct assay PubMed 12218053. Source: UniProtKB

intracellular steroid hormone receptor signaling pathway

Inferred from direct assay PubMed 11867769. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA stabilization

Inferred from mutant phenotype Ref.12. Source: UniProtKB

nuclear-transcribed mRNA catabolic process

Inferred from direct assay Ref.22. Source: UniProtKB

positive regulation of mRNA splicing, via spliceosome

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12037571. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype Ref.21. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 12218053. Source: UniProtKB

   Cellular_componentmediator complex

Inferred from direct assay Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 10235267Ref.22. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II transcription cofactor activity

Inferred from direct assay Ref.1. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Non-traceable author statement PubMed 10235266. Source: UniProtKB

phosphoprotein binding

Inferred from direct assay Ref.21. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

receptor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 12037571. Source: MGI

transcription cofactor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

vitamin D receptor binding

Non-traceable author statement PubMed 10235266. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.27
Chain2 – 955954Thyroid hormone receptor-associated protein 3
PRO_0000065583

Regions

Nucleotide binding552 – 5598ATP Potential
Region2 – 190189Required for mRNA splicing activation
Region359 – 955597Required for mRNA decay activity
Compositional bias7 – 339333Ser-rich
Compositional bias12 – 161150Arg-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.27
Modified residue171Dimethylated arginine Ref.5
Modified residue2211N6-acetyllysine Ref.20
Modified residue2321Phosphoserine Ref.16 Ref.23
Modified residue2371Phosphoserine Ref.16
Modified residue2401Phosphoserine Ref.7 Ref.16
Modified residue2431Phosphoserine Ref.5 Ref.7 Ref.8 Ref.13 Ref.14 Ref.15 Ref.16 Ref.23 Ref.25
Modified residue2481Phosphoserine Ref.7 Ref.13 Ref.16 Ref.23
Modified residue2531Phosphoserine Ref.7 Ref.13 Ref.16 Ref.23 Ref.25
Modified residue2571Phosphoserine Ref.23
Modified residue3151Phosphoserine Ref.7 Ref.23 Ref.25
Modified residue3201Phosphoserine Ref.5 Ref.7 Ref.23 Ref.25
Modified residue3391Phosphoserine Ref.25
Modified residue3461N6-acetyllysine By similarity
Modified residue3791Phosphoserine Ref.16 Ref.23 Ref.25
Modified residue4061Phosphoserine Ref.16 Ref.25
Modified residue4081Phosphoserine Ref.16 Ref.23 Ref.25
Modified residue4551N6-acetyllysine Ref.20
Modified residue4701N6-acetyllysine By similarity
Modified residue4811N6-acetyllysine By similarity
Modified residue5191N6-acetyllysine Ref.20
Modified residue5271N6-acetyllysine By similarity
Modified residue5351Phosphoserine Ref.25
Modified residue5581N6-acetyllysine By similarity
Modified residue5751Phosphoserine Ref.7 Ref.16 Ref.23 Ref.25
Modified residue6221Phosphoserine Ref.23 Ref.25
Modified residue6721Phosphoserine Ref.7
Modified residue6821Phosphoserine Ref.5 Ref.16 Ref.23 Ref.25
Modified residue6981Phosphoserine Ref.23 Ref.25
Modified residue8111N6-acetyllysine Ref.20
Modified residue8741Phosphothreonine Ref.16 Ref.19
Modified residue9281Phosphoserine Ref.7 Ref.16 Ref.17 Ref.19 Ref.23 Ref.25
Modified residue9391Phosphoserine Ref.16 Ref.19 Ref.23 Ref.25

Natural variations

Natural variant2011A → V. Ref.1 Ref.3 Ref.4
Corresponds to variant rs6425977 [ dbSNP | Ensembl ].
VAR_024552

Experimental info

Mutagenesis4061S → A: Reduces phosphorylation upon DNA damage; when associated with A-408. Ref.26
Mutagenesis4081S → A: Reduces phosphorylation upon DNA damage; when associated with A-406. Ref.26

Sequences

Sequence LengthMass (Da)Tools
Q9Y2W1 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 01131D2479B8C0F4

FASTA955108,666
        10         20         30         40         50         60 
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR SRSYSPAHNR 

        70         80         90        100        110        120 
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP 

       130        140        150        160        170        180 
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK 

       190        200        210        220        230        240 
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS 

       250        260        270        280        290        300 
ELSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG 

       310        320        330        340        350        360 
QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE EQKTENGKDK 

       370        380        390        400        410        420 
EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE KPFRGSQSPK RYKLRDDFEK 

       430        440        450        460        470        480 
KMADFHKEEM DDQDKDKAKG RKESEFDDEP KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG 

       490        500        510        520        530        540 
KEKQRKTEEL EEESFPERSK KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK 

       550        560        570        580        590        600 
TSESRDKLGA KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS 

       610        620        630        640        650        660 
NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL HERFTKYLKR 

       670        680        690        700        710        720 
GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR EPGYKAEGKY KDDPVDLRLD 

       730        740        750        760        770        780 
IERRKKHKER DLKRGKSRES VDSRDSSHSR ERSAEKTEKT HKGSKKQKKH RRARDRSRSS 

       790        800        810        820        830        840 
SSSSQSSHSY KAEEYTEETE EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG 

       850        860        870        880        890        900 
RGWGRGNYSG NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG 

       910        920        930        940        950 
RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI QPTTE 

