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Q99JY0 (ECHB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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:
Trifunctional enzyme subunit beta, mitochondrial
Alternative name(s):
TP-beta

Including the following 1 domains:

  1. 3-ketoacyl-CoA thiolase
    EC=2.3.1.16
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
Gene names
Name:Hadhb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits By similarity. Interacts with RSAD2/viperin By similarity.

Subcellular location

Mitochondrion By similarity. Mitochondrion inner membrane By similarity. Mitochondrion outer membrane By similarity. Endoplasmic reticulum By similarity.

Post-translational modification

Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion inner membrane
Mitochondrion outer membrane
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Traceable author statement PubMed 11390422. Source: MGI

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial fatty acid beta-oxidation multienzyme complex

Inferred by curator PubMed 17116638. Source: MGI

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: Ensembl

acetyl-CoA C-acyltransferase activity

Inferred from direct assay PubMed 15240869. Source: MGI

enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: Ensembl

fatty-acyl-CoA binding

Inferred from electronic annotation. Source: Ensembl

long-chain-3-hydroxyacyl-CoA dehydrogenase activity

Inferred from mutant phenotype PubMed 17116638. Source: MGI

long-chain-enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion By similarity
Chain35 – 475441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034082

Sites

Active site1391Acyl-thioester intermediate By similarity
Active site4291Proton acceptor By similarity
Active site4591Proton acceptor By similarity

Amino acid modifications

Modified residue531N6-succinyllysine Ref.3
Modified residue731N6-acetyllysine; alternate Ref.4
Modified residue731N6-succinyllysine; alternate Ref.3
Modified residue1891N6-acetyllysine; alternate Ref.4
Modified residue1891N6-succinyllysine; alternate Ref.3
Modified residue1911N6-succinyllysine Ref.3
Modified residue2731N6-succinyllysine Ref.3
Modified residue2921N6-succinyllysine Ref.3
Modified residue2941N6-acetyllysine; alternate Ref.4
Modified residue2941N6-succinyllysine; alternate Ref.3
Modified residue2991N6-acetyllysine Ref.4
Modified residue3331N6-acetyllysine; alternate Ref.4
Modified residue3331N6-succinyllysine; alternate Ref.3
Modified residue3491N6-acetyllysine Ref.4
Modified residue3621N6-acetyllysine Ref.4

Experimental info

Sequence conflict24 – 252IR → HK in BAC36493. Ref.1
Sequence conflict4251L → M in BAC38790. Ref.1
Sequence conflict4501G → R in BAC38790. Ref.1
Sequence conflict4501G → V in BAC39015. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99JY0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F131B497C4F5FAF4

FASTA47551,386
        10         20         30         40         50         60 
MTTILTSTFR NLSTTSKWAL RSSIRPLSCS SQLHSAPAVQ TKSKKTLAKP NMKNIVVVEG 

        70         80         90        100        110        120 
VRIPFLLSGT SYKDLMPHDL ARAALSGLLH RTNIPKDVVD YIIFGTVIQE VKTSNVAREA 

       130        140        150        160        170        180 
ALGAGFSDKT PAHTVTMACI SSNQAMTTAV GLIASGQCDV VVAGGVELMS DVPIRHSRNM 

       190        200        210        220        230        240 
RKMMLDLNKA KTLGQRLSLL SKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM 

       250        260        270        280        290        300 
EQDEYALRSH SLAKKAQDEG HLSDIVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP 

       310        320        330        340        350        360 
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD QLLLGPTYAT 

       370        380        390        400        410        420 
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA QNYMGRKTKV GSPPLEKFNI 

       430        440        450        460        470 
WGGSLSLGHP FGATGCRLVM AAANRLRKDG GQYALVAACA AGGQGHAMIV EAYPK 

« 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: Bone marrow, Colon, Hippocampus, Spinal ganglion, Testis and Thymus.
[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: Mammary tumor.
[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-53; LYS-73; LYS-189; LYS-191; LYS-273; LYS-292; LYS-294 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and 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-73; LYS-189; LYS-294; LYS-299; LYS-333; LYS-349 AND LYS-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK033462 mRNA. Translation: BAC28300.1.
AK076814 mRNA. Translation: BAC36493.1.
AK083164 mRNA. Translation: BAC38790.1.
AK083767 mRNA. Translation: BAC39015.1.
AK150889 mRNA. Translation: BAE29936.1.
AK169637 mRNA. Translation: BAE41269.1.
BC005585 mRNA. Translation: AAH05585.1.
RefSeqNP_663533.1. NM_145558.2.
UniGeneMm.291463.
Mm.389348.

3D structure databases

ProteinModelPortalQ99JY0.
SMRQ99JY0. Positions 57-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231080. 1 interaction.
IntActQ99JY0. 6 interactions.
MINTMINT-1839643.
STRING10090.ENSMUSP00000110434.

PTM databases

PhosphoSiteQ99JY0.

Proteomic databases

PaxDbQ99JY0.
PRIDEQ99JY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447.
ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447.
ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447.
GeneID231086.
KEGGmmu:231086.
UCSCuc008wve.1. mouse.

Organism-specific databases

CTD3032.
MGIMGI:2136381. Hadhb.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012240.
HOVERGENHBG104782.
InParanoidQ99JY0.
KOK07509.
OMAKMFASDK.
OrthoDBEOG7DRJ2Z.
PhylomeDBQ99JY0.
TreeFamTF315243.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ99JY0.
BgeeQ99JY0.
GenevestigatorQ99JY0.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHADHB. mouse.
NextBio380391.
PROQ99JY0.
SOURCESearch...

Entry information

Entry nameECHB_MOUSE
AccessionPrimary (citable) accession number: Q99JY0
Secondary accession number(s): Q3TEH9 expand/collapse secondary AC list , Q8BJI5, Q8BJM0, Q8BK52
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 105 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