MCCB_HUMAN - dbPTM
MCCB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCCB_HUMAN
UniProt AC Q9HCC0
Protein Name Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Gene Name MCCC2
Organism Homo sapiens (Human).
Sequence Length 563
Subcellular Localization Mitochondrion matrix .
Protein Description Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism..
Protein Sequence MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM
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
16PhosphorylationLRPCARASPAGPRAY
HHHHHCCCCCCCCCC		15.1024706070
47 (in isoform 2)Ubiquitination-56.34-
50UbiquitinationQENYKQMKALVNQLH
HHHHHHHHHHHHHHH		35.75-
642-HydroxyisobutyrylationHERVEHIKLGGGEKA
HHHHHHCCCCCHHHC		42.88-
64UbiquitinationHERVEHIKLGGGEKA
HHHHHHCCCCCHHHC		42.88-
702-HydroxyisobutyrylationIKLGGGEKARALHIS
CCCCCHHHCHHHEEC		46.58-
70SuccinylationIKLGGGEKARALHIS
CCCCCHHHCHHHEEC		46.58-
70SuccinylationIKLGGGEKARALHIS
CCCCCHHHCHHHEEC		46.5823954790
70UbiquitinationIKLGGGEKARALHIS
CCCCCHHHCHHHEEC		46.58-
70AcetylationIKLGGGEKARALHIS
CCCCCHHHCHHHEEC		46.58-
141SuccinylationIANDATVKGGAYYPV
EECCCEECCCCEECE		47.47-
141SuccinylationIANDATVKGGAYYPV
EECCCEECCCCEECE		47.47-
145PhosphorylationATVKGGAYYPVTVKK
CEECCCCEECEEHHH		16.1629496907
151 (in isoform 2)Ubiquitination-25.99-
1512-HydroxyisobutyrylationAYYPVTVKKQLRAQE
CEECEEHHHHHHHHH		25.99-
169PhosphorylationQNRLPCIYLVDSGGA
HHCCCEEEEECCCCC		13.8523898821
173PhosphorylationPCIYLVDSGGAYLPR
CEEEEECCCCCCCCC		31.4825690035
177PhosphorylationLVDSGGAYLPRQADV
EECCCCCCCCCCCCC		22.1025690035
188MethylationQADVFPDRDHFGRTF
CCCCCCCCCCCCHHH		39.27115482765
235MalonylationDENIIVRKQGTIFLA
CCCEEEECCCEEEEE		42.0326320211
267GlutathionylationLGGADLHCRKSGVSD
HCCCCCCCCCCCCCC		8.3422555962
269UbiquitinationGADLHCRKSGVSDHW
CCCCCCCCCCCCCCC		57.88-
298UbiquitinationVRNLNYQKKLDVTIE
HHHCCCCCCCCEEEC		44.97-
2982-HydroxyisobutyrylationVRNLNYQKKLDVTIE
HHHCCCCCCCCEEEC		44.97-
326AcetylationGIVGANLKRSFDVRE
CCCCCCCCCCCCHHH		45.8930590319
342PhosphorylationIARIVDGSRFTEFKA
HHHHHCCCCCEEEHH		21.54-
351PhosphorylationFTEFKAFYGDTLVTG
CEEEHHHHCCCEEHH		20.9628152594
382 (in isoform 2)Ubiquitination-62.1021906983
382AcetylationVLFSESAKKGTHFVQ
EECCCCCCCCCHHHH		62.1024885453
382UbiquitinationVLFSESAKKGTHFVQ
EECCCCCCCCCHHHH		62.10-
383AcetylationLFSESAKKGTHFVQL
ECCCCCCCCCHHHHH		69.6230590325
383UbiquitinationLFSESAKKGTHFVQL
ECCCCCCCCCHHHHH		69.62-
420MalonylationYEAEGIAKDGAKMVA
EECCCCCCCHHHHHH		55.5726320211
420AcetylationYEAEGIAKDGAKMVA
EECCCCCCCHHHHHH		55.5730590331
420UbiquitinationYEAEGIAKDGAKMVA
EECCCCCCCHHHHHH		55.5721906983
420 (in isoform 1)Ubiquitination-55.5721906983
