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P55084

- ECHB_HUMAN

UniProt

P55084 - ECHB_HUMAN

Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene

HADHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei138 – 1381Acyl-thioester intermediateBy similarity
    Active sitei428 – 4281Proton acceptorPROSITE-ProRule annotation
    Active sitei458 – 4581Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: ProtInc
    2. acetyl-CoA C-acyltransferase activity Source: ProtInc
    3. enoyl-CoA hydratase activity Source: ProtInc
    4. fatty-acyl-CoA binding Source: Ensembl
    5. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: Ensembl
    6. long-chain-enoyl-CoA hydratase activity Source: Ensembl
    7. NAD binding Source: Ensembl
    8. poly(A) RNA binding Source: UniProtKB
    9. protein binding Source: UniProtKB

    GO - Biological processi

    1. cardiolipin acyl-chain remodeling Source: Reactome
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation Source: Reactome
    4. glycerophospholipid biosynthetic process Source: Reactome
    5. phospholipid metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06436-MONOMER.
    ReactomeiREACT_121006. Acyl chain remodeling of CL.
    REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
    REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    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
    ORF Names:MSTP029
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4803. HADHB.

    Subcellular locationi

    Mitochondrion 1 Publication. Mitochondrion inner membrane 1 Publication. Mitochondrion outer membrane 1 Publication. Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial envelope Source: ProtInc
    4. mitochondrial fatty acid beta-oxidation multienzyme complex Source: Ensembl
    5. mitochondrial inner membrane Source: UniProtKB
    6. mitochondrial nucleoid Source: BHF-UCL
    7. mitochondrial outer membrane Source: UniProtKB
    8. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Trifunctional protein deficiency (TFP deficiency) [MIM:609015]: The clinical manifestations are very variable and include hypoglycemia, cardiomyopathy and sudden death. Phenotypes with mainly hepatic and neuromyopathic involvement can also be distinguished. Biochemically, TFP deficiency is defined by the loss of all three enzyme activities of the TFP complex.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591G → D in TFP deficiency. 1 Publication
    VAR_021128
    Natural varianti61 – 611R → C in TFP deficiency. 1 Publication
    VAR_021129
    Natural varianti61 – 611R → H in TFP deficiency. 2 Publications
    VAR_007493
    Natural varianti117 – 1171R → G in TFP deficiency. 1 Publication
    VAR_021130
    Natural varianti121 – 1211L → P in TFP deficiency. 1 Publication
    VAR_021131
    Natural varianti133 – 1331T → P in TFP deficiency. 1 Publication
    VAR_021132
    Natural varianti242 – 2421D → G in TFP deficiency. 1 Publication
    VAR_021133
    Natural varianti247 – 2471R → H in TFP deficiency. 2 Publications
    VAR_007494
    Natural varianti259 – 27012Missing in TFP deficiency.
    VAR_021134Add
    BLAST
    Natural varianti263 – 2631D → G in TFP deficiency. 2 Publications
    VAR_007495
    Natural varianti280 – 2801G → D in TFP deficiency. 1 Publication
    VAR_021135
    Natural varianti294 – 2941P → L in TFP deficiency. 1 Publication
    VAR_021136
    Natural varianti294 – 2941P → R in TFP deficiency. 1 Publication
    VAR_021137
    Natural varianti301 – 3011G → S in TFP deficiency. 1 Publication
    VAR_021138
    Natural varianti444 – 4441R → K in TFP deficiency. 2 Publications
    VAR_017409

