OMA1_HUMAN - dbPTM
OMA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OMA1_HUMAN
UniProt AC Q96E52
Protein Name Metalloendopeptidase OMA1, mitochondrial
Gene Name OMA1
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. May also cleave UQCC3 under these conditions. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions..
Protein Sequence MSFICGLQSAARNHVFFRFNSLSNWRKCNTLASTSRGCHQVQVNHIVNKYQGLGVNQCDRWSFLPGNFHFYSTFNNKRTGGLSSTKSKEIWRITSKCTVWNDAFSRQLLIKEVTAVPSLSVLHPLSPASIRAIRNFHTSPRFQAAPVPLLLMILKPVQKLFAIIVGRGIRKWWQALPPNKKEVVKENIRKNKWKLFLGLSSFGLLFVVFYFTHLEVSPITGRSKLLLLGKEQFRLLSELEYEAWMEEFKNDMLTEKDARYLAVKEVLCHLIECNKDVPGISQINWVIHVVDSPIINAFVLPNGQMFVFTGFLNSVTDIHQLSFLLGHEIAHAVLGHAAEKAGMVHLLDFLGMIFLTMIWAICPRDSLALLCQWIQSKLQEYMFNRPYSRKLEAEADKIGLLLAAKACADIRASSVFWQQMEFVDSLHGQPKMPEWLSTHPSHGNRVEYLDRLIPQALKIREMCNCPPLSNPDPRLLFKLSTKHFLEESEKEDLNITKKQKMDTLPIQKQEQIPLTYIVEKRTGS
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
23PhosphorylationFFRFNSLSNWRKCNT
EEEECCCCCHHHHCC
33.8824719451
129PhosphorylationLHPLSPASIRAIRNF
CCCCCHHHHHHHHCC
18.9127535140
192AcetylationKENIRKNKWKLFLGL
HHHHHHCCHHHHHHH
49.067307393
223PhosphorylationVSPITGRSKLLLLGK
CCCCCCCCHHHCCCH
29.06-
230UbiquitinationSKLLLLGKEQFRLLS
CHHHCCCHHHHHHHH
48.59-
2302-HydroxyisobutyrylationSKLLLLGKEQFRLLS
CHHHCCCHHHHHHHH
48.59-
237PhosphorylationKEQFRLLSELEYEAW
HHHHHHHHHHHHHHH
44.73-
407S-palmitoylationLLLAAKACADIRASS
HHHHHHHHCHHHHHH
3.2629575903
448PhosphorylationSHGNRVEYLDRLIPQ
CCCCHHHHHHHHHHH
15.8529083192
478UbiquitinationPDPRLLFKLSTKHFL
CCHHHHHHHHHHHHH
41.31-
480PhosphorylationPRLLFKLSTKHFLEE
HHHHHHHHHHHHHHH
35.6827251275
481PhosphorylationRLLFKLSTKHFLEES
HHHHHHHHHHHHHHH
38.6927251275

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 OMA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OMA1_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 OMA1_HUMAN !!

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

Oops, there are no PPI records of OMA1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OMA1_HUMAN

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Related Literatures of Post-Translational Modification

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