HCDH_HUMAN - dbPTM
HCDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HCDH_HUMAN
UniProt AC Q16836
Protein Name Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Gene Name HADH
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Mitochondrion matrix.
Protein Description Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA..
Protein Sequence MAFVTRQFMRSVSSSSTASASAKKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENLKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK
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
11PhosphorylationVTRQFMRSVSSSSTA
HHHHHHHHHCCCCCC		17.9830576142
13PhosphorylationRQFMRSVSSSSTASA
HHHHHHHCCCCCCCH		26.2520068231
14PhosphorylationQFMRSVSSSSTASAS
HHHHHHCCCCCCCHH		26.5920860994
15PhosphorylationFMRSVSSSSTASASA
HHHHHCCCCCCCHHH		24.9730576142
16PhosphorylationMRSVSSSSTASASAK
HHHHCCCCCCCHHHC		29.9130576142
17PhosphorylationRSVSSSSTASASAKK
HHHCCCCCCCHHHCE		26.9520068231
19PhosphorylationVSSSSTASASAKKII
HCCCCCCCHHHCEEE		23.8920068231
21PhosphorylationSSSTASASAKKIIVK
CCCCCCHHHCEEEEE		37.8220860994
23AcetylationSTASASAKKIIVKHV
CCCCHHHCEEEEEEE		41.8525953088
68UbiquitinationDILAKSKKGIEESLR
HHHHHCCCCHHHHHH		72.68-
68MalonylationDILAKSKKGIEESLR
HHHHHCCCCHHHHHH		72.6826320211
68SuccinylationDILAKSKKGIEESLR
HHHHHCCCCHHHHHH		72.6827452117
73PhosphorylationSKKGIEESLRKVAKK
CCCCHHHHHHHHHHH		22.2320068231
75MethylationKGIEESLRKVAKKKF
CCHHHHHHHHHHHHH		40.45-
76AcetylationGIEESLRKVAKKKFA
CHHHHHHHHHHHHHH		52.4118525509
80AcetylationSLRKVAKKKFAENLK
HHHHHHHHHHHHHHH		43.302403857
80SuccinylationSLRKVAKKKFAENLK
HHHHHHHHHHHHHHH		43.30-
80SuccinylationSLRKVAKKKFAENLK
HHHHHHHHHHHHHHH		43.30-
81AcetylationLRKVAKKKFAENLKA
HHHHHHHHHHHHHHC		49.452403859
81SuccinylationLRKVAKKKFAENLKA
HHHHHHHHHHHHHHC		49.45-
81SuccinylationLRKVAKKKFAENLKA
HHHHHHHHHHHHHHC		49.45-
87AcetylationKKFAENLKAGDEFVE
HHHHHHHHCCHHHHH		63.00155995
87SuccinylationKKFAENLKAGDEFVE
HHHHHHHHCCHHHHH		63.00-
87UbiquitinationKKFAENLKAGDEFVE
HHHHHHHHCCHHHHH		63.00-
87SuccinylationKKFAENLKAGDEFVE
HHHHHHHHCCHHHHH		63.0021906983
87 (in isoform 1)Ubiquitination-63.0021890473
104PhosphorylationLSTIATSTDAASVVH
HHHHHCCCCHHHHHH		25.8822468782
112PhosphorylationDAASVVHSTDLVVEA
CHHHHHHCHHHHHHH		16.4128857561
113PhosphorylationAASVVHSTDLVVEAI
HHHHHHCHHHHHHHH		20.6228857561
125AcetylationEAIVENLKVKNELFK
HHHHHHHHHHHHHHH		63.85-
127UbiquitinationIVENLKVKNELFKRL
HHHHHHHHHHHHHHH		43.02-
127 (in isoform 2)Malonylation-43.0226320211
127AcetylationIVENLKVKNELFKRL
HHHHHHHHHHHHHHH		43.0226822725
132AcetylationKVKNELFKRLDKFAA
