CMC2_HUMAN - dbPTM
CMC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMC2_HUMAN
UniProt AC Q9UJS0
Protein Name Calcium-binding mitochondrial carrier protein Aralar2
Gene Name SLC25A13
Organism Homo sapiens (Human).
Sequence Length 675
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. [PubMed: 11566871]
Protein Sequence MAAAKVALTKRADPAELRTIFLKYASIEKNGEFFMSPNDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVKQVFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNARTGRVTAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTTSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGTRKDVEVTKEEFVLAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGTLPFNLAEAQRQKASGDSARPVLLQVAESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLTVNDFVRDKFMHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGVTLLTYELLQRWFYIDFGGVKPMGSEPVPKSRINLPAPNPDHVGGYKLAVATFAGIENKFGLYLPLFKPSVSTSKAIGGGP
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------MAAAKVALT
------CCCHHHHHH		19.0025944712
9PhosphorylationAAAKVALTKRADPAE
CCHHHHHHCCCCHHH		14.5624670416
23AcetylationELRTIFLKYASIEKN
HHHHHHHHHHEEECC		28.2025825284
23UbiquitinationELRTIFLKYASIEKN
HHHHHHHHHHEEECC		28.2029967540
26PhosphorylationTIFLKYASIEKNGEF
HHHHHHHEEECCCEE		28.3420860994
36PhosphorylationKNGEFFMSPNDFVTR
CCCEEECCHHHHHHH		18.5220860994
51PhosphorylationYLNIFGESQPNPKTV
HHHHHCCCCCCHHHH		51.8524275569
68PhosphorylationLSGVVDQTKDGLISF
HHHCCCCCCCCEEEH		27.0020068231
69UbiquitinationSGVVDQTKDGLISFQ
HHCCCCCCCCEEEHH		44.1321890473
104UbiquitinationQLFDKAGKGEVTFED
HHHHCCCCCCEEHHH		57.6829967540
124UbiquitinationGQTTIHQHIPFNWDS
CCCEEEECCCCCCCC		18.6121890473
200UbiquitinationHVLTPFVEECLVAAA
HHCCHHHHHHHHHHC		43.2921890473
203UbiquitinationTPFVEECLVAAAGGT
CHHHHHHHHHHCCCC		3.1221890473
218PhosphorylationTSHQVSFSYFNGFNS
CCEEEEHHHHCCHHH		22.70-
219PhosphorylationSHQVSFSYFNGFNSL
CEEEEHHHHCCHHHH		10.07-
237PhosphorylationMELIRKIYSTLAGTR
HHHHHHHHHHHCCCC		9.9121406692
238PhosphorylationELIRKIYSTLAGTRK
HHHHHHHHHHCCCCC		22.0326437602
239PhosphorylationLIRKIYSTLAGTRKD
HHHHHHHHHCCCCCC		12.0321406692
243PhosphorylationIYSTLAGTRKDVEVT
HHHHHCCCCCCEEEC		29.0126437602
250PhosphorylationTRKDVEVTKEEFVLA
CCCCEEECHHHHHHH		21.1630576142
251AcetylationRKDVEVTKEEFVLAA
CCCEEECHHHHHHHH		61.4926051181
251UbiquitinationRKDVEVTKEEFVLAA
CCCEEECHHHHHHHH		61.4929967540
267SulfoxidationKFGQVTPMEVDILFQ
HHCCCCCCCHHHHHH		5.9928183972
314PhosphorylationEAQRQKASGDSARPV
HHHHHHCCCCCHHHH		50.6024275569
350UbiquitinationATAVYPIDLVKTRMQ
CEEEEEHHHHHHHHH		40.6921890473
353AcetylationVYPIDLVKTRMQNQR
EEEHHHHHHHHHCCC		37.40-
353UbiquitinationVYPIDLVKTRMQNQR
EEEHHHHHHHHHCCC		37.4021890473
354UbiquitinationYPIDLVKTRMQNQRS
EEHHHHHHHHHCCCC		24.7221890473
354UbiquitinationYPIDLVKTRMQNQRS
EEHHHHHHHHHCCCC		24.7221890473
361PhosphorylationTRMQNQRSTGSFVGE
HHHHCCCCCCCHHHH		27.6228857561
361O-linked_GlycosylationTRMQNQRSTGSFVGE
HHHHCCCCCCCHHHH		27.6230379171
362PhosphorylationRMQNQRSTGSFVGEL
HHHCCCCCCCHHHHH		38.7528857561
364PhosphorylationQNQRSTGSFVGELMY
HCCCCCCCHHHHHHH		19.4928857561
364UbiquitinationQNQRSTGSFVGELMY
HCCCCCCCHHHHHHH		19.4921890473
372AcetylationFVGELMYKNSFDCFK
HHHHHHHHCCHHHHH		31.95-
379AcetylationKNSFDCFKKVLRYEG
HCCHHHHHHHHHHHC		48.592380343
379UbiquitinationKNSFDCFKKVLRYEG
HCCHHHHHHHHHHHC		48.5932142685
379MethylationKNSFDCFKKVLRYEG
HCCHHHHHHHHHHHC		48.592380343
380UbiquitinationNSFDCFKKVLRYEGF
CCHHHHHHHHHHHCH		26.6732142685
405AcetylationLLGVAPEKAIKLTVN
HHCCCCHHHEEEEHH		55.1266691141
405UbiquitinationLLGVAPEKAIKLTVN
HHCCCCHHHEEEEHH		55.1221890473
408UbiquitinationVAPEKAIKLTVNDFV
CCCHHHEEEEHHHHH		42.8621890473
409 (in isoform 2)Ubiquitination-5.44-
