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Q99L13 (3HIDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxyisobutyrate dehydrogenase, mitochondrial

Short name=HIBADH
EC=1.1.1.31
Gene names
Name:Hibadh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH.

Pathway

Amino-acid degradation; L-valine degradation.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the 3-hydroxyisobutyrate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 3353003-hydroxyisobutyrate dehydrogenase, mitochondrial
PRO_0000007159

Regions

Nucleotide binding39 – 6830NAD By similarity
Nucleotide binding102 – 1032NAD By similarity

Sites

Active site2081 By similarity
Binding site1071NAD By similarity
Binding site1331NAD; via amide nitrogen By similarity
Binding site2831NAD By similarity

Amino acid modifications

Modified residue591N6-acetyllysine; alternate Ref.4
Modified residue591N6-succinyllysine; alternate Ref.3
Modified residue751N6-acetyllysine; alternate Ref.4
Modified residue751N6-succinyllysine; alternate Ref.3
Modified residue781N6-acetyllysine; alternate Ref.4
Modified residue781N6-succinyllysine; alternate Ref.3
Modified residue941N6-succinyllysine Ref.3
Modified residue1201N6-acetyllysine Ref.4
Modified residue1401N6-succinyllysine Ref.3
Modified residue1441N6-acetyllysine Ref.4
Modified residue1481N6-acetyllysine; alternate Ref.4
Modified residue1481N6-succinyllysine; alternate Ref.3
Modified residue2371N6-acetyllysine; alternate Ref.4
Modified residue2371N6-succinyllysine; alternate Ref.3
Modified residue2411N6-acetyllysine; alternate Ref.4
Modified residue2411N6-succinyllysine; alternate Ref.3
Modified residue2961N6-succinyllysine Ref.3
Modified residue3201N6-acetyllysine; alternate Ref.4
Modified residue3201N6-succinyllysine; alternate Ref.3

Experimental info

Sequence conflict21A → S in BAC37162. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99L13 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5E9ECB03997DB110

FASTA33535,440
        10         20         30         40         50         60 
MAASLGFRGA ASGLWYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLMKH 

        70         80         90        100        110        120 
GYPLILYDVF PDVCKEFKEA GEQVASSPAE VAEKADRIIT MLPSSMNAVE VYSGANGILK 

       130        140        150        160        170        180 
KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVEDE 

       190        200        210        220        230        240 
FAAAQELLEC MGSNVVYCGA VGTGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA 

       250        260        270        280        290        300 
KILNMSSGRC WSSDTYNPVP GVMHGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL 

       310        320        330 
LGSLAHQIYR MMCSKGYSKK DFSSVFQYLR EEEPF 

« Hide

References

[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. expand/collapse author list , 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.
Tissue: Olfactory bulb.
[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].
[3]"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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; LYS-94; LYS-140; LYS-148; LYS-237; LYS-241; LYS-296 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"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-59; LYS-75; LYS-78; LYS-120; LYS-144; LYS-148; LYS-237; LYS-241 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC003914 mRNA. Translation: AAH03914.1.
AK078175 mRNA. Translation: BAC37162.1.
RefSeqNP_663542.1. NM_145567.1.
UniGeneMm.286458.

3D structure databases

ProteinModelPortalQ99L13.
SMRQ99L13. Positions 40-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99L13. 2 interactions.
MINTMINT-1841750.

PTM databases

PhosphoSiteQ99L13.

2D gel databases

REPRODUCTION-2DPAGEQ99L13.

Proteomic databases

PaxDbQ99L13.
PRIDEQ99L13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031788; ENSMUSP00000031788; ENSMUSG00000029776.
GeneID58875.
KEGGmmu:58875.
UCSCuc009byw.1. mouse.

Organism-specific databases

CTD11112.
MGIMGI:1889802. Hibadh.

Phylogenomic databases

eggNOGCOG2084.
GeneTreeENSGT00530000063270.
HOGENOMHOG000219610.
HOVERGENHBG050424.
InParanoidQ99L13.
KOK00020.
OMANIVHCGE.
OrthoDBEOG7NSB31.
PhylomeDBQ99L13.
TreeFamTF314043.

Enzyme and pathway databases

UniPathwayUPA00362.

Gene expression databases

BgeeQ99L13.
CleanExMM_HIBADH.
GenevestigatorQ99L13.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR006115. 6PGDH_NADP-bd.
IPR013328. DH_multihelical.
IPR015815. HIBADH-type.
IPR011548. IsoBut3OH_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR22981. PTHR22981. 1 hit.
PfamPF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000103. HIBADH. 1 hit.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR01692. HIBADH. 1 hit.
PROSITEPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHIBADH. mouse.
NextBio314442.
PROQ99L13.
SOURCESearch...

Entry information

Entry name3HIDH_MOUSE
AccessionPrimary (citable) accession number: Q99L13
Secondary accession number(s): Q8BJY2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot