HIBCH_HUMAN - dbPTM
HIBCH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIBCH_HUMAN
UniProt AC Q6NVY1
Protein Name 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
Gene Name HIBCH
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Mitochondrion.
Protein Description Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA..
Protein Sequence MGQREMWRLMSRFNAFKRTNTILHHLRMSKHTDAAEEVLLEKKGCTGVITLNRPKFLNALTLNMIRQIYPQLKKWEQDPETFLIIIKGAGGKAFCAGGDIRVISEAEKAKQKIAPVFFREEYMLNNAVGSCQKPYVALIHGITMGGGVGLSVHGQFRVATEKCLFAMPETAIGLFPDVGGGYFLPRLQGKLGYFLALTGFRLKGRDVYRAGIATHFVDSEKLAMLEEDLLALKSPSKENIASVLENYHTESKIDRDKSFILEEHMDKINSCFSANTVEEIIENLQQDGSSFALEQLKVINKMSPTSLKITLRQLMEGSSKTLQEVLTMEYRLSQACMRGHDFHEGVRAVLIDKDQSPKWKPADLKEVTEEDLNNHFKSLGSSDLKF
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
29PhosphorylationILHHLRMSKHTDAAE
HHHHHHHHCCCCHHH		18.1722210691
32PhosphorylationHLRMSKHTDAAEEVL
HHHHHCCCCHHHHHH		30.9426270265
42UbiquitinationAEEVLLEKKGCTGVI
HHHHHHHCCCCCEEE		55.20-
55AcetylationVITLNRPKFLNALTL
EEEECCHHHHHHHHH		60.28-
55SuccinylationVITLNRPKFLNALTL
EEEECCHHHHHHHHH		60.28-
55SuccinylationVITLNRPKFLNALTL
EEEECCHHHHHHHHH		60.28-
73AcetylationRQIYPQLKKWEQDPE
HHHHHHHHHHCCCCC		51.0625953088
87AcetylationETFLIIIKGAGGKAF
CCEEEEEECCCCCEE		32.0925038526
92AcetylationIIKGAGGKAFCAGGD
EEECCCCCEEECCCC		37.0519608861
92UbiquitinationIIKGAGGKAFCAGGD
EEECCCCCEEECCCC		37.0519608861
92SuccinylationIIKGAGGKAFCAGGD
EEECCCCCEEECCCC		37.0527452117
92SuccinylationIIKGAGGKAFCAGGD
EEECCCCCEEECCCC		37.05-
92MalonylationIIKGAGGKAFCAGGD
EEECCCCCEEECCCC		37.0526320211
112 (in isoform 2)Ubiquitination-39.8821890473
112 (in isoform 1)Ubiquitination-39.8821890473
112UbiquitinationEAEKAKQKIAPVFFR
HHHHHHHHCCCHHHC		39.8821890473
198PhosphorylationLGYFLALTGFRLKGR
HHHHHHHHCCEECCH		28.7724719451
203SuccinylationALTGFRLKGRDVYRA
HHHCCEECCHHHHHC		47.8723954790
221SuccinylationTHFVDSEKLAMLEED
HHCCCHHHHHHHHHH		45.56-
221AcetylationTHFVDSEKLAMLEED
HHCCCHHHHHHHHHH		45.56-
221SuccinylationTHFVDSEKLAMLEED
HHCCCHHHHHHHHHH		45.56-
224SulfoxidationVDSEKLAMLEEDLLA
CCHHHHHHHHHHHHH		7.5821406390
233UbiquitinationEEDLLALKSPSKENI
HHHHHHCCCCCHHHH		55.50-
234PhosphorylationEDLLALKSPSKENIA
HHHHHCCCCCHHHHH		34.9428102081
236PhosphorylationLLALKSPSKENIASV
HHHCCCCCHHHHHHH		60.7428192239
237UbiquitinationLALKSPSKENIASVL
HHCCCCCHHHHHHHH		59.15-
237MalonylationLALKSPSKENIASVL
HHCCCCCHHHHHHHH		59.1526320211
237AcetylationLALKSPSKENIASVL
HHCCCCCHHHHHHHH		59.1525038526
242PhosphorylationPSKENIASVLENYHT
CCHHHHHHHHHHCCC		24.3627080861
247PhosphorylationIASVLENYHTESKID
HHHHHHHCCCCCCCC		10.76-
252UbiquitinationENYHTESKIDRDKSF
HHCCCCCCCCCCHHH		42.25-
252AcetylationENYHTESKIDRDKSF
HHCCCCCCCCCCHHH		42.2525038526
257SuccinylationESKIDRDKSFILEEH
CCCCCCCHHHHHHHH		48.43-
2572-HydroxyisobutyrylationESKIDRDKSFILEEH
CCCCCCCHHHHHHHH		48.43-
257SuccinylationESKIDRDKSFILEEH
CCCCCCCHHHHHHHH		48.43-
