CMC2_MOUSE - dbPTM
CMC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMC2_MOUSE
UniProt AC Q9QXX4
Protein Name Calcium-binding mitochondrial carrier protein Aralar2
Gene Name Slc25a13
Organism Mus musculus (Mouse).
Sequence Length 676
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. May have a function in the urea cycle..
Protein Sequence MAAAKVALTKRADPAELKAIFLKYASIEKNGEFFMSPHDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVKQIFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNAKTGKVSAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTRSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGNRKDVEVTKEEFALAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGMLPFNLAEAQRQQKASGDAARPFLLQLAESAYRFGLGSIAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLTVNDFVRDKFMHKDGSVPLLAEIFAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYNGVTDCFRKILREEGPKALWKGVAARVFRSSPQFGVTLLTYELLQRWFYVDFGGVKPVGSEPVPKSRITLPAPNPDHVGGYKLAVATFAGIENKFGLYLPLFKPSASTSKVTAGDS
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		19.00-
5Malonylation---MAAAKVALTKRA
---CCCHHHHHHCCC		24.2626320211
18AcetylationRADPAELKAIFLKYA
CCCHHHHHHHHHHHH		30.8323576753
18MalonylationRADPAELKAIFLKYA
CCCHHHHHHHHHHHH		30.8326320211
18UbiquitinationRADPAELKAIFLKYA
CCCHHHHHHHHHHHH		30.83-
18SuccinylationRADPAELKAIFLKYA
CCCHHHHHHHHHHHH		30.8323954790
23AcetylationELKAIFLKYASIEKN
HHHHHHHHHHHHHCC		28.2023954790
26PhosphorylationAIFLKYASIEKNGEF
HHHHHHHHHHCCCEE		28.3425338131
29AcetylationLKYASIEKNGEFFMS
HHHHHHHCCCEECCC		69.4523954790
29MalonylationLKYASIEKNGEFFMS
HHHHHHHCCCEECCC		69.4526320211
29UbiquitinationLKYASIEKNGEFFMS
HHHHHHHCCCEECCC		69.45-
51PhosphorylationYLNIFGESQPNPKTV
HHHHHCCCCCCHHHH		51.8529472430
56SuccinylationGESQPNPKTVELLSG
CCCCCCHHHHHHHHH		72.3623954790
56AcetylationGESQPNPKTVELLSG
CCCCCCHHHHHHHHH		72.3623954790
62PhosphorylationPKTVELLSGVVDQTK
HHHHHHHHHCCCCCC		42.0126370283
68PhosphorylationLSGVVDQTKDGLISF
HHHCCCCCCCCEEEH		27.0026370283
104SuccinylationQLFDKAGKGEVTFED
HHHHCCCCCCCCHHH		57.6823954790
104AcetylationQLFDKAGKGEVTFED
HHHHCCCCCCCCHHH		57.6822902405
104MalonylationQLFDKAGKGEVTFED
HHHHCCCCCCCCHHH		57.6826320211
113AcetylationEVTFEDVKQIFGQTT
CCCHHHHHHHHCCCC		50.4223954790
177SuccinylationRDNAKTGKVSAIDFR
HCCCCCCCCEEEEHH		37.9424315375
177PhosphoglycerylationRDNAKTGKVSAIDFR
HCCCCCCCCEEEEHH		37.94-
177AcetylationRDNAKTGKVSAIDFR
HCCCCCCCCEEEEHH		37.9423864654
177MalonylationRDNAKTGKVSAIDFR
HCCCCCCCCEEEEHH		37.9426320211
235AcetylationNNMELIRKIYSTLAG
HHHHHHHHHHHHHCC		38.7223576753
235MalonylationNNMELIRKIYSTLAG
HHHHHHHHHHHHHCC		38.7226320211
245AcetylationSTLAGNRKDVEVTKE
HHHCCCCCCEEECHH		70.8523201123
251SuccinylationRKDVEVTKEEFALAA
CCCEEECHHHHHHHH		61.4923954790
251UbiquitinationRKDVEVTKEEFALAA
CCCEEECHHHHHHHH		61.49-
251AcetylationRKDVEVTKEEFALAA
CCCEEECHHHHHHHH		61.4923201123
354UbiquitinationVYPIDLVKTRMQNQR
EEEHHHHHHHHHCCC		37.40-
354AcetylationVYPIDLVKTRMQNQR
EEEHHHHHHHHHCCC		37.4023576753
362PhosphorylationTRMQNQRSTGSFVGE
HHHHCCCCCCCHHHH		27.6229472430
