MUTA_HUMAN - dbPTM
MUTA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MUTA_HUMAN
UniProt AC P22033
Protein Name Methylmalonyl-CoA mutase, mitochondrial
Gene Name MUT {ECO:0000312|HGNC:HGNC:7526}
Organism Homo sapiens (Human).
Sequence Length 750
Subcellular Localization Mitochondrion matrix.
Protein Description Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species..
Protein Sequence MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV
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
12PhosphorylationKNQLFLLSPHYLRQV
CCHHEECCHHHHHHH		16.2729083192
15PhosphorylationLFLLSPHYLRQVKES
HEECCHHHHHHHHHC		13.6329083192
68PhosphorylationWHTPEGISIKPLYSK
EECCCCCCCCCCCCC		35.1024719451
78PhosphorylationPLYSKRDTMDLPEEL
CCCCCCCCCCCCCCC		19.3320068231
79SulfoxidationLYSKRDTMDLPEELP
CCCCCCCCCCCCCCC		6.1221406390
89AcetylationPEELPGVKPFTRGPY
CCCCCCCCCCCCCCC		40.092380339
89UbiquitinationPEELPGVKPFTRGPY
CCCCCCCCCCCCCCC		40.09-
124UbiquitinationEESNKFYKDNIKAGQ
HHCCHHHHHHHCCCC		47.64-
159SulfoxidationRVRGDVGMAGVAIDT
CCCCCCEECCEEEEE		2.7021406390
166PhosphorylationMAGVAIDTVEDTKIL
ECCEEEEEECCCEEE		21.4921406692
170PhosphorylationAIDTVEDTKILFDGI
EEEEECCCEEEECCC		13.3821406692
212MalonylationEQGVPKEKLTGTIQN
CCCCCHHHHCHHHHH		58.4326320211
212AcetylationEQGVPKEKLTGTIQN
CCCCCHHHHCHHHHH		58.4325953088
212UbiquitinationEQGVPKEKLTGTIQN
CCCCCHHHHCHHHHH		58.43-
216PhosphorylationPKEKLTGTIQNDILK
CHHHHCHHHHHHHHH		17.72-
223UbiquitinationTIQNDILKEFMVRNT
HHHHHHHHHHHHCCC		49.60-
230PhosphorylationKEFMVRNTYIFPPEP
HHHHHCCCEECCCCC		13.8720068231
231PhosphorylationEFMVRNTYIFPPEPS
HHHHCCCEECCCCCC		12.2420068231
238PhosphorylationYIFPPEPSMKIIADI
EECCCCCCHHHHHHH		30.9220068231
248PhosphorylationIIADIFEYTAKHMPK
HHHHHHHHHHHHCCC		10.9720068231
249PhosphorylationIADIFEYTAKHMPKF
HHHHHHHHHHHCCCC		23.2520068231
287PhosphorylationTLADGLEYSRTGLQA
HHHHCCCCCCHHHHC		14.43-
335AcetylationLWAHLIEKMFQPKNS
HHHHHHHHHHCCCCC		37.7120167786
343UbiquitinationMFQPKNSKSLLLRAH
HHCCCCCCHHHHHHH		55.29-
343SuccinylationMFQPKNSKSLLLRAH
HHCCCCCCHHHHHHH		55.29-
343MalonylationMFQPKNSKSLLLRAH
HHCCCCCCHHHHHHH		55.2926320211
343SuccinylationMFQPKNSKSLLLRAH
HHCCCCCCHHHHHHH		55.29-
343AcetylationMFQPKNSKSLLLRAH
HHCCCCCCHHHHHHH		55.2921339330
353PhosphorylationLLRAHCQTSGWSLTE
HHHHHHHHCCCCCCC		34.3028857561
354PhosphorylationLRAHCQTSGWSLTEQ
HHHHHHHCCCCCCCC		16.6428857561
357PhosphorylationHCQTSGWSLTEQDPY
HHHHCCCCCCCCCCC		29.0128857561
359PhosphorylationQTSGWSLTEQDPYNN
HHCCCCCCCCCCCCH		26.5328857561
364PhosphorylationSLTEQDPYNNIVRTA
CCCCCCCCCHHHHHH		29.18-
389PhosphorylationTQSLHTNSFDEALGL
CCCCCCCCHHHHHCC		34.9222210691
398PhosphorylationDEALGLPTVKSARIA
HHHHCCCCHHCHHHH		45.6822210691
400UbiquitinationALGLPTVKSARIARN
HHCCCCHHCHHHHHC		40.66-
401PhosphorylationLGLPTVKSARIARNT
HCCCCHHCHHHHHCC		20.6022210691
465MalonylationAVAEGIPKLRIEECA
HHHCCCCCCCHHHHH		48.7732601280
465AcetylationAVAEGIPKLRIEECA
HHHCCCCCCCHHHHH		48.7725953088
481PhosphorylationRRQARIDSGSEVIVG
HHHHCCCCCCEEEEE		41.6827251275
483PhosphorylationQARIDSGSEVIVGVN
HHCCCCCCEEEEECC		32.4227251275
491UbiquitinationEVIVGVNKYQLEKED
EEEEECCEEECCCCC		31.78-
595SuccinylationRQEFGESKEITSAIK
HHHHHCCHHHHHHHH		49.16-
595SuccinylationRQEFGESKEITSAIK
HHHHHCCHHHHHHHH		49.16-
602AcetylationKEITSAIKRVHKFME
HHHHHHHHHHHHHHH		48.35-
621MalonylationRPRLLVAKMGQDGHD
CCEEEEEECCCCCCH		35.7626320211
621AcetylationRPRLLVAKMGQDGHD
CCEEEEEECCCCCCH		35.7625953088
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 MUTA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MUTA_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 MUTA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUTA_HUMANMUTphysical
20876572
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
251000Methylmalonic aciduria type mut (MMAM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00115Cyanocobalamin
DB00200Hydroxocobalamin
Regulatory Network of MUTA_HUMAN

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Related Literatures of Post-Translational Modification

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