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Protein

Acyl-coenzyme A thioesterase THEM4

Gene

THEM4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays an role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane.6 Publications

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.2 Publications

Kineticsi

  1. KM=2.4 µM for myristoyl-CoA2 Publications
  2. KM=2.6 µM for palmitoyl-CoA2 Publications
  3. KM=5.2 µM for oleoyl-CoA2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei161 – 1611Proton donor/acceptor1 Publication
    Binding sitei183 – 1831Substrate
    Binding sitei185 – 1851Substrate

    GO - Molecular functioni

    • acyl-CoA hydrolase activity Source: Reactome
    • palmitoyl-CoA hydrolase activity Source: UniProtKB

    GO - Biological processi

    • fatty acid metabolic process Source: UniProtKB
    • long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
    • protein kinase B signaling Source: UniProtKB
    • regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Apoptosis, Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
    R-HSA-165158. Activation of AKT2.
    R-HSA-199418. Negative regulation of the PI3K/AKT network.
    R-HSA-389357. CD28 dependent PI3K/Akt signaling.
    R-HSA-5218920. VEGFR2 mediated vascular permeability.
    R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
    SIGNORiQ5T1C6.

    Chemistry

    SwissLipidsiSLP:000000657.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase THEM4 (EC:3.1.2.2)
    Short name:
    Acyl-CoA thioesterase THEM4
    Alternative name(s):
    Carboxyl-terminal modulator protein
    Thioesterase superfamily member 4
    Gene namesi
    Name:THEM4
    Synonyms:CTMP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17947. THEM4.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • mitochondrial inner membrane Source: UniProtKB-SubCell
    • mitochondrial intermembrane space Source: UniProtKB-SubCell
    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: UniProtKB
    • plasma membrane Source: Reactome
    • ruffle membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi37 – 382SS → DD: Abolishes import into the mitochondria. 1 Publication
    Mutagenesisi37 – 371S → A: Abolishes cleavage of mitochondrial transit peptide. 1 Publication
    Mutagenesisi152 – 1521H → A or F: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi161 – 1611D → E or N: Nearly abolishes enzyme activity. Strongly reduced affinity for myristoyl-CoA. 1 Publication
    Mutagenesisi177 – 1771T → A: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi183 – 1831N → A: No effect on enzyme activity. 1 Publication
    Mutagenesisi206 – 2061R → A: Reduces enzyme activity. 1 Publication
    Mutagenesisi207 – 2071K → A: Slightly reduced enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670813.

    Polymorphism and mutation databases

    BioMutaiTHEM4.
    DMDMi74744451.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636MitochondrionSequence analysisAdd
    BLAST
    Chaini37 – 240204Acyl-coenzyme A thioesterase THEM4PRO_0000314179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371Phosphoserine1 Publication
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei55 – 551N6-succinyllysineBy similarity
    Modified residuei66 – 661N6-succinyllysineBy similarity
    Modified residuei74 – 741N6-acetyllysineBy similarity
    Modified residuei98 – 981N6-succinyllysineBy similarity
    Modified residuei207 – 2071N6-succinyllysineBy similarity

    Post-translational modificationi

    Phosphorylated.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ5T1C6.
    MaxQBiQ5T1C6.
    PaxDbiQ5T1C6.
    PRIDEiQ5T1C6.

    PTM databases

    iPTMnetiQ5T1C6.
    PhosphoSiteiQ5T1C6.

    Expressioni

    Tissue specificityi

    Expressed predominantly in skeletal muscle, testis, uterus, brain and kidney. Down-regulated in glioblastoma or glioma compared to non-neoplastic brain due to promoter hypermethylation.2 Publications

    Gene expression databases

    BgeeiQ5T1C6.
    CleanExiHS_THEM4.
    ExpressionAtlasiQ5T1C6. baseline and differential.
    GenevisibleiQ5T1C6. HS.

    Organism-specific databases

    HPAiHPA028161.

