TARB1_HUMAN - dbPTM
TARB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TARB1_HUMAN
UniProt AC Q13395
Protein Name Probable methyltransferase TARBP1
Gene Name TARBP1
Organism Homo sapiens (Human).
Sequence Length 1621
Subcellular Localization
Protein 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..
Protein Sequence MEWVLAEALLSQSRDPRALLGALCQGEASAERVETLRFLLQRLEDEEARGSGGAGALPEAAREVAAGYLVPLLRSLRGRPAGGPDPSLQPRHRRRVLRAAGAALRSCVRLAGRPQLAAALAEEALRDLLAGWRAPGAEAAVEVLAAVGPCLRPREDGPLLERVAGTAVALALGGGGDGDEAGPAEDAAALVAGRLLPVLVQCGGAALRAVWGGLAAPGASLGSGRVEEKLLVLSALAEKLLPEPGGDRARGAREAGPDARRCWRFWRTVQAGLGQADALTRKRARYLLQRAVEVSAELGADCTCGPQEGNGPSLFWWSERKKDELLKFWENYILIMETLEGNQIHVIKPVLPKLNNLFEYAVSEENGCWLFHPSWHMCIYKRMFESENKILSKEGVIHFLELYETKILPFSPEFSEFIIGPLMDALSESSLYSRSPGQPIGSCSPLGLKLQKFLVTYISLLPEEIKSSFLLKFIRKMTSRHWCAVPILFLSKALANVPRHKALGIDGLLALRDVIHCTMITHQILLRGAAQCYLLQTAMNLLDVEKVSLSDVSTFLMSLRQEESLGRGTSLWTELCDWLRVNESYFKPSPTCSSIGLHKTSLNAYVKSIVQEYVKSSAWETGENCFMPDWFEAKLVSLMVLLAVDVEGMKTQYSGKQRTENVLRIFLDPLLDVLMKFSTNAYMPLLKTDRCLQLLLKLLNTCRLKGSSAQDDEVSTVLQNFFMSTTESISEFILRRLTMNELNSVSDLDRCHLYLMVLTELINLHLKVGWKRGNPIWRVISLLKNASIQHLQEMDSGQEPTVGSQIQRVVSMAALAMVCEAIDQKPELQLDSLHAGPLESFLSSLQLNQTLQKPHAEEQSSYAHPLECSSVLEESSSSQGWGKIVAQYIHDQWVCLSFLLKKYHTLIPTTGSEILEPFLPAVQMPIRTLQSALEALTVLSSDQVLPVFHCLKVLVPKLLTSSESLCIESFDMAWKIISSLSNTQLIFWANLKAFVQFVFDNKVLTIAAKIKGQAYFKIKEIMYKIIEMSAIKTGVFNTLISYCCQSWIVSASNVSQGSLSSAKNYSELILEACIFGTVFRRDQRLVQDVQTFIENLGHDCAANIVMENTKREDHYVRICAVKFLCLLDGSNMSHKLFIEDLAIKLLDKDELVSKSKKRYYVNSLQHRVKNRVWQTLLVLFPRLDQNFLNGIIDRIFQAGFTNNQASIKYFIEWIIILILHKFPQFLPKFWDCFSYGEENLKTSICTFLAVLSHLDIITQNIPEKKLILKQALIVVLQWCFNHNFSVRLYALVALKKLWTVCKVLSVEEFDALTPVIESSLHQVESMHGAGNAKKNWQRIQEHFFFATFHPLKDYCLETIFYILPRLSGLIEDEWITIDKFTRFTDVPLAAGFQWYLSQTQLSKLKPGDWSQQDIGTNLVEADNQAEWTDVQKKIIPWNSRVSDLDLELLFQDRAARLGKSISRLIVVASLIDKPTNLGGLCRTCEVFGASVLVVGSLQCISDKQFQHLSVSAEQWLPLVEVKPPQLIDYLQQKKTEGYTIIGVEQTAKSLDLTQYCFPEKSLLLLGNEREGIPANLIQQLDVCVEIPQQGIIRSLNVHVSGALLIWEYTRQQLLSHGDTKP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEWVLAEA
-------CHHHHHHH		40.6322223895
75PhosphorylationYLVPLLRSLRGRPAG
HHHHHHHHHCCCCCC		23.5322210691
239UbiquitinationVLSALAEKLLPEPGG
HHHHHHHHHCCCCCC		50.11-
280PhosphorylationLGQADALTRKRARYL
CCCHHHHHHHHHHHH		35.5520071362
392PhosphorylationESENKILSKEGVIHF
HCCCCCCCCCCCHHH		31.94-
393UbiquitinationSENKILSKEGVIHFL
CCCCCCCCCCCHHHH		55.8529967540
433PhosphorylationLSESSLYSRSPGQPI
HCCCCCCCCCCCCCC		31.4124719451
449UbiquitinationSCSPLGLKLQKFLVT
CCCHHHHHHHHHHHH		47.2621963094
452UbiquitinationPLGLKLQKFLVTYIS
HHHHHHHHHHHHHHH		51.6122817900
491PhosphorylationAVPILFLSKALANVP
HHHHHHHHHHHHCCC		14.46-
738PhosphorylationEFILRRLTMNELNSV
HHHHHHHCHHHCCCC		19.0123403867
744PhosphorylationLTMNELNSVSDLDRC
HCHHHCCCCCCHHHH		35.3123403867
746PhosphorylationMNELNSVSDLDRCHL
HHHCCCCCCHHHHHH		32.0723403867
754PhosphorylationDLDRCHLYLMVLTEL
