CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013748
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
221IKGSESSKPWPDATTacetylation[1]
375DKEKLKEKGGFSDADacetylation[1]
398APKTDTEKPFRGSQSacetylation[1]
417KLRDDFEKKMADFHKacetylation[1]
432EEMDEQDKDKCKGRKacetylation[1]
452DEPKFISKVIAGASKacetylation[1]
516HRGFVPEKNFRVTAYacetylation[1]
555KGDFSSGKSSFSITRacetylation[1]
653TLHERFTKYLKRGNEacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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 (By similarity). 
Sequence Annotation
 NP_BIND 549 556 ATP (Potential).
 REGION 1 190 Required for mRNA splicing activation (By
 REGION 359 951 Required for mRNA decay activity (By
 MOD_RES 17 17 Dimethylated arginine (By similarity).
 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 (By similarity).
 MOD_RES 233 233 Phosphoserine (By similarity).
 MOD_RES 238 238 Phosphoserine (By similarity).
 MOD_RES 240 240 Phosphoserine (By similarity).
 MOD_RES 243 243 Phosphoserine (By similarity).
 MOD_RES 248 248 Phosphoserine.
 MOD_RES 253 253 Phosphoserine.
 MOD_RES 257 257 Phosphoserine (By similarity).
 MOD_RES 264 264 Phosphoserine (By similarity).
 MOD_RES 268 268 Phosphoserine (By similarity).
 MOD_RES 315 315 Phosphoserine (By similarity).
 MOD_RES 320 320 Phosphoserine (By similarity).
 MOD_RES 324 324 Phosphothreonine (By similarity).
 MOD_RES 339 339 Phosphoserine (By similarity).
 MOD_RES 379 379 Phosphoserine (By similarity).
 MOD_RES 403 403 Phosphoserine (By similarity).
 MOD_RES 405 405 Phosphoserine (By similarity).
 MOD_RES 452 452 N6-acetyllysine (By similarity).
 MOD_RES 516 516 N6-acetyllysine (By similarity).
 MOD_RES 532 532 Phosphoserine (By similarity).
 MOD_RES 572 572 Phosphoserine (By similarity).
 MOD_RES 619 619 Phosphoserine (By similarity).
 MOD_RES 669 669 Phosphoserine (By similarity).
 MOD_RES 679 679 Phosphoserine (By similarity).
 MOD_RES 695 695 Phosphoserine (By similarity).
 MOD_RES 808 808 N6-acetyllysine (By similarity).
 MOD_RES 860 860 Phosphoserine (By similarity).
 MOD_RES 870 870 Phosphothreonine (By similarity).
 MOD_RES 924 924 Phosphoserine (By similarity).
 MOD_RES 935 935 Phosphoserine (By similarity).
 MOD_RES 937 937 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Activator; ATP-binding; Complete proteome; Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 951 AA 
Protein Sequence
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSVSRS RKRRLSSRSR SRSYSPAHNR 60
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP 120
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSTKEK 180
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDIKGSESS KPWPDATTYG TGSASRASVS 240
DLSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSNA SQMGSSMSGG AGYQSGAHQG 300
PFDHGSGSLS PSKKSPVGKS PPATGSAYGS SQKEESAASG GAAYTKRYLE EQKTENGKDK 360
EQKQTNTDKE KLKEKGGFSD ADVKMKSDPF APKTDTEKPF RGSQSPKRYK LRDDFEKKMA 420
DFHKEEMDEQ DKDKCKGRKE PEFDDEPKFI SKVIAGASKN QEEEKSGKWE SLHAGKEKQR 480
KAEELEEEPF TERSRKEERG GSKRSESGHR GFVPEKNFRV TAYKAVQEKS SSPPPRKTSE 540
SRDKLGNKGD FSSGKSSFSI TREAQVNVRM DSFDEDLARP SGLLAQERKL CRDLVHSNKK 600
EQEFRSIFQH IQSAQSQRSP SELFAQHIVT IVHHVKEHHF GSSGMTLHER FTKYLKRGNE 660
QEAAKTKKSP EIHRRIDISP STFRKHGLTH EELKSPREPG YKAEGKYKDD PVDLRLDIER 720
RKKHKERDLK RGKSRESVDS RDSSHSRERS TEKTEKTHKG SKKQKKHRRA RDRSRSSSSS 780
SQSSHSYKAE EYPEEAEDRE ESTTGFDKSR LGTKDFVGPN ERGGRARGTF QFRARGRGWG 840
RGNYSGNNNN NSNNDFQKRS REEEWDPEYT PKSKKYYLHD DREGEGSDKW MSRGRGRGAF 900
PRGRGRFMFR KSSTSPKWAH DKFSGEEGEI EDDESGTENR EEKDSLQPSA E 951 
Gene Ontology
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051219; F:phosphoprotein binding; ISS:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
 GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISS:UniProtKB.
 GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR026667; THRAP3. 
Pfam
  
SMART
  
PROSITE
  
PRINTS