TRM1_HUMAN - dbPTM
TRM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM1_HUMAN
UniProt AC Q9NXH9
Protein Name tRNA (guanine(26)-N(2))-dimethyltransferase
Gene Name TRMT1
Organism Homo sapiens (Human).
Sequence Length 659
Subcellular Localization
Protein Description Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups..
Protein Sequence MQGSSLWLSLTFRSARVLSRARFFEWQSPGLPNTAAMENGTGPYGEERPREVQETTVTEGAAKIAFPSANEVFYNPVQEFNRDLTCAVITEFARIQLGAKGIQIKVPGEKDTQKVVVDLSEQEEEKVELKESENLASGDQPRTAAVGEICEEGLHVLEGLAASGLRSIRFALEVPGLRSVVANDASTRAVDLIRRNVQLNDVAHLVQPSQADARMLMYQHQRVSERFDVIDLDPYGSPATFLDAAVQAVSEGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLRANCYQRFVVPLLSISADFYVRVFVRVFTGQAKVKASASKQALVFQCVGCGAFHLQRLGKASGVPSGRAKFSAACGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLEAVSANPGRFHTSERIRGVLSVITEELPDVPLYYTLDQLSSTIHCNTPSLLQLRSALLHADFRVSLSHACKNAVKTDAPASALWDIMRCWEKECPVKRERLSETSPAFRILSVEPRLQANFTIREDANPSSRQRGLKRFQANPEANWGPRPRARPGGKAADEAMEERRRLLQNKRKEPPEDVAQRAARLKTFPCKRFKEGTCQRGDQCCYSHSPPTPRVSADAAPDCPETSNQTPPGPGAAAGPGID
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
4Phosphorylation----MQGSSLWLSLT
----CCCCCEEHEHH		12.8328450419
5Phosphorylation---MQGSSLWLSLTF
---CCCCCEEHEHHH		30.3228450419
9PhosphorylationQGSSLWLSLTFRSAR
CCCCEEHEHHHHHHH		17.4928450419
11PhosphorylationSSLWLSLTFRSARVL
CCEEHEHHHHHHHHH		17.3928450419
14PhosphorylationWLSLTFRSARVLSRA
EHEHHHHHHHHHHHH		19.0820068231
19PhosphorylationFRSARVLSRARFFEW
HHHHHHHHHHHHCEE		22.4920068231
100UbiquitinationARIQLGAKGIQIKVP
HHHHHCCCCEEEECC		55.54-
105 (in isoform 2)Ubiquitination-26.4621906983
105 (in isoform 1)Ubiquitination-26.4621906983
105UbiquitinationGAKGIQIKVPGEKDT
CCCCEEEECCCCCCC		26.4621906983
120PhosphorylationQKVVVDLSEQEEEKV
EEEEEECCHHHHHHC		32.5430266825
130 (in isoform 2)Ubiquitination-45.7621906983
130 (in isoform 1)Ubiquitination-45.7621906983
130UbiquitinationEEEKVELKESENLAS
HHHHCCHHHCCCCCC		45.7621906983
137PhosphorylationKESENLASGDQPRTA
HHCCCCCCCCCCCCH		46.1721815630
150GlutathionylationTAAVGEICEEGLHVL
CHHHHHHHHHHHHHH		3.2022555962
179PhosphorylationLEVPGLRSVVANDAS
EECCCCCHHHCCCHH		26.4520068231
186PhosphorylationSVVANDASTRAVDLI
HHHCCCHHHHHHHHH		22.6820068231
187PhosphorylationVVANDASTRAVDLIR
HHCCCHHHHHHHHHH		25.1124043423
209PhosphorylationVAHLVQPSQADARML
HHHHHCCCHHHHHHH		22.40-
283 (in isoform 2)Ubiquitination-28.49-
283UbiquitinationKYGAMALKSRACHEM
HHHHHHHHHHHHHHH		28.49-
361MalonylationFHLQRLGKASGVPSG
HHHHHHHHCCCCCCC		43.9326320211
361UbiquitinationFHLQRLGKASGVPSG
HHHHHHHHCCCCCCC		43.93-
371AcetylationGVPSGRAKFSAACGP
CCCCCCCCCCHHHCC		38.1923749302
371UbiquitinationGVPSGRAKFSAACGP
CCCCCCCCCCHHHCC		38.19-
381PhosphorylationAACGPPVTPECEHCG
HHHCCCCCCCCCCCC		21.1027050516
416PhosphorylationGRVLEAVSANPGRFH
HHHHHHHHCCCCCCC		29.4020068231
458 (in isoform 2)Ubiquitination-40.6421906983
479PhosphorylationADFRVSLSHACKNAV
CCHHHHHHHHHHHCC		11.09-
483UbiquitinationVSLSHACKNAVKTDA