HHHHHHHHHHHHHHH		65.7525953088
132SuccinylationKVKNELFKRLDKFAA
HHHHHHHHHHHHHHH		65.7523954790
136AcetylationELFKRLDKFAAEHTI
HHHHHHHHHHHHCEE		41.3025038526
136SuccinylationELFKRLDKFAAEHTI
HHHHHHHHHHHHCEE		41.30-
136SuccinylationELFKRLDKFAAEHTI
HHHHHHHHHHHHCEE		41.30-
146 (in isoform 2)Ubiquitination-29.8621890473
154 (in isoform 2)Ubiquitination-10.91-
179AcetylationFNPVPVMKLVEVIKT
CCCCEEHHHHHHHCC		50.0023954790
179SuccinylationFNPVPVMKLVEVIKT
CCCCEEHHHHHHHCC		50.0027452117
185AcetylationMKLVEVIKTPMTSQK
HHHHHHHCCCCCCCH		52.3219608861
185SuccinylationMKLVEVIKTPMTSQK
HHHHHHHCCCCCCCH		52.32-
185UbiquitinationMKLVEVIKTPMTSQK
HHHHHHHCCCCCCCH		52.32-
185SuccinylationMKLVEVIKTPMTSQK
HHHHHHHCCCCCCCH		52.32-
185MalonylationMKLVEVIKTPMTSQK
HHHHHHHCCCCCCCH		52.3226320211
192AcetylationKTPMTSQKTFESLVD
CCCCCCCHHHHHHHH		55.7525953088
192SuccinylationKTPMTSQKTFESLVD
CCCCCCCHHHHHHHH		55.75-
192UbiquitinationKTPMTSQKTFESLVD
CCCCCCCHHHHHHHH		55.75-
192SuccinylationKTPMTSQKTFESLVD
CCCCCCCHHHHHHHH		55.7523954790
193PhosphorylationTPMTSQKTFESLVDF
CCCCCCHHHHHHHHH		25.6230622161
195 (in isoform 2)Ubiquitination-48.68-
196PhosphorylationTSQKTFESLVDFSKA
CCCHHHHHHHHHHHH		29.5121712546
201PhosphorylationFESLVDFSKALGKHP
HHHHHHHHHHHCCCC		16.7421712546
202AcetylationESLVDFSKALGKHPV
HHHHHHHHHHCCCCC		47.8519608861
202SuccinylationESLVDFSKALGKHPV
HHHHHHHHHHCCCCC		47.85-
202UbiquitinationESLVDFSKALGKHPV
HHHHHHHHHHCCCCC		47.85-
202SuccinylationESLVDFSKALGKHPV
HHHHHHHHHHCCCCC		47.8527452117
202 (in isoform 1)Ubiquitination-47.8521890473
202UbiquitinationESLVDFSKALGKHPV
HHHHHHHHHHCCCCC		47.8521890473
206SuccinylationDFSKALGKHPVSCKD
HHHHHHCCCCCCCCC		45.65-
206UbiquitinationDFSKALGKHPVSCKD
HHHHHHCCCCCCCCC		45.65-
206SuccinylationDFSKALGKHPVSCKD
HHHHHHCCCCCCCCC		45.65-
212AcetylationGKHPVSCKDTPGFIV
CCCCCCCCCCCCCHH		58.0723749302
212SuccinylationGKHPVSCKDTPGFIV
CCCCCCCCCCCCCHH		58.07-
212UbiquitinationGKHPVSCKDTPGFIV
CCCCCCCCCCCCCHH		58.07-
212SuccinylationGKHPVSCKDTPGFIV
CCCCCCCCCCCCCHH		58.0723954790
214PhosphorylationHPVSCKDTPGFIVNR
CCCCCCCCCCCHHHH		15.71-
226PhosphorylationVNRLLVPYLMEAIRL
HHHHHHHHHHHHHHH		15.9420068231
234PhosphorylationLMEAIRLYERGDASK
HHHHHHHHHCCCCCH		8.17-
241AcetylationYERGDASKEDIDTAM
HHCCCCCHHHHHHHH		62.2119608861
241SuccinylationYERGDASKEDIDTAM
HHCCCCCHHHHHHHH		62.21-
241UbiquitinationYERGDASKEDIDTAM
HHCCCCCHHHHHHHH		62.21-
241SuccinylationYERGDASKEDIDTAM
HHCCCCCHHHHHHHH		62.2123954790
244 (in isoform 2)Malonylation-5.4926320211
246PhosphorylationASKEDIDTAMKLGAG
CCHHHHHHHHHHCCC		29.0529116813
249AcetylationEDIDTAMKLGAGYPM
