M2OM_HUMAN - dbPTM
M2OM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M2OM_HUMAN
UniProt AC Q02978
Protein Name Mitochondrial 2-oxoglutarate/malate carrier protein
Gene Name SLC25A11
Organism Homo sapiens (Human).
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. [PubMed: 21448454 Involved in the regulation of apoptosis (By similarity]
Protein Sequence MAATASAGAGGIDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKAEGLRGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKAVIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALIRITREEGVLTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIAKTRIQNMRMIDGKPEYKNGLDVLFKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG
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------MAATASAGA
------CCCCCCCCC
17.3319413330
4Phosphorylation----MAATASAGAGG
----CCCCCCCCCCC
16.1725850435
6Phosphorylation--MAATASAGAGGID
--CCCCCCCCCCCCC
23.9229255136
15UbiquitinationGAGGIDGKPRTSPKS
CCCCCCCCCCCCHHH
27.81-
15AcetylationGAGGIDGKPRTSPKS
CCCCCCCCCCCCHHH
27.8121339330
18 (in isoform 2)Phosphorylation-58.8925056879
18PhosphorylationGIDGKPRTSPKSVKF
CCCCCCCCCHHHHHH
58.8922199227
19 (in isoform 2)Phosphorylation-31.4525056879
19PhosphorylationIDGKPRTSPKSVKFL
CCCCCCCCHHHHHHH
31.4522199227
22PhosphorylationKPRTSPKSVKFLFGG
CCCCCHHHHHHHHCC
33.64-
33SulfoxidationLFGGLAGMGATVFVQ
HHCCCCCCCCEEEEE
2.4828183972
34 (in isoform 2)Phosphorylation-19.71-
34PhosphorylationFGGLAGMGATVFVQP
HCCCCCCCCEEEEEE
19.71-
52PhosphorylationVKNRMQLSGEGAKTR
HHHHHHHCCCCCCCH
20.2221406692
572-HydroxyisobutyrylationQLSGEGAKTREYKTS
HHCCCCCCCHHHHHH
60.00-
57UbiquitinationQLSGEGAKTREYKTS
HHCCCCCCCHHHHHH
60.0021890473
57SuccinylationQLSGEGAKTREYKTS
HHCCCCCCCHHHHHH
60.0021890473
57SuccinylationQLSGEGAKTREYKTS
HHCCCCCCCHHHHHH
60.00-
62UbiquitinationGAKTREYKTSFHALT
CCCCHHHHHHHHHHH
32.7021890473
63PhosphorylationAKTREYKTSFHALTS
CCCHHHHHHHHHHHH
35.4127050516
64PhosphorylationKTREYKTSFHALTSI
CCHHHHHHHHHHHHH
15.7527050516
69PhosphorylationKTSFHALTSILKAEG
HHHHHHHHHHHHHCC
17.9527050516
70PhosphorylationTSFHALTSILKAEGL
HHHHHHHHHHHHCCC
27.1227050516
73UbiquitinationHALTSILKAEGLRGI
HHHHHHHHHCCCCHH
42.6073
73AcetylationHALTSILKAEGLRGI
HHHHHHHHHCCCCHH
42.6019608861
78MethylationILKAEGLRGIYTGLS
HHHHCCCCHHHHHHC
40.08115917065
95PhosphorylationLLRQATYTTTRLGIY
HHHHCCCCCHHHCHH
19.8226437602
102PhosphorylationTTTRLGIYTVLFERL
CCHHHCHHHHHHHHH
6.7625147952
103PhosphorylationTTRLGIYTVLFERLT
CHHHCHHHHHHHHHH
14.6022673903
115PhosphorylationRLTGADGTPPGFLLK
HHHCCCCCCCCHHHH
27.1924641631
127SulfoxidationLLKAVIGMTAGATGA
HHHHHHCCCCCCCCC
1.2728183972
161PhosphorylationPADQRRGYKNVFNAL
CHHHHHCHHHHHHHH
9.51-
162UbiquitinationADQRRGYKNVFNALI
HHHHHCHHHHHHHHH
49.8421890473
201PhosphorylationVNAAQLASYSQSKQF
HCHHHHHHHHCCCCH
33.6328152594
202PhosphorylationNAAQLASYSQSKQFL
CHHHHHHHHCCCCHH
12.7228152594
203PhosphorylationAAQLASYSQSKQFLL
HHHHHHHHCCCCHHH
26.0328152594
205PhosphorylationQLASYSQSKQFLLDS
HHHHHHCCCCHHHHC
23.6028152594
256SuccinylationNMRMIDGKPEYKNGL
HCEEECCCCCCCCCH
30.8123954790
256AcetylationNMRMIDGKPEYKNGL
HCEEECCCCCCCCCH
30.81-
256UbiquitinationNMRMIDGKPEYKNGL
HCEEECCCCCCCCCH
30.81-
303SulfoxidationTFIFLEQMNKAYKRL
HHHHHHHHHHHHHHH
3.9728183972

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M2OM_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 M2OM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPA_HUMANCOPAphysical
16169070
M2OM_HUMANSLC25A11physical
8597574
POTEI_HUMANPOTEIphysical
26186194
ACTBL_HUMANACTBL2physical
26186194
YTHD1_HUMANYTHDF1physical
26186194
FYN_HUMANFYNphysical
26186194
YES_HUMANYES1physical
26186194
PPR1A_HUMANPPP1R1Aphysical
26186194
REN3B_HUMANUPF3Bphysical
26186194
SMAP2_HUMANSMAP2physical
26186194
KPCA_HUMANPRKCAphysical
26186194
ZN703_HUMANZNF703physical
26186194
WIPI4_HUMANWDR45physical
26186194
PRG2_HUMANPRG2physical
26186194
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
VDAC3_HUMANVDAC3physical
26344197
POTEI_HUMANPOTEIphysical
28514442
PPR1A_HUMANPPP1R1Aphysical
28514442
SMAP2_HUMANSMAP2physical
28514442
ACTBL_HUMANACTBL2physical
28514442
YTHD1_HUMANYTHDF1physical
28514442
PRG2_HUMANPRG2physical
28514442
WIPI4_HUMANWDR45physical
28514442
ACTB_HUMANACTBphysical
28514442
YES_HUMANYES1physical
28514442
ZN703_HUMANZNF703physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of M2OM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-73, AND MASS SPECTROMETRY.

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