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Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

HIBCH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate.1 Publication

Pathwayi: L-valine degradation

This protein is involved in the pathway L-valine degradation, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-valine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei121Substrate1
Binding sitei146Substrate; via amide nitrogen1
Binding sitei169Substrate1
Binding sitei177Substrate1

GO - Molecular functioni

  • 3-hydroxyisobutyryl-CoA hydrolase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Branched-chain amino acid catabolism

Enzyme and pathway databases

BioCyciZFISH:HS03883-MONOMER.
BRENDAi3.1.2.4. 2681.
ReactomeiR-HSA-70895. Branched-chain amino acid catabolism.
SABIO-RKQ6NVY1.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC:3.1.2.4)
Alternative name(s):
3-hydroxyisobutyryl-coenzyme A hydrolase
Short name:
HIB-CoA hydrolase
Short name:
HIBYL-CoA-H
Gene namesi
Name:HIBCH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4908. HIBCH.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

3-hydroxyisobutryl-CoA hydrolase deficiency (HIBCHD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive inborn error of valine metabolism. It causes severely delayed psychomotor development, neurodegeneration, increased lactic acid, and brain lesions in the basal ganglia.
See also OMIM:250620
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031870122Y → C in HIBCHD. 1 PublicationCorresponds to variant rs121918329dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi26275.
MalaCardsiHIBCH.
MIMi250620. phenotype.
OpenTargetsiENSG00000198130.
Orphaneti88639. Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
PharmGKBiPA29281.

Polymorphism and mutation databases

BioMutaiHIBCH.
DMDMi146324905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32MitochondrionBy similarityAdd BLAST32
ChainiPRO_000028492933 – 3863-hydroxyisobutyryl-CoA hydrolase, mitochondrialAdd BLAST354

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55N6-acetyllysine; alternateBy similarity1
Modified residuei55N6-succinyllysine; alternateBy similarity1
Modified residuei92N6-acetyllysine; alternateCombined sources1
Modified residuei92N6-succinyllysine; alternateBy similarity1
Modified residuei221N6-acetyllysine; alternateBy similarity1
Modified residuei221N6-succinyllysine; alternateBy similarity1
Modified residuei234PhosphoserineCombined sources1
Modified residuei257N6-succinyllysineBy similarity1
Modified residuei297N6-acetyllysine; alternateBy similarity1
Modified residuei297N6-succinyllysine; alternateBy similarity1
Modified residuei301N6-succinyllysineBy similarity1
Modified residuei353N6-acetyllysine; alternateBy similarity1
Modified residuei353N6-succinyllysine; alternateBy similarity1
Modified residuei356PhosphoserineCombined sources1
Modified residuei360N6-acetyllysineBy similarity1
Modified residuei365N6-acetyllysineBy similarity1
Modified residuei377N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6NVY1.
MaxQBiQ6NVY1.
PaxDbiQ6NVY1.
PeptideAtlasiQ6NVY1.
PRIDEiQ6NVY1.

2D gel databases

REPRODUCTION-2DPAGEIPI00419802.

PTM databases

iPTMnetiQ6NVY1.
PhosphoSitePlusiQ6NVY1.

Expressioni

Tissue specificityi

Highly expressed in liver and kidney, also detected in heart, muscle and brain (at protein level). Not detected in lung.1 Publication

Gene expression databases

BgeeiENSG00000198130.
CleanExiHS_HIBCH.
ExpressionAtlasiQ6NVY1. baseline and differential.
GenevisibleiQ6NVY1. HS.

Organism-specific databases

HPAiHPA036540.
HPA036541.

Interactioni

Protein-protein interaction databases

BioGridi117658. 35 interactors.
IntActiQ6NVY1. 2 interactors.
STRINGi9606.ENSP00000352706.