    Interactioni

    Subunit structurei

    Homodimer and homotetramer. Interacts with AKT1 in the cytosol.3 Publications

    Protein-protein interaction databases

    BioGridi125557. 15 interactions.
    DIPiDIP-60764N.
    IntActiQ5T1C6. 1 interaction.
    MINTiMINT-8306269.
    STRINGi9606.ENSP00000357804.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi55 – 6713Combined sources
    Turni68 – 703Combined sources
    Beta strandi71 – 766Combined sources
    Helixi84 – 9310Combined sources
    Helixi111 – 1133Combined sources
    Turni117 – 1193Combined sources
    Beta strandi120 – 1289Combined sources
    Turni129 – 1324Combined sources
    Beta strandi133 – 1408Combined sources
    Helixi142 – 1443Combined sources
    Beta strandi145 – 1473Combined sources
    Helixi153 – 17220Combined sources
    Beta strandi175 – 18410Combined sources
    Beta strandi193 – 20412Combined sources
    Beta strandi207 – 21610Combined sources
    Beta strandi222 – 23211Combined sources
    Turni235 – 2373Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AE8X-ray1.59A/B/C/D37-240[»]
    4GAHX-ray2.30A/B40-240[»]
    ProteinModelPortaliQ5T1C6.
    SMRiQ5T1C6. Positions 43-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni206 – 2072Substrate binding

    Sequence similaritiesi

    Belongs to the THEM4/THEM5 thioesterase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG4781. Eukaryota.
    ENOG4111ZF6. LUCA.
    GeneTreeiENSGT00390000018826.
    HOGENOMiHOG000220857.
    HOVERGENiHBG054340.
    InParanoidiQ5T1C6.
    KOiK16339.
    OMAiRKFFVSC.
    OrthoDBiEOG7Q5HFM.
    PhylomeDBiQ5T1C6.
    TreeFamiTF332518.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q5T1C6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLRSCAARLR TLGALCLPPV GRRLPGSEPR PELRSFSSEE VILKDCSVPN
    60 70 80 90 100
    PSWNKDLRLL FDQFMKKCED GSWKRLPSYK RTPTEWIQDF KTHFLDPKLM
    110 120 130 140 150
    KEEQMSQAQL FTRSFDDGLG FEYVMFYNDI EKRMVCLFQG GPYLEGPPGF
    160 170 180 190 200
    IHGGAIATMI DATVGMCAMM AGGIVMTANL NINYKRPIPL CSVVMINSQL
    210 220 230 240
    DKVEGRKFFV SCNVQSVDEK TLYSEATSLF IKLNPAKSLT
    Length:240
    Mass (Da):27,130
    Last modified:December 21, 2004 - v1
    Checksum:iA01071B07A1B5FB2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171L → R.5 Publications
    Corresponds to variant rs3748805 [ dbSNP | Ensembl ].
    VAR_037865
    Natural varianti38 – 381S → C.1 Publication
    Corresponds to variant rs144257719 [ dbSNP | Ensembl ].
    VAR_037866

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ313515 mRNA. Translation: CAC86384.1.
    AK314852 mRNA. Translation: BAG37369.1.
    AL450992 Genomic DNA. Translation: CAI12162.1.
    CH471121 Genomic DNA. Translation: EAW53400.1.
    BC065277 mRNA. Translation: AAH65277.1.
    CCDSiCCDS1006.1.
    RefSeqiNP_444283.2. NM_053055.4.
    UniGeneiHs.164070.

    Genome annotation databases

    EnsembliENST00000368814; ENSP00000357804; ENSG00000159445.
    GeneIDi117145.
    KEGGihsa:117145.
    UCSCiuc001ezj.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ313515 mRNA. Translation: CAC86384.1.
    AK314852 mRNA. Translation: BAG37369.1.
    AL450992 Genomic DNA. Translation: CAI12162.1.
    CH471121 Genomic DNA. Translation: EAW53400.1.
    BC065277 mRNA. Translation: AAH65277.1.
    CCDSiCCDS1006.1.
    RefSeqiNP_444283.2. NM_053055.4.
    UniGeneiHs.164070.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AE8X-ray1.59A/B/C/D37-240[»]
    4GAHX-ray2.30A/B40-240[»]
    ProteinModelPortaliQ5T1C6.
    SMRiQ5T1C6. Positions 43-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi125557. 15 interactions.
    DIPiDIP-60764N.
    IntActiQ5T1C6. 1 interaction.
    MINTiMINT-8306269.
    STRINGi9606.ENSP00000357804.

    Chemistry

    SwissLipidsiSLP:000000657.

    PTM databases

    iPTMnetiQ5T1C6.
    PhosphoSiteiQ5T1C6.

    Polymorphism and mutation databases

    BioMutaiTHEM4.
    DMDMi74744451.

