YMEL1_MOUSE - dbPTM
YMEL1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YMEL1_MOUSE
UniProt AC O88967
Protein Name ATP-dependent zinc metalloprotease YME1L1
Gene Name Yme1l1
Organism Mus musculus (Mouse).
Sequence Length 715
Subcellular Localization Mitochondrion inner membrane . Mitochondrion .
Protein Description ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (By similarity). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure. [PubMed: 17709429]
Protein Sequence MFSLSSTVQPQVTIPLSHLINAFHSPKNISVSVNTPVSQKQHRDTVPEHEAPSSEPVLNLRDLGLSELKIGQIDKMVENLLPGFYKDKRVSSCWHTSHISAQSFFENKYGHLDMFSTLRSSSLYRQHPKTLRSICSDLQYFPVFIQSRGFKTLKSRTRRLQSTSERLVEAQNIAPSFVKGFLLRDRGTDLESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTVLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDKSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRESYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
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
30PhosphorylationFHSPKNISVSVNTPV
HCCCCCEEEEECCCC
20.10-
32PhosphorylationSPKNISVSVNTPVSQ
CCCCEEEEECCCCCC
11.67-
35PhosphorylationNISVSVNTPVSQKQH
CEEEEECCCCCCCCC
23.94-
38PhosphorylationVSVNTPVSQKQHRDT
EEECCCCCCCCCCCC
32.63-
69UbiquitinationDLGLSELKIGQIDKM
HHCCCCCCHHHHHHH
40.51-
162PhosphorylationSRTRRLQSTSERLVE
HHHHHHHHHHHHHHH
38.19-
163PhosphorylationRTRRLQSTSERLVEA
HHHHHHHHHHHHHHH
22.9622817900
179UbiquitinationNIAPSFVKGFLLRDR
HHCHHHHHHHHHCCC
41.77-
200UbiquitinationLDKLMKTKNIPEAHQ
HHHHHHCCCCCHHHH
47.5727667366
275UbiquitinationSAVDPVQMKNVTFEH
CCCCCEECCCCCHHH
3.2927667366
392PhosphorylationVGGKRIESPMHPYSR
CCCEECCCCCCCCCH
25.7525338131
644PhosphorylationSEKLGVMTYSDTGKL
CCCCCCEECCCCCCC
19.9128066266
645PhosphorylationEKLGVMTYSDTGKLS
CCCCCEECCCCCCCC
6.1029472430
646PhosphorylationKLGVMTYSDTGKLSP
CCCCEECCCCCCCCH
21.3828066266
648PhosphorylationGVMTYSDTGKLSPET
CCEECCCCCCCCHHH
30.2128066266

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 YMEL1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YMEL1_MOUSE !!

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 YMEL1_MOUSE !!

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

Oops, there are no PPI records of YMEL1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YMEL1_MOUSE

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Related Literatures of Post-Translational Modification

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