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Q9Y2W1

- TR150_HUMAN

UniProt

Q9Y2W1 - TR150_HUMAN

Protein

Thyroid hormone receptor-associated protein 3

Gene

THRAP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi552 – 5598ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    3. phosphoprotein binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. receptor activity Source: UniProtKB
    7. RNA polymerase II transcription cofactor activity Source: UniProtKB
    8. thyroid hormone receptor binding Source: UniProtKB
    9. transcription coactivator activity Source: MGI
    10. transcription cofactor activity Source: UniProtKB
    11. vitamin D receptor binding Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    3. mRNA processing Source: UniProtKB-KW
    4. mRNA stabilization Source: UniProtKB
    5. nuclear-transcribed mRNA catabolic process Source: UniProtKB
    6. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    9. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    10. RNA splicing Source: UniProtKB-KW
    11. transcription initiation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9Y2W1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thyroid hormone receptor-associated protein 3
    Alternative name(s):
    Thyroid hormone receptor-associated protein complex 150 kDa component
    Short name:
    Trap150
    Gene namesi
    Name:THRAP3
    Synonyms:TRAP150
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:22964. THRAP3.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. mediator complex Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi406 – 4061S → A: Reduces phosphorylation upon DNA damage; when associated with A-408. 1 Publication
    Mutagenesisi408 – 4081S → A: Reduces phosphorylation upon DNA damage; when associated with A-406. 1 Publication

    Organism-specific databases

    PharmGKBiPA134893249.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 955954Thyroid hormone receptor-associated protein 3PRO_0000065583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei17 – 171Dimethylated arginine1 Publication
    Modified residuei221 – 2211N6-acetyllysine1 Publication
    Modified residuei232 – 2321Phosphoserine3 Publications
    Modified residuei237 – 2371Phosphoserine2 Publications
    Modified residuei240 – 2401Phosphoserine3 Publications
    Modified residuei243 – 2431Phosphoserine10 Publications
    Modified residuei248 – 2481Phosphoserine5 Publications
    Modified residuei253 – 2531Phosphoserine6 Publications
    Modified residuei257 – 2571Phosphoserine2 Publications
    Modified residuei315 – 3151Phosphoserine4 Publications
    Modified residuei320 – 3201Phosphoserine5 Publications
    Modified residuei339 – 3391Phosphoserine2 Publications
    Modified residuei346 – 3461N6-acetyllysineBy similarity
    Modified residuei379 – 3791Phosphoserine4 Publications
    Modified residuei406 – 4061Phosphoserine3 Publications
    Modified residuei408 – 4081Phosphoserine4 Publications
    Modified residuei455 – 4551N6-acetyllysine1 Publication
    Modified residuei470 – 4701N6-acetyllysineBy similarity
    Modified residuei481 – 4811N6-acetyllysineBy similarity
    Modified residuei519 – 5191N6-acetyllysine1 Publication
    Modified residuei527 – 5271N6-acetyllysineBy similarity
    Modified residuei535 – 5351Phosphoserine2 Publications
    Modified residuei558 – 5581N6-acetyllysineBy similarity
    Modified residuei575 – 5751Phosphoserine5 Publications
    Modified residuei622 – 6221Phosphoserine3 Publications
    Modified residuei672 – 6721Phosphoserine2 Publications
    Modified residuei682 – 6821Phosphoserine5 Publications
    Modified residuei698 – 6981Phosphoserine3 Publications
    Modified residuei811 – 8111N6-acetyllysine1 Publication
    Modified residuei874 – 8741Phosphothreonine3 Publications
    Modified residuei928 – 9281Phosphoserine7 Publications
    Modified residuei939 – 9391Phosphoserine5 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2W1.
    PaxDbiQ9Y2W1.
    PeptideAtlasiQ9Y2W1.
    PRIDEiQ9Y2W1.

    PTM databases

    PhosphoSiteiQ9Y2W1.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2W1.
    BgeeiQ9Y2W1.
    CleanExiHS_THRAP3.
    GenevestigatoriQ9Y2W1.

    Organism-specific databases

    HPAiCAB017472.
    HPA012041.

    Interactioni

    Subunit structurei

    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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF4A3P389192EBI-352039,EBI-299104
    NXF1Q9UBU94EBI-352039,EBI-398874
    SFPQP232466EBI-352039,EBI-355453
    SNW1Q135734EBI-352039,EBI-632715

    Protein-protein interaction databases

    BioGridi115292. 87 interactions.
    IntActiQ9Y2W1. 38 interactions.
    MINTiMINT-1684118.
    STRINGi9606.ENSP00000346634.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2W1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 190189Required for mRNA splicing activationAdd
    BLAST
    Regioni359 – 955597Required for mRNA decay activityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 339333Ser-richAdd
    BLAST
    Compositional biasi12 – 161150Arg-richAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG43306.
    HOGENOMiHOG000231570.
    HOVERGENiHBG054554.
    InParanoidiQ9Y2W1.
    KOiK13112.
    OMAiRSTEKTE.
    OrthoDBiEOG7RBZ7X.
    PhylomeDBiQ9Y2W1.
    TreeFamiTF335939.

