TRMO_HUMAN - dbPTM
TRMO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRMO_HUMAN
UniProt AC Q9BU70
Protein Name tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305}
Gene Name TRMO {ECO:0000303|PubMed:25063302, ECO:0000312|HGNC:HGNC:30967}
Organism Homo sapiens (Human).
Sequence Length 441
Subcellular Localization
Protein Description S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU). [PubMed: 25063302 The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability. May bind to tRNA (By similarity]
Protein Sequence MRGLEESGPRPTATPCGCVKPALETGNLLTEPVGYLESCFSAKNGTPRQPSICSYSRACLRIRKRIFNNPEHSLMGLEQFSHVWILFVFHKNGHLSCKAKVQPPRLNGAKTGVFSTRSPHRPNAIGLTLAKLEKVEGGAIYLSGIDMIHGTPVLDIKPYIAEYDSPQNVMEPLADFNLQNNQHTPNTVSQSDSKTDSCDQRQLSGCDEPQPHHSTKRKPKCPEDRTSEENYLTHSDTARIQQAFPMHREIAVDFGLESRRDQSSSVAEEQIGPYCPEKSFSEKGTDKKLERVEGAAVLQGSRAETQPMAPHCPAGRADGAPRSVVPAWVTEAPVATLEVRFTPHAEMDLGQLSSQDVGQASFKYFQSAEEAKRAIEAVLSADPRSVYRRKLCQDRLFYFTVDIAHVTCWFGDGFAEVLRIKPASEPVHMTGPVGSLVSLGS
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
100UbiquitinationGHLSCKAKVQPPRLN
CCEEEEEEECCCCCC
-
110UbiquitinationPPRLNGAKTGVFSTR
CCCCCCCCEECEECC
-
118PhosphorylationTGVFSTRSPHRPNAI
EECEECCCCCCCCCC
25159151
163PhosphorylationIKPYIAEYDSPQNVM
CCCCEECCCCCCCCC
-
184PhosphorylationNLQNNQHTPNTVSQS
CCCCCCCCCCCCCCC
25159151
204PhosphorylationSCDQRQLSGCDEPQP
CCCHHHHCCCCCCCC
-
214PhosphorylationDEPQPHHSTKRKPKC
CCCCCCCCCCCCCCC
25627689
215PhosphorylationEPQPHHSTKRKPKCP
CCCCCCCCCCCCCCC
25627689
231PhosphorylationDRTSEENYLTHSDTA
CCCCCCCCCCHHHHH
22468782
235PhosphorylationEENYLTHSDTARIQQ
CCCCCCHHHHHHHHH
22468782
237PhosphorylationNYLTHSDTARIQQAF
CCCCHHHHHHHHHHC
-
265PhosphorylationSRRDQSSSVAEEQIG
CCCCCCCCHHHHHHC
28555341
361PhosphorylationSQDVGQASFKYFQSA
CCCHHHHHHHHHHCH
24719451
363UbiquitinationDVGQASFKYFQSAEE
CHHHHHHHHHHCHHH
-
372UbiquitinationFQSAEEAKRAIEAVL
HHCHHHHHHHHHHHH
-
380PhosphorylationRAIEAVLSADPRSVY
HHHHHHHHCCHHHHH
30257219
421UbiquitinationFAEVLRIKPASEPVH
HHHCCEEEECCCCEE
-

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 TRMO_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRMO_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 TRMO_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHPN2_HUMANRHPN2physical
26186194
STA5B_HUMANSTAT5Bphysical
28514442
RHPN2_HUMANRHPN2physical
28514442
VP26B_HUMANVPS26Bphysical
28514442

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

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Related Literatures of Post-Translational Modification

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