MTO1_HUMAN - dbPTM
MTO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTO1_HUMAN
UniProt AC Q9Y2Z2
Protein Name Protein MTO1 homolog, mitochondrial
Gene Name MTO1
Organism Homo sapiens (Human).
Sequence Length 717
Subcellular Localization Mitochondrion.
Protein Description Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs..
Protein Sequence MFYFRGCGRWVAVSFTKQQFPLARLSSDSAAPRTPHFDVIVIGGGHAGTEAATAAARCGSRTLLLTHRVDTIGQMSCNPSFGGIGKGHLMREVDALDGLCSRICDQSGVHYKVLNRRKGPAVWGLRAQIDRKLYKQNMQKEILNTPLLTVQEGAVEDLILTEPEPEHTGKCRVSGVVLVDGSTVYAESVILTTGTFLRGMIVIGLETHPAGRLGDQPSIGLAQTLEKLGFVVGRLKTGTPPRIAKESINFSILNKHIPDNPSIPFSFTNETVWIKPEDQLPCYLTHTNPRVDEIVLKNLHLNSHVKETTRGPRYCPSIESKVLRFPNRLHQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPDGVLLLLPRMECNGAISAHHNLPLPGYGVQYDYLDPRQITPSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVEFRLSLRPDNADSRLTLRGYKDAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVLKYEEVDMDSLAKAVPEPLKKYTKCRELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRDVSLSHEVREKLHFSRPQTIGAASRIPGVTPAAIINLLRFVKTTQRRQSAMNESSKTDQYLCDADRLQEREL
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
12UbiquitinationRGCGRWVAVSFTKQQ
CCCCCEEEEEEECCC
5.5822817900
14PhosphorylationCGRWVAVSFTKQQFP
CCCEEEEEEECCCCC
19.9124719451
32UbiquitinationLSSDSAAPRTPHFDV
HCCCCCCCCCCCCCE
40.1523503661
34UbiquitinationSDSAAPRTPHFDVIV
CCCCCCCCCCCCEEE
21.7621963094
34PhosphorylationSDSAAPRTPHFDVIV
CCCCCCCCCCCCEEE
21.7622210691
44UbiquitinationFDVIVIGGGHAGTEA
CCEEEECCCCHHHHH
17.3727667366
60PhosphorylationTAAARCGSRTLLLTH
HHHHHCCCCEEEEEE
26.22-
61UbiquitinationAAARCGSRTLLLTHR
HHHHCCCCEEEEEEE
18.0627667366
62PhosphorylationAARCGSRTLLLTHRV
HHHCCCCEEEEEEEC
24.37-
86UbiquitinationPSFGGIGKGHLMREV
CCCCCCCHHHHHHHH
41.0321963094
86 (in isoform 6)Ubiquitination-41.03-
90UbiquitinationGIGKGHLMREVDALD
CCCHHHHHHHHHHHH
2.5923503661
96UbiquitinationLMREVDALDGLCSRI
HHHHHHHHHHHHHHH
4.6721963094
97UbiquitinationMREVDALDGLCSRIC
HHHHHHHHHHHHHHH
50.1427667366
99UbiquitinationEVDALDGLCSRICDQ
HHHHHHHHHHHHHCC
2.0927667366
107PhosphorylationCSRICDQSGVHYKVL
HHHHHCCCCCEEEEE
29.5425599653
108UbiquitinationSRICDQSGVHYKVLN
HHHHCCCCCEEEEEC
12.4621963094
111PhosphorylationCDQSGVHYKVLNRRK
HCCCCCEEEEECCCC
10.6125599653
112UbiquitinationDQSGVHYKVLNRRKG
CCCCCEEEEECCCCC
25.9329967540
112 (in isoform 6)Ubiquitination-25.93-
118UbiquitinationYKVLNRRKGPAVWGL
EEEECCCCCCCHHHH
67.0427667366
118 (in isoform 6)Ubiquitination-67.04-
135UbiquitinationQIDRKLYKQNMQKEI
HHHHHHHHHHHHHHH
45.7027667366
140UbiquitinationLYKQNMQKEILNTPL
HHHHHHHHHHHCCCC
35.6329967540
153UbiquitinationPLLTVQEGAVEDLIL
CCEEEECCCEEEEEE
20.1723503661
160UbiquitinationGAVEDLILTEPEPEH
CCEEEEEECCCCCCC
6.0421890473
162UbiquitinationVEDLILTEPEPEHTG
EEEEEECCCCCCCCC
44.1927667366
170UbiquitinationPEPEHTGKCRVSGVV