    Family and domain databases

    InterProiIPR026667. THRAP3.
    IPR029199. THRAP3_BCLAF1.
    [Graphical view]
    PANTHERiPTHR15268:SF16. PTHR15268:SF16. 1 hit.
    PfamiPF15440. THRAP3_BCLAF1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y2W1-1 [UniParc]FASTAAdd to Basket

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    MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR    50
    SRSYSPAHNR ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN 100
    RGGYGNYRSN WQNYRQAYSP RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS 150
    SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK KSSSKDSRPS QAAGDNQGDE 200
    AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS ELSPRERSPA 250
    LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG 300
    QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE 350
    EQKTENGKDK EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE 400
    KPFRGSQSPK RYKLRDDFEK KMADFHKEEM DDQDKDKAKG RKESEFDDEP 450
    KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG KEKQRKTEEL EEESFPERSK 500
    KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK TSESRDKLGA 550
    KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS 600
    NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL 650
    HERFTKYLKR GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR 700
    EPGYKAEGKY KDDPVDLRLD IERRKKHKER DLKRGKSRES VDSRDSSHSR 750
    ERSAEKTEKT HKGSKKQKKH RRARDRSRSS SSSSQSSHSY KAEEYTEETE 800
    EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG RGWGRGNYSG 850
    NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG 900
    RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI 950
    QPTTE 955
    Length:955
    Mass (Da):108,666
    Last modified:May 16, 2006 - v2
    Checksum:i01131D2479B8C0F4
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011A → V.3 Publications
    Corresponds to variant rs6425977 [ dbSNP | Ensembl ].
    VAR_024552

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS405.1.
    RefSeqiNP_005110.2. NM_005119.3.
    UniGeneiHs.744057.

    Genome annotation databases

    EnsembliENST00000354618; ENSP00000346634; ENSG00000054118.
    ENST00000469141; ENSP00000433825; ENSG00000054118.
    GeneIDi9967.
    KEGGihsa:9967.
    UCSCiuc001cae.4. human.

    Polymorphism databases

    DMDMi97537467.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS405.1.
    RefSeqi NP_005110.2. NM_005119.3.
    UniGenei Hs.744057.

    3D structure databases

    ProteinModelPortali Q9Y2W1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115292. 87 interactions.
    IntActi Q9Y2W1. 38 interactions.
    MINTi MINT-1684118.
    STRINGi 9606.ENSP00000346634.

    PTM databases

    PhosphoSitei Q9Y2W1.

    Polymorphism databases

    DMDMi 97537467.

    Proteomic databases

    MaxQBi Q9Y2W1.
    PaxDbi Q9Y2W1.
    PeptideAtlasi Q9Y2W1.
    PRIDEi Q9Y2W1.

    Protocols and materials databases

    DNASUi 9967.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354618 ; ENSP00000346634 ; ENSG00000054118 .
    ENST00000469141 ; ENSP00000433825 ; ENSG00000054118 .
    GeneIDi 9967.
    KEGGi hsa:9967.
    UCSCi uc001cae.4. human.

    Organism-specific databases

    CTDi 9967.
    GeneCardsi GC01P036690.
    HGNCi HGNC:22964. THRAP3.
    HPAi CAB017472.
    HPA012041.
    MIMi 603809. gene.
    neXtProti NX_Q9Y2W1.
    PharmGKBi PA134893249.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43306.
    HOGENOMi HOG000231570.
    HOVERGENi HBG054554.
    InParanoidi Q9Y2W1.
    KOi K13112.
    OMAi RSTEKTE.
    OrthoDBi EOG7RBZ7X.
    PhylomeDBi Q9Y2W1.
    TreeFami TF335939.

    Enzyme and pathway databases

    SignaLinki Q9Y2W1.

    Miscellaneous databases

    ChiTaRSi THRAP3. human.
    GeneWikii THRAP3.
    GenomeRNAii 9967.
    NextBioi 37614.
    PROi Q9Y2W1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2W1.
    Bgeei Q9Y2W1.
    CleanExi HS_THRAP3.
    Genevestigatori Q9Y2W1.

    Family and domain databases

    InterProi IPR026667. THRAP3.
    IPR029199. THRAP3_BCLAF1.
    [Graphical view ]
    PANTHERi PTHR15268:SF16. PTHR15268:SF16. 1 hit.
    Pfami PF15440. THRAP3_BCLAF1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. 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. 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. 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. 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. Cited for: FUNCTION, INTERACTION WITH HELZ2 AND PPARG, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiTR150_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2W1
    Secondary accession number(s): D3DPS5, Q5VTK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3