GCDH_HUMAN - dbPTM
GCDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCDH_HUMAN
UniProt AC Q92947
Protein Name Glutaryl-CoA dehydrogenase, mitochondrial
Gene Name GCDH
Organism Homo sapiens (Human).
Sequence Length 438
Subcellular Localization Mitochondrion matrix.
Protein Description Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive..
Protein Sequence MALRGVSVRLLSRGPGLHVLRTWVSSAAQTEKGGRTQSQLAKSSRPEFDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTASK
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
32UbiquitinationSSAAQTEKGGRTQSQ
HHHHCCCCCCCCHHH
70.79-
38PhosphorylationEKGGRTQSQLAKSSR
CCCCCCHHHHHHHCC
26.9225332170
88MethylationPRILLANRNEVFHRE
HHHHHHCCCHHHHHH
34.77-
137PhosphorylationLERVDSGYRSAMSVQ
HHHHCCCCCCCHHHH
12.8327196784
142PhosphorylationSGYRSAMSVQSSLVM
CCCCCCHHHHHHHHH
19.4024275569
155PhosphorylationVMHPIYAYGSEEQRQ
HHCCHHHCCCHHHHH
12.2924275569
157PhosphorylationHPIYAYGSEEQRQKY
CCHHHCCCHHHHHHH
25.8624275569
163UbiquitinationGSEEQRQKYLPQLAK
CCHHHHHHHHHHHHH
51.44-
202UbiquitinationAHYNSSNKSYTLNGT
EEECCCCCEEEECCE
46.95-
240AcetylationIRGFLLEKGMRGLSA
HHHHHHHCCCCCCCC
58.96-
240UbiquitinationIRGFLLEKGMRGLSA
HHHHHHHCCCCCCCC
58.96-
240MalonylationIRGFLLEKGMRGLSA
HHHHHHHCCCCCCCC
58.9626320211
2402-HydroxyisobutyrylationIRGFLLEKGMRGLSA
HHHHHHHCCCCCCCC
58.96-
246PhosphorylationEKGMRGLSAPRIQGK
HCCCCCCCCCCCCCC
38.7720068231
255PhosphorylationPRIQGKFSLRASATG
CCCCCCEEECCCCCE
22.0425394399
319MethylationARQYALDRMQFGVPL
HHHHHHHHHHHCCCH
22.96-
361UbiquitinationGRLKDQDKAAPEMVS
CCCCCCCCCHHHHHH
40.59-
368PhosphorylationKAAPEMVSLLKRNNC
CCHHHHHHHHHHCCC
27.0324719451
371UbiquitinationPEMVSLLKRNNCGKA
HHHHHHHHHCCCHHH
59.37-
377UbiquitinationLKRNNCGKALDIARQ
HHHCCCHHHHHHHHH
48.23-
398PhosphorylationGNGISDEYHVIRHAM
CCCCCCHHHHHHHCC
13.33-
429PhosphorylationLILGRAITGIQAFTA
HHHHHHHHHHHHHHC
27.5220068231
435PhosphorylationITGIQAFTASK----
HHHHHHHHCCC----
32.7928857561
437PhosphorylationGIQAFTASK------
HHHHHHCCC------
35.5228857561
438AcetylationIQAFTASK-------
HHHHHCCC-------
62.992380819

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 GCDH_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCDH_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 GCDH_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOS3_HUMANNOS3physical
21163940
ISCA1_HUMANISCA1physical
26186194
SYMM_HUMANMARS2physical
26186194
ISCA1_HUMANISCA1physical
28514442
SYMM_HUMANMARS2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
231670Glutaric aciduria 1 (GA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB03147Flavin adenine dinucleotide
Regulatory Network of GCDH_HUMAN

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Related Literatures of Post-Translational Modification

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