CCCCCCCCCEEEEEE
21.7421963094
170 (in isoform 6)Ubiquitination-21.74-
171UbiquitinationEPEHTGKCRVSGVVL
CCCCCCCCEEEEEEE
5.7021963094
181UbiquitinationSGVVLVDGSTVYAES
EEEEEECCCEEEEEE
20.1021963094
184UbiquitinationVLVDGSTVYAESVIL
EEECCCEEEEEEEEE
4.5827667366
189UbiquitinationSTVYAESVILTTGTF
CEEEEEEEEEECCCC
2.9023503661
191UbiquitinationVYAESVILTTGTFLR
EEEEEEEEECCCCCC
3.0823503661
192UbiquitinationYAESVILTTGTFLRG
EEEEEEEECCCCCCE
16.4421890473
200 (in isoform 2)Ubiquitination-1.4621890473
214UbiquitinationTHPAGRLGDQPSIGL
CCCCCCCCCCCCCCH
30.1023503661
223UbiquitinationQPSIGLAQTLEKLGF
CCCCCHHHHHHHHCC
52.2221890473
223 (in isoform 5)Ubiquitination-52.2221890473
227UbiquitinationGLAQTLEKLGFVVGR
CHHHHHHHHCCEEEE
57.9623503661
227 (in isoform 6)Ubiquitination-57.96-
227 (in isoform 4)Ubiquitination-57.96-
233UbiquitinationEKLGFVVGRLKTGTP
HHHCCEEEEECCCCC
24.7323503661
235UbiquitinationLGFVVGRLKTGTPPR
HCCEEEEECCCCCCH
4.8521963094
236UbiquitinationGFVVGRLKTGTPPRI
CCEEEEECCCCCCHH
43.4827667366
245MethylationGTPPRIAKESINFSI
CCCCHHCHHHCCHHH
50.01115973373
245UbiquitinationGTPPRIAKESINFSI
CCCCHHCHHHCCHHH
50.0121963094
245 (in isoform 6)Ubiquitination-50.01-
247UbiquitinationPPRIAKESINFSILN
CCHHCHHHCCHHHHC
23.3327667366
247PhosphorylationPPRIAKESINFSILN
CCHHCHHHCCHHHHC
23.3323684312
251PhosphorylationAKESINFSILNKHIP
CHHHCCHHHHCCCCC
22.9824719451
274UbiquitinationFTNETVWIKPEDQLP
CCCCEEEECHHHHCC
4.6623503661
275UbiquitinationTNETVWIKPEDQLPC
CCCEEEECHHHHCCE
27.0029967540
275 (in isoform 2)Ubiquitination-27.0021890473
285 (in isoform 2)Phosphorylation-10.53-
296UbiquitinationPRVDEIVLKNLHLNS
CCCCCEEEECCCCCC
3.6023503661
297UbiquitinationRVDEIVLKNLHLNSH
CCCCEEEECCCCCCC
46.7127667366
297 (in isoform 6)Ubiquitination-46.71-
297 (in isoform 1)Ubiquitination-46.7121890473
297 (in isoform 3)Ubiquitination-46.7121890473
297 (in isoform 4)Ubiquitination-46.7121890473
298UbiquitinationVDEIVLKNLHLNSHV
CCCEEEECCCCCCCC
28.6521963094
306UbiquitinationLHLNSHVKETTRGPR
CCCCCCCCCCCCCCC
43.8729967540
306 (in isoform 6)Ubiquitination-43.87-
321UbiquitinationYCPSIESKVLRFPNR
CCCCCHHHHCCCCCC
32.2827667366
321 (in isoform 6)Ubiquitination-32.28-
338UbiquitinationQVWLEPEGMDSDLIY
EEECCCCCCCCCCCC
35.5921963094
361UbiquitinationPAELQEKMITCIRGL
CHHHHHHHHHHHHCH
2.7827667366
370UbiquitinationTCIRGLEKAKVIQPD
HHHHCHHHCCEECCC
59.5623503661
372UbiquitinationIRGLEKAKVIQPDGV
HHCHHHCCEECCCCE
51.4427667366
372 (in isoform 4)Ubiquitination-51.4421890473
372 (in isoform 6)Ubiquitination-51.44-
382UbiquitinationQPDGVLLLLPRMECN
CCCCEEEEEECCEEC
5.6021963094
382 (in isoform 4)Phosphorylation-5.60-
382 (in isoform 6)Phosphorylation-5.60-
390UbiquitinationLPRMECNGAISAHHN
EECCEECCCCCCCCC
35.6323503661
392UbiquitinationRMECNGAISAHHNLP
CCEECCCCCCCCCCC
3.8623503661
