PREP_MOUSE - dbPTM
PREP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PREP_MOUSE
UniProt AC Q8K411
Protein Name Presequence protease, mitochondrial {ECO:0000305}
Gene Name Pitrm1 {ECO:0000312|MGI:MGI:1916867}
Organism Mus musculus (Mouse).
Sequence Length 1036
Subcellular Localization Mitochondrion matrix .
Protein Description Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently..
Protein Sequence MWRFSGRRGLCAVQRLSCGRVHHRVWREKSDQACERALQYKVGEKIHGFTVNQVTPVPELFLTAVKLSHDNTGARYLHLAREDKNNLFSVQFRTTPMDSTGVPHVLEHTVLCGSQKYPCRDPFFKMLNRSLSTFMNAMTASDYTIYPFSTQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENPRDPQTPLIFKGVVFNEMKGAFTDNERIFSQHLQNKLLPDHTYSVVSGGDPLCIPELTWEQLKQFHATHYHPSNARFFTYGNFQLEGHLKQIHEEALSKFQRLEQSTAVPAQPHWDKPREFHITCGPDSLATETAKQTTVSVSFLLPDITDTFEAFTLSLLSSLLIAGPNSPFYKALIESGLGTDFSPDVGYNGYTREAYFSVGLQGIAEKDVKTVRELVDRTIEEVIEKGFEDDRIEALLHKIEIQTKHQSASFGLTLTSYIASCWNHDGDPVELLQIGSQLTRFRKCLKENPKFLQEKVEQYFKNNQHKLTLSMKPDDKYYEKQTQMETEKLEQKVNSLSPADKQQIYEKGLELQTQQSKHQDASCLPALKVSDIEPSMPFTKLDIGLAAGDIPVQYCPQPTNGMVYFRAFSSLNTLPEDLRPIVPLFCSVLTKLGCGILNYREQAQQIELKTGGMSVTPHVLPDDSQLDTYEQGVLFSSLCLERNLPDMMHLWSEIFNNPCFEEEEHFKVLVKMTAQELSNGISDSGHLYAALRASKTLTPSGDLQETFSGMDQVKVMKRIAEMTDIKPILRKLPRIKKYLLNCDNMRCSVNATPQQMPQAEKEVENFLRNVGRSKKERKPVRPHIVEKPTPSGPSGAAHVSGSQIVRKLVTDPTFKPCQMKTHFVLPFPVNYIGECVRTVPYADPDHASLKILARLMTAKFLHTEIREKGGAYGGGAKLTHSGIFTLYSYRDPNSIETLQSFGKAVDWAKSGKFTQQDIDEAKLSVFSTVDSPVAPSDKGMDHFLYGLSDEMKQAYREQLFAVNHDKLTSVSHKYLGIGKSTHGLAILGPENSKIAKDPSWIIK
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
41SuccinylationCERALQYKVGEKIHG
HHHHHHHHHCCEECC
30.7023806337
41AcetylationCERALQYKVGEKIHG
HHHHHHHHHCCEECC
30.7023806337
84AcetylationLHLAREDKNNLFSVQ
EEEEECCCCCCEEEE
42.8723236377
287AcetylationIHEEALSKFQRLEQS
HHHHHHHHHHHHHHC
46.4923954790
305AcetylationPAQPHWDKPREFHIT
CCCCCCCCCCEEEEE
40.5623201123
312PhosphorylationKPREFHITCGPDSLA
CCCEEEEEECCCCCC
11.6622817900
322PhosphorylationPDSLATETAKQTTVS
CCCCCCCCCCCCEEE
34.5022817900
418AcetylationTIEEVIEKGFEDDRI
HHHHHHHCCCCCHHH
58.7523954790
476AcetylationSQLTRFRKCLKENPK
HHHHHHHHHHHHCHH
41.007721377
479AcetylationTRFRKCLKENPKFLQ
HHHHHHHHHCHHHHH
65.997721387
483AcetylationKCLKENPKFLQEKVE
HHHHHCHHHHHHHHH
71.0022826441
488AcetylationNPKFLQEKVEQYFKN
CHHHHHHHHHHHHHH
37.8022826441
505AcetylationHKLTLSMKPDDKYYE
CEEEEEECCCHHHHH
41.7523201123
509AcetylationLSMKPDDKYYEKQTQ
EEECCCHHHHHHHHH
58.0523954790
521AcetylationQTQMETEKLEQKVNS
HHHHHHHHHHHHHHC
65.8223954790
528PhosphorylationKLEQKVNSLSPADKQ
HHHHHHHCCCHHHHH
32.9628066266
530PhosphorylationEQKVNSLSPADKQQI
HHHHHCCCHHHHHHH
20.1928066266
550AcetylationELQTQQSKHQDASCL
HHHHHHCCCCCCCCC
40.7323806337
556S-nitrosylationSKHQDASCLPALKVS
CCCCCCCCCCCEEHH
5.9021278135
556S-nitrosocysteineSKHQDASCLPALKVS
CCCCCCCCCCCEEHH
5.90-
