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O75390

- CISY_HUMAN

UniProt

O75390 - CISY_HUMAN

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      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
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB
    2. cellular carbohydrate metabolic process Source: InterPro
    3. cellular metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000062485-MONOMER.
    ReactomeiREACT_118595. Mitochondrial protein import.
    REACT_1785. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2422. CS.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: UniProtKB
    3. mitochondrion Source: UniProt
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26928.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionAdd
    BLAST
    Chaini28 – 466439Citrate synthase, mitochondrialPRO_0000005471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
    Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
    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; alternate1 Publication
    Modified residuei327 – 3271N6-succinyllysine; alternateBy similarity
    Modified residuei375 – 3751N6-acetyllysine; alternate1 Publication
    Modified residuei375 – 3751N6-succinyllysine; alternateBy similarity
    Modified residuei382 – 3821N6-acetyllysine1 Publication
    Modified residuei393 – 3931N6-acetyllysine; alternate1 Publication
    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

    MaxQBiO75390.
    PaxDbiO75390.
    PRIDEiO75390.

    PTM databases

    PhosphoSiteiO75390.

    Expressioni

    Gene expression databases

    ArrayExpressiO75390.
    BgeeiO75390.
    CleanExiHS_CS.
    GenevestigatoriO75390.

    Organism-specific databases

    HPAiHPA038460.
    HPA038461.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi107818. 16 interactions.
    IntActiO75390. 4 interactions.
    MINTiMINT-1162839.
    STRINGi9606.ENSP00000342056.

    Structurei

    3D structure databases

    ProteinModelPortaliO75390.
    SMRiO75390. Positions 28-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000130831.
    HOVERGENiHBG005336.
    InParanoidiO75390.
    KOiK01647.
    OMAiELIYEDC.
    PhylomeDBiO75390.
    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.

    O75390-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLTAAARL LGTKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT    50
    FRQQHGKTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGFSIPE 100
    CQKLLPKAKG GEEPLPEGLF WLLVTGHIPT EEQVSWLSKE WAKRAALPSH 150
    VVTMLDNFPT NLHPMSQLSA AVTALNSESN FARAYAQGIS RTKYWELIYE 200
    DSMDLIAKLP CVAAKIYRNL YREGSGIGAI DSNLDWSHNF TNMLGYTDHQ 250
    FTELTRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL 300
    HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL 350
    RKTDPRYTCQ REFALKHLPN DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN 400
    VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK 450
    SMSTEGLMKF VDSKSG 466
    Length:466
    Mass (Da):51,712
    Last modified:January 4, 2005 - v2
    Checksum:i459CB29C0BA06997
    GO

    Sequence cautioni

    The sequence CAE45911.1 differs from that shown. Reason: Intron retention.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551H → R in CAE45911. (PubMed:17974005)Curated
    Sequence conflicti127 – 1271H → C in AAC25560. (PubMed:9809442)Curated
    Sequence conflicti183 – 1831R → Q in AAC25560. (PubMed:9809442)Curated
    Sequence conflicti187 – 1871Q → R in AAC25560. (PubMed:9809442)Curated
    Sequence conflicti203 – 2031M → V in AAC25560. (PubMed:9809442)Curated
    Sequence conflicti222 – 2221R → W in AAC25560. (PubMed:9809442)Curated
    Sequence conflicti255 – 2551T → M in AAC25560. (PubMed:9809442)Curated
    Sequence conflicti282 – 2821L → F in AAQ13428. (PubMed:12549038)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047042 mRNA. Translation: AAC25560.1.
    AF053631 mRNA. Translation: AAQ13428.1.
    AK074956 mRNA. Translation: BAC11314.1.
    BX640838 mRNA. Translation: CAE45911.1. Sequence problems.
    BC000105 mRNA. Translation: AAH00105.3.
    BC010106 mRNA. Translation: AAH10106.1.
    BC072016 mRNA. Translation: AAH72016.1.
    BT007414 mRNA. Translation: AAP36082.1.
    CCDSiCCDS8913.1.
    RefSeqiNP_004068.2. NM_004077.2.
    UniGeneiHs.743252.

    Genome annotation databases

    EnsembliENST00000351328; ENSP00000342056; ENSG00000062485.
    ENST00000548567; ENSP00000446779; ENSG00000062485.
    GeneIDi1431.
    KEGGihsa:1431.
    UCSCiuc001skr.1. human.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Citrate synthase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047042 mRNA. Translation: AAC25560.1 .
    AF053631 mRNA. Translation: AAQ13428.1 .
    AK074956 mRNA. Translation: BAC11314.1 .
    BX640838 mRNA. Translation: CAE45911.1 . Sequence problems.
    BC000105 mRNA. Translation: AAH00105.3 .
    BC010106 mRNA. Translation: AAH10106.1 .
    BC072016 mRNA. Translation: AAH72016.1 .
    BT007414 mRNA. Translation: AAP36082.1 .
    CCDSi CCDS8913.1.
    RefSeqi NP_004068.2. NM_004077.2.
    UniGenei Hs.743252.

    3D structure databases

    ProteinModelPortali O75390.
    SMRi O75390. Positions 28-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107818. 16 interactions.
    IntActi O75390. 4 interactions.
    MINTi MINT-1162839.
    STRINGi 9606.ENSP00000342056.

    PTM databases

    PhosphoSitei O75390.

    Proteomic databases

    MaxQBi O75390.
    PaxDbi O75390.
    PRIDEi O75390.

    Protocols and materials databases

    DNASUi 1431.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351328 ; ENSP00000342056 ; ENSG00000062485 .
    ENST00000548567 ; ENSP00000446779 ; ENSG00000062485 .
    GeneIDi 1431.
    KEGGi hsa:1431.
    UCSCi uc001skr.1. human.

    Organism-specific databases

    CTDi 1431.
    GeneCardsi GC12M056666.
    HGNCi HGNC:2422. CS.
    HPAi HPA038460.
    HPA038461.
    MIMi 118950. gene.
    neXtProti NX_O75390.
    PharmGKBi PA26928.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000130831.
    HOVERGENi HBG005336.
    InParanoidi O75390.
    KOi K01647.
    OMAi ELIYEDC.
    PhylomeDBi O75390.
    TreeFami TF300398.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BioCyci MetaCyc:ENSG00000062485-MONOMER.
    Reactomei REACT_118595. Mitochondrial protein import.
    REACT_1785. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    ChiTaRSi CS. human.
    GenomeRNAii 1431.
    NextBioi 5835.
    PROi O75390.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75390.
    Bgeei O75390.
    CleanExi HS_CS.
    Genevestigatori O75390.

    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. "Cloning and molecular analysis of the human citrate synthase gene."
      Goldenthal M.J., Marin-Garcia J., Ananthakrishnan R.
      Genome 41:733-738(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Cloning and tissue expression pattern analysis of the human citrate synthase cDNA."
      Liu Q., Yu L., Han X.F., Fu Q., Zhang J.X., Tang H., Zhao S.Y.
      Shi Yan Sheng Wu Xue Bao 33:207-214(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Rectum tumor.
    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].
      Tissue: Brain, Lymph and Prostate.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-466.
    7. "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 77-92 AND 383-393.
      Tissue: Adipocyte.
    8. "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-327; LYS-375; LYS-382 AND LYS-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCISY_HUMAN
    AccessioniPrimary (citable) accession number: O75390
    Secondary accession number(s): Q71UT9
    , Q7KZH0, Q96FZ8, Q9BWN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 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

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3