MCCA_HUMAN - dbPTM
MCCA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCCA_HUMAN
UniProt AC Q96RQ3
Protein Name Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
Gene Name MCCC1
Organism Homo sapiens (Human).
Sequence Length 725
Subcellular Localization Mitochondrion matrix .
Protein Description Biotin-attachment 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 MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEIACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSSSGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKCSVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE
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
5Phosphorylation---MAAASAVSVLLV
---CCHHHHHHHHHH		25.2021659604
8PhosphorylationMAAASAVSVLLVAAE
CCHHHHHHHHHHHHH		13.5321659604
24PhosphorylationNRWHRLPSLLLPPRT
CCHHCCCHHCCCCCC		35.9221964256
41PhosphorylationWRQRTMKYTTATGRN
EECCCEEEECCCCCC		9.8620068231
43PhosphorylationQRTMKYTTATGRNIT
CCCEEEECCCCCCCE		21.0920068231
80PhosphorylationVQTVAVYSEADRNSM
CEEEEEEECCCCCCC		21.51-
86PhosphorylationYSEADRNSMHVDMAD
EECCCCCCCCCCCCC		15.9128348404
103PhosphorylationYSIGPAPSQQSYLSM
HCCCCCCCCHHCCCH		42.8528348404
106PhosphorylationGPAPSQQSYLSMEKI
CCCCCCHHCCCHHHH		22.0228348404
107PhosphorylationPAPSQQSYLSMEKII
CCCCCHHCCCHHHHH		9.8428348404
109PhosphorylationPSQQSYLSMEKIIQV
CCCHHCCCHHHHHHH		19.3628348404
155PhosphorylationIFIGPPPSAIRDMGI
EEECCCHHHHHHCCC		41.9422210691
165PhosphorylationRDMGIKSTSKSIMAA
HHCCCCCCCHHHHHH		34.8630576142
168PhosphorylationGIKSTSKSIMAAAGV
CCCCCCHHHHHHCCC		19.8430576142
220PhosphorylationKGMRIVRSEQEFQEQ
CCCEEECCHHHHHHH		32.5123312004
230PhosphorylationEFQEQLESARREAKK
HHHHHHHHHHHHHHH		35.35-
237AcetylationSARREAKKSFNDDAM
HHHHHHHHHCCCCHH		68.29-
237MalonylationSARREAKKSFNDDAM
HHHHHHHHHCCCCHH		68.2926320211
238PhosphorylationARREAKKSFNDDAML
HHHHHHHHCCCCHHH		28.6824719451
248AcetylationDDAMLIEKFVDTPRH
CCHHHHHHHCCCCCE		43.6320167786
295MalonylationEAPAPGIKSEVRKKL
HCCCCCCCHHHHHHH		46.6226320211
295UbiquitinationEAPAPGIKSEVRKKL
HCCCCCCCHHHHHHH		46.62-
295AcetylationEAPAPGIKSEVRKKL
HCCCCCCCHHHHHHH		46.6225953088
296PhosphorylationAPAPGIKSEVRKKLG
CCCCCCCHHHHHHHH		39.1328857561
315PhosphorylationRAAKAVNYVGAGTVE
HHHHHCCEECCCEEE		8.1522210691
327PhosphorylationTVEFIMDSKHNFCFM
EEEEEEECCCCEEEE		20.5922210691
367MalonylationLRIAAGEKIPLSQEE
HHHHCCCCCCCCHHE		49.0226320211
406PhosphorylationAGPLVHLSTPRADPS
CCCEEEECCCCCCCC		22.84-
407PhosphorylationGPLVHLSTPRADPST
CCEEEECCCCCCCCC		24.13-
418O-linked_GlycosylationDPSTRIETGVRQGDE
CCCCCEECCCCCCCE		38.3129351928
454PhosphorylationALTKLRYSLRQYNIV
HHHHHHHHHHHCCEE		15.6124719451
494AcetylationDFIPQHHKQLLLSRK
CCCCHHHHHHHHHHH		40.28-
509S-palmitoylationAAAKESLCQAALGLI
HHHHHHHHHHHHHHH		3.4429575903
518UbiquitinationAALGLILKEKAMTDT
HHHHHHHHHHHCCCE		50.61-
535PhosphorylationLQAHDQFSPFSSSSG
EEECCCCCCCCCCCC		21.28-
539PhosphorylationDQFSPFSSSSGRRLN
CCCCCCCCCCCCEEE		28.98-
540PhosphorylationQFSPFSSSSGRRLNI
CCCCCCCCCCCEEEE		35.30-
541PhosphorylationFSPFSSSSGRRLNIS
CCCCCCCCCCEEEEE		37.96-
549PhosphorylationGRRLNISYTRNMTLK
CCEEEEEEEECCEEC		13.1120393185
550PhosphorylationRRLNISYTRNMTLKD
CEEEEEEEECCEECC		14.5830631047
581SuccinylationYSMQIEDKTFQVLGN
EEEEEECCEEEEECC		38.15-
581SuccinylationYSMQIEDKTFQVLGN
EEEEEECCEEEEECC		38.15-
581AcetylationYSMQIEDKTFQVLGN
EEEEEECCEEEEECC		38.15-
622PhosphorylationENTIYLFSKEGSIEI
ECEEEEEECCCCEEE		27.4824719451
654PhosphorylationGGPLAPMTGTIEKVF
CCCCCCCCCEEEEEE		30.07-
681BiotinylationLMVMIAMKMEHTIKS
EEEEEEHHHHCEECC		31.92-
681N6-biotinyllysineLMVMIAMKMEHTIKS
EEEEEEHHHHCEECC		31.92-
709PhosphorylationGAQANRHTPLVEFEE
CCCCCCCCCCEEECH		18.3227251275
719PhosphorylationVEFEEEESDKRESE-
EEECHHHHHHHCCC-		52.2730108239
724PhosphorylationEESDKRESE------
HHHHHHCCC------		53.2728192239
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 MCCA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of MCCA_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
2102003-methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00121Biotin
Regulatory Network of MCCA_HUMAN

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Related Literatures of Post-Translational Modification

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