THG1_HUMAN - dbPTM
THG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THG1_HUMAN
UniProt AC Q9NWX6
Protein Name Probable tRNA(His) guanylyltransferase
Gene Name THG1L
Organism Homo sapiens (Human).
Sequence Length 298
Subcellular Localization Cytoplasm . Found near the nuclear membrane.
Protein Description Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis..
Protein Sequence MWGACKVKVHDSLATISITLRRYLRLGATMAKSKFEYVRDFEADDTCLAHCWVVVRLDGRNFHRFAEKHNFAKPNDSRALQLMTKCAQTVMEELEDIVIAYGQSDEYSFVFKRKTNWFKRRASKFMTHVASQFASSYVFYWRDYFEDQPLLYPPGFDGRVVVYPSNQTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKVDEVMTKEIKLPTEMEGKKMAVTRTRTKPVPLHCDIIGDAFWKEHPEILDEDS
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
33O-linked_GlycosylationLGATMAKSKFEYVRD
HCCEEECCCCEECCC
32.7930379171
34AcetylationGATMAKSKFEYVRDF
CCEEECCCCEECCCC
41.3225953088
68AcetylationNFHRFAEKHNFAKPN
CHHHHHHHCCCCCCC
40.1819608861
73UbiquitinationAEKHNFAKPNDSRAL
HHHCCCCCCCHHHHH
39.97-
114AcetylationYSFVFKRKTNWFKRR
CEEEEECCCCHHHHH
46.967377641
119UbiquitinationKRKTNWFKRRASKFM
ECCCCHHHHHHHHHH
32.3721890473
119AcetylationKRKTNWFKRRASKFM
ECCCCHHHHHHHHHH
32.377377651
170UbiquitinationYPSNQTLKDYLSWRQ
ECCCCCHHHHHHHHH
47.95-
174PhosphorylationQTLKDYLSWRQADCH
CCHHHHHHHHHCCCH
17.6224719451
222PhosphorylationDKNEILFSEFNINYN
CCCCEEEEEECCCCC
37.5220068231
228PhosphorylationFSEFNINYNNELPMY
EEEECCCCCCCCCCC
18.6320068231
235PhosphorylationYNNELPMYRKGTVLI
CCCCCCCCCCCEEEE
13.7720068231
237MalonylationNELPMYRKGTVLIWQ
CCCCCCCCCEEEEEE
41.2526320211
239PhosphorylationLPMYRKGTVLIWQKV
CCCCCCCEEEEEEEH
18.38-
251PhosphorylationQKVDEVMTKEIKLPT
EEHHHHHHCCCCCCC
30.60-
252UbiquitinationKVDEVMTKEIKLPTE
EHHHHHHCCCCCCCC
39.0721890473
263AcetylationLPTEMEGKKMAVTRT
CCCCCCCCEEEEEEC
26.5223749302
2632-HydroxyisobutyrylationLPTEMEGKKMAVTRT
CCCCCCCCEEEEEEC
26.52-
264AcetylationPTEMEGKKMAVTRTR
CCCCCCCEEEEEECC
42.847339661

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 THG1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THG1_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 THG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELMD1_HUMANELMOD1physical
16189514
AASD1_HUMANAARSD1physical
22863883
DPP9_HUMANDPP9physical
22863883
EF2K_HUMANEEF2Kphysical
22863883
METH_HUMANMTRphysical
22863883
RAGP1_HUMANRANGAP1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
TPRKB_HUMANTPRKBphysical
22863883
THG1_HUMANTHG1Lphysical
25416956
THG1_HUMANTHG1Lphysical
21516116

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 THG1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.

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