    Proteomic databases

    EPDiQ5T1C6.
    MaxQBiQ5T1C6.
    PaxDbiQ5T1C6.
    PRIDEiQ5T1C6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000368814; ENSP00000357804; ENSG00000159445.
    GeneIDi117145.
    KEGGihsa:117145.
    UCSCiuc001ezj.3. human.

    Organism-specific databases

    CTDi117145.
    GeneCardsiTHEM4.
    HGNCiHGNC:17947. THEM4.
    HPAiHPA028161.
    MIMi606388. gene.
    neXtProtiNX_Q5T1C6.
    PharmGKBiPA142670813.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG4781. Eukaryota.
    ENOG4111ZF6. LUCA.
    GeneTreeiENSGT00390000018826.
    HOGENOMiHOG000220857.
    HOVERGENiHBG054340.
    InParanoidiQ5T1C6.
    KOiK16339.
    OMAiRKFFVSC.
    OrthoDBiEOG7Q5HFM.
    PhylomeDBiQ5T1C6.
    TreeFamiTF332518.

    Enzyme and pathway databases

    ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
    R-HSA-165158. Activation of AKT2.
    R-HSA-199418. Negative regulation of the PI3K/AKT network.
    R-HSA-389357. CD28 dependent PI3K/Akt signaling.
    R-HSA-5218920. VEGFR2 mediated vascular permeability.
    R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
    SIGNORiQ5T1C6.

    Miscellaneous databases

    ChiTaRSiTHEM4. human.
    GenomeRNAii117145.
    PROiQ5T1C6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ5T1C6.
    CleanExiHS_THEM4.
    ExpressionAtlasiQ5T1C6. baseline and differential.
    GenevisibleiQ5T1C6. HS.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
      Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
      Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17.
    2. "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], VARIANT ARG-17.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-17.
    5. "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], VARIANT ARG-17.
    6. "Hypermethylation and transcriptional downregulation of the carboxyl-terminal modulator protein gene in glioblastomas."
      Knobbe C.B., Reifenberger J., Blaschke B., Reifenberger G.
      J. Natl. Cancer Inst. 96:483-486(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways."
      Ono H., Sakoda H., Fujishiro M., Anai M., Kushiyama A., Fukushima Y., Katagiri H., Ogihara T., Oka Y., Kamata H., Horike N., Uchijima Y., Kurihara H., Asano T.
      Am. J. Physiol. 293:C1576-C1585(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Heat shock protein 70-mediated sensitization of cells to apoptosis by carboxyl-terminal modulator protein."
      Piao L., Li Y., Yang K.J., Park K.A., Byun H.S., Won M., Hong J., Kim J.L., Kweon G.R., Hur G.M., Seok J.H., Cho J.Y., Chun T., Hess D., Sack R., Maira S.M., Brazil D.P., Hemmings B.A., Park J.
      BMC Cell Biol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-37 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 37-SER-SER-38, SUBCELLULAR LOCATION.
    9. "The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family."
      Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.
      Biochemistry 48:5507-5509(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis."
      Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S., Bozulic L., Hemmings B.A.
      Cell. Signal. 21:639-650(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-37.
    11. "The carboxy-terminal modulator protein (CTMP) regulates mitochondrial dynamics."
      Parcellier A., Tintignac L.A., Zhuravleva E., Dummler B., Brazil D.P., Hynx D., Cron P., Schenk S., Olivieri V., Hemmings B.A.
      PLoS ONE 4:E5471-E5471(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
      Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
      Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
    13. "Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development."
      Zhuravleva E., Gut H., Hynx D., Marcellin D., Bleck C.K., Genoud C., Cron P., Keusch J.J., Dummler B., Esposti M.D., Hemmings B.A.
      Mol. Cell. Biol. 32:2685-2697(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 37-240, SUBUNIT.
    14. "Activation of Akt independent of PTEN and CTMP tumor-suppressor gene mutations in epilepsy-associated Taylor-type focal cortical dysplasias."
      Schick V., Majores M., Engels G., Spitoni S., Koch A., Elger C.E., Simon M., Knobbe C., Bluemcke I., Becker A.J.
      Acta Neuropathol. 112:715-725(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-17 AND CYS-38.

    Entry informationi

    Entry nameiTHEM4_HUMAN
    AccessioniPrimary (citable) accession number: Q5T1C6
    Secondary accession number(s): B2RBX2, Q96KR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: December 21, 2004
    Last modified: June 8, 2016
    This is version 105 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. 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.