MPPA_HUMAN - dbPTM
MPPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPPA_HUMAN
UniProt AC Q10713
Protein Name Mitochondrial-processing peptidase subunit alpha
Gene Name PMPCA
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Mitochondrion matrix . Mitochondrion inner membrane .
Protein Description Cleaves presequences (transit peptides) from mitochondrial protein precursors..
Protein Sequence MAAVVLAATRLLRGSGSWGCSRLRFGPPAYRRFSSGGAYPNIPLSSPLPGVPKPVFATVDGQEKFETKVTTLDNGLRVASQNKFGQFCTVGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKHGGICDCQTSRDTTMYAVSADSKGLDTVVALLADVVLQPRLTDEEVEMTRMAVQFELEDLNLRPDPEPLLTEMIHEAAYRENTVGLHRFCPTENVAKINREVLHSYLRNYYTPDRMVLAGVGVEHEHLVDCARKYLLGVQPAWGSAEAVDIDRSVAQYTGGIAKLERDMSNVSLGPTPIPELTHIMVGLESCSFLEEDFIPFAVLNMMMGGGGSFSAGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKEFILMGGTVDTVELERAKTQLTSMLMMNLESRPVIFEDVGRQVLATRSRKLPHELCTLIRNVKPEDVKRVASKMLRGKPAVAALGDLTDLPTYEHIQTALSSKDGRLPRTYRLFR
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
50UbiquitinationPLSSPLPGVPKPVFA
CCCCCCCCCCCCEEE
56.9221963094
53UbiquitinationSPLPGVPKPVFATVD
CCCCCCCCCEEEEEC
51.9422817900
53UbiquitinationSPLPGVPKPVFATVD
CCCCCCCCCEEEEEC
51.9421890473
64SuccinylationATVDGQEKFETKVTT
EEECCCCCEEEEEEE
40.38-
64UbiquitinationATVDGQEKFETKVTT
EEECCCCCEEEEEEE
40.3821963094
64SuccinylationATVDGQEKFETKVTT
EEECCCCCEEEEEEE
40.3821890473
68UbiquitinationGQEKFETKVTTLDNG
CCCCEEEEEEECCCC
30.3221906983
77MethylationTTLDNGLRVASQNKF
EECCCCEEEECCCCC
24.29115487993
87UbiquitinationSQNKFGQFCTVGILI
CCCCCCCCEEEEEEE
3.7421963094
101UbiquitinationINSGSRYEAKYLSGI
ECCCCHHHHHHHHHH
37.26-
101UbiquitinationINSGSRYEAKYLSGI
ECCCCHHHHHHHHHH
37.2621963094
103UbiquitinationSGSRYEAKYLSGIAH
CCCHHHHHHHHHHHH
34.4821890473
103AcetylationSGSRYEAKYLSGIAH
CCCHHHHHHHHHHHH
34.4825038526
103UbiquitinationSGSRYEAKYLSGIAH
CCCHHHHHHHHHHHH
34.4821906983
104PhosphorylationGSRYEAKYLSGIAHF
CCHHHHHHHHHHHHH
17.1028152594
106PhosphorylationRYEAKYLSGIAHFLE
HHHHHHHHHHHHHHH
25.6828152594
117UbiquitinationHFLEKLAFSSTARFD
HHHHHHHCCCCCCCC
9.5627667366
126UbiquitinationSTARFDSKDEILLTL
CCCCCCCCCEEEEEE
62.3121906983
132UbiquitinationSKDEILLTLEKHGGI
CCCEEEEEEEECCCC
29.4421963094
135UbiquitinationEILLTLEKHGGICDC
EEEEEEEECCCCCEE
51.1421963094
135MalonylationEILLTLEKHGGICDC
EEEEEEEECCCCCEE
51.1426320211
138UbiquitinationLTLEKHGGICDCQTS
EEEEECCCCCEECCC
19.64-
138UbiquitinationLTLEKHGGICDCQTS
EEEEECCCCCEECCC
19.6427667366
150SulfoxidationQTSRDTTMYAVSADS
CCCCCCEEEEEECCC
1.8828465586
151PhosphorylationTSRDTTMYAVSADSK
CCCCCEEEEEECCCC
11.19-
168AcetylationDTVVALLADVVLQPR
HHHHHHHHHHHHCCC
14.3819608861
168AcetylationDTVVALLADVVLQPR
HHHHHHHHHHHHCCC
14.38-
168UbiquitinationDTVVALLADVVLQPR
HHHHHHHHHHHHCCC
14.38-
168UbiquitinationDTVVALLADVVLQPR
HHHHHHHHHHHHCCC
14.3827667366
169UbiquitinationTVVALLADVVLQPRL
HHHHHHHHHHHCCCC
30.9027667366
183SulfoxidationLTDEEVEMTRMAVQF
CCHHHHHHHEEHEEE
3.3021406390
199AcetylationLEDLNLRPDPEPLLT
HHHCCCCCCCHHHHH
65.7519608861
199UbiquitinationLEDLNLRPDPEPLLT
HHHCCCCCCCHHHHH
65.7527667366
232MalonylationCPTENVAKINREVLH
CCCCCHHHHCHHHHH
35.9126320211
232AcetylationCPTENVAKINREVLH
CCCCCHHHHCHHHHH
35.9125953088
232UbiquitinationCPTENVAKINREVLH
CCCCCHHHHCHHHHH
35.9121906983
243MethylationEVLHSYLRNYYTPDR
HHHHHHHHHCCCCCC
22.37115487985
269UbiquitinationHLVDCARKYLLGVQP
HHHHHHHHHHHCCCC
23.0221906983