363PhosphorylationRMQNQRSTGSFVGEL
HHHCCCCCCCHHHHH		38.7523140645
365PhosphorylationQNQRSTGSFVGELMY
HCCCCCCCHHHHHHH		19.4923140645
373SuccinylationFVGELMYKNSFDCFK
HHHHHHHHCCHHHHH		31.9524315375
373AcetylationFVGELMYKNSFDCFK
HHHHHHHHCCHHHHH		31.9523576753
378S-nitrosylationMYKNSFDCFKKVLRY
HHHCCHHHHHHHHHH		5.1921278135
378S-palmitoylationMYKNSFDCFKKVLRY
HHHCCHHHHHHHHHH		5.1928526873
378S-nitrosocysteineMYKNSFDCFKKVLRY
HHHCCHHHHHHHHHH		5.19-
380AcetylationKNSFDCFKKVLRYEG
HCCHHHHHHHHHHHC		48.592374551
385PhosphorylationCFKKVLRYEGFFGLY
HHHHHHHHHCHHHHH		19.0825195567
406SuccinylationLLGVAPEKAIKLTVN
HHCCCCHHHEEEEHH		55.1224315375
406UbiquitinationLLGVAPEKAIKLTVN
HHCCCCHHHEEEEHH		55.12-
406AcetylationLLGVAPEKAIKLTVN
HHCCCCHHHEEEEHH		55.1223864654
409MalonylationVAPEKAIKLTVNDFV
CCCHHHEEEEHHHHH		42.8626320211
409UbiquitinationVAPEKAIKLTVNDFV
CCCHHHEEEEHHHHH		42.86-
438S-palmitoylationAEIFAGGCAGGSQVI
EEHHCCCCCCCCEEE		2.8828526873
454MethylationTNPLEIVKIRLQVAG
CCCCEEEEEEEEECC		27.98-
465PhosphorylationQVAGEITTGPRVSAL
EECCCCCCCCCCCHH		51.3428059163
473PhosphorylationGPRVSALSVVRDLGF
CCCCCHHHHHHHHCC		20.4829514104
485SuccinylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.9323806337
485SuccinylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.93-
485UbiquitinationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.93-
485AcetylationLGFFGIYKGAKACFL
HCCCCCCCCCEEEEC		50.9323576753
490S-nitrosocysteineIYKGAKACFLRDIPF
CCCCCEEEECCCCCH		3.04-
490S-nitrosylationIYKGAKACFLRDIPF
CCCCCEEEECCCCCH		3.0421278135
504S-palmitoylationFSAIYFPCYAHVKAS
HHHEEECEEEHHHHH		3.1728526873
546AcetylationVTPADVIKTRLQVAA
CCHHHHHHHHHHHHH		27.69-
566S-palmitoylationTYNGVTDCFRKILRE
EECHHHHHHHHHHHH		2.3128526873
566S-nitrosocysteineTYNGVTDCFRKILRE
EECHHHHHHHHHHHH		2.31-
566S-nitrosylationTYNGVTDCFRKILRE
EECHHHHHHHHHHHH		2.3122178444
577AcetylationILREEGPKALWKGVA
HHHHHCCHHHHHHHH		67.9524062335
581AcetylationEGPKALWKGVAARVF
HCCHHHHHHHHHHHH		44.3423864654
581SuccinylationEGPKALWKGVAARVF
HCCHHHHHHHHHHHH		44.3423806337
581SuccinylationEGPKALWKGVAARVF
HCCHHHHHHHHHHHH		44.34-
642AcetylationPDHVGGYKLAVATFA
CCCCCCCEEEEEEEE		32.9923864654
663AcetylationGLYLPLFKPSASTSK
CCEEEEECCCCCCCC		45.8323576753
665PhosphorylationYLPLFKPSASTSKVT
EEEEECCCCCCCCCC		35.1326643407
667PhosphorylationPLFKPSASTSKVTAG
EEECCCCCCCCCCCC		37.2426643407
668PhosphorylationLFKPSASTSKVTAGD
EECCCCCCCCCCCCC		32.0823984901
669PhosphorylationFKPSASTSKVTAGDS
ECCCCCCCCCCCCCC		23.7226643407
672PhosphorylationSASTSKVTAGDS---
CCCCCCCCCCCC---		28.7623984901
676PhosphorylationSKVTAGDS-------
CCCCCCCC-------		41.0023984901
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMC2_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 CMC2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DC1I1_MOUSEDync1i1physical
21703542
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CMC2_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-18 AND LYS-485, AND MASSSPECTROMETRY.

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