SCMC1_HUMAN - dbPTM
SCMC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCMC1_HUMAN
UniProt AC Q6NUK1
Protein Name Calcium-binding mitochondrial carrier protein SCaMC-1
Gene Name SLC25A24
Organism Homo sapiens (Human).
Sequence Length 477
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Calcium-dependent mitochondrial solute carrier. Mediates the reversible, electroneutral exchange of Mg-ATP or Mg-ADP against phosphate ions, catalyzing the net uptake or efflux of adenine nucleotides across the mitochondrial inner membrane. Nucleotide transport is inactive when cytosolic calcium levels are low, and is activated by an increase in cytosolic calcium levels. May play a role in protecting cells against oxidative stress-induced cell death, probably by promoting the formation of calcium-phosphate precipitates in the mitochondrial matrix, and thereby buffering calcium levels in the mitochondrial matrix..
Protein Sequence MLRWLRDFVLPTAACQDAEQPTRYETLFQALDRNGDGVVDIGELQEGLRNLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDVDGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKIMMQVHGSKSDKMNIFGGFRQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTGQYSGIYDCAKKILKHEGLGAFYKGYVPNLLGIIPYAGIDLAVYELLKSYWLDNFAKDSVNPGVMVLLGCGALSSTCGQLASYPLALVRTRMQAQAMLEGSPQLNMVGLFRRIISKEGIPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK
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
37UbiquitinationALDRNGDGVVDIGEL
HHHHCCCCCEEHHHH		23.8124816145
46 (in isoform 2)Phosphorylation-73.2024275569
62UbiquitinationLGQDAEEKIFTTGDV
CCCCCCHHCEECCCC		34.3322817900
62 (in isoform 1)Ubiquitination-34.3321890473
622-HydroxyisobutyrylationLGQDAEEKIFTTGDV
CCCCCCHHCEECCCC		34.33-
71UbiquitinationFTTGDVNKDGKLDFE
EECCCCCCCCCCCHH		68.6429967540
74UbiquitinationGDVNKDGKLDFEEFM
CCCCCCCCCCHHHHH		55.8329967540
81SulfoxidationKLDFEEFMKYLKDHE
CCCHHHHHHHHHHHH		2.9321406390
185PhosphorylationLTIPDEFTEDEKKSG
EECCCCCCCCHHHCC		40.24-
208PhosphorylationGGIAGAVSRTSTAPL
HHHHHCCCCCCCCCH		29.3420068231
224UbiquitinationRLKIMMQVHGSKSDK
HHHHHHHHHCCCCCC		2.7624816145
228AcetylationMMQVHGSKSDKMNIF
HHHHHCCCCCCCCCC		68.2326210075
228MalonylationMMQVHGSKSDKMNIF
HHHHHCCCCCCCCCC		68.2326320211
229PhosphorylationMQVHGSKSDKMNIFG
HHHHCCCCCCCCCCH		44.1320068231
231MalonylationVHGSKSDKMNIFGGF
HHCCCCCCCCCCHHH		40.7226320211
232SulfoxidationHGSKSDKMNIFGGFR
HCCCCCCCCCCHHHH		5.8128465586
243SuccinylationGGFRQMVKEGGIRSL
HHHHHHHHHCCCCCE		45.3527452117
243AcetylationGGFRQMVKEGGIRSL
HHHHHHHHHCCCCCE		45.3523236377
243UbiquitinationGGFRQMVKEGGIRSL
HHHHHHHHHCCCCCE		45.3524816145
249PhosphorylationVKEGGIRSLWRGNGT
HHHCCCCCEEECCCC		30.2924719451
266UbiquitinationIKIAPETAVKFWAYE
EEECHHHHHHHHHHH		10.8032015554
276AcetylationFWAYEQYKKLLTEEG
HHHHHHHHHHHCHHH		36.3227452117
2852-HydroxyisobutyrylationLLTEEGQKIGTFERF
HHCHHHCCEECHHHH		54.69-
