OTC_HUMAN - dbPTM
OTC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTC_HUMAN
UniProt AC P00480
Protein Name Ornithine carbamoyltransferase, mitochondrial
Gene Name OTC
Organism Homo sapiens (Human).
Sequence Length 354
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MLFNLRILLNNAAFRNGHNFMVRNFRCGQPLQNKVQLKGRDLLTLKNFTGEEIKYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPCFLTTQDIHLGVNESLTDTARVLSSMADAVLARVYKQSDLDTLAKEASIPIINGLSDLYHPIQILADYLTLQEHYSSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDASVTKLAEQYAKENGTKLLLTNDPLEAAHGGNVLITDTWISMGQEEEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPQLQKPKF
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
46AcetylationGRDLLTLKNFTGEEI
CCEEEEECCCCHHHH
44.7920167786
55PhosphorylationFTGEEIKYMLWLSAD
CCHHHHHHHHHHCCC
11.78-
70AcetylationLKFRIKQKGEYLPLL
CEEECCCCCCEEEEC
49.02-
70SuccinylationLKFRIKQKGEYLPLL
CEEECCCCCCEEEEC
49.02-
70SuccinylationLKFRIKQKGEYLPLL
CEEECCCCCCEEEEC
49.02-
80SuccinylationYLPLLQGKSLGMIFE
EEEECCCCCHHEEEE
29.55-
80SuccinylationYLPLLQGKSLGMIFE
EEEECCCCCHHEEEE
29.55-
88SuccinylationSLGMIFEKRSTRTRL
CHHEEEECCCCCCEE
40.68-
88SuccinylationSLGMIFEKRSTRTRL
CHHEEEECCCCCCEE
40.68-
882-HydroxyisobutyrylationSLGMIFEKRSTRTRL
CHHEEEECCCCCCEE
40.68-
88AcetylationSLGMIFEKRSTRTRL
CHHEEEECCCCCCEE
40.6819318352
132PhosphorylationTDTARVLSSMADAVL
HHHHHHHHHHHHHHH
18.4025072903
133PhosphorylationDTARVLSSMADAVLA
HHHHHHHHHHHHHHH
17.5225072903
144SuccinylationAVLARVYKQSDLDTL
HHHHHHHCCCCHHHH
40.23-
144AcetylationAVLARVYKQSDLDTL
HHHHHHHCCCCHHHH
40.2327178108
144SuccinylationAVLARVYKQSDLDTL
HHHHHHHCCCCHHHH
40.23-
146PhosphorylationLARVYKQSDLDTLAK
HHHHHCCCCHHHHHH
35.67-
221AcetylationHLQAATPKGYEPDAS
EECCCCCCCCCCCCH
70.53-
221SuccinylationHLQAATPKGYEPDAS
EECCCCCCCCCCCCH
70.53-
221SuccinylationHLQAATPKGYEPDAS
EECCCCCCCCCCCCH
70.53-
223PhosphorylationQAATPKGYEPDASVT
CCCCCCCCCCCCHHH
30.34-
231AcetylationEPDASVTKLAEQYAK
CCCCHHHHHHHHHHH
43.4792453
231SuccinylationEPDASVTKLAEQYAK
CCCCHHHHHHHHHHH
43.47-
231SuccinylationEPDASVTKLAEQYAK
CCCCHHHHHHHHHHH
43.47-
238AcetylationKLAEQYAKENGTKLL
HHHHHHHHHCCCEEE
46.94-
238SuccinylationKLAEQYAKENGTKLL
HHHHHHHHHCCCEEE
46.94-
238SuccinylationKLAEQYAKENGTKLL
HHHHHHHHHCCCEEE
46.94-
243AcetylationYAKENGTKLLLTNDP
HHHHCCCEEEEECCH
38.24-
274SuccinylationSMGQEEEKKKRLQAF
CCCCHHHHHHHHHHH
67.86-
274SuccinylationSMGQEEEKKKRLQAF
CCCCHHHHHHHHHHH
67.86-
284PhosphorylationRLQAFQGYQVTMKTA
HHHHHCCCCEEEEEH
6.77-
289SuccinylationQGYQVTMKTAKVAAS
CCCCEEEEEHHHHHC
35.65-
289SuccinylationQGYQVTMKTAKVAAS
CCCCEEEEEHHHHHC
35.65-
292SuccinylationQVTMKTAKVAASDWT
CEEEEEHHHHHCCCE
37.32-
292SuccinylationQVTMKTAKVAASDWT
CEEEEEHHHHHCCCE
37.32-
292AcetylationQVTMKTAKVAASDWT
CEEEEEHHHHHCCCE
37.32-
307SuccinylationFLHCLPRKPEEVDDE
EEEECCCCCCCCCCC
55.64-
307AcetylationFLHCLPRKPEEVDDE
EEEECCCCCCCCCCC
55.64-
307SuccinylationFLHCLPRKPEEVDDE
EEEECCCCCCCCCCC
55.64-
317PhosphorylationEVDDEVFYSPRSLVF
CCCCCCCCCCCHHCC
23.96-

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 OTC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
88KAcetylation

19318352

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 OTC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBB1_HUMANTUBB1physical
28514442
DPOG1_HUMANPOLGphysical
28514442
NPS3A_HUMANNIPSNAP3Aphysical
28514442
NDUF7_HUMANNDUFAF7physical
28514442
ADRO_HUMANFDXRphysical
28514442
ATPF1_HUMANATPAF1physical
28514442
GLSK_HUMANGLSphysical
28514442
SYNM_HUMANNARS2physical
28514442
RTL8C_HUMANFAM127Aphysical
28514442
SYHM_HUMANHARS2physical
28514442
CPSM_HUMANCPS1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
311250Ornithine carbamoyltransferase deficiency (OTCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00155L-Citrulline
DB00129L-Ornithine
Regulatory Network of OTC_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine 88 acetylation negatively regulates ornithinecarbamoyltransferase activity in response to nutrient signals.";
Yu W., Lin Y., Yao J., Huang W., Lei Q., Xiong Y., Zhao S., Guan K.L.;
J. Biol. Chem. 284:13669-13675(2009).
Cited for: ACETYLATION AT LYS-88, AND ENZYME REGULATION.

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