TRM2A_HUMAN - dbPTM
TRM2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM2A_HUMAN
UniProt AC Q8IZ69
Protein Name tRNA (uracil-5-)-methyltransferase homolog A
Gene Name TRMT2A
Organism Homo sapiens (Human).
Sequence Length 625
Subcellular Localization
Protein Description May be involved in nucleic acid metabolism and/or modifications..
Protein Sequence MSENLDNEGPKPMESCGQESSSALSCPTVSVPPAAPAALEEVEKEGAGAATGPGPQPGLYSYIRDDLFTSEIFKLELQNVPRHASFSDVRRFLGRFGLQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKADPMARRRRQEGESEPPVTRVADVVTPLWTVPYAEQLERKQLECEQVLQKLAKEIGSTNRALLPWLLEQRHKHNKACCPLEGVRPSPQQTEYRNKCEFLVGVGVDGEDNTVGCRLGKYKGGTCAVAAPFDTVHIPEATKQVVKAFQEFIRSTPYSAYDPETYTGHWKQLTVRTSRRHQAMAIAYFHPQKLSPEELAELKTSLAQHFTAGPGRASGVTCLYFVEEGQRKTPSQEGLPLEHVAGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVAILDPPRAGLHSKVILAIRRAKNLRRLLYVSCNPRAAMGNFVDLCRAPSNRVKGIPFRPVKAVAVDLFPQTPHCEMLILFERVEHPNGTGVLGPHSPPAQPTPGPPDNTLQETGTFPSS
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
60PhosphorylationPGPQPGLYSYIRDDL
CCCCCCHHHHHCCCC		12.8228796482
61PhosphorylationGPQPGLYSYIRDDLF
CCCCCHHHHHCCCCC		21.0828796482
62PhosphorylationPQPGLYSYIRDDLFT
CCCCHHHHHCCCCCC		6.0928796482
69PhosphorylationYIRDDLFTSEIFKLE
HHCCCCCCCCHHHHH		32.5222210691
70PhosphorylationIRDDLFTSEIFKLEL
HCCCCCCCCHHHHHH		22.7422210691
104UbiquitinationGLQPHKTKLFGQPPC
CCCCCCCCCCCCCCE		46.77-
135UbiquitinationVLHGALWKGRPLSVR
HHHHHHHCCCCCEEE		45.98-
147UbiquitinationSVRLARPKADPMARR
EEEECCCCCCHHHHH		60.92-
173PhosphorylationTRVADVVTPLWTVPY
CCHHCEECCCCCCCH		16.71-
187UbiquitinationYAEQLERKQLECEQV
HHHHHHHHHCHHHHH		50.27-
197UbiquitinationECEQVLQKLAKEIGS
HHHHHHHHHHHHHCC		46.37-
200UbiquitinationQVLQKLAKEIGSTNR
HHHHHHHHHHCCCHH		61.37-
222UbiquitinationEQRHKHNKACCPLEG
HHHHHCCCCCCCCCC		42.39-
242AcetylationQQTEYRNKCEFLVGV
HHHHHHCCCEEEEEC		26.5826051181
242UbiquitinationQQTEYRNKCEFLVGV
HHHHHHCCCEEEEEC		26.58-
266UbiquitinationGCRLGKYKGGTCAVA
EEECCCCCCCEEEEE		55.11-
266AcetylationGCRLGKYKGGTCAVA
EEECCCCCCCEEEEE		55.1126051181
286UbiquitinationVHIPEATKQVVKAFQ
ECCCHHHHHHHHHHH		48.41-
290UbiquitinationEATKQVVKAFQEFIR
HHHHHHHHHHHHHHH		44.6321890473
290 (in isoform 1)Ubiquitination-44.6321890473
290 (in isoform 2)Ubiquitination-44.6321890473
314UbiquitinationETYTGHWKQLTVRTS
CCCCCCEEEEEEHHC		29.7421890473
314 (in isoform 1)Ubiquitination-29.7421890473
314 (in isoform 2)Ubiquitination-29.7421890473
320PhosphorylationWKQLTVRTSRRHQAM
EEEEEEHHCHHHHHE		23.4222210691
321PhosphorylationKQLTVRTSRRHQAMA
EEEEEHHCHHHHHEH		19.4222210691
331PhosphorylationHQAMAIAYFHPQKLS