424UbiquitinationGIAKDGAKMVAAVAC
CCCCCHHHHHHHHHH		39.16-
438PhosphorylationCAQVPKITLIIGGSY
HCCCCEEEEEECCCC		20.3125867546
444PhosphorylationITLIIGGSYGAGNYG
EEEEECCCCCCCCCC		18.3825867546
445PhosphorylationTLIIGGSYGAGNYGM
EEEECCCCCCCCCCC		17.8025867546
449 (in isoform 2)Ubiquitination-29.65-
450PhosphorylationGSYGAGNYGMCGRAY
CCCCCCCCCCCCCCC		12.8125867546
458PhosphorylationGMCGRAYSPRFLYIW
CCCCCCCCCCEEEEC		14.4924719451
468 (in isoform 2)Ubiquitination-13.2021906983
471PhosphorylationIWPNARISVMGGEQA
ECCCCEEEECCHHHH		10.6620068231
474 (in isoform 2)Ubiquitination-34.0421906983
484PhosphorylationQAANVLATITKDQRA
HHHHHHHEECHHHHH		25.6427362937
486PhosphorylationANVLATITKDQRARE
HHHHHEECHHHHHHC		24.9827362937
487UbiquitinationNVLATITKDQRAREG
HHHHEECHHHHHHCC		48.27-
495AcetylationDQRAREGKQFSSADE
HHHHHCCCCCCCHHH		43.34-
495SuccinylationDQRAREGKQFSSADE
HHHHHCCCCCCCHHH		43.34-
495SuccinylationDQRAREGKQFSSADE
HHHHHCCCCCCCHHH		43.34-
495UbiquitinationDQRAREGKQFSSADE
HHHHHCCCCCCCHHH		43.34-
498PhosphorylationAREGKQFSSADEAAL
HHCCCCCCCHHHHHH		23.3220873877
499PhosphorylationREGKQFSSADEAALK
HCCCCCCCHHHHHHH		40.8226657352
506UbiquitinationSADEAALKEPIIKKF
CHHHHHHHCHHHHHH		57.6321906983
506 (in isoform 1)Ubiquitination-57.6321906983
511UbiquitinationALKEPIIKKFEEEGN
HHHCHHHHHHHHCCC		52.72-
511AcetylationALKEPIIKKFEEEGN
HHHCHHHHHHHHCCC		52.72-
512 (in isoform 1)Ubiquitination-47.8221906983
512UbiquitinationLKEPIIKKFEEEGNP
HHCHHHHHHHHCCCC		47.822190698
520PhosphorylationFEEEGNPYYSSARVW
HHHCCCCCCCCCEEE		21.71-
537PhosphorylationGIIDPADTRLVLGLS
CCCCHHHCEEEEEEE		28.1924275569
562MethylationKTDFGIFRM------
HCCCCEECC------		28.16115482773
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 MCCB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCCB_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 MCCB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMGCL_HUMANHMGCLphysical
26344197
MCCA_HUMANMCCC1physical
26344197
MCCB_HUMANMCCC2physical
27499296
MPPA_HUMANPMPCAphysical
27499296
MCCA_HUMANMCCC1physical
27499296
CYB5B_HUMANCYB5Bphysical
27499296
ECH1_HUMANECH1physical
27499296
ATP5E_HUMANATP5Ephysical
27499296
C1QBP_HUMANC1QBPphysical
27499296
MPPB_HUMANPMPCBphysical
27499296
ATPG_HUMANATP5C1physical
27499296
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
2102103-methylcrotonoyl-CoA carboxylase 2 deficiency (MCC2D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00121Biotin
Regulatory Network of MCCB_HUMAN

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Related Literatures of Post-Translational Modification

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