CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023710
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thyroid hormone receptor-associated protein 3 
Protein Synonyms/Alias
 Thyroid hormone receptor-associated protein complex 150 kDa component; Trap150 
Gene Name
 THRAP3 
Gene Synonyms/Alias
 TRAP150 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
221TKASESSKPWPDATYacetylation[1, 2, 3]
221TKASESSKPWPDATYubiquitination[4, 5, 6, 7]
387DTGLGDGKMKSDSFAacetylation[3, 8]
401APKTDSEKPFRGSQSacetylation[1, 2, 8]
420KLRDDFEKKMADFHKacetylation[1, 8]
451SEFDDEPKFMSKVIGubiquitination[4, 7]
455DEPKFMSKVIGANKNacetylation[1]
461SKVIGANKNQEEEKSubiquitination[9]
470QEEEKSGKWEGLVYAacetylation[8]
470QEEEKSGKWEGLVYAubiquitination[4, 7]
519HRGFVPEKNFRVTAYacetylation[1, 2, 8]
519HRGFVPEKNFRVTAYubiquitination[4, 7]
527NFRVTAYKAVQEKSSacetylation[2, 8]
558KGDFPTGKSSFSITRubiquitination[4, 7]
709PGYKAEGKYKDDPVDacetylation[1]
756SRERSAEKTEKTHKGmethylation[10]
811ESTTGFDKSRLGTKDacetylation[1, 3]
926SPKWAHDKFSGEEGEacetylation[3]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837] 
Functional Description
 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 indepenedent 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. 
Sequence Annotation
 NP_BIND 552 559 ATP (Potential).
 REGION 1 190 Required for mRNA splicing activation.
 REGION 359 955 Required for mRNA decay activity.
 MOD_RES 17 17 Dimethylated arginine.
 MOD_RES 51 51 Phosphoserine (By similarity).
 MOD_RES 53 53 Phosphoserine (By similarity).
 MOD_RES 55 55 Phosphoserine (By similarity).
 MOD_RES 119 119 Phosphoserine (By similarity).
 MOD_RES 134 134 Phosphoserine (By similarity).
 MOD_RES 221 221 N6-acetyllysine.
 MOD_RES 232 232 Phosphoserine.
 MOD_RES 237 237 Phosphoserine.
 MOD_RES 240 240 Phosphoserine.
 MOD_RES 243 243 Phosphoserine.
 MOD_RES 248 248 Phosphoserine.
 MOD_RES 253 253 Phosphoserine.
 MOD_RES 257 257 Phosphoserine.
 MOD_RES 264 264 Phosphoserine (By similarity).
 MOD_RES 268 268 Phosphoserine (By similarity).
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 320 320 Phosphoserine.
 MOD_RES 324 324 Phosphothreonine (By similarity).
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 379 379 Phosphoserine.
 MOD_RES 406 406 Phosphoserine.
 MOD_RES 408 408 Phosphoserine.
 MOD_RES 455 455 N6-acetyllysine.
 MOD_RES 519 519 N6-acetyllysine.
 MOD_RES 535 535 Phosphoserine.
 MOD_RES 575 575 Phosphoserine.
 MOD_RES 622 622 Phosphoserine.
 MOD_RES 672 672 Phosphoserine.
 MOD_RES 682 682 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.
 MOD_RES 811 811 N6-acetyllysine.
 MOD_RES 874 874 Phosphothreonine.
 MOD_RES 928 928 Phosphoserine.
 MOD_RES 939 939 Phosphoserine.
 MOD_RES 941 941 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Activator; ATP-binding; Complete proteome; Direct protein sequencing; Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 955 AA 
Protein Sequence
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR SRSYSPAHNR 60
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP 120
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK 180
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS 240
ELSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG 300
QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE EQKTENGKDK 360
EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE KPFRGSQSPK RYKLRDDFEK 420
KMADFHKEEM DDQDKDKAKG RKESEFDDEP KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG 480
KEKQRKTEEL EEESFPERSK KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK 540
TSESRDKLGA KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS 600
NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL HERFTKYLKR 660
GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR EPGYKAEGKY KDDPVDLRLD 720
IERRKKHKER DLKRGKSRES VDSRDSSHSR ERSAEKTEKT HKGSKKQKKH RRARDRSRSS 780
SSSSQSSHSY KAEEYTEETE EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG 840
RGWGRGNYSG NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG 900
RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI QPTTE 955 
Gene Ontology
 GO:0016592; C:mediator complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
 GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
 GO:0004872; F:receptor activity; IDA:UniProtKB.
 GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
 GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
 GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
 GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
 GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
 GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB. 
Interpro
 IPR026667; THRAP3. 
Pfam
  
SMART
  
PROSITE
  
PRINTS