HHHHHHHHHCCCCCC		49.04-
487 (in isoform 1)Ubiquitination-37.9721906983
487UbiquitinationHACKNAVKTDAPASA
HHHHHCCCCCCCHHH		37.972190698
488PhosphorylationACKNAVKTDAPASAL
HHHHCCCCCCCHHHH		30.6920068231
493PhosphorylationVKTDAPASALWDIMR
CCCCCCHHHHHHHHH		23.8820068231
504UbiquitinationDIMRCWEKECPVKRE
HHHHHHHHCCCCCHH		39.87-
514PhosphorylationPVKRERLSETSPAFR
CCCHHHHCCCCCCEE		45.0821815630
516PhosphorylationKRERLSETSPAFRIL
CHHHHCCCCCCEEEE		36.3129214152
517PhosphorylationRERLSETSPAFRILS
HHHHCCCCCCEEEEE		15.3521815630
521MethylationSETSPAFRILSVEPR
CCCCCCEEEEEECCC		30.92115919013
528MethylationRILSVEPRLQANFTI
EEEEECCCCCCCEEE		26.40115919017
534PhosphorylationPRLQANFTIREDANP
CCCCCCEEECCCCCH		20.9424719451
562MethylationPEANWGPRPRARPGG
CCCCCCCCCCCCCCC		29.4281453767
570UbiquitinationPRARPGGKAADEAME
CCCCCCCHHHHHHHH		46.44-
588UbiquitinationRLLQNKRKEPPEDVA
HHHHHCCCCCHHHHH		75.96-
602UbiquitinationAQRAARLKTFPCKRF
HHHHHHHHCCCCCCC		42.43-
610UbiquitinationTFPCKRFKEGTCQRG
CCCCCCCCCCCCCCC		60.30-
613PhosphorylationCKRFKEGTCQRGDQC
CCCCCCCCCCCCCCC		13.4223312004
622PhosphorylationQRGDQCCYSHSPPTP
CCCCCCCCCCCCCCC		19.6230266825
623PhosphorylationRGDQCCYSHSPPTPR
CCCCCCCCCCCCCCC		11.9923401153
625PhosphorylationDQCCYSHSPPTPRVS
CCCCCCCCCCCCCCC		27.0025159151
628PhosphorylationCYSHSPPTPRVSADA
CCCCCCCCCCCCCCC		27.4130266825
632PhosphorylationSPPTPRVSADAAPDC
CCCCCCCCCCCCCCC		23.0123403867
642PhosphorylationAAPDCPETSNQTPPG
CCCCCCCCCCCCCCC		20.3723403867
643PhosphorylationAPDCPETSNQTPPGP
CCCCCCCCCCCCCCC		25.8625262027
646PhosphorylationCPETSNQTPPGPGAA
CCCCCCCCCCCCCCC		35.3830278072
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 TRM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM1_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 TRM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN598_HUMANZNF598physical
22939629
VATB2_HUMANATP6V1B2physical
22939629
TWF1_HUMANTWF1physical
22939629
TXND5_HUMANTXNDC5physical
22939629
VATB1_HUMANATP6V1B1physical
22939629
C1QBP_HUMANC1QBPphysical
22863883
PLAK_HUMANJUPphysical
22863883
PYRG1_HUMANCTPS1physical
26344197
SEPT2_HUMANSEPT2physical
26344197
CHDH_HUMANCHDHphysical
28514442
HEMK1_HUMANHEMK1physical
28514442
UBP4_HUMANUSP4physical
28514442
PDP1_HUMANPDP1physical
28514442
RSAD1_HUMANRSAD1physical
28514442
PDPR_HUMANPDPRphysical
28514442
D2HDH_HUMAND2HGDHphysical
28514442
NDUAC_HUMANNDUFA12physical
28514442
CLPX_HUMANCLPXphysical
28514442
DPP9_HUMANDPP9physical
28514442
HDAC3_HUMANHDAC3physical
28514442
AKA11_HUMANAKAP11physical
28514442
SYAM_HUMANAARS2physical
28514442
NDUS6_HUMANNDUFS6physical
28514442
NOCT_HUMANCCRN4Lphysical
28514442
SENP1_HUMANSENP1physical
28514442
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 TRM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; THR-628 ANDTHR-646, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, AND MASSSPECTROMETRY.

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