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi609015. phenotype.
    Orphaneti746. Mitochondrial trifunctional protein deficiency.
    PharmGKBiPA29177.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333Mitochondrion1 PublicationAdd
    BLAST
    Chaini34 – 474441Trifunctional enzyme subunit beta, mitochondrialPRO_0000034080Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei72 – 721N6-acetyllysine; alternate1 Publication
    Modified residuei72 – 721N6-succinyllysine; alternateBy similarity
    Modified residuei188 – 1881N6-acetyllysine; alternate1 Publication
    Modified residuei188 – 1881N6-succinyllysine; alternateBy similarity
    Modified residuei190 – 1901N6-succinyllysineBy similarity
    Modified residuei272 – 2721N6-succinyllysineBy similarity
    Modified residuei291 – 2911N6-succinyllysineBy similarity
    Modified residuei293 – 2931N6-acetyllysine; alternateBy similarity
    Modified residuei293 – 2931N6-succinyllysine; alternateBy similarity
    Modified residuei298 – 2981N6-acetyllysineBy similarity
    Modified residuei332 – 3321N6-acetyllysine; alternateBy similarity
    Modified residuei332 – 3321N6-succinyllysine; alternateBy similarity
    Modified residuei348 – 3481N6-acetyllysineBy similarity
    Modified residuei361 – 3611N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP55084.
    PaxDbiP55084.
    PRIDEiP55084.

    2D gel databases

    UCD-2DPAGEP55084.

    PTM databases

    PhosphoSiteiP55084.

    Expressioni

    Gene expression databases

    ArrayExpressiP55084.
    BgeeiP55084.
    CleanExiHS_HADHB.
    GenevestigatoriP55084.

    Organism-specific databases

    HPAiHPA037539.

    Interactioni

    Subunit structurei

    Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPL1Q9H0R84EBI-356635,EBI-746969

    Protein-protein interaction databases

    BioGridi109282. 41 interactions.
    IntActiP55084. 33 interactions.
    MINTiMINT-1154861.
    STRINGi9606.ENSP00000325136.

    Structurei

    3D structure databases

    ProteinModelPortaliP55084.
    SMRiP55084. Positions 56-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    HOGENOMiHOG000012240.
    HOVERGENiHBG104782.
    InParanoidiP55084.
    KOiK07509.
    OMAiMHNISRE.
    PhylomeDBiP55084.
    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]

    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. Align

    Isoform 1 (identifier: P55084-1) [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

    MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN    50
    IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY 100
    IIFGTVIQEV KTSNVAREAA LGAGFSDKTP AHTVTMACIS ANQAMTTGVG 150
    LIASGQCDVI VAGGVELMSD VPIRHSRKMR KLMLDLNKAK SMGQRLSLIS 200
    KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE QDEYALRSHS 250
    LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY 300
    GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ 350
    LLLGPTYATP KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE 400
    NYMGRKTKVG LPPLEKFNNW GGSLSLGHPF GATGCRLVMA AANRLRKEGG 450
    QYGLVAACAA GGQGHAMIVE AYPK 474
    Length:474
    Mass (Da):51,294
    Last modified:October 17, 2006 - v3
    Checksum:iA7B41C37BEC1E6AD
    GO
    Isoform 2 (identifier: P55084-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAP → MTLVSGWLLYGWII

    Note: No experimental confirmation available.