627S-nitrosylationSVLTKLGCGILNYRE
HHHHHHCCCCCCHHH
4.4321278135
627S-nitrosocysteineSVLTKLGCGILNYRE
HHHHHHCCCCCCHHH
4.43-
747SuccinylationFSGMDQVKVMKRIAE
HCCHHHHHHHHHHHH
30.8623954790
747AcetylationFSGMDQVKVMKRIAE
HCCHHHHHHHHHHHH
30.8623236377
759SuccinylationIAEMTDIKPILRKLP
HHHHCCCHHHHHHCH
28.9026388266
759AcetylationIAEMTDIKPILRKLP
HHHHCCCHHHHHHCH
28.9023806337
770SuccinylationRKLPRIKKYLLNCDN
HHCHHHHHHHHCCCC
38.4723806337
770SuccinylationRKLPRIKKYLLNCDN
HHCHHHHHHHHCCCC
38.47-
770MalonylationRKLPRIKKYLLNCDN
HHCHHHHHHHHCCCC
38.4726320211
770AcetylationRKLPRIKKYLLNCDN
HHCHHHHHHHHCCCC
38.4723576753
771PhosphorylationKLPRIKKYLLNCDNM
HCHHHHHHHHCCCCC
16.0625195567
780S-nitrosylationLNCDNMRCSVNATPQ
HCCCCCCEECCCCHH
3.5621278135
780S-nitrosocysteineLNCDNMRCSVNATPQ
HCCCCCCEECCCCHH
3.56-
811AcetylationGRSKKERKPVRPHIV
CCCCCCCCCCCCCEE
49.2924062335
840AcetylationSGSQIVRKLVTDPTF
CHHHHHHHHHCCCCC
36.0922826441
848SuccinylationLVTDPTFKPCQMKTH
HHCCCCCCCCCCEEE
47.57-
848AcetylationLVTDPTFKPCQMKTH
HHCCCCCCCCCCEEE
47.5723864654
848SuccinylationLVTDPTFKPCQMKTH
HHCCCCCCCCCCEEE
47.5723806337
883SuccinylationDPDHASLKILARLMT
CCCHHHHHHHHHHHH
32.9323806337
883AcetylationDPDHASLKILARLMT
CCCHHHHHHHHHHHH
32.9323576753
892AcetylationLARLMTAKFLHTEIR
HHHHHHHHHHCHHHH
39.0122826441
942AcetylationGKAVDWAKSGKFTQQ
HHHHHHHHCCCCCHH
56.3323806337
942SuccinylationGKAVDWAKSGKFTQQ
HHHHHHHHCCCCCHH
56.3323806337
945AcetylationVDWAKSGKFTQQDID
HHHHHCCCCCHHHHH
52.9423864654
945SuccinylationVDWAKSGKFTQQDID
HHHHHCCCCCHHHHH
52.9423806337
945SuccinylationVDWAKSGKFTQQDID
HHHHHCCCCCHHHHH
52.94-
960PhosphorylationEAKLSVFSTVDSPVA
HHHHEEEEEECCCCC
25.9321743459
961PhosphorylationAKLSVFSTVDSPVAP
HHHEEEEEECCCCCC
19.5021743459
964PhosphorylationSVFSTVDSPVAPSDK
EEEEEECCCCCCCCC
19.5526745281
1001PhosphorylationAVNHDKLTSVSHKYL
CCCHHHHHCCCCCCC
32.5923140645
1002PhosphorylationVNHDKLTSVSHKYLG
CCHHHHHCCCCCCCC
31.8723140645
1004PhosphorylationHDKLTSVSHKYLGIG
HHHHHCCCCCCCCCC
17.6523140645
1006AcetylationKLTSVSHKYLGIGKS
HHHCCCCCCCCCCCC
34.3622826441
1026AcetylationILGPENSKIAKDPSW
EECCCCCCCCCCCCC
59.2623806337
1026SuccinylationILGPENSKIAKDPSW
EECCCCCCCCCCCCC
59.2623806337
1036SuccinylationKDPSWIIK-------
CCCCCCCC-------
45.1926388266
1036AcetylationKDPSWIIK-------
CCCCCCCC-------
45.1924062335

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 PREP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PREP_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 PREP_MOUSE !!

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

Oops, there are no PPI records of PREP_MOUSE !!

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

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Related Literatures of Post-Translational Modification

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