285UbiquitinationLLTEEGQKIGTFERF
HHCHHHCCEECHHHH		54.6932015554
288PhosphorylationEEGQKIGTFERFISG
HHHCCEECHHHHHCC		26.2922210691
294PhosphorylationGTFERFISGSMAGAT
ECHHHHHCCCCCCCC		23.3122210691
317UbiquitinationEVMKTRLAVGKTGQY
HHHHHEEECCCCCCC		12.5329967540
317AcetylationEVMKTRLAVGKTGQY
HHHHHEEECCCCCCC		12.5319608861
320SuccinylationKTRLAVGKTGQYSGI
HHEEECCCCCCCCCH		42.7727452117
320AcetylationKTRLAVGKTGQYSGI
HHEEECCCCCCCCCH		42.7725825284
320SuccinylationKTRLAVGKTGQYSGI
HHEEECCCCCCCCCH		42.77-
3202-HydroxyisobutyrylationKTRLAVGKTGQYSGI
HHEEECCCCCCCCCH		42.77-
320MalonylationKTRLAVGKTGQYSGI
HHEEECCCCCCCCCH		42.7726320211
324PhosphorylationAVGKTGQYSGIYDCA
ECCCCCCCCCHHHHH		15.3722817900
328PhosphorylationTGQYSGIYDCAKKIL
CCCCCCHHHHHHHHH		14.4325839225
332AcetylationSGIYDCAKKILKHEG
CCHHHHHHHHHHHCC		46.8326051181
332SuccinylationSGIYDCAKKILKHEG
CCHHHHHHHHHHHCC		46.8323954790
332MalonylationSGIYDCAKKILKHEG
CCHHHHHHHHHHHCC		46.8326320211
3362-HydroxyisobutyrylationDCAKKILKHEGLGAF
HHHHHHHHHCCCCHH		42.98-
336MalonylationDCAKKILKHEGLGAF
HHHHHHHHHCCCCHH		42.9826320211
336AcetylationDCAKKILKHEGLGAF
HHHHHHHHHCCCCHH		42.9819608861
336UbiquitinationDCAKKILKHEGLGAF
HHHHHHHHHCCCCHH		42.9829967540
336SuccinylationDCAKKILKHEGLGAF
HHHHHHHHHCCCCHH		42.9827452117
357PhosphorylationNLLGIIPYAGIDLAV
CHHCCCCCCCHHHHH		13.67-
370PhosphorylationAVYELLKSYWLDNFA
HHHHHHHHHHHHHCH		22.85-
371PhosphorylationVYELLKSYWLDNFAK
HHHHHHHHHHHHCHH		14.3821712546
380PhosphorylationLDNFAKDSVNPGVMV
HHHCHHCCCCCCCEE		24.0820068231
395PhosphorylationLLGCGALSSTCGQLA
EECCCHHHCHHHHHH		24.0620068231
396PhosphorylationLGCGALSSTCGQLAS
ECCCHHHCHHHHHHC		28.6820068231
397PhosphorylationGCGALSSTCGQLASY
CCCHHHCHHHHHHCH		19.7820068231
403PhosphorylationSTCGQLASYPLALVR
CHHHHHHCHHHHHHH		35.5620068231
404PhosphorylationTCGQLASYPLALVRT
HHHHHHCHHHHHHHH		9.1720068231
418AcetylationTRMQAQAMLEGSPQL
HHHHHHHHHCCCCCC		2.0219608861
422PhosphorylationAQAMLEGSPQLNMVG
HHHHHCCCCCCCHHH		10.49-
437MalonylationLFRRIISKEGIPGLY
HHHHHHHHCCCCCHH		49.9426320211
437SuccinylationLFRRIISKEGIPGLY
HHHHHHHHCCCCCHH		49.94-
437SuccinylationLFRRIISKEGIPGLY
HHHHHHHHCCCCCHH		49.9427452117
437AcetylationLFRRIISKEGIPGLY
HHHHHHHHCCCCCHH		49.9419608861
448PhosphorylationPGLYRGITPNFMKVL
CCHHCCCCCCHHHHH		18.27-
461PhosphorylationVLPAVGISYVVYENM
HHHHCCCEEEEEECH		13.12-
462PhosphorylationLPAVGISYVVYENMK
HHHCCCEEEEEECHH		7.63-
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 SCMC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCMC1_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 SCMC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SCMC1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCMC1_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-336 AND LYS-437, AND MASSSPECTROMETRY.

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