CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012079
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable methyltransferase TARBP1 
Protein Synonyms/Alias
 TAR RNA-binding protein 1; TAR RNA-binding protein of 185 kDa; TRP-185 
Gene Name
 TARBP1 
Gene Synonyms/Alias
 TRM3; TRP185 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
239VLSALAEKLLPEPGGubiquitination[1, 2]
449SCSPLGLKLQKFLVTubiquitination[1, 2, 3, 4, 5]
1154DKDELVSKSKKRYYVubiquitination[1, 2, 6]
1432AEWTDVQKKIIPWNSubiquitination[6]
1433EWTDVQKKIIPWNSRubiquitination[1]
1560TQYCFPEKSLLLLGNubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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] 
Functional Description
 Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA. 
Sequence Annotation
 BINDING 1566 1566 S-adenosyl-L-methionine; via carbonyl
 BINDING 1586 1586 S-adenosyl-L-methionine; via amide
 BINDING 1595 1595 S-adenosyl-L-methionine; via amide
 MOD_RES 1442 1442 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Methyltransferase; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1621 AA 
Protein Sequence
MEWVLAEALL SQSRDPRALL GALCQGEASA ERVETLRFLL QRLEDEEARG SGGAGALPEA 60
AREVAAGYLV PLLRSLRGRP AGGPDPSLQP RHRRRVLRAA GAALRSCVRL AGRPQLAAAL 120
AEEALRDLLA GWRAPGAEAA VEVLAAVGPC LRPREDGPLL ERVAGTAVAL ALGGGGDGDE 180
AGPAEDAAAL VAGRLLPVLV QCGGAALRAV WGGLAAPGAS LGSGRVEEKL LVLSALAEKL 240
LPEPGGDRAR GAREAGPDAR RCWRFWRTVQ AGLGQADALT RKRARYLLQR AVEVSAELGA 300
DCTCGPQEGN GPSLFWWSER KKDELLKFWE NYILIMETLE GNQIHVIKPV LPKLNNLFEY 360
AVSEENGCWL FHPSWHMCIY KRMFESENKI LSKEGVIHFL ELYETKILPF SPEFSEFIIG 420
PLMDALSESS LYSRSPGQPI GSCSPLGLKL QKFLVTYISL LPEEIKSSFL LKFIRKMTSR 480
HWCAVPILFL SKALANVPRH KALGIDGLLA LRDVIHCTMI THQILLRGAA QCYLLQTAMN 540
LLDVEKVSLS DVSTFLMSLR QEESLGRGTS LWTELCDWLR VNESYFKPSP TCSSIGLHKT 600
SLNAYVKSIV QEYVKSSAWE TGENCFMPDW FEAKLVSLMV LLAVDVEGMK TQYSGKQRTE 660
NVLRIFLDPL LDVLMKFSTN AYMPLLKTDR CLQLLLKLLN TCRLKGSSAQ DDEVSTVLQN 720
FFMSTTESIS EFILRRLTMN ELNSVSDLDR CHLYLMVLTE LINLHLKVGW KRGNPIWRVI 780
SLLKNASIQH LQEMDSGQEP TVGSQIQRVV SMAALAMVCE AIDQKPELQL DSLHAGPLES 840
FLSSLQLNQT LQKPHAEEQS SYAHPLECSS VLEESSSSQG WGKIVAQYIH DQWVCLSFLL 900
KKYHTLIPTT GSEILEPFLP AVQMPIRTLQ SALEALTVLS SDQVLPVFHC LKVLVPKLLT 960
SSESLCIESF DMAWKIISSL SNTQLIFWAN LKAFVQFVFD NKVLTIAAKI KGQAYFKIKE 1020
IMYKIIEMSA IKTGVFNTLI SYCCQSWIVS ASNVSQGSLS SAKNYSELIL EACIFGTVFR 1080
RDQRLVQDVQ TFIENLGHDC AANIVMENTK REDHYVRICA VKFLCLLDGS NMSHKLFIED 1140
LAIKLLDKDE LVSKSKKRYY VNSLQHRVKN RVWQTLLVLF PRLDQNFLNG IIDRIFQAGF 1200
TNNQASIKYF IEWIIILILH KFPQFLPKFW DCFSYGEENL KTSICTFLAV LSHLDIITQN 1260
IPEKKLILKQ ALIVVLQWCF NHNFSVRLYA LVALKKLWTV CKVLSVEEFD ALTPVIESSL 1320
HQVESMHGAG NAKKNWQRIQ EHFFFATFHP LKDYCLETIF YILPRLSGLI EDEWITIDKF 1380
TRFTDVPLAA GFQWYLSQTQ LSKLKPGDWS QQDIGTNLVE ADNQAEWTDV QKKIIPWNSR 1440
VSDLDLELLF QDRAARLGKS ISRLIVVASL IDKPTNLGGL CRTCEVFGAS VLVVGSLQCI 1500
SDKQFQHLSV SAEQWLPLVE VKPPQLIDYL QQKKTEGYTI IGVEQTAKSL DLTQYCFPEK 1560
SLLLLGNERE GIPANLIQQL DVCVEIPQQG IIRSLNVHVS GALLIWEYTR QQLLSHGDTK 1620
P 1621 
Gene Ontology
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0001510; P:RNA methylation; IEA:GOC.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR016024; ARM-type_fold.
 IPR025806; Prob_MeTrfase_TARBP1.
 IPR001537; SpoU_MeTrfase. 
Pfam
 PF00588; SpoU_methylase 
SMART
  
PROSITE
  
PRINTS