TRM2_HUMAN - dbPTM
TRM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM2_HUMAN
UniProt AC Q96GJ1
Protein Name tRNA (uracil(54)-C(5))-methyltransferase homolog
Gene Name TRMT2B
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization
Protein Description Probable S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation (By similarity)..
Protein Sequence MAGLKRRVPLHSLRYFISMVGLFSKPGLLPWYARNPPGWSQLFLGTVCKGDFTRVIATKCQKGQKSQKKPSHLGPLDGSWQERLADVVTPLWRLSYEEQLKVKFAAQKKILQRLESYIQMLNGVSVTTAVPKSERLSCLLHPIIPSPVINGYRNKSTFSVNRGPDGNPKTVGFYLGTWRDGNVVCVQSNHLKNIPEKHSQVAQYYEVFLRQSPLEPCLVFHEGGYWRELTVRTNSQGHTMAIITFHPQKLSQEELHVQKEIVKEFFIRGPGAACGLTSLYFQESTMTRCSHQQSPYQLLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKEDGQSIVAVVNPARAGLHYKVIQAIRNFRAIHTLVFVSCKLHGESTRNVIELCCPPDPAKKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR
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
12PhosphorylationKRRVPLHSLRYFISM
CCCCCHHHHHHHHHH
23.4023403867
24PhosphorylationISMVGLFSKPGLLPW
HHHHHHHCCCCCCHH
42.8824719451
89PhosphorylationERLADVVTPLWRLSY
HHHHHHHHHHHHCCH
16.71-
96 (in isoform 3)Phosphorylation-28.25-
125PhosphorylationIQMLNGVSVTTAVPK
HHHHCCCCEEECCCH
18.3629759185
133PhosphorylationVTTAVPKSERLSCLL
EEECCCHHHHHHHHH
23.1429759185
156PhosphorylationINGYRNKSTFSVNRG
CCCCCCCCCEEEEEC
37.9328348404
157PhosphorylationNGYRNKSTFSVNRGP
CCCCCCCCEEEEECC
22.8728348404
159PhosphorylationYRNKSTFSVNRGPDG
CCCCCCEEEEECCCC
20.6927251275
233PhosphorylationWRELTVRTNSQGHTM
EEEEEEEECCCCCEE
34.58-
235PhosphorylationELTVRTNSQGHTMAI
EEEEEECCCCCEEEE
36.61-
251PhosphorylationTFHPQKLSQEELHVQ
EECHHHCCHHHHHHC
42.45-
259UbiquitinationQEELHVQKEIVKEFF
HHHHHHCHHHHHHHH
48.60-
263UbiquitinationHVQKEIVKEFFIRGP
HHCHHHHHHHHHCCC
55.24-
296PhosphorylationCSHQQSPYQLLFGEP
CCCCCCCCHHHHCCC
19.62-
304PhosphorylationQLLFGEPYIFEELLS
HHHHCCCCHHHHHHC
17.59-
311PhosphorylationYIFEELLSLKIRISP
CHHHHHHCCCEEECC
40.0024719451
333PhosphorylationTAGAEMLYRTVGELT
CCHHHHHHCHHHHHH
11.70-
403UbiquitinationFHTGQAEKILPGLLK
CCCCCHHHHCCCHHC
53.19-
410UbiquitinationKILPGLLKSKEDGQS
HHCCCHHCCCCCCCE
65.60-
412UbiquitinationLPGLLKSKEDGQSIV
CCCHHCCCCCCCEEE
59.23-

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 TRM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM2_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 TRM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TRM2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRM2_HUMAN

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Related Literatures of Post-Translational Modification

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