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Protein

Thyroid hormone receptor-associated protein 3

Gene

THRAP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798).5 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. receptor activity Source: UniProtKB
  6. RNA polymerase II transcription cofactor activity Source: UniProtKB
  7. thyroid hormone receptor binding Source: UniProtKB
  8. transcription coactivator activity Source: MGI
  9. transcription cofactor activity Source: UniProtKB
  10. 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
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, 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. extracellular vesicular exosome Source: UniProtKB
  2. mediator complex Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: UniProtKB
Complete GO annotation...

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 – 2321Phosphoserine2 Publications
Modified residuei237 – 2371Phosphoserine1 Publication
Modified residuei240 – 2401Phosphoserine2 Publications
Modified residuei243 – 2431Phosphoserine9 Publications
Modified residuei248 – 2481Phosphoserine4 Publications
Modified residuei253 – 2531Phosphoserine5 Publications
Modified residuei257 – 2571Phosphoserine1 Publication
Modified residuei315 – 3151Phosphoserine3 Publications
Modified residuei320 – 3201Phosphoserine4 Publications
Modified residuei339 – 3391Phosphoserine1 Publication
Modified residuei346 – 3461N6-acetyllysineBy similarity
Modified residuei379 – 3791Phosphoserine3 Publications
Modified residuei406 – 4061Phosphoserine2 Publications
Modified residuei408 – 4081Phosphoserine3 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 – 5351Phosphoserine1 Publication
Modified residuei558 – 5581N6-acetyllysineBy similarity
Modified residuei575 – 5751Phosphoserine4 Publications
Modified residuei622 – 6221Phosphoserine2 Publications
Modified residuei672 – 6721Phosphoserine1 Publication
Modified residuei682 – 6821Phosphoserine4 Publications
Modified residuei698 – 6981Phosphoserine2 Publications
Modified residuei811 – 8111N6-acetyllysine1 Publication
Modified residuei874 – 8741Phosphothreonine2 Publications
Modified residuei928 – 9281Phosphoserine6 Publications
Modified residuei939 – 9391Phosphoserine4 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

BgeeiQ9Y2W1.
CleanExiHS_THRAP3.
ExpressionAtlasiQ9Y2W1. baseline and differential.
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. Interacts with CLOCK and ARNTL/BMAL1 (By similarity).By similarity6 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. 97 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.
GeneTreeiENSGT00530000063211.
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

« Hide

        10         20         30         40         50
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR
60 70 80 90 100
SRSYSPAHNR ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN
110 120 130 140 150
RGGYGNYRSN WQNYRQAYSP RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS
160 170 180 190 200
SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK KSSSKDSRPS QAAGDNQGDE
210 220 230 240 250
AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS ELSPRERSPA
260 270 280 290 300
LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG
310 320 330 340 350
QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE
360 370 380 390 400
EQKTENGKDK EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE
410 420 430 440 450
KPFRGSQSPK RYKLRDDFEK KMADFHKEEM DDQDKDKAKG RKESEFDDEP
460 470 480 490 500
KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG KEKQRKTEEL EEESFPERSK
510 520 530 540 550
KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK TSESRDKLGA
560 570 580 590 600
KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS
610 620 630 640 650
NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL
660 670 680 690 700
HERFTKYLKR GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR
710 720 730 740 750
EPGYKAEGKY KDDPVDLRLD IERRKKHKER DLKRGKSRES VDSRDSSHSR
760 770 780 790 800
ERSAEKTEKT HKGSKKQKKH RRARDRSRSS SSSSQSSHSY KAEEYTEETE
810 820 830 840 850
EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG RGWGRGNYSG
860 870 880 890 900
NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG
910 920 930 940 950
RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI

QPTTE
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.Contaminating sequence. Potential poly-A sequence.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9Y2W1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115292. 97 interactions.
IntActiQ9Y2W1. 38 interactions.
MINTiMINT-1684118.
STRINGi9606.ENSP00000346634.

PTM databases

PhosphoSiteiQ9Y2W1.

Polymorphism databases

DMDMi97537467.

Proteomic databases

MaxQBiQ9Y2W1.
PaxDbiQ9Y2W1.
PeptideAtlasiQ9Y2W1.
PRIDEiQ9Y2W1.

Protocols and materials databases

DNASUi9967.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9967.
GeneCardsiGC01P036690.
HGNCiHGNC:22964. THRAP3.
HPAiCAB017472.
HPA012041.
MIMi603809. gene.
neXtProtiNX_Q9Y2W1.
PharmGKBiPA134893249.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43306.
GeneTreeiENSGT00530000063211.
HOGENOMiHOG000231570.
HOVERGENiHBG054554.
InParanoidiQ9Y2W1.
KOiK13112.
OMAiRSTEKTE.
OrthoDBiEOG7RBZ7X.
PhylomeDBiQ9Y2W1.
TreeFamiTF335939.

Enzyme and pathway databases

SignaLinkiQ9Y2W1.

Miscellaneous databases

ChiTaRSiTHRAP3. human.
GeneWikiiTHRAP3.
GenomeRNAii9967.
NextBioi37614.
PROiQ9Y2W1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2W1.
CleanExiHS_THRAP3.
ExpressionAtlasiQ9Y2W1. baseline and differential.
GenevestigatoriQ9Y2W1.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
  30. "A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the basic transcriptional machinery."
    Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.
    Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

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: February 4, 2015
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.