MPCP_MOUSE - dbPTM
MPCP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPCP_MOUSE
UniProt AC Q8VEM8
Protein Name Phosphate carrier protein, mitochondrial
Gene Name Slc25a3
Organism Mus musculus (Mouse).
Sequence Length 357
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein.
Protein Description Transport of phosphate groups from the cytosol to mitochondrial matrix. Phosphate is cotransported with H(+). May play a role regulation of the mitochondrial permeability transition pore (mPTP) (By similarity)..
Protein Sequence MFSSVAHLARANPFNAPHLQLVHDGLSGPRSPPAPPRRSRHLAAAAVEEYSCEFGSMKYYALCGFGGVLSCGLTHTAVVPLDLVKCRMQVDPQKYKGIFNGFSITLKEDGVRGLAKGWAPTLIGYSMQGLCKFGFYEVFKALYSNILGEENTYLWRTSLYLASSASAEFFADIALAPMEAAKVRIQTQPGYANTLREAVPKMYKEEGLNAFYKGVAPLWMRQIPYTMMKFACFERTVEALYKFVVPKPRSECTKAEQLVVTFVAGYIAGVFCAIVSHPADSVVSVLNKEKGSTASQVLQRLGFRGVWKGLFARIIMIGTLTALQWFIYDSVKVYFRLPRPPPPEMPESLKKKLGLTE
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
27PhosphorylationQLVHDGLSGPRSPPA
EEECCCCCCCCCCCC
52.8923140645
31PhosphorylationDGLSGPRSPPAPPRR
CCCCCCCCCCCCCCH
38.0722817900
39PhosphorylationPPAPPRRSRHLAAAA
CCCCCCHHHHHHHHH
25.9022817900
50PhosphorylationAAAAVEEYSCEFGSM
HHHHHHHHHCCCCCC
12.71-
52S-nitrosylationAAVEEYSCEFGSMKY
HHHHHHHCCCCCCCC
5.0022178444
86S-nitrosocysteineVPLDLVKCRMQVDPQ
EEHHHHCCCCCCCHH
3.23-
86S-nitrosylationVPLDLVKCRMQVDPQ
EEHHHHCCCCCCCHH
3.2321278135
94AcetylationRMQVDPQKYKGIFNG
CCCCCHHHCCEECCC
55.0823864654
94UbiquitinationRMQVDPQKYKGIFNG
CCCCCHHHCCEECCC
55.08-
96AcetylationQVDPQKYKGIFNGFS
CCCHHHCCEECCCEE
53.1923864654
96SuccinylationQVDPQKYKGIFNGFS
CCCHHHCCEECCCEE
53.1924315375
107MethylationNGFSITLKEDGVRGL
CCEEEEEECCCCCHH
45.14-
107AcetylationNGFSITLKEDGVRGL
CCEEEEEECCCCCHH
45.1423576753
107SuccinylationNGFSITLKEDGVRGL
CCEEEEEECCCCCHH
45.1426388266
131S-palmitoylationGYSMQGLCKFGFYEV
CCCHHHHHHHHHHHH
4.3728526873
131S-nitrosylationGYSMQGLCKFGFYEV
CCCHHHHHHHHHHHH
4.3721278135
131S-nitrosocysteineGYSMQGLCKFGFYEV
CCCHHHHHHHHHHHH
4.37-
132AcetylationYSMQGLCKFGFYEVF
CCHHHHHHHHHHHHH
54.2723576753
132MalonylationYSMQGLCKFGFYEVF
CCHHHHHHHHHHHHH
54.2726073543
136PhosphorylationGLCKFGFYEVFKALY
HHHHHHHHHHHHHHH
16.1525195567
152PhosphorylationNILGEENTYLWRTSL
HHCCCCCCCHHHHHH
24.2229899451
153PhosphorylationILGEENTYLWRTSLY
HCCCCCCCHHHHHHH
18.8222817900
191PhosphorylationRIQTQPGYANTLREA
HHCCCCCHHHHHHHH
11.8925195567
201AcetylationTLREAVPKMYKEEGL
HHHHHHHHHHHHHCH
48.5423864654
204SuccinylationEAVPKMYKEEGLNAF
HHHHHHHHHHCHHHH
45.8723806337
204UbiquitinationEAVPKMYKEEGLNAF
HHHHHHHHHHCHHHH
45.87-
204AcetylationEAVPKMYKEEGLNAF
HHHHHHHHHHCHHHH
45.8723806337
212PhosphorylationEEGLNAFYKGVAPLW
HHCHHHHHHCCHHHH
12.3825195567
213AcetylationEGLNAFYKGVAPLWM
HCHHHHHHCCHHHHH
40.2223864654
213SuccinylationEGLNAFYKGVAPLWM
HCHHHHHHCCHHHHH
40.2223954790
225PhosphorylationLWMRQIPYTMMKFAC
HHHHHCCHHHHHHHH
14.6425195567
229AcetylationQIPYTMMKFACFERT
HCCHHHHHHHHHHHH
20.9823864654
229SuccinylationQIPYTMMKFACFERT
HCCHHHHHHHHHHHH
20.9824315375
229UbiquitinationQIPYTMMKFACFERT
HCCHHHHHHHHHHHH
20.98-
232S-nitrosylationYTMMKFACFERTVEA
HHHHHHHHHHHHHHH
4.0221278135
232S-nitrosocysteineYTMMKFACFERTVEA
HHHHHHHHHHHHHHH
4.02-
242AcetylationRTVEALYKFVVPKPR
HHHHHHHHHHCCCCH
32.3124062335
242SuccinylationRTVEALYKFVVPKPR
HHHHHHHHHHCCCCH
32.3123954790
272S-nitrosylationGYIAGVFCAIVSHPA
HHHHHHHHHHHCCCC
2.0422178444
290AcetylationVSVLNKEKGSTASQV
HHHHCCCCCCCHHHH
60.8223864654
290MalonylationVSVLNKEKGSTASQV
HHHHCCCCCCCHHHH
60.8226320211
290SuccinylationVSVLNKEKGSTASQV
HHHHCCCCCCCHHHH
60.8224315375
290UbiquitinationVSVLNKEKGSTASQV
HHHHCCCCCCCHHHH
60.82-
295PhosphorylationKEKGSTASQVLQRLG
CCCCCCHHHHHHHHC
22.4028464351
308AcetylationLGFRGVWKGLFARII
HCCCHHHHHHHHHHH
43.2423806337
308SuccinylationLGFRGVWKGLFARII
HCCCHHHHHHHHHHH
43.2423806337

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 MPCP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPCP_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 MPCP_MOUSE !!

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

Oops, there are no PPI records of MPCP_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-204, AND MASSSPECTROMETRY.

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