CHHHHHHHHHHHHHH		2.97-
759PhosphorylationHLYLMVLTELINLHL
HHHHHHHHHHHHHHH		19.82-
781PhosphorylationNPIWRVISLLKNASI
CHHHHHHHHHHHHCH		25.4524719451
804PhosphorylationGQEPTVGSQIQRVVS
CCCCCHHHHHHHHHH		21.55-
981PhosphorylationWKIISSLSNTQLIFW
HHHHHHCCCCEEEEE		39.52-
983PhosphorylationIISSLSNTQLIFWAN
HHHHCCCCEEEEEEC		22.75-
1023PhosphorylationFKIKEIMYKIIEMSA
EHHHHHHHHHHHHHH		12.5129083192
1029PhosphorylationMYKIIEMSAIKTGVF
HHHHHHHHHHHHCHH		17.6629083192
1122AcetylationYVRICAVKFLCLLDG
HHHHHHHHHHHHCCC		17.697367025
1144UbiquitinationFIEDLAIKLLDKDEL
HHHHHHHHHCCHHHH		37.0729967540
1148AcetylationLAIKLLDKDELVSKS
HHHHHCCHHHHHCCC		53.7425953088
1148UbiquitinationLAIKLLDKDELVSKS
HHHHHCCHHHHHCCC		53.7429967540
1154UbiquitinationDKDELVSKSKKRYYV
CHHHHHCCCCHHHHH		59.8329967540
1159PhosphorylationVSKSKKRYYVNSLQH
HCCCCHHHHHHHHHH		22.20-
1160PhosphorylationSKSKKRYYVNSLQHR
CCCCHHHHHHHHHHH		9.37-
1209PhosphorylationNNQASIKYFIEWIII
CCHHHHHHHHHHHHH		14.2325690035
1289PhosphorylationHNFSVRLYALVALKK
CCHHHHHHHHHHHHH		6.3220068231
1305PhosphorylationWTVCKVLSVEEFDAL
HHHHHHCCHHHHHHH		30.3929978859
1313PhosphorylationVEEFDALTPVIESSL
HHHHHHHHHHHHHHH		19.7529978859
1318PhosphorylationALTPVIESSLHQVES
HHHHHHHHHHHHHHH		27.3729978859
1319PhosphorylationLTPVIESSLHQVESM
HHHHHHHHHHHHHHH		19.6529978859
1325PhosphorylationSSLHQVESMHGAGNA
HHHHHHHHHCCCCCH		19.7529978859
1405UbiquitinationQTQLSKLKPGDWSQQ
CCCHHCCCCCCCCCC		51.1729967540
1410PhosphorylationKLKPGDWSQQDIGTN
CCCCCCCCCCCCCCC		23.78-
1432UbiquitinationAEWTDVQKKIIPWNS
CCCCCHHHHHCCCCC		45.8729967540
1433UbiquitinationEWTDVQKKIIPWNSR
CCCCHHHHHCCCCCC		28.8629967540
1442PhosphorylationIPWNSRVSDLDLELL
CCCCCCCCCCCHHHH		31.2017192257
1462PhosphorylationARLGKSISRLIVVAS
HHHCCCHHHHHHHHH		28.29-
1473AcetylationVVASLIDKPTNLGGL
HHHHHCCCCCCCCHH		46.9125953088
1475PhosphorylationASLIDKPTNLGGLCR
HHHCCCCCCCCHHHH		49.14-
1534UbiquitinationIDYLQQKKTEGYTII
HHHHHHCCCCCEEEE		47.6929967540
1535PhosphorylationDYLQQKKTEGYTIIG
HHHHHCCCCCEEEEE		41.5029083192
1538PhosphorylationQQKKTEGYTIIGVEQ
HHCCCCCEEEEEEEE		6.6329083192
1539PhosphorylationQKKTEGYTIIGVEQT
HCCCCCEEEEEEEEC		19.5829083192
1546PhosphorylationTIIGVEQTAKSLDLT
EEEEEEECCCCCCCH		23.6529083192
1560UbiquitinationTQYCFPEKSLLLLGN
HHHHCCHHEEECCCC		46.79-
1594PhosphorylationPQQGIIRSLNVHVSG
CCCCHHHHHEEECCC		17.5628509920
1609PhosphorylationALLIWEYTRQQLLSH
CCHHHHHHHHHHHHC		15.5328509920
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TARB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TARB1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TARB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASNA_HUMANASNA1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TARB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1442, AND MASSSPECTROMETRY.

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