TRM11_HUMAN - dbPTM
TRM11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM11_HUMAN
UniProt AC Q7Z4G4
Protein Name tRNA (guanine(10)-N2)-methyltransferase homolog
Gene Name TRMT11
Organism Homo sapiens (Human).
Sequence Length 463
Subcellular Localization
Protein Description Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs..
Protein Sequence MALSCTLNRYLLLMAQEHLEFRLPEIKSLLLLFGGQFASSQETYGKSPFWILSIPSEDIARNLMKRTVCAKSIFELWGHGQSPEELYSSLKNYPVEKMVPFLHSDSTYKIKIHTFNKTLTQEEKIKRIDALEFLPFEGKVNLKKPQHVFSVLEDYGLDPNCIPENPHNIYFGRWIADGQRELIESYSVKKRHFIGNTSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVHGLGKATRKNQKWRGPDENIRANLRQYGLEKYYLDVLVSDASKPSWRKGTYFDAIITDPPYGIRESTRRTGSQKEIPKGIEKWEKCPESHVPVSLSYHLSDMFLDLLNFAAETLVLGGRLVYWLPVYTPEYTEEMVPWHPCLELVSNCEQKLSSHTSRRLITMEKVKKFENRDQYSHLLSDHFLPYQGHNSFREKYFSGVTKRIAKEEKSTQE
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
2Acetylation------MALSCTLNR
------CCHHHHHHH
14.2622223895
5Carbamidation---MALSCTLNRYLL
---CCHHHHHHHHHH
5.3617322306
10PhosphorylationLSCTLNRYLLLMAQE
HHHHHHHHHHHHHHH
10.7117322306
39PhosphorylationLFGGQFASSQETYGK
HHCCCCCCCCCCCCC
33.5722210691
44PhosphorylationFASSQETYGKSPFWI
CCCCCCCCCCCCEEE
23.0822817900
109MalonylationLHSDSTYKIKIHTFN
CCCCCEEEEEEEECC
37.3026320211
109UbiquitinationLHSDSTYKIKIHTFN
CCCCCEEEEEEEECC
37.3029967540
111UbiquitinationSDSTYKIKIHTFNKT
CCCEEEEEEEECCCC
25.0429967540
117UbiquitinationIKIHTFNKTLTQEEK
EEEEECCCCCCHHHH
40.4929967540
118PhosphorylationKIHTFNKTLTQEEKI
EEEECCCCCCHHHHH
35.8230622161
120PhosphorylationHTFNKTLTQEEKIKR
EECCCCCCHHHHHHC
38.8830622161
124UbiquitinationKTLTQEEKIKRIDAL
CCCCHHHHHHCCCEE
53.4229967540
139 (in isoform 2)Ubiquitination-22.28-
139UbiquitinationEFLPFEGKVNLKKPQ
HHCCCCCCCCCCCCH
22.2823503661
143UbiquitinationFEGKVNLKKPQHVFS
CCCCCCCCCCHHHHH
58.1523503661
144UbiquitinationEGKVNLKKPQHVFSV
CCCCCCCCCHHHHHH
53.7423503661
186PhosphorylationQRELIESYSVKKRHF
CHHHHHHHCCCCCEE
12.51-
189UbiquitinationLIESYSVKKRHFIGN
HHHHHCCCCCEECCC
37.8429967540
261UbiquitinationGKATRKNQKWRGPDE
CHHCCCCCCCCCCCH
50.1224816145
295PhosphorylationVSDASKPSWRKGTYF
ECCCCCCCCCCCCEE
43.1626091039
311PhosphorylationAIITDPPYGIRESTR
EEECCCCCCCCHHHC
30.49-
316PhosphorylationPPYGIRESTRRTGSQ
CCCCCCHHHCCCCCC
19.8424719451
317PhosphorylationPYGIRESTRRTGSQK
CCCCCHHHCCCCCCC
21.2924719451
322PhosphorylationESTRRTGSQKEIPKG
HHHCCCCCCCCCCCC
37.1524719451
324UbiquitinationTRRTGSQKEIPKGIE
HCCCCCCCCCCCCHH
60.3529967540
332UbiquitinationEIPKGIEKWEKCPES
CCCCCHHHHHHCCCC
59.7529967540
430PhosphorylationDQYSHLLSDHFLPYQ
HHHHHHHHHCCCCCC
35.0928555341
436PhosphorylationLSDHFLPYQGHNSFR
HHHCCCCCCCCCHHH
29.3126425664
441PhosphorylationLPYQGHNSFREKYFS
CCCCCCCHHHHHHHH
21.7220873877
445UbiquitinationGHNSFREKYFSGVTK
CCCHHHHHHHHHHHH
47.5429967540
446PhosphorylationHNSFREKYFSGVTKR
CCHHHHHHHHHHHHH
9.75-
448PhosphorylationSFREKYFSGVTKRIA
HHHHHHHHHHHHHHH
29.30-
452UbiquitinationKYFSGVTKRIAKEEK
HHHHHHHHHHHHHHH
39.1329967540
452AcetylationKYFSGVTKRIAKEEK
HHHHHHHHHHHHHHH
39.1325953088
459UbiquitinationKRIAKEEKSTQE---
HHHHHHHHHCCC---
60.9524816145
461PhosphorylationIAKEEKSTQE-----
HHHHHHHCCC-----
48.02-

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 TRM11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM11_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 TRM11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GALC_HUMANGALCphysical
28514442
TR112_HUMANTRMT112physical
28514442
SYNC_HUMANNARSphysical
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 TRM11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASSSPECTROMETRY.

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