409UbiquitinationAPEKAIKLTVNDFVR
CCHHHEEEEHHHHHH		5.4421890473
409UbiquitinationAPEKAIKLTVNDFVR
CCHHHEEEEHHHHHH		5.4421890473
419UbiquitinationNDFVRDKFMHKDGSV
HHHHHHHHCCCCCCC		7.9021890473
453MethylationTNPLEIVKIRLQVAG
CCCCEEEEEEEEECC		27.9824129315
463PhosphorylationLQVAGEITTGPRVSA
EEECCCCCCCCCCCH		22.7722210691
464PhosphorylationQVAGEITTGPRVSAL
EECCCCCCCCCCCHH		51.3428111955
469PhosphorylationITTGPRVSALSVVRD
CCCCCCCCHHHHHHH		25.4428111955
472PhosphorylationGPRVSALSVVRDLGF
CCCCCHHHHHHHHCC		20.4828111955
481UbiquitinationVRDLGFFGIYKGAKA
HHHHCCCCCCCCCEE		21.7621890473
484SuccinylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.9319608861
484UbiquitinationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.9321890473
484MethylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.9390075
484SuccinylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.93-
484AcetylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.9319608861
485AcetylationGFFGIYKGAKACFLR
CCCCCCCCCEEEECC		18.4819608861
485UbiquitinationGFFGIYKGAKACFLR
CCCCCCCCCEEEECC		18.4821890473
485UbiquitinationGFFGIYKGAKACFLR
CCCCCCCCCEEEECC		18.4821890473
487UbiquitinationFGIYKGAKACFLRDI
CCCCCCCEEEECCCC		55.1221890473
488UbiquitinationGIYKGAKACFLRDIP
CCCCCCEEEECCCCC		6.6921890473
488UbiquitinationGIYKGAKACFLRDIP
CCCCCCEEEECCCCC		6.6921890473
495UbiquitinationACFLRDIPFSAIYFP
EEECCCCCHHHEEEC		22.7921890473
498UbiquitinationLRDIPFSAIYFPCYA
CCCCCHHHEEECEEE		10.8121890473
510PhosphorylationCYAHVKASFANEDGQ
EEEHHHHHCCCCCCC		21.1220068231
519PhosphorylationANEDGQVSPGSLLLA
CCCCCCCCCHHHHHH		18.6920068231
522PhosphorylationDGQVSPGSLLLAGAI
CCCCCCHHHHHHHHH		21.1620068231
536PhosphorylationIAGMPAASLVTPADV
HCCCCHHHCCCHHHH		26.0220068231
539PhosphorylationMPAASLVTPADVIKT
CCHHHCCCHHHHHHH		20.3220068231
580SuccinylationEGPKALWKGAGARVF
HCCHHHHCCCCCEEC		39.47-
580SuccinylationEGPKALWKGAGARVF
HCCHHHHCCCCCEEC		39.47-
580MalonylationEGPKALWKGAGARVF
HCCHHHHCCCCCEEC		39.4726320211
581 (in isoform 2)Malonylation-20.0526320211
599PhosphorylationQFGVTLLTYELLQRW
CCCCCHHHHHHHHHC		20.3322468782
600PhosphorylationFGVTLLTYELLQRWF
CCCCHHHHHHHHHCC		12.4422468782
619O-linked_GlycosylationGGVKPMGSEPVPKSR
CCCCCCCCCCCCHHH		32.2630379171
619PhosphorylationGGVKPMGSEPVPKSR
CCCCCCCCCCCCHHH		32.2623312004
625O-linked_GlycosylationGSEPVPKSRINLPAP
CCCCCCHHHCCCCCC		32.1130379171
657PhosphorylationIENKFGLYLPLFKPS
CCCCCCCEEECCCCC		13.4724719451
658PhosphorylationENKFGLYLPLFKPSV
CCCCCCEEECCCCCC		3.4124719451
662AcetylationGLYLPLFKPSVSTSK
CCEEECCCCCCCCCC		44.0326051181
664PhosphorylationYLPLFKPSVSTSKAI
EEECCCCCCCCCCCC		29.3223403867
665PhosphorylationLPLFKPSVSTSKAIG
EECCCCCCCCCCCCC		11.1124719451
666PhosphorylationPLFKPSVSTSKAIGG
ECCCCCCCCCCCCCC		31.1623403867
667PhosphorylationLFKPSVSTSKAIGGG
CCCCCCCCCCCCCCC		31.9023403867
668PhosphorylationFKPSVSTSKAIGGGP
CCCCCCCCCCCCCCC		16.7523403867
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 CMC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMC2_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 CMC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RM46_HUMANMRPL46physical
22939629
ELAV1_HUMANELAVL1physical
26344197
MIC60_HUMANIMMTphysical
26344197
CMC1_HUMANSLC25A12physical
28514442
Drug and Disease Associations
Kegg Disease
H00185 Citrullinemia (CTLN)
OMIM Disease
603471Citrullinemia 2 (CTLN2)
605814Cholestasis, neonatal intrahepatic, caused by citrin deficiency (NICCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00128L-Aspartic Acid
Regulatory Network of CMC2_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-484, AND MASS SPECTROMETRY.

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