393UbiquitinationMECNGAISAHHNLPL
CEECCCCCCCCCCCC
22.4821890473
415UbiquitinationDYLDPRQITPSLETH
EECCHHHCCCCHHHH
6.8923503661
433 (in isoform 2)Ubiquitination-5.1321890473
435UbiquitinationFFAGQINGTTGYEEA
HHCCCCCCCCCHHHH
26.7027667366
445UbiquitinationGYEEAAAQGVIAGIN
CHHHHHHHCCEEEHH
41.7921963094
453UbiquitinationGVIAGINASLRVSRK
CCEEEHHCCCEECCC
14.1823503661
455UbiquitinationIAGINASLRVSRKPP
EEEHHCCCEECCCCC
6.1123503661
455 (in isoform 2)Ubiquitination-6.1121890473
456UbiquitinationAGINASLRVSRKPPF
EEHHCCCEECCCCCE
23.1321890473
460UbiquitinationASLRVSRKPPFVVSR
CCCEECCCCCEEEEC
49.9227667366
466 (in isoform 2)Ubiquitination-28.3421890473
471PhosphorylationVVSRTEGYIGVLIDD
EEECCCCEEEEEEEC
6.5622817900
475UbiquitinationTEGYIGVLIDDLTTL
CCCEEEEEEECCCCC
2.7527667366
475 (in isoform 6)Ubiquitination-2.75-
478UbiquitinationYIGVLIDDLTTLGTS
EEEEEEECCCCCCCC
38.6323503661
480PhosphorylationGVLIDDLTTLGTSEP
EEEEECCCCCCCCCC
27.28-
481PhosphorylationVLIDDLTTLGTSEPY
EEEECCCCCCCCCCC
30.41-
481 (in isoform 5)Ubiquitination-30.4121890473
484PhosphorylationDDLTTLGTSEPYRMF
ECCCCCCCCCCCEEE
32.79-
488PhosphorylationTLGTSEPYRMFTSRV
CCCCCCCCEEEEECE
15.6222817900
500PhosphorylationSRVEFRLSLRPDNAD
ECEEEEEECCCCCCC
20.3423532336
503 (in isoform 2)Ubiquitination-44.4921890473
503 (in isoform 5)Ubiquitination-44.4921890473
508UbiquitinationLRPDNADSRLTLRGY
CCCCCCCCCEEECEE
27.1229967540
514 (in isoform 5)Ubiquitination-36.6321890473
515 (in isoform 2)Ubiquitination-10.1621890473
516UbiquitinationRLTLRGYKDAGCVSQ
CEEECEECCCCCCCH
43.88-
519UbiquitinationLRGYKDAGCVSQQRY
ECEECCCCCCCHHHH
23.6121963094
519 (in isoform 4)Ubiquitination-23.61-
527UbiquitinationCVSQQRYERACWMKS
CCCHHHHHHHHHHHC
35.6723503661
527 (in isoform 4)Ubiquitination-35.67-
529UbiquitinationSQQRYERACWMKSSL
CHHHHHHHHHHHCCH
4.5623503661
530UbiquitinationQQRYERACWMKSSLE
HHHHHHHHHHHCCHH
4.5821890473
530 (in isoform 4)Ubiquitination-4.5821890473
531 (in isoform 6)Ubiquitination-9.03-
533MethylationYERACWMKSSLEEGI
HHHHHHHHCCHHHHH
16.6424129315
533UbiquitinationYERACWMKSSLEEGI
HHHHHHHHCCHHHHH
16.6429967540
538UbiquitinationWMKSSLEEGISVLKS
HHHCCHHHHHHHHHH
68.0923503661
539UbiquitinationMKSSLEEGISVLKSI
HHCCHHHHHHHHHHH
14.2221963094
544UbiquitinationEEGISVLKSIEFLSS
HHHHHHHHHHHHHHH
47.4321963094
548UbiquitinationSVLKSIEFLSSKWKK
HHHHHHHHHHHHHHH
8.3729967540
548 (in isoform 6)Ubiquitination-8.37-
551 (in isoform 5)Ubiquitination-44.6921890473
552UbiquitinationSIEFLSSKWKKLIPE
HHHHHHHHHHHHCCH
60.7123503661
552 (in isoform 4)Ubiquitination-60.7121890473
554UbiquitinationEFLSSKWKKLIPEAS
HHHHHHHHHHCCHHH
41.2523503661
555UbiquitinationFLSSKWKKLIPEASI
HHHHHHHHHCCHHHC
51.0029967540
555 (in isoform 1)Ubiquitination-51.0021890473
559UbiquitinationKWKKLIPEASISTSR
HHHHHCCHHHCCCCC
48.3221963094
559 (in isoform 6)Ubiquitination-48.32-
