TRM44_HUMAN - dbPTM
TRM44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM44_HUMAN
UniProt AC Q8IYL2
Protein Name Probable tRNA (uracil-O(2)-)-methyltransferase
Gene Name TRMT44
Organism Homo sapiens (Human).
Sequence Length 757
Subcellular Localization Cytoplasm .
Protein Description Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase..
Protein Sequence MAEVGRTGISYPGALLPQGFWAAVEVWLERPQVANKRLCGARLEARWSAALPCAEARGPGTSAGSEQKERGPGPGQGSPGGGPGPRSLSGPEQGTACCELEEAQGQCQQEEAQREAASVPLRDSGHPGHAEGREGDFPAADLDSLWEDFSQSLARGNSELLAFLTSSGAGSQPEAQRELDVVLRTVIPKTSPHCPLTTPRREIVVQDVLNGTITFLPLEEDDEGNLKVKMSNVYQIQLSHSKEEWFISVLIFCPERWHSDGIVYPKPTWLGEELLAKLAKWSVENKKSDFKSTLSLISIMKYSKAYQELKEKYKEMVKVWPEVTDPEKFVYEDVAIAAYLLILWEEERAERRLTARQSFVDLGCGNGLLVHILSSEGHPGRGIDVRRRKIWDMYGPQTQLEEDAITPNDKTLFPDVDWLIGNHSDELTPWIPVIAARSSYNCRFFVLPCCFFDFIGRYSRRQSKKTQYREYLDFIKEVGFTCGFHVDEDCLRIPSTKRVCLVGKSRTYPSSREASVDEKRTQYIKSRRGCPVSPPGWELSPSPRWVAAGSAGHCDGQQALDARVGCVTRAWAAEHGAGPQAEGPWLPGFHPREKAERVRNCAALPRDFIDQVVLQVANLLLGGKQLNTRSSRNGSLKTWNGGESLSLAEVANELDTETLRRLKRECGGLQTLLRNSHQVFQVVNGRVHIRDWREETLWKTKQPEAKQRLLSEACKTRLCWFFMHHPDGCALSTDCCPFAHGPAELRPPRTTPRKKIS
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
63UbiquitinationARGPGTSAGSEQKER
HCCCCCCCCCCCCCC
25.9327667366
65PhosphorylationGPGTSAGSEQKERGP
CCCCCCCCCCCCCCC
36.2524719451
68 (in isoform 1)Ubiquitination-45.3821906983
68UbiquitinationTSAGSEQKERGPGPG
CCCCCCCCCCCCCCC
45.3822817900
75UbiquitinationKERGPGPGQGSPGGG
CCCCCCCCCCCCCCC
50.8527667366
78PhosphorylationGPGPGQGSPGGGPGP
CCCCCCCCCCCCCCC
16.6929255136
87PhosphorylationGGGPGPRSLSGPEQG
CCCCCCCCCCCCCCC
29.9826074081
89PhosphorylationGPGPRSLSGPEQGTA
CCCCCCCCCCCCCCC
54.2526074081
118PhosphorylationEAQREAASVPLRDSG
HHHHHHHCCCCCCCC
31.1722985185
148 (in isoform 2)Ubiquitination-36.5921906983
148UbiquitinationDLDSLWEDFSQSLAR
HHHHHHHHHHHHHHC
36.5922817900
160UbiquitinationLARGNSELLAFLTSS
HHCCCHHHHHHHHCC
4.1422817900
189UbiquitinationVLRTVIPKTSPHCPL
EEEECCCCCCCCCCC
50.97-
197PhosphorylationTSPHCPLTTPRREIV
CCCCCCCCCCCCEEE
21.6424719451
227UbiquitinationEDDEGNLKVKMSNVY
CCCCCCEEEEEEEEE
43.7532015554
248PhosphorylationSKEEWFISVLIFCPE
CCCCEEEEEEEECCH
11.0327732954
263UbiquitinationRWHSDGIVYPKPTWL
HHCCCCCCCCCCCCC
9.0527667366
275UbiquitinationTWLGEELLAKLAKWS
CCCCHHHHHHHHHHH
4.4627667366
280UbiquitinationELLAKLAKWSVENKK
HHHHHHHHHHHHCCC
50.9029967540
286UbiquitinationAKWSVENKKSDFKST
HHHHHHCCCCHHHHH
39.9029967540
287UbiquitinationKWSVENKKSDFKSTL
HHHHHCCCCHHHHHH
67.83-
304UbiquitinationISIMKYSKAYQELKE
HHHHHHHHHHHHHHH
48.2827667366
306PhosphorylationIMKYSKAYQELKEKY
HHHHHHHHHHHHHHH
13.2729496907
310UbiquitinationSKAYQELKEKYKEMV
HHHHHHHHHHHHHHH
51.94-
318UbiquitinationEKYKEMVKVWPEVTD
HHHHHHHHHCCCCCC
36.9529967540
389 (in isoform 1)Ubiquitination-46.4621906983
389UbiquitinationGIDVRRRKIWDMYGP
CCCHHHHHHHHHHCC
46.4622817900
504UbiquitinationKRVCLVGKSRTYPSS
CEEEEEECCCCCCCC
29.3227667366
505PhosphorylationRVCLVGKSRTYPSSR
EEEEEECCCCCCCCC
24.7526552605
507PhosphorylationCLVGKSRTYPSSREA
EEEECCCCCCCCCCC
47.0427251275
508PhosphorylationLVGKSRTYPSSREAS
EEECCCCCCCCCCCC
10.4527251275
510PhosphorylationGKSRTYPSSREASVD
ECCCCCCCCCCCCCC
31.4526552605
511PhosphorylationKSRTYPSSREASVDE
CCCCCCCCCCCCCCH
29.6326552605
515PhosphorylationYPSSREASVDEKRTQ
CCCCCCCCCCHHHHH
25.9127251275
519UbiquitinationREASVDEKRTQYIKS
CCCCCCHHHHHHHHH
57.1729967540
521PhosphorylationASVDEKRTQYIKSRR
CCCCHHHHHHHHHHC
36.47-
526PhosphorylationKRTQYIKSRRGCPVS
HHHHHHHHHCCCCCC
20.04-
533PhosphorylationSRRGCPVSPPGWELS
HHCCCCCCCCCCCCC
15.5428348404
540PhosphorylationSPPGWELSPSPRWVA
CCCCCCCCCCCCEEE
16.3026074081
542PhosphorylationPGWELSPSPRWVAAG
CCCCCCCCCCEEECC
24.5817081983
628PhosphorylationLGGKQLNTRSSRNGS
HCCCCCCCCCCCCCC
40.2920166139
630PhosphorylationGKQLNTRSSRNGSLK
CCCCCCCCCCCCCCC
31.4520166139
631PhosphorylationKQLNTRSSRNGSLKT
CCCCCCCCCCCCCCE
26.8629052541
635PhosphorylationTRSSRNGSLKTWNGG
CCCCCCCCCCEECCC
30.1820166139
644PhosphorylationKTWNGGESLSLAEVA
CEECCCCCCCHHHHH
26.91-
646PhosphorylationWNGGESLSLAEVANE
ECCCCCCCHHHHHHH
34.51-
658PhosphorylationANELDTETLRRLKRE
HHHCCHHHHHHHHHH
27.88-
715UbiquitinationRLLSEACKTRLCWFF
HHHHHHHHHHHHHHH
43.67-

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 TRM44_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM44_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 TRM44_HUMAN !!

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

Oops, there are no PPI records of TRM44_HUMAN !!

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 TRM44_HUMAN

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Related Literatures of Post-Translational Modification

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