    Show »
    Length:452
    Mass (Da):48,880
    Checksum:i3633B6AE6528FC78
    GO

    Sequence cautioni

    The sequence BAA22061.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → MT in AAG39280. 1 PublicationCurated
    Sequence conflicti1 – 11M → MT in AAH14572. (PubMed:15489334)Curated
    Sequence conflicti1 – 11M → MT in AAH17564. (PubMed:15489334)Curated
    Sequence conflicti1 – 11M → MT in AAH30824. (PubMed:15489334)Curated
    Sequence conflicti1 – 11M → MT in AAH66963. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591G → D in TFP deficiency. 1 Publication
    VAR_021128
    Natural varianti61 – 611R → C in TFP deficiency. 1 Publication
    VAR_021129
    Natural varianti61 – 611R → H in TFP deficiency. 2 Publications
    VAR_007493
    Natural varianti117 – 1171R → G in TFP deficiency. 1 Publication
    VAR_021130
    Natural varianti119 – 1191A → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035705
    Natural varianti121 – 1211L → P in TFP deficiency. 1 Publication
    VAR_021131
    Natural varianti133 – 1331T → P in TFP deficiency. 1 Publication
    VAR_021132
    Natural varianti209 – 2091P → S.1 Publication
    Corresponds to variant rs17851200 [ dbSNP | Ensembl ].
    VAR_028231
    Natural varianti242 – 2421D → G in TFP deficiency. 1 Publication
    VAR_021133
    Natural varianti247 – 2471R → H in TFP deficiency. 2 Publications
    VAR_007494
    Natural varianti259 – 27012Missing in TFP deficiency.
    VAR_021134Add
    BLAST
    Natural varianti263 – 2631D → G in TFP deficiency. 2 Publications
    VAR_007495
    Natural varianti277 – 2771K → R.
    Corresponds to variant rs57969630 [ dbSNP | Ensembl ].
    VAR_061897
    Natural varianti280 – 2801G → D in TFP deficiency. 1 Publication
    VAR_021135
    Natural varianti294 – 2941P → L in TFP deficiency. 1 Publication
    VAR_021136
    Natural varianti294 – 2941P → R in TFP deficiency. 1 Publication
    VAR_021137
    Natural varianti301 – 3011G → S in TFP deficiency. 1 Publication
    VAR_021138
    Natural varianti444 – 4441R → K in TFP deficiency. 2 Publications
    VAR_017409

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3636MTILT…LRAAP → MTLVSGWLLYGWII in isoform 2. 1 PublicationVSP_054426Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16481 mRNA. Translation: BAA03942.1.
    D86850 Genomic DNA. Translation: BAA22061.1. Sequence problems.
    AF113209 mRNA. Translation: AAG39280.1.
    AK304455 mRNA. Translation: BAG65272.1.
    AK314455 mRNA. Translation: BAG37063.1.
    AC010896 Genomic DNA. Translation: AAY14644.1.
    BC014572 mRNA. Translation: AAH14572.1.
    BC017564 mRNA. Translation: AAH17564.1.
    BC030824 mRNA. Translation: AAH30824.1.
    BC066963 mRNA. Translation: AAH66963.1.
    CCDSiCCDS1722.1. [P55084-1]
    CCDS62872.1. [P55084-2]
    PIRiJC2109.
    RefSeqiNP_000174.1. NM_000183.2. [P55084-1]
    NP_001268441.1. NM_001281512.1.
    NP_001268442.1. NM_001281513.1. [P55084-2]
    UniGeneiHs.515848.

    Genome annotation databases

    EnsembliENST00000317799; ENSP00000325136; ENSG00000138029. [P55084-1]
    ENST00000545822; ENSP00000442665; ENSG00000138029. [P55084-2]
    GeneIDi3032.
    KEGGihsa:3032.
    UCSCiuc002rgz.3. human. [P55084-1]

    Polymorphism databases

    DMDMi116241345.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16481 mRNA. Translation: BAA03942.1 .
    D86850 Genomic DNA. Translation: BAA22061.1 . Sequence problems.
    AF113209 mRNA. Translation: AAG39280.1 .
    AK304455 mRNA. Translation: BAG65272.1 .
    AK314455 mRNA. Translation: BAG37063.1 .
    AC010896 Genomic DNA. Translation: AAY14644.1 .
    BC014572 mRNA. Translation: AAH14572.1 .
    BC017564 mRNA. Translation: AAH17564.1 .
    BC030824 mRNA. Translation: AAH30824.1 .
    BC066963 mRNA. Translation: AAH66963.1 .
    CCDSi CCDS1722.1. [P55084-1 ]
    CCDS62872.1. [P55084-2 ]
    PIRi JC2109.
    RefSeqi NP_000174.1. NM_000183.2. [P55084-1 ]
    NP_001268441.1. NM_001281512.1.
    NP_001268442.1. NM_001281513.1. [P55084-2 ]
    UniGenei Hs.515848.

    3D structure databases

    ProteinModelPortali P55084.
    SMRi P55084. Positions 56-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109282. 41 interactions.
    IntActi P55084. 33 interactions.
    MINTi MINT-1154861.
    STRINGi 9606.ENSP00000325136.

    PTM databases

    PhosphoSitei P55084.