258PhosphorylationSKIDRDKSFILEEHM
CCCCCCHHHHHHHHH		23.0823312004
270PhosphorylationEHMDKINSCFSANTV
HHHHHHHHCCCCCCH		21.7328258704
273PhosphorylationDKINSCFSANTVEEI
HHHHHCCCCCCHHHH		25.5722673903
276PhosphorylationNSCFSANTVEEIIEN
HHCCCCCCHHHHHHH		29.0728258704
289PhosphorylationENLQQDGSSFALEQL
HHHHHCCCCHHHHHH		30.4922673903
290PhosphorylationNLQQDGSSFALEQLK
HHHHCCCCHHHHHHH		21.7722673903
297AcetylationSFALEQLKVINKMSP
CHHHHHHHHHHHCCC		40.54-
297SuccinylationSFALEQLKVINKMSP
CHHHHHHHHHHHCCC		40.54-
297SuccinylationSFALEQLKVINKMSP
CHHHHHHHHHHHCCC		40.54-
301AcetylationEQLKVINKMSPTSLK
HHHHHHHHCCCCHHH		29.6325953088
301SuccinylationEQLKVINKMSPTSLK
HHHHHHHHCCCCHHH		29.63-
301MalonylationEQLKVINKMSPTSLK
HHHHHHHHCCCCHHH		29.6326320211
301UbiquitinationEQLKVINKMSPTSLK
HHHHHHHHCCCCHHH		29.63-
301SuccinylationEQLKVINKMSPTSLK
HHHHHHHHCCCCHHH		29.63-
330PhosphorylationQEVLTMEYRLSQACM
HHHHHHHHHHHHHHH		13.16-
353SuccinylationVRAVLIDKDQSPKWK
EEEEEECCCCCCCCC		51.1527452117
353SuccinylationVRAVLIDKDQSPKWK
EEEEEECCCCCCCCC		51.15-
353MalonylationVRAVLIDKDQSPKWK
EEEEEECCCCCCCCC		51.1526320211
353AcetylationVRAVLIDKDQSPKWK
EEEEEECCCCCCCCC		51.1525825284
356PhosphorylationVLIDKDQSPKWKPAD
EEECCCCCCCCCCCC		38.2825003641
360AcetylationKDQSPKWKPADLKEV
CCCCCCCCCCCHHHC		36.1326210075
365AcetylationKWKPADLKEVTEEDL
CCCCCCHHHCCHHHH		51.1625038526
368PhosphorylationPADLKEVTEEDLNNH
CCCHHHCCHHHHHHH		34.4522468782
377MalonylationEDLNNHFKSLGSSDL
HHHHHHHHHCCCCCC		36.9026320211
377SuccinylationEDLNNHFKSLGSSDL
HHHHHHHHHCCCCCC		36.90-
377SuccinylationEDLNNHFKSLGSSDL
HHHHHHHHHCCCCCC		36.90-
377AcetylationEDLNNHFKSLGSSDL
HHHHHHHHHCCCCCC		36.9025953088
381PhosphorylationNHFKSLGSSDLKF--
HHHHHCCCCCCCC--		26.4428857561
382PhosphorylationHFKSLGSSDLKF---
HHHHCCCCCCCC---		45.2028348404
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 HIBCH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIBCH_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 HIBCH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACADV_HUMANACADVLphysical
26186194
MRRP3_HUMANKIAA0391physical
26186194
MKRN2_HUMANMKRN2physical
26186194
ACOT9_HUMANACOT9physical
26344197
MMSA_HUMANALDH6A1physical
26344197
CAB39_HUMANCAB39physical
26344197
CLIC1_HUMANCLIC1physical
26344197
CLIC4_HUMANCLIC4physical
26344197
CLIC5_HUMANCLIC5physical
26344197
HNRH1_HUMANHNRNPH1physical
26344197
HNRH2_HUMANHNRNPH2physical
26344197
LSM12_HUMANLSM12physical
26344197
NDKB_HUMANNME2physical
26344197
PCP_HUMANPRCPphysical
26344197
UFM1_HUMANUFM1physical
26344197
UMPS_HUMANUMPSphysical
26344197
ACADV_HUMANACADVLphysical
28514442
MKRN2_HUMANMKRN2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
2506203-hydroxyisobutryl-CoA hydrolase deficiency (HIBCHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HIBCH_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-92, AND MASS SPECTROMETRY.

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