MTU1_HUMAN - dbPTM
MTU1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTU1_HUMAN
UniProt AC O75648
Protein Name Mitochondrial tRNA-specific 2-thiouridylase 1
Gene Name TRMU
Organism Homo sapiens (Human).
Sequence Length 421
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base..
Protein Sequence MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPLL
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
4 (in isoform 4)Phosphorylation-1.8818669648
4 (in isoform 3)Phosphorylation-1.8818669648
17PhosphorylationALSGGVDSAVAALLL
HHCCCHHHHHHHHHH
23.41-
52UbiquitinationHGVCTADKDCEDAYR
CCCCCCCCCHHHHHH
62.91-
91UbiquitinationDFLNEYEKGRTPNPD
HHHHHHHCCCCCCCC
53.44-
94PhosphorylationNEYEKGRTPNPDIVC
HHHHCCCCCCCCCCC
35.77-
103AcetylationNPDIVCNKHIKFSCF
CCCCCCCCCCEEEHH
41.3925953088
103UbiquitinationNPDIVCNKHIKFSCF
CCCCCCCCCCEEEHH
41.39-
103MalonylationNPDIVCNKHIKFSCF
CCCCCCCCCCEEEHH
41.3926320211
131PhosphorylationATGHYARTSLEDEEV
HCCCCCCCCCCCHHH
29.5026471730
132PhosphorylationTGHYARTSLEDEEVF
CCCCCCCCCCCHHHH
24.9826471730
132 (in isoform 3)Ubiquitination-24.9821906983
132 (in isoform 4)Ubiquitination-24.9821906983
142UbiquitinationDEEVFEQKHVKKPEG
CHHHHHHHCCCCCCC
43.07-
145UbiquitinationVFEQKHVKKPEGLFR
HHHHHCCCCCCCCCC
63.43-
146MalonylationFEQKHVKKPEGLFRN
HHHHCCCCCCCCCCC
47.4126320211
146UbiquitinationFEQKHVKKPEGLFRN
HHHHCCCCCCCCCCC
47.41-
215UbiquitinationRLHHVLQKKESMGMC
CHHHHHHHCCCCCEE
55.11-
286UbiquitinationVVEKDSVKGDVFVAP
EEECCCCCCEEEEEE
54.032190698
286 (in isoform 2)Ubiquitination-54.0321906983
332MethylationKMMECHFRFRHQMAL
HHHHHCHHHHHHHHC
12.2024380761
332DimethylationKMMECHFRFRHQMAL
HHHHHCHHHHHHHHC
12.20-
391PhosphorylationLRLGPSAYTLQKGQR
EEECCCEEECCCCCC
16.60-
395UbiquitinationPSAYTLQKGQRRAGM
CCEEECCCCCCCCCC
61.19-

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 MTU1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTU1_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 MTU1_HUMAN !!

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

Oops, there are no PPI records of MTU1_HUMAN !!

Drug and Disease Associations
Kegg Disease
OMIM Disease
613070Liver failure, infantile, transient (LFIT)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTU1_HUMAN

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Related Literatures of Post-Translational Modification

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