    Polymorphism databases

    DMDMi 116241345.

    2D gel databases

    UCD-2DPAGE P55084.

    Proteomic databases

    MaxQBi P55084.
    PaxDbi P55084.
    PRIDEi P55084.

    Protocols and materials databases

    DNASUi 3032.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317799 ; ENSP00000325136 ; ENSG00000138029 . [P55084-1 ]
    ENST00000545822 ; ENSP00000442665 ; ENSG00000138029 . [P55084-2 ]
    GeneIDi 3032.
    KEGGi hsa:3032.
    UCSCi uc002rgz.3. human. [P55084-1 ]

    Organism-specific databases

    CTDi 3032.
    GeneCardsi GC02P026466.
    HGNCi HGNC:4803. HADHB.
    HPAi HPA037539.
    MIMi 143450. gene.
    609015. phenotype.
    neXtProti NX_P55084.
    Orphaneti 746. Mitochondrial trifunctional protein deficiency.
    PharmGKBi PA29177.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0183.
    HOGENOMi HOG000012240.
    HOVERGENi HBG104782.
    InParanoidi P55084.
    KOi K07509.
    OMAi MHNISRE.
    PhylomeDBi P55084.
    TreeFami TF315243.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:HS06436-MONOMER.
    Reactomei REACT_121006. Acyl chain remodeling of CL.
    REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
    REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.

    Miscellaneous databases

    ChiTaRSi HADHB. human.
    GeneWikii HADHB.
    GenomeRNAii 3032.
    NextBioi 12002.
    PROi P55084.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55084.
    Bgeei P55084.
    CleanExi HS_HADHB.
    Genevestigatori P55084.

    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. "Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein."
      Kamijo T., Aoyama T., Komiyama A., Hashimoto T.
      Biochem. Biophys. Res. Commun. 199:818-825(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency."
      Orii K.E., Aoyama T., Wakui K., Fukushima Y., Miyajima H., Yamaguchi S., Orii T., Kondo N., Hashimoto T.
      Hum. Mol. Genet. 6:1215-1224(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TFP DEFICIENCY LYS-444.
      Tissue: Blood.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Stomach and Tongue.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1), VARIANT SER-209.
      Tissue: Colon, Hypothalamus, Skeletal muscle and Urinary bladder.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-52.
      Tissue: Platelet.
    8. "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase."
      Middleton B.
      Biochem. Soc. Trans. 22:427-431(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 48-63, CATALYTIC ACTIVITY.
      Tissue: Liver.
    9. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 62-72 AND 96-111.
      Tissue: Adipocyte.
    10. "Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients."
      Kamijo T., Wanders R.J., Saudubray J.-M., Aoyama T., Komiyama A., Hashimoto T.
      J. Clin. Invest. 93:1740-1747(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Human cytomegalovirus directly induces the antiviral protein viperin to enhance infectivity."
      Seo J.Y., Yaneva R., Hinson E.R., Cresswell P.
      Science 332:1093-1097(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH RSAD2.
    14. "Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits."
      Ushikubo S., Aoyama T., Kamijo T., Wanders R.J.A., Rinaldo P., Vockley J., Hashimoto T.
      Am. J. Hum. Genet. 58:979-988(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TFP DEFICIENCY HIS-61; HIS-247 AND GLY-263.
    15. "Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations."
      Spiekerkoetter U., Sun B., Khuchua Z., Bennett M.J., Strauss A.W.
      Hum. Mutat. 21:598-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TFP DEFICIENCY ASP-59; CYS-61; HIS-61; GLY-117; PRO-121; PRO-133; GLY-242; HIS-247; 259-GLY--PRO-270 DEL; GLY-263; ASP-280; ARG-294; LEU-294; SER-301 AND LYS-444.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-119.

    Entry informationi

    Entry nameiECHB_HUMAN
    AccessioniPrimary (citable) accession number: P55084
    Secondary accession number(s): B2RB16
    , B4E2W0, O14969, Q53TA6, Q96C77, Q9H3F5, Q9T2V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3