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 43Combined sources7
Beta strandi46 – 51Combined sources6
Helixi54 – 56Combined sources3
Helixi62 – 77Combined sources16
Beta strandi83 – 88Combined sources6
Beta strandi91 – 95Combined sources5
Helixi100 – 107Combined sources8
Helixi114 – 129Combined sources16
Beta strandi135 – 139Combined sources5
Beta strandi141 – 144Combined sources4
Helixi146 – 149Combined sources4
Turni150 – 153Combined sources4
Beta strandi154 – 159Combined sources6
Beta strandi164 – 166Combined sources3
Helixi169 – 171Combined sources3
Helixi180 – 186Combined sources7
Helixi191 – 198Combined sources8
Helixi205 – 209Combined sources5
Beta strandi214 – 216Combined sources3
Helixi219 – 221Combined sources3
Helixi222 – 231Combined sources10
Helixi237 – 250Combined sources14
Turni253 – 256Combined sources4
Helixi262 – 264Combined sources3
Helixi265 – 271Combined sources7
Beta strandi274 – 276Combined sources3
Helixi277 – 287Combined sources11
Helixi290 – 299Combined sources10
Helixi304 – 317Combined sources14
Helixi322 – 337Combined sources16
Helixi341 – 349Combined sources9
Helixi364 – 366Combined sources3
Helixi369 – 376Combined sources8
Helixi380 – 382Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BPTX-ray1.50A32-386[»]
ProteinModelPortaliQ6NVY1.
SMRiQ6NVY1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6NVY1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1684. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00570000079226.
HOVERGENiHBG054809.
InParanoidiQ6NVY1.
KOiK05605.
OrthoDBiEOG091G07GX.
PhylomeDBiQ6NVY1.
TreeFamiTF314329.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6NVY1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQREMWRLM SRFNAFKRTN TILHHLRMSK HTDAAEEVLL EKKGCTGVIT
60 70 80 90 100
LNRPKFLNAL TLNMIRQIYP QLKKWEQDPE TFLIIIKGAG GKAFCAGGDI
110 120 130 140 150
RVISEAEKAK QKIAPVFFRE EYMLNNAVGS CQKPYVALIH GITMGGGVGL
160 170 180 190 200
SVHGQFRVAT EKCLFAMPET AIGLFPDVGG GYFLPRLQGK LGYFLALTGF
210 220 230 240 250
RLKGRDVYRA GIATHFVDSE KLAMLEEDLL ALKSPSKENI ASVLENYHTE
260 270 280 290 300
SKIDRDKSFI LEEHMDKINS CFSANTVEEI IENLQQDGSS FALEQLKVIN
310 320 330 340 350
KMSPTSLKIT LRQLMEGSSK TLQEVLTMEY RLSQACMRGH DFHEGVRAVL
360 370 380
IDKDQSPKWK PADLKEVTEE DLNNHFKSLG SSDLKF
Length:386
Mass (Da):43,482
Last modified:May 1, 2007 - v2
Checksum:i11B0632ED1DF2FFA
GO
Isoform 2 (identifier: Q6NVY1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     338-385: Missing.

Note: No experimental confirmation available.
Show »
Length:338
Mass (Da):38,012
Checksum:i747FD3FC0745E844
GO

Sequence cautioni

The sequence AAC52114 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH05190 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAY24178 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAD96699 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAD96743 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41E → G in AAH67822 (PubMed:15489334).Curated1
Sequence conflicti83L → V in AAC52114 (PubMed:8824301).Curated1
Sequence conflicti111Q → R in BAD96699 (Ref. 2) Curated1
Sequence conflicti184 – 198LPRLQ…FLALT → FATTPRKTWLLPCIN in AAC52114 (PubMed:8824301).CuratedAdd BLAST15
Sequence conflicti369E → K in BAD96699 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03186946T → A.3 PublicationsCorresponds to variant rs1058180dbSNPEnsembl.1
Natural variantiVAR_031870122Y → C in HIBCHD. 1 PublicationCorresponds to variant rs121918329dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_024780338 – 385Missing in isoform 2. CuratedAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66669 mRNA. Translation: AAC52114.1. Different initiation.
AK222979 mRNA. Translation: BAD96699.1. Different initiation.
AK223023 mRNA. Translation: BAD96743.1. Different initiation.
AC092178 Genomic DNA. Translation: AAY24178.1. Different initiation.
AC010679 Genomic DNA. Translation: AAX93234.1.
CH471058 Genomic DNA. Translation: EAX10873.1.
CH471058 Genomic DNA. Translation: EAX10875.1.
BC005190 mRNA. Translation: AAH05190.2. Different initiation.
BC067822 mRNA. Translation: AAH67822.1.
CCDSiCCDS2304.1. [Q6NVY1-1]
CCDS46475.1. [Q6NVY1-2]
RefSeqiNP_055177.2. NM_014362.3. [Q6NVY1-1]
NP_932164.1. NM_198047.2. [Q6NVY1-2]
XP_011509255.1. XM_011510953.1. [Q6NVY1-1]
UniGeneiHs.656685.

