M2OM_MOUSE - dbPTM
M2OM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M2OM_MOUSE
UniProt AC Q9CR62
Protein Name Mitochondrial 2-oxoglutarate/malate carrier protein
Gene Name Slc25a11
Organism Mus musculus (Mouse).
Sequence Length 314
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis. [PubMed: 21448454]
Protein Sequence MAATASPGAGRMDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKTEGLKGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALVRIAREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIVKTRIQNMRMIDGKPEYKNGLDVLLKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG
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
2Acetylation------MAATASPGA
------CCCCCCCCC
17.33-
4Phosphorylation----MAATASPGAGR
----CCCCCCCCCCC
20.3820531401
6Phosphorylation--MAATASPGAGRMD
--CCCCCCCCCCCCC
21.3629895711
57SuccinylationQLSGEGAKTREYKTS
HHCCCCCCCHHHHHH
60.0023806337
57SuccinylationQLSGEGAKTREYKTS
HHCCCCCCCHHHHHH
60.00-
61PhosphorylationEGAKTREYKTSFHAL
CCCCCHHHHHHHHHH
19.1024925903
69PhosphorylationKTSFHALTSILKTEG
HHHHHHHHHHHHHCC
17.9524925903
70PhosphorylationTSFHALTSILKTEGL
HHHHHHHHHHHHCCC
27.1224925903
73AcetylationHALTSILKTEGLKGI
HHHHHHHHHCCCCHH
42.75-
93PhosphorylationAGLLRQATYTTTRLG
HHHHHHCCCCCHHHC
17.0522871156
94PhosphorylationGLLRQATYTTTRLGI
HHHHHCCCCCHHHCH
12.7122871156
95PhosphorylationLLRQATYTTTRLGIY
HHHHCCCCCHHHCHH
19.8228576409
102PhosphorylationTTTRLGIYTVLFERL
CCHHHCHHHHHHHHH
6.7622817900
103PhosphorylationTTRLGIYTVLFERLT
CHHHCHHHHHHHHHH
14.6020415495
110PhosphorylationTVLFERLTGADGTPP
HHHHHHHHCCCCCCC
36.2221454597
162UbiquitinationADQRRGYKNVFNALV
HHHHHCHHHHHHHHH
49.84-
162AcetylationADQRRGYKNVFNALV
HHHHHCHHHHHHHHH
49.8424062335
184S-nitrosocysteineVPTLWRGCIPTMARA
CCCHHHCHHHHHHHH
2.24-
184S-nitrosylationVPTLWRGCIPTMARA
CCCHHHCHHHHHHHH
2.2421278135
201PhosphorylationVNAAQLASYSQSKQF
HCHHHHHHHHCCCCH
33.6320415495
202PhosphorylationNAAQLASYSQSKQFL
CHHHHHHHHCCCCHH
12.7222817900
203PhosphorylationAAQLASYSQSKQFLL
HHHHHHHHCCCCHHH
26.0329899451
205PhosphorylationQLASYSQSKQFLLDS
HHHHHHCCCCHHHHC
23.6022871156
256AcetylationNMRMIDGKPEYKNGL
HCEECCCCCCCCCHH
30.8123576753
268AcetylationNGLDVLLKVVRYEGF
CHHHHHHHHHHHCCH
34.2323201123

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 M2OM_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M2OM_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 M2OM_MOUSE !!

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

Oops, there are no PPI records of M2OM_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of M2OM_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102 AND TYR-202, ANDMASS SPECTROMETRY.

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