HHHEHHHHCCCCCCC		9.0522210691
338PhosphorylationYFHPQKLSPEELAEL
HCCCCCCCHHHHHHH		36.9822210691
346 (in isoform 2)Ubiquitination-27.8121890473
346UbiquitinationPEELAELKTSLAQHF
HHHHHHHHHHHHHHH		27.8121890473
346 (in isoform 1)Ubiquitination-27.8121890473
375UbiquitinationFVEEGQRKTPSQEGL
EEECCCCCCCCCCCC		57.83-
376PhosphorylationVEEGQRKTPSQEGLP
EECCCCCCCCCCCCC		30.2923186163
378PhosphorylationEGQRKTPSQEGLPLE
CCCCCCCCCCCCCHH		46.2028450419
502PhosphorylationTLVSRLASQHLVAIL
HHHHHHHHCCHHCCC		23.7927461979
518PhosphorylationPPRAGLHSKVILAIR
CCCCCCCHHHHHHHH		33.3927461979
559UbiquitinationRAPSNRVKGIPFRPV
CCCCCCCCCCCCCCE		48.13-
595PhosphorylationRVEHPNGTGVLGPHS
EECCCCCCCCCCCCC		30.6623401153
602PhosphorylationTGVLGPHSPPAQPTP
CCCCCCCCCCCCCCC		35.3923401153
608PhosphorylationHSPPAQPTPGPPDNT
CCCCCCCCCCCCCCC		28.8823927012
615PhosphorylationTPGPPDNTLQETGTF
CCCCCCCCCCCCCCC		36.8820068231
619PhosphorylationPDNTLQETGTFPSS-
CCCCCCCCCCCCCC-		28.6720068231
621PhosphorylationNTLQETGTFPSS---
CCCCCCCCCCCC---		39.5320068231
624PhosphorylationQETGTFPSS------
CCCCCCCCC------		44.4820068231
625PhosphorylationETGTFPSS-------
CCCCCCCC-------		44.4720068231
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 TRM2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM2A_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 TRM2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SMYD3_HUMANSMYD3physical
26344197
SMRCD_HUMANSMARCAD1physical
28514442
ANR44_HUMANANKRD44physical
28514442
TOPK_HUMANPBKphysical
28514442
PP6R2_HUMANPPP6R2physical
28514442
ANR52_HUMANANKRD52physical
28514442
ATP5S_HUMANATP5Sphysical
28514442
FEZ2_HUMANFEZ2physical
28514442
ANR28_HUMANANKRD28physical
28514442
TRBP2_HUMANTARBP2physical
28514442
DICER_HUMANDICER1physical
28514442
ACOT9_HUMANACOT9physical
28514442
PP6R1_HUMANPPP6R1physical
28514442
THNS1_HUMANTHNSL1physical
28514442
LA_HUMANSSBphysical
28514442
UBP47_HUMANUSP47physical
28514442
ERBIN_HUMANERBB2IPphysical
28514442
ANM7_HUMANPRMT7physical
28514442
PASK_HUMANPASKphysical
28514442
SF3A1_HUMANSF3A1physical
28514442
ASAH1_HUMANASAH1physical
28514442
ANR17_HUMANANKRD17physical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
PP6R3_HUMANPPP6R3physical
28514442
SF3A3_HUMANSF3A3physical
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 TRM2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595 AND SER-602, ANDMASS SPECTROMETRY.
"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-602, AND MASSSPECTROMETRY.

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