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Q29RK1

- CISY_BOVIN

UniProt

Q29RK1 - CISY_BOVIN

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei301 – 3011PROSITE-ProRule annotation
    Active sitei347 – 3471PROSITE-ProRule annotation
    Active sitei402 – 4021PROSITE-ProRule annotation

    GO - Molecular functioni

    1. citrate (Si)-synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_227707. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase, mitochondrial (EC:2.3.3.1)
    Alternative name(s):
    Citrate (Si)-synthase
    Gene namesi
    Name:CS
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 5

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionBy similarityAdd
    BLAST
    Chaini28 – 466439Citrate synthase, mitochondrialPRO_0000244377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei76 – 761N6-acetyllysine; alternate1 Publication
    Modified residuei76 – 761N6-succinyllysine; alternate1 Publication
    Modified residuei103 – 1031N6-succinyllysineBy similarity
    Modified residuei193 – 1931N6-succinyllysineBy similarity
    Modified residuei321 – 3211N6-acetyllysine; alternateBy similarity
    Modified residuei321 – 3211N6-succinyllysine; alternateBy similarity
    Modified residuei327 – 3271N6-acetyllysine; alternateBy similarity
    Modified residuei327 – 3271N6-succinyllysine; alternateBy similarity
    Modified residuei375 – 3751N6-acetyllysine; alternateBy similarity
    Modified residuei375 – 3751N6-succinyllysine; alternateBy similarity
    Modified residuei382 – 3821N6-acetyllysineBy similarity
    Modified residuei393 – 3931N6-acetyllysine; alternateBy similarity
    Modified residuei393 – 3931N6-succinyllysine; alternateBy similarity
    Modified residuei395 – 3951N6,N6,N6-trimethyllysineBy similarity
    Modified residuei450 – 4501N6-succinyllysineBy similarity
    Modified residuei459 – 4591N6-acetyllysine; alternateBy similarity
    Modified residuei459 – 4591N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    PaxDbiQ29RK1.
    PRIDEiQ29RK1.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiQ29RK1. 1 interaction.
    STRINGi9913.ENSBTAP00000005730.

    Structurei

    3D structure databases

    ProteinModelPortaliQ29RK1.
    SMRiQ29RK1. Positions 28-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0372.
    GeneTreeiENSGT00390000006813.
    HOGENOMiHOG000130831.
    HOVERGENiHBG005336.
    InParanoidiQ29RK1.
    KOiK01647.
    OMAiELIYEDC.
    OrthoDBiEOG73BVCB.
    TreeFamiTF300398.

    Family and domain databases

    Gene3Di1.10.580.10. 1 hit.
    InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR010109. Citrate_synthase_euk.
    [Graphical view]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q29RK1-1 [UniParc]FASTAAdd to Basket

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    MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQTRVKA    50
    FRQQHGKTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE 100
    CQKLLPKAKG GEEPLPEGLF WLLVTGQIPT EEQVSWLSQE WAKRAALPSH 150
    VVTMLDNFPT NLHPMSQLSA AVTALNSEST FARAYSEGIN RTKYWELIYE 200
    DSMDLIAKLP CVAAKIYRNL YREGSSIGAI DPKLDWSHNF TNMLGYTDAQ 250
    FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL 300
    HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL 350
    RKTDPRYTCQ REFALKHLPQ DPMFKLVAQL YKIVPNILLE QGKAKNPWPN 400
    VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK 450
    SMSTDGLMKF VDSKSG 466
    Length:466
    Mass (Da):51,773
    Last modified:April 4, 2006 - v1
    Checksum:i73C2CB93589084B3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC114138 mRNA. Translation: AAI14139.1.
    RefSeqiNP_001038186.1. NM_001044721.1.
    UniGeneiBt.106917.

    Genome annotation databases

    EnsembliENSBTAT00000005730; ENSBTAP00000005730; ENSBTAG00000004371.
    GeneIDi280682.
    KEGGibta:280682.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC114138 mRNA. Translation: AAI14139.1 .
    RefSeqi NP_001038186.1. NM_001044721.1.
    UniGenei Bt.106917.

    3D structure databases

    ProteinModelPortali Q29RK1.
    SMRi Q29RK1. Positions 28-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q29RK1. 1 interaction.
    STRINGi 9913.ENSBTAP00000005730.

    Chemistry

    ChEMBLi CHEMBL2406901.

    Proteomic databases

    PaxDbi Q29RK1.
    PRIDEi Q29RK1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000005730 ; ENSBTAP00000005730 ; ENSBTAG00000004371 .
    GeneIDi 280682.
    KEGGi bta:280682.

    Organism-specific databases

    CTDi 1431.

    Phylogenomic databases

    eggNOGi COG0372.
    GeneTreei ENSGT00390000006813.
    HOGENOMi HOG000130831.
    HOVERGENi HBG005336.
    InParanoidi Q29RK1.
    KOi K01647.
    OMAi ELIYEDC.
    OrthoDBi EOG73BVCB.
    TreeFami TF300398.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    Reactomei REACT_227707. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    NextBioi 20804872.

    Family and domain databases

    Gene3Di 1.10.580.10. 1 hit.
    InterProi IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR010109. Citrate_synthase_euk.
    [Graphical view ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    TIGRFAMsi TIGR01793. cit_synth_euk. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Heart ventricle.
    2. "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
      Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
      Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-76, SUCCINYLATION AT LYS-76.

    Entry informationi

    Entry nameiCISY_BOVIN
    AccessioniPrimary (citable) accession number: Q29RK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Citrate synthase is found in nearly all cells capable of oxidative metabolism.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3