563UbiquitinationLIPEASISTSRSLPV
HCCHHHCCCCCCCCC
20.1729967540
563 (in isoform 4)Ubiquitination-20.1721890473
563 (in isoform 5)Ubiquitination-20.1721890473
564PhosphorylationIPEASISTSRSLPVR
CCHHHCCCCCCCCCH
26.87-
567PhosphorylationASISTSRSLPVRALD
HHCCCCCCCCCHHHE
36.47-
567UbiquitinationASISTSRSLPVRALD
HHCCCCCCCCCHHHE
36.4723503661
567 (in isoform 6)Ubiquitination-36.47-
569UbiquitinationISTSRSLPVRALDVL
CCCCCCCCCHHHEEE
18.1323503661
570UbiquitinationSTSRSLPVRALDVLK
CCCCCCCCHHHEEEE
7.3021890473
570 (in isoform 6)Ubiquitination-7.30-
577UbiquitinationVRALDVLKYEEVDMD
CHHHEEEEEEECCHH
50.9221906983
577 (in isoform 1)Ubiquitination-50.9221890473
578PhosphorylationRALDVLKYEEVDMDS
HHHEEEEEEECCHHH
17.11-
588UbiquitinationVDMDSLAKAVPEPLK
CCHHHHHHHCCHHHH
56.0321906983
588 (in isoform 1)Ubiquitination-56.0321890473
592UbiquitinationSLAKAVPEPLKKYTK
HHHHHCCHHHHHHHH
57.5823503661
592 (in isoform 6)Ubiquitination-57.58-
600UbiquitinationPLKKYTKCRELAERL
HHHHHHHHHHHHHHH
2.9329967540
600 (in isoform 4)Ubiquitination-2.9321890473
602UbiquitinationKKYTKCRELAERLKI
HHHHHHHHHHHHHCC
62.9021963094
603UbiquitinationKYTKCRELAERLKIE
HHHHHHHHHHHHCCE
2.8729967540
611 (in isoform 6)Ubiquitination-20.96-
612UbiquitinationERLKIEATYESVLFH
HHHCCEEEHHHHHHH
18.2923503661
612 (in isoform 4)Ubiquitination-18.2921890473
613PhosphorylationRLKIEATYESVLFHQ
HHCCEEEHHHHHHHH
17.1625159151
625UbiquitinationFHQLQEIKGVQQDEA
HHHHHHCCCCCHHHH
52.8821906983
625 (in isoform 1)Ubiquitination-52.8821890473
631UbiquitinationIKGVQQDEALQLPKD
CCCCCHHHHHCCCCC
47.1129967540
637UbiquitinationDEALQLPKDLDYLTI
HHHHCCCCCCCEEEE
78.5029967540
637 (in isoform 1)Ubiquitination-78.5021890473
640UbiquitinationLQLPKDLDYLTIRDV
HCCCCCCCEEEEEEE
46.6729967540
652UbiquitinationRDVSLSHEVREKLHF
EEEECCHHHHHHHCC
39.6423503661
652 (in isoform 6)Ubiquitination-39.64-
656UbiquitinationLSHEVREKLHFSRPQ
CCHHHHHHHCCCCCC
36.3829967540
660PhosphorylationVREKLHFSRPQTIGA
HHHHHCCCCCCCCCH
32.10-
669PhosphorylationPQTIGAASRIPGVTP
CCCCCHHHCCCCCCH
30.15-
671UbiquitinationTIGAASRIPGVTPAA
CCCHHHCCCCCCHHH
3.0129967540
676UbiquitinationSRIPGVTPAAIINLL
HCCCCCCHHHHHHHH
19.7921963094
701UbiquitinationSAMNESSKTDQYLCD
HHHCCCCHHHHHCCC
66.4521963094
716UbiquitinationADRLQEREL------
HHHHHHHCC------
59.0621963094

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 MTO1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTO1_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 MTO1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614702Combined oxidative phosphorylation deficiency 10 (COXPD10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTO1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-471 AND TYR-488, ANDMASS SPECTROMETRY.

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