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Q99JY0

- ECHB_MOUSE

UniProt

Q99JY0 - ECHB_MOUSE

Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene

Hadhb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei139 – 1391Acyl-thioester intermediateBy similarity
    Active sitei429 – 4291Proton acceptorPROSITE-ProRule annotation
    Active sitei459 – 4591Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA C-acyltransferase activity Source: MGI
    2. enoyl-CoA hydratase activity Source: Ensembl
    3. fatty-acyl-CoA binding Source: Ensembl
    4. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: MGI
    5. long-chain-enoyl-CoA hydratase activity Source: Ensembl
    6. NAD binding Source: Ensembl

    GO - Biological processi

    1. fatty acid beta-oxidation Source: MGI

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199034. Acyl chain remodeling of CL.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trifunctional enzyme subunit beta, mitochondrial
    Alternative name(s):
    TP-beta
    Including the following 1 domains:
    3-ketoacyl-CoA thiolase (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
    Gene namesi
    Name:Hadhb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2136381. Hadhb.

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. mitochondrial fatty acid beta-oxidation multienzyme complex Source: MGI
    3. mitochondrial inner membrane Source: MGI
    4. mitochondrial nucleoid Source: Ensembl
    5. mitochondrial outer membrane Source: UniProtKB
    6. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434MitochondrionBy similarityAdd
    BLAST
    Chaini35 – 475441Trifunctional enzyme subunit beta, mitochondrialPRO_0000034082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-succinyllysine1 Publication
    Modified residuei73 – 731N6-acetyllysine; alternate1 Publication
    Modified residuei73 – 731N6-succinyllysine; alternate1 Publication
    Modified residuei189 – 1891N6-acetyllysine; alternate1 Publication
    Modified residuei189 – 1891N6-succinyllysine; alternate1 Publication
    Modified residuei191 – 1911N6-succinyllysine1 Publication
    Modified residuei273 – 2731N6-succinyllysine1 Publication
    Modified residuei292 – 2921N6-succinyllysine1 Publication
    Modified residuei294 – 2941N6-acetyllysine; alternate1 Publication
    Modified residuei294 – 2941N6-succinyllysine; alternate1 Publication
    Modified residuei299 – 2991N6-acetyllysine1 Publication
    Modified residuei333 – 3331N6-acetyllysine; alternate1 Publication
    Modified residuei333 – 3331N6-succinyllysine; alternate1 Publication
    Modified residuei349 – 3491N6-acetyllysine1 Publication
    Modified residuei362 – 3621N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99JY0.
    PaxDbiQ99JY0.
    PRIDEiQ99JY0.

    PTM databases

    PhosphoSiteiQ99JY0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99JY0.
    BgeeiQ99JY0.
    GenevestigatoriQ99JY0.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi231080. 1 interaction.
    IntActiQ99JY0. 6 interactions.
    MINTiMINT-1839643.
    STRINGi10090.ENSMUSP00000110434.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99JY0.
    SMRiQ99JY0. Positions 57-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012240.
    HOVERGENiHBG104782.
    InParanoidiQ99JY0.
    KOiK07509.
    OMAiKMFASDK.
    OrthoDBiEOG7DRJ2Z.
    PhylomeDBiQ99JY0.
    TreeFamiTF315243.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. 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]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99JY0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTILTSTFR NLSTTSKWAL RSSIRPLSCS SQLHSAPAVQ TKSKKTLAKP    50
    NMKNIVVVEG VRIPFLLSGT SYKDLMPHDL ARAALSGLLH RTNIPKDVVD 100
    YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV 150
    GLIASGQCDV VVAGGVELMS DVPIRHSRNM RKMMLDLNKA KTLGQRLSLL 200
    SKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM EQDEYALRSH 250
    SLAKKAQDEG HLSDIVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP 300
    YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD 350
    QLLLGPTYAT PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA 400
    QNYMGRKTKV GSPPLEKFNI WGGSLSLGHP FGATGCRLVM AAANRLRKDG 450
    GQYALVAACA AGGQGHAMIV EAYPK 475
    Length:475
    Mass (Da):51,386
    Last modified:June 1, 2001 - v1
    Checksum:iF131B497C4F5FAF4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 252IR → HK in BAC36493. (PubMed:16141072)Curated
    Sequence conflicti425 – 4251L → M in BAC38790. (PubMed:16141072)Curated
    Sequence conflicti450 – 4501G → R in BAC38790. (PubMed:16141072)Curated
    Sequence conflicti450 – 4501G → V in BAC39015. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS39045.1.
    RefSeqiNP_001276727.1. NM_001289798.1.
    NP_001276728.1. NM_001289799.1.
    NP_663533.1. NM_145558.2.
    UniGeneiMm.291463.
    Mm.389348.

    Genome annotation databases

    EnsembliENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447.
    ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447.
    ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447.
    GeneIDi231086.
    KEGGimmu:231086.
    UCSCiuc008wve.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS39045.1.
    RefSeqi NP_001276727.1. NM_001289798.1.
    NP_001276728.1. NM_001289799.1.
    NP_663533.1. NM_145558.2.
    UniGenei Mm.291463.
    Mm.389348.

    3D structure databases

    ProteinModelPortali Q99JY0.
    SMRi Q99JY0. Positions 57-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 231080. 1 interaction.
    IntActi Q99JY0. 6 interactions.
    MINTi MINT-1839643.
    STRINGi 10090.ENSMUSP00000110434.

    PTM databases

    PhosphoSitei Q99JY0.

    Proteomic databases

    MaxQBi Q99JY0.
    PaxDbi Q99JY0.
    PRIDEi Q99JY0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026841 ; ENSMUSP00000026841 ; ENSMUSG00000059447 .
    ENSMUST00000114783 ; ENSMUSP00000110431 ; ENSMUSG00000059447 .
    ENSMUST00000114786 ; ENSMUSP00000110434 ; ENSMUSG00000059447 .
    GeneIDi 231086.
    KEGGi mmu:231086.
    UCSCi uc008wve.1. mouse.

    Organism-specific databases

    CTDi 3032.
    MGIi MGI:2136381. Hadhb.

    Phylogenomic databases

    eggNOGi COG0183.
    GeneTreei ENSGT00390000009412.
    HOGENOMi HOG000012240.
    HOVERGENi HBG104782.
    InParanoidi Q99JY0.
    KOi K07509.
    OMAi KMFASDK.
    OrthoDBi EOG7DRJ2Z.
    PhylomeDBi Q99JY0.
    TreeFami TF315243.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    Reactomei REACT_199034. Acyl chain remodeling of CL.

    Miscellaneous databases

    ChiTaRSi HADHB. mouse.
    NextBioi 380391.
    PROi Q99JY0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99JY0.
    Bgeei Q99JY0.
    Genevestigatori Q99JY0.

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. 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 ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      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.

    Entry informationi

    Entry nameiECHB_MOUSE
    AccessioniPrimary (citable) accession number: Q99JY0
    Secondary accession number(s): Q3TEH9
    , Q8BJI5, Q8BJM0, Q8BK52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 110 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, 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

    External Data

    Dasty 3