Genome annotation databases

EnsembliENST00000359678; ENSP00000352706; ENSG00000198130. [Q6NVY1-1]
ENST00000392332; ENSP00000376144; ENSG00000198130. [Q6NVY1-2]
GeneIDi26275.
KEGGihsa:26275.
UCSCiuc002uru.3. human. [Q6NVY1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66669 mRNA. Translation: AAC52114.1. Different initiation.
AK222979 mRNA. Translation: BAD96699.1. Different initiation.
AK223023 mRNA. Translation: BAD96743.1. Different initiation.
AC092178 Genomic DNA. Translation: AAY24178.1. Different initiation.
AC010679 Genomic DNA. Translation: AAX93234.1.
CH471058 Genomic DNA. Translation: EAX10873.1.
CH471058 Genomic DNA. Translation: EAX10875.1.
BC005190 mRNA. Translation: AAH05190.2. Different initiation.
BC067822 mRNA. Translation: AAH67822.1.
CCDSiCCDS2304.1. [Q6NVY1-1]
CCDS46475.1. [Q6NVY1-2]
RefSeqiNP_055177.2. NM_014362.3. [Q6NVY1-1]
NP_932164.1. NM_198047.2. [Q6NVY1-2]
XP_011509255.1. XM_011510953.1. [Q6NVY1-1]
UniGeneiHs.656685.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BPTX-ray1.50A32-386[»]
ProteinModelPortaliQ6NVY1.
SMRiQ6NVY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117658. 35 interactors.
IntActiQ6NVY1. 2 interactors.
STRINGi9606.ENSP00000352706.

PTM databases

iPTMnetiQ6NVY1.
PhosphoSitePlusiQ6NVY1.

Polymorphism and mutation databases

BioMutaiHIBCH.
DMDMi146324905.

2D gel databases

REPRODUCTION-2DPAGEIPI00419802.

Proteomic databases

EPDiQ6NVY1.
MaxQBiQ6NVY1.
PaxDbiQ6NVY1.
PeptideAtlasiQ6NVY1.
PRIDEiQ6NVY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359678; ENSP00000352706; ENSG00000198130. [Q6NVY1-1]
ENST00000392332; ENSP00000376144; ENSG00000198130. [Q6NVY1-2]
GeneIDi26275.
KEGGihsa:26275.
UCSCiuc002uru.3. human. [Q6NVY1-1]

Organism-specific databases

CTDi26275.
DisGeNETi26275.
GeneCardsiHIBCH.
HGNCiHGNC:4908. HIBCH.
HPAiHPA036540.
HPA036541.
MalaCardsiHIBCH.
MIMi250620. phenotype.
610690. gene.
neXtProtiNX_Q6NVY1.
OpenTargetsiENSG00000198130.
Orphaneti88639. Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
PharmGKBiPA29281.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1684. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00570000079226.
HOVERGENiHBG054809.
InParanoidiQ6NVY1.
KOiK05605.
OrthoDBiEOG091G07GX.
PhylomeDBiQ6NVY1.
TreeFamiTF314329.

Enzyme and pathway databases

UniPathwayiUPA00362.
BioCyciZFISH:HS03883-MONOMER.
BRENDAi3.1.2.4. 2681.
ReactomeiR-HSA-70895. Branched-chain amino acid catabolism.
SABIO-RKQ6NVY1.

Miscellaneous databases

EvolutionaryTraceiQ6NVY1.
GenomeRNAii26275.
PROiQ6NVY1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198130.
CleanExiHS_HIBCH.
ExpressionAtlasiQ6NVY1. baseline and differential.
GenevisibleiQ6NVY1. HS.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiHIBCH_HUMAN
AccessioniPrimary (citable) accession number: Q6NVY1
Secondary accession number(s): D3DPI4
, Q53GA8, Q53GF2, Q53RF7, Q53TC6, Q92931, Q9BS94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: November 2, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.