HHHHHHHHHCCCCCC		41.1125038526
251 (in isoform 2)Malonylation-16.0730639696
254PhosphorylationAMKLGAGYPMGPFEL
HHHHCCCCCCCHHHH		6.9029116813
258AcetylationGAGYPMGPFELLDYV
CCCCCCCHHHHHHHC		17.1819608861
261 (in isoform 2)Ubiquitination-4.5121890473
264PhosphorylationGPFELLDYVGLDTTK
CHHHHHHHCCCCCCE		9.0829116813
265 (in isoform 2)Ubiquitination-6.48-
269PhosphorylationLDYVGLDTTKFIVDG
HHHCCCCCCEEEECC		36.6120068231
270PhosphorylationDYVGLDTTKFIVDGW
HHCCCCCCEEEECCH		24.5120068231
271 (in isoform 2)Ubiquitination-34.88-
290PhosphorylationENPLHQPSPSLNKLV
CCCCCCCCCCHHHHH		22.1325159151
295AcetylationQPSPSLNKLVAENKF
CCCCCHHHHHHCCCC		50.0225953088
301UbiquitinationNKLVAENKFGKKTGE
HHHHHCCCCCCCCCC		47.18-
301AcetylationNKLVAENKFGKKTGE
HHHHHCCCCCCCCCC		47.1825953088
301MalonylationNKLVAENKFGKKTGE
HHHHHCCCCCCCCCC		47.1826320211
304AcetylationVAENKFGKKTGEGFY
HHCCCCCCCCCCCCC		50.7424885329
311PhosphorylationKKTGEGFYKYK----
CCCCCCCCCCC----		25.0229496907
312MethylationKTGEGFYKYK-----
CCCCCCCCCC-----		44.28-
312AcetylationKTGEGFYKYK-----
CCCCCCCCCC-----		44.2819608861
312SuccinylationKTGEGFYKYK-----
CCCCCCCCCC-----		44.28-
312UbiquitinationKTGEGFYKYK-----
CCCCCCCCCC-----		44.28-
312SuccinylationKTGEGFYKYK-----
CCCCCCCCCC-----		44.2823954790
313PhosphorylationTGEGFYKYK------
CCCCCCCCC------		15.5629496907
317 (in isoform 2)Ubiquitination--
329Acetylation----------------------
----------------------		19608861
377 (in isoform 2)Malonylation-26320211
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 HCDH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
81KSuccinylation

-
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 HCDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
STAT1_HUMANSTAT1physical
21988832
CLIC3_HUMANCLIC3physical
26344197
CLIC4_HUMANCLIC4physical
26344197
ETFA_HUMANETFAphysical
26344197
ETFB_HUMANETFBphysical
26344197
FKBP2_HUMANFKBP2physical
26344197
MMAB_HUMANMMABphysical
26344197
PIPNA_HUMANPITPNAphysical
26344197
PSA1_HUMANPSMA1physical
26344197
PSA2_HUMANPSMA2physical
26344197
PSB8_HUMANPSMB8physical
26344197
RSU1_HUMANRSU1physical
26344197
SF01_HUMANSF1physical
26344197
UBE2N_HUMANUBE2Nphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
2315303-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency)
609975Familial hyperinsulinemic hypoglycemia 4 (HHF4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HCDH_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-179; LYS-185; LYS-202;LYS-241 AND LYS-312, AND MASS SPECTROMETRY.

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