« Hide

References

« Hide 'large scale' references
[1]"Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators."
Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y., Zhang X., Qin J., Roeder R.G.
Mol. Cell 3:361-370(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 490-500, TISSUE SPECIFICITY, IDENTIFICATION IN TRAP COMPLEX, VARIANT VAL-201.
Tissue: Cervix carcinoma.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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], VARIANT VAL-201.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-201.
Tissue: Brain.
[5]Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 186-202; 216-245; 253-261; 314-333; 376-387; 443-451; 468-481; 486-498; 573-591; 609-653; 678-687; 710-718; 792-802; 864-876; 879-893 AND 927-944, METHYLATION AT ARG-17, PHOSPHORYLATION AT SER-243; SER-320 AND SER-682, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[6]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; SER-248; SER-253; SER-315; SER-320; SER-575; SER-672 AND SER-928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Protein composition of human mRNPs spliced in vitro and differential requirements for mRNP protein recruitment."
Merz C., Urlaub H., Will C.L., Luhrmann R.
RNA 13:116-128(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"Regulation of cyclin D1 RNA stability by SNIP1."
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.
Cancer Res. 68:7621-7628(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SNARP COMPLEX.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248 AND SER-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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; SER-237; SER-240; SER-243; SER-248; SER-253; SER-379; SER-406; SER-408; SER-575; SER-682; THR-874; SER-928 AND SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-874; SER-928 AND SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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 LYS-221; LYS-455; LYS-519 AND LYS-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing."
Heyd F., Lynch K.W.
Mol. Cell 40:126-137(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SFPQ.
[22]"TRAP150 activates pre-mRNA splicing and promotes nuclear mRNA degradation."
Lee K.M., Hsu I.W., Tarn W.Y.
Nucleic Acids Res. 38:3340-3350(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1.
[23]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-243; SER-248; SER-253; SER-257; SER-315; SER-320; SER-379; SER-408; SER-575; SER-622; SER-682; SER-698; SER-928 AND SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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].
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-253; SER-315; SER-320; SER-339; SER-379; SER-406; SER-408; SER-535; SER-575; SER-622; SER-682; SER-698; SER-928 AND SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response."
Beli P., Lukashchuk N., Wagner S.A., Weinert B.T., Olsen J.V., Baskcomb L., Mann M., Jackson S.P., Choudhary C.
Mol. Cell 46:212-225(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF SER-406 AND SER-408.
[27]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[28]"Proteome-wide identification of poly(ADP-Ribosyl)ation targets in different genotoxic stress responses."
Jungmichel S., Rosenthal F., Altmeyer M., Lukas J., Hottiger M.O., Nielsen M.L.
Mol. Cell 52:272-285(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ADP-RIBOSYLATION.
[29]"THRAP3 interacts with HELZ2 and plays a novel role in adipocyte differentiation."
Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S., Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K., Okada S., Yamada M., Mori M.
Mol. Endocrinol. 27:769-780(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HELZ2 AND PPARG, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117756 mRNA. Translation: AAD22034.1.
AL591845 Genomic DNA. Translation: CAH71859.1.
CH471059 Genomic DNA. Translation: EAX07379.1.
CH471059 Genomic DNA. Translation: EAX07380.1.
BC037554 mRNA. Translation: AAH37554.1. Sequence problems.
BC112330 mRNA. Translation: AAI12331.1.
BC112350 mRNA. Translation: AAI12351.1.
RefSeqNP_005110.2. NM_005119.3.
UniGeneHs.744057.

3D structure databases

ProteinModelPortalQ9Y2W1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115292. 78 interactions.
IntActQ9Y2W1. 38 interactions.
MINTMINT-1684118.
STRING9606.ENSP00000346634.

PTM databases

PhosphoSiteQ9Y2W1.

Polymorphism databases

DMDM97537467.

Proteomic databases

PaxDbQ9Y2W1.
PeptideAtlasQ9Y2W1.
PRIDEQ9Y2W1.

Protocols and materials databases

DNASU9967.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354618; ENSP00000346634; ENSG00000054118.
ENST00000469141; ENSP00000433825; ENSG00000054118.
GeneID9967.
KEGGhsa:9967.
UCSCuc001cae.4. human.

Organism-specific databases

CTD9967.
GeneCardsGC01P036690.
HGNCHGNC:22964. THRAP3.
HPACAB017472.
HPA012041.
MIM603809. gene.
neXtProtNX_Q9Y2W1.
PharmGKBPA134893249.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43306.
HOGENOMHOG000231570.
HOVERGENHBG054554.
InParanoidQ9Y2W1.
KOK13112.
OMARSTEKTE.
OrthoDBEOG7RBZ7X.
PhylomeDBQ9Y2W1.
TreeFamTF335939.

Enzyme and pathway databases

SignaLinkQ9Y2W1.

Gene expression databases

ArrayExpressQ9Y2W1.
BgeeQ9Y2W1.
CleanExHS_THRAP3.
GenevestigatorQ9Y2W1.

Family and domain databases

InterProIPR026667. THRAP3.
[Graphical view]
PANTHERPTHR15268:SF7. PTHR15268:SF7. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTHRAP3. human.
GeneWikiTHRAP3.
GenomeRNAi9967.
NextBio37614.
PROQ9Y2W1.
SOURCESearch...

Entry information

Entry nameTR150_HUMAN
AccessionPrimary (citable) accession number: Q9Y2W1
Secondary accession number(s): D3DPS5, Q5VTK6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 134 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM