TRM13_HUMAN - dbPTM
TRM13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM13_HUMAN
UniProt AC Q9NUP7
Protein Name tRNA:m(4)X modification enzyme TRM13 homolog
Gene Name TRMT13
Organism Homo sapiens (Human).
Sequence Length 481
Subcellular Localization
Protein Description tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His)..
Protein Sequence MATSATSPHAPGFPAEGRCGYYVEKKKRFCRMVVAAGKRFCGEHAGAAEEEDARKRILCPLDPKHTVYEDQLAKHLKKCNSREKPKPDFYIQDINAGLRDETEIPEQLVPISSLSEEQLEKLIKKLRKASEGLNSTLKDHIMSHPALHDALNDPKNGDSATKHLKQQASILGNIENLKLLGPRRCFVEFGAGKGKLSHWVDIALKDAEKVHFILVEKVTTRFKVDGKHRKKNSVFERLQIDIQHLCLNKIPVLREEKLPVVGIGKHLCGMATDLALRCLVETYAASFEERNEEPLAKRIKNDKTEKEIYTLAKEGNEKNVPEKWNPVAGIVIALCCHHRCDWRHYVGKEYFRALGLGAVEFHYFQRMSSWATCGMRKTSLETSNSTTKRQDNQNDDSEEHDDGGYRITDDGADCLPGLLSVEEKKKIGHLCKLLIDQGRIQYLQQKGFSPALQYYTDPLVSLENVLLTALPNHSSSPETTA
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------MATSATSPH
------CCCCCCCCC		15.4022223895
3Phosphorylation-----MATSATSPHA
-----CCCCCCCCCC		20.0030266825
4Phosphorylation----MATSATSPHAP
----CCCCCCCCCCC		21.7330266825
6Phosphorylation--MATSATSPHAPGF
--CCCCCCCCCCCCC		42.4330266825
7Phosphorylation-MATSATSPHAPGFP
-CCCCCCCCCCCCCC		17.8830266825
21PhosphorylationPAEGRCGYYVEKKKR
CCCCCCCEEECCCHH		14.1526074081
22PhosphorylationAEGRCGYYVEKKKRF
CCCCCCEEECCCHHH		6.3426074081
68PhosphorylationLDPKHTVYEDQLAKH
CCCCCCHHHHHHHHH		18.2327642862
130PhosphorylationIKKLRKASEGLNSTL
HHHHHHHHHHHHHHH		34.92-
138UbiquitinationEGLNSTLKDHIMSHP
HHHHHHHHHHHHHCH		47.5529967540
165UbiquitinationDSATKHLKQQASILG
CHHHHHHHHHHHHHH		39.8329967540
178UbiquitinationLGNIENLKLLGPRRC
HHCHHHHHHCCCCEE		53.93-
233PhosphorylationGKHRKKNSVFERLQI
CCCCCCCCHHHHHHH		36.7424719451
257UbiquitinationIPVLREEKLPVVGIG
CCCCCCCCCCEEECC		54.0329967540
286PhosphorylationLVETYAASFEERNEE
HHHHHHHCHHHHCCC		25.6424719451
309PhosphorylationDKTEKEIYTLAKEGN
CCCHHHHHHHHHHCC		9.2226074081
310PhosphorylationKTEKEIYTLAKEGNE
CCHHHHHHHHHHCCC		26.3826074081
368PhosphorylationFHYFQRMSSWATCGM
EEEHHHHCCCCCCCC		25.56-
369PhosphorylationHYFQRMSSWATCGMR
EEHHHHCCCCCCCCC		16.04-
372PhosphorylationQRMSSWATCGMRKTS
HHHCCCCCCCCCCCC		11.88-
378PhosphorylationATCGMRKTSLETSNS
CCCCCCCCCCCCCCC		28.3423312004
379PhosphorylationTCGMRKTSLETSNST
CCCCCCCCCCCCCCC		27.5223312004
382PhosphorylationMRKTSLETSNSTTKR
CCCCCCCCCCCCCCC		38.2030576142
383PhosphorylationRKTSLETSNSTTKRQ
CCCCCCCCCCCCCCC		21.2930576142
385PhosphorylationTSLETSNSTTKRQDN
CCCCCCCCCCCCCCC		36.9030576142
386PhosphorylationSLETSNSTTKRQDNQ
CCCCCCCCCCCCCCC		40.3623312004
387PhosphorylationLETSNSTTKRQDNQN
CCCCCCCCCCCCCCC		24.8523312004
397PhosphorylationQDNQNDDSEEHDDGG
CCCCCCCCCCCCCCC		47.9825159151
405PhosphorylationEEHDDGGYRITDDGA
CCCCCCCCEECCCCC		12.36-
408PhosphorylationDDGGYRITDDGADCL
CCCCCEECCCCCCCC		21.0230624053
424AcetylationGLLSVEEKKKIGHLC
CCCCHHHHHHHHHHH		45.9523749302
425AcetylationLLSVEEKKKIGHLCK
CCCHHHHHHHHHHHH		53.5625953088
455PhosphorylationFSPALQYYTDPLVSL
CCHHHHHHCCCCCCH		7.5420068231
456PhosphorylationSPALQYYTDPLVSLE
CHHHHHHCCCCCCHH		26.6320068231
461PhosphorylationYYTDPLVSLENVLLT
HHCCCCCCHHHHHHH		37.3320068231
468PhosphorylationSLENVLLTALPNHSS
CHHHHHHHHCCCCCC		23.2220068231
474PhosphorylationLTALPNHSSSPETTA
HHHCCCCCCCCCCCC		38.8720068231
475PhosphorylationTALPNHSSSPETTA-
HHCCCCCCCCCCCC-		42.2226074081
476PhosphorylationALPNHSSSPETTA--
HCCCCCCCCCCCC--		29.7526074081
479PhosphorylationNHSSSPETTA-----
CCCCCCCCCC-----		31.2620068231
480PhosphorylationHSSSPETTA------
CCCCCCCCC------		28.8020068231
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 TRM13_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM13_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 TRM13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAG1_HUMANSTAG1physical
28514442
OSER1_HUMANOSER1physical
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 TRM13_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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