HMGCL_HUMAN - dbPTM
HMGCL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMGCL_HUMAN
UniProt AC P35914
Protein Name Hydroxymethylglutaryl-CoA lyase, mitochondrial
Gene Name HMGCL
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization Mitochondrion matrix. Peroxisome. Unprocessed form is peroxisomal.
Protein Description Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism..
Protein Sequence MAAMRKALPRRLVGLASLRAVSTSSMGTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKL
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
17PhosphorylationRRLVGLASLRAVSTS
HHHHHHHHHHHCCCC
24.3523186163
22PhosphorylationLASLRAVSTSSMGTL
HHHHHHCCCCCCCCC
22.9126434776
23PhosphorylationASLRAVSTSSMGTLP
HHHHHCCCCCCCCCC
20.4426434776
48SuccinylationRDGLQNEKNIVSTPV
CCCCCCCCCCCCCCC
60.5723954790
48MalonylationRDGLQNEKNIVSTPV
CCCCCCCCCCCCCCC
60.5726320211
48UbiquitinationRDGLQNEKNIVSTPV
CCCCCCCCCCCCCCC
60.5719608861
48AcetylationRDGLQNEKNIVSTPV
CCCCCCCCCCCCCCC
60.5719608861
48SuccinylationRDGLQNEKNIVSTPV
CCCCCCCCCCCCCCC
60.57-
52PhosphorylationQNEKNIVSTPVKIKL
CCCCCCCCCCCHHHH
24.1730266825
53PhosphorylationNEKNIVSTPVKIKLI
CCCCCCCCCCHHHHH
22.6230266825
78PhosphorylationIETTSFVSPKWVPQM
EEECCCCCCCCCCCC
20.8224275569
80MethylationTTSFVSPKWVPQMGD
ECCCCCCCCCCCCCC
54.00-
93AcetylationGDHTEVLKGIQKFPG
CCHHHHHHHHHHCCC
60.1723954790
93MalonylationGDHTEVLKGIQKFPG
CCHHHHHHHHHHCCC
60.1726320211
93UbiquitinationGDHTEVLKGIQKFPG
CCHHHHHHHHHHCCC
60.1719608861
111MalonylationPVLTPNLKGFEAAVA
CEECCCCCHHHHHHH
69.1026320211
111AcetylationPVLTPNLKGFEAAVA
CEECCCCCHHHHHHH
69.1023236377
137MalonylationASELFTKKNINCSIE
HHHHHHCCCCCCCHH
61.0626320211
137SuccinylationASELFTKKNINCSIE
HHHHHHCCCCCCCHH
61.06-
137AcetylationASELFTKKNINCSIE
HHHHHHCCCCCCCHH
61.0623749302
137SuccinylationASELFTKKNINCSIE
HHHHHHCCCCCCCHH
61.06-
179SuccinylationLGCPYEGKISPAKVA
CCCCCCCCCCHHHHH
28.24-
179AcetylationLGCPYEGKISPAKVA
CCCCCCCCCCHHHHH
28.24-
179SuccinylationLGCPYEGKISPAKVA
CCCCCCCCCCHHHHH
28.24-
181PhosphorylationCPYEGKISPAKVAEV
CCCCCCCCHHHHHHH
23.4524719451
198PhosphorylationKFYSMGCYEISLGDT
HHHHCCCEEEECCCC
15.5722817900
314PhosphorylationCQALNRKTSSKVAQA
HHHHCCCCCHHHHHH
34.6926074081
315PhosphorylationQALNRKTSSKVAQAT
HHHCCCCCHHHHHHH
31.0626074081
316PhosphorylationALNRKTSSKVAQATC
HHCCCCCHHHHHHHH
36.0626074081
324AcetylationKVAQATCKL------
HHHHHHHCC------
53.5325953088
324MalonylationKVAQATCKL------
HHHHHHHCC------
53.5326320211

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 HMGCL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMGCL_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 HMGCL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HES1_HUMANHES1physical
21900206
DNJA1_HUMANDNAJA1physical
21900206
RN126_HUMANRNF126physical
21900206
ATS10_HUMANADAMTS10physical
21900206
AR6P1_HUMANARL6IP1physical
21900206
PNPT1_HUMANPNPT1physical
26186194
FOLC_HUMANFPGSphysical
26186194
GLSK_HUMANGLSphysical
26186194
HEM1_HUMANALAS1physical
26186194
ACADV_HUMANACADVLphysical
26186194
MGME1_HUMANMGME1physical
26186194
FBX21_HUMANFBXO21physical
26186194
LSM12_HUMANLSM12physical
26344197
TOM40_HUMANTOMM40physical
26344197
FOLC_HUMANFPGSphysical
28514442
GLSK_HUMANGLSphysical
28514442
HEM1_HUMANALAS1physical
28514442
ACADV_HUMANACADVLphysical
28514442
MGME1_HUMANMGME1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
2464503-hydroxy-3-methylglutaryl-CoA lyase deficiency (HMGCLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMGCL_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-48, AND MASS SPECTROMETRY.

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