291UbiquitinationVDIDRSVAQYTGGIA
HCCCHHHHHHHCHHH
9.6322817900
296UbiquitinationSVAQYTGGIAKLERD
HHHHHHCHHHHEECC
14.6422817900
299UbiquitinationQYTGGIAKLERDMSN
HHHCHHHHEECCCCC
49.3027667366
299MalonylationQYTGGIAKLERDMSN
HHHCHHHHEECCCCC
49.3026320211
299AcetylationQYTGGIAKLERDMSN
HHHCHHHHEECCCCC
49.3019608861
301UbiquitinationTGGIAKLERDMSNVS
HCHHHHEECCCCCCC
46.0222817900
306UbiquitinationKLERDMSNVSLGPTP
HEECCCCCCCCCCCC
22.2821963094
329UbiquitinationVGLESCSFLEEDFIP
HCHHCCCCCCCCCHH
13.44-
329UbiquitinationVGLESCSFLEEDFIP
HCHHCCCCCCCCCHH
13.4429967540
331UbiquitinationLESCSFLEEDFIPFA
HHCCCCCCCCCHHHH
54.2121963094
342UbiquitinationIPFAVLNMMMGGGGS
HHHHHHHHHCCCCCC
1.39-
342UbiquitinationIPFAVLNMMMGGGGS
HHHHHHHHHCCCCCC
1.3922817900
347UbiquitinationLNMMMGGGGSFSAGG
HHHHCCCCCCCCCCC
23.8922817900
347UbiquitinationLNMMMGGGGSFSAGG
HHHHCCCCCCCCCCC
23.89-
352UbiquitinationGGGGSFSAGGPGKGM
CCCCCCCCCCCCCCH
25.58-
352UbiquitinationGGGGSFSAGGPGKGM
CCCCCCCCCCCCCCH
25.5822817900
357UbiquitinationFSAGGPGKGMFSRLY
CCCCCCCCCHHHHHH
50.7921963094
357UbiquitinationFSAGGPGKGMFSRLY
CCCCCCCCCHHHHHH
50.79-
360UbiquitinationGGPGKGMFSRLYLNV
CCCCCCHHHHHHHHH
5.3929967540
361PhosphorylationGPGKGMFSRLYLNVL
CCCCCHHHHHHHHHH
16.69-
364PhosphorylationKGMFSRLYLNVLNRH
CCHHHHHHHHHHHCC
8.6328152594
373UbiquitinationNVLNRHHWMYNATSY
HHHHCCCCCCCCCCC
5.7122817900
378UbiquitinationHHWMYNATSYHHSYE
CCCCCCCCCCCCCCC
26.6122817900
382UbiquitinationYNATSYHHSYEDTGL
CCCCCCCCCCCCCCE
24.6821963094
382UbiquitinationYNATSYHHSYEDTGL
CCCCCCCCCCCCCCE
24.68-
383UbiquitinationNATSYHHSYEDTGLL
CCCCCCCCCCCCCEE
19.5322817900
388UbiquitinationHHSYEDTGLLCIHAS
CCCCCCCCEEEEEEC
29.0421963094
413UbiquitinationEIITKEFILMGGTVD
HHHHHHHHHCCCCCC
2.4421963094
429PhosphorylationVELERAKTQLTSMLM
HHHHHHHHHHHHHHH
28.0322210691
441PhosphorylationMLMMNLESRPVIFED
HHHHCCCCCCEEEEH
45.0822210691
456PhosphorylationVGRQVLATRSRKLPH
HHHHHHHHCCCCCCH
25.6422210691
458PhosphorylationRQVLATRSRKLPHEL
HHHHHHCCCCCCHHH
29.4322210691
460UbiquitinationVLATRSRKLPHELCT
HHHHCCCCCCHHHHH
68.5629967540
460AcetylationVLATRSRKLPHELCT
HHHHCCCCCCHHHHH
68.5626051181
467O-linked_GlycosylationKLPHELCTLIRNVKP
CCCHHHHHHHHCCCH
37.5330379171
473UbiquitinationCTLIRNVKPEDVKRV
HHHHHCCCHHHHHHH
46.3627667366
478UbiquitinationNVKPEDVKRVASKML
CCCHHHHHHHHHHHH
54.1827667366
478AcetylationNVKPEDVKRVASKML
CCCHHHHHHHHHHHH
54.1825953088
478SuccinylationNVKPEDVKRVASKML
CCCHHHHHHHHHHHH
54.1827452117
4782-HydroxyisobutyrylationNVKPEDVKRVASKML
CCCHHHHHHHHHHHH
54.18-
483UbiquitinationDVKRVASKMLRGKPA
HHHHHHHHHHCCCCH
32.0122817900
483AcetylationDVKRVASKMLRGKPA
HHHHHHHHHHCCCCH
32.0125953088
488UbiquitinationASKMLRGKPAVAALG
HHHHHCCCCHHHHCC
24.3021906983
513UbiquitinationIQTALSSKDGRLPRT
HHHHHHCCCCCCCCE
61.9121906983

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 MPPA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPPA_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 MPPA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPPB_HUMANPMPCBphysical
26344197
QCR1_HUMANUQCRC1physical
26344197
NUDT8_HUMANNUDT8physical
28514442
HLTF_HUMANHLTFphysical
28514442
RUSD2_HUMANRPUSD2physical
28514442
MPPB_HUMANPMPCBphysical
28514442
CLU_HUMANCLUHphysical
28514442
GHITM_HUMANGHITMphysical
28514442

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND MASS SPECTROMETRY.

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