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Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

Hibch

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

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

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201SubstrateBy similarity
Binding sitei145 – 1451Substrate; via amide nitrogenBy similarity
Binding sitei168 – 1681SubstrateBy similarity
Binding sitei176 – 1761SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Branched-chain amino acid catabolism

Enzyme and pathway databases

ReactomeiR-MMU-70895. Branched-chain amino acid catabolism.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1923792. Hibch.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionBy similarityAdd
BLAST
Chaini33 – 3853533-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000284930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysine; alternateCombined sources
Modified residuei54 – 541N6-succinyllysine; alternateCombined sources
Modified residuei91 – 911N6-acetyllysine; alternateCombined sources
Modified residuei91 – 911N6-succinyllysine; alternateCombined sources
Modified residuei100 – 1001N6-acetyllysine; alternateCombined sources
Modified residuei100 – 1001N6-succinyllysine; alternateCombined sources
Modified residuei220 – 2201N6-acetyllysine; alternateCombined sources
Modified residuei220 – 2201N6-succinyllysine; alternateCombined sources
Modified residuei249 – 2491N6-succinyllysineCombined sources
Modified residuei256 – 2561N6-succinyllysineCombined sources
Modified residuei296 – 2961N6-acetyllysine; alternateCombined sources
Modified residuei296 – 2961N6-succinyllysine; alternateCombined sources
Modified residuei300 – 3001N6-succinyllysineCombined sources
Modified residuei352 – 3521N6-acetyllysine; alternateCombined sources
Modified residuei352 – 3521N6-succinyllysine; alternateCombined sources
Modified residuei359 – 3591N6-acetyllysineCombined sources
Modified residuei364 – 3641N6-acetyllysineCombined sources
Modified residuei376 – 3761N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8QZS1.
MaxQBiQ8QZS1.
PaxDbiQ8QZS1.
PRIDEiQ8QZS1.

PTM databases

iPTMnetiQ8QZS1.
PhosphoSiteiQ8QZS1.
SwissPalmiQ8QZS1.

Expressioni

Gene expression databases

BgeeiQ8QZS1.
CleanExiMM_HIBCH.
ExpressionAtlasiQ8QZS1. baseline and differential.
GenevisibleiQ8QZS1. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8QZS1. 2 interactions.
MINTiMINT-1859357.
STRINGi10090.ENSMUSP00000045606.

Structurei

3D structure databases

ProteinModelPortaliQ8QZS1.
SMRiQ8QZS1. Positions 34-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1684. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00570000079226.
HOGENOMiHOG000217005.
HOVERGENiHBG054809.
InParanoidiQ8QZS1.
KOiK05605.
OMAiCVPSSWL.
PhylomeDBiQ8QZS1.
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.

Sequencei

Sequence statusi: Complete.

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

Q8QZS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQPYAWRLL SRVSSFRRAS VILQHLRMSM HTEAAEVLLE RRGCGGVITL
60 70 80 90 100
NRPKFLNALS LNMIRQIYPQ LKTWEQDPDT FLIIIKGAGG KAFCAGGDIK
110 120 130 140 150
ALSEAKKARQ NLTQDLFREE YILNNAIASC QKPYVALIDG ITMGGGVGLS
160 170 180 190 200
VHGQFRVATE RSLFAMPETG IGLFPDVGGG YFLPRLQGKL GYFLALTGYR
210 220 230 240 250
LKGRDVHRAG IATHFVDSEK LRVLEEELLA LKSPSAEDVA GVLESYHAKS
260 270 280 290 300
KMDQDKSIIF EEHMDKINSC FSANTVEQII ENLRQDGSPF AIEQMKVINK
310 320 330 340 350
MSPTSLKITL RQLMEGSSKT LQEVLIMEYR ITQACMEGHD FHEGVRAVLI
360 370 380
DKDQTPKWKP ANLKDVTDED LNSYFKSLGS SDLKF
Length:385
Mass (Da):43,038
Last modified:June 1, 2002 - v1
Checksum:iFC2B45BF4DF4BE55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076038 mRNA. Translation: BAC36138.1.
BC026437 mRNA. Translation: AAH26437.1.
CCDSiCCDS14948.1.
RefSeqiNP_666220.1. NM_146108.2.
UniGeneiMm.222063.

Genome annotation databases

EnsembliENSMUST00000044478; ENSMUSP00000045606; ENSMUSG00000041426.
GeneIDi227095.
KEGGimmu:227095.
UCSCiuc007ayp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076038 mRNA. Translation: BAC36138.1.
BC026437 mRNA. Translation: AAH26437.1.
CCDSiCCDS14948.1.
RefSeqiNP_666220.1. NM_146108.2.
UniGeneiMm.222063.

3D structure databases

ProteinModelPortaliQ8QZS1.
SMRiQ8QZS1. Positions 34-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8QZS1. 2 interactions.
MINTiMINT-1859357.
STRINGi10090.ENSMUSP00000045606.

PTM databases

iPTMnetiQ8QZS1.
PhosphoSiteiQ8QZS1.
SwissPalmiQ8QZS1.

Proteomic databases

EPDiQ8QZS1.
MaxQBiQ8QZS1.
PaxDbiQ8QZS1.
PRIDEiQ8QZS1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044478; ENSMUSP00000045606; ENSMUSG00000041426.
GeneIDi227095.
KEGGimmu:227095.
UCSCiuc007ayp.1. mouse.

Organism-specific databases

CTDi26275.
MGIiMGI:1923792. Hibch.

Phylogenomic databases

eggNOGiKOG1684. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00570000079226.
HOGENOMiHOG000217005.
HOVERGENiHBG054809.
InParanoidiQ8QZS1.
KOiK05605.
OMAiCVPSSWL.
PhylomeDBiQ8QZS1.
TreeFamiTF314329.

Enzyme and pathway databases

UniPathwayiUPA00362.
ReactomeiR-MMU-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiHibch. mouse.
PROiQ8QZS1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8QZS1.
CleanExiMM_HIBCH.
ExpressionAtlasiQ8QZS1. baseline and differential.
GenevisibleiQ8QZS1. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 223-232, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-352, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-91; LYS-100; LYS-220; LYS-249; LYS-256; LYS-296; LYS-300; LYS-352 AND LYS-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-91; LYS-100; LYS-220; LYS-296; LYS-352; LYS-359 AND LYS-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHIBCH_MOUSE
AccessioniPrimary (citable) accession number: Q8QZS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.