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O75390 (CISY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Citrate synthase, mitochondrial

EC=2.3.3.1
Gene names
Name:CS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion
Chain28 – 466439Citrate synthase, mitochondrial
PRO_0000005471

Sites

Active site3011 By similarity
Active site3471 By similarity
Active site4021 By similarity

Amino acid modifications

Modified residue571N6-succinyllysine By similarity
Modified residue761N6-acetyllysine; alternate By similarity
Modified residue761N6-succinyllysine; alternate By similarity
Modified residue1031N6-succinyllysine By similarity
Modified residue1931N6-succinyllysine By similarity
Modified residue3211N6-acetyllysine; alternate By similarity
Modified residue3211N6-succinyllysine; alternate By similarity
Modified residue3271N6-acetyllysine; alternate Ref.8
Modified residue3271N6-succinyllysine; alternate By similarity
Modified residue3751N6-acetyllysine; alternate Ref.8
Modified residue3751N6-succinyllysine; alternate By similarity
Modified residue3821N6-acetyllysine Ref.8
Modified residue3931N6-acetyllysine; alternate Ref.8
Modified residue3931N6-succinyllysine; alternate By similarity
Modified residue3951N6,N6,N6-trimethyllysine By similarity
Modified residue4501N6-succinyllysine By similarity
Modified residue4591N6-acetyllysine; alternate By similarity
Modified residue4591N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict551H → R in CAE45911. Ref.4
Sequence conflict1271H → C in AAC25560. Ref.1
Sequence conflict1831R → Q in AAC25560. Ref.1
Sequence conflict1871Q → R in AAC25560. Ref.1
Sequence conflict2031M → V in AAC25560. Ref.1
Sequence conflict2221R → W in AAC25560. Ref.1
Sequence conflict2551T → M in AAC25560. Ref.1
Sequence conflict2821L → F in AAQ13428. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O75390 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 459CB29C0BA06997

FASTA46651,712
        10         20         30         40         50         60 
MALLTAAARL LGTKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT FRQQHGKTVV 

        70         80         90        100        110        120 
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGFSIPE CQKLLPKAKG GEEPLPEGLF 

       130        140        150        160        170        180 
WLLVTGHIPT EEQVSWLSKE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AVTALNSESN 

       190        200        210        220        230        240 
FARAYAQGIS RTKYWELIYE DSMDLIAKLP CVAAKIYRNL YREGSGIGAI DSNLDWSHNF 

       250        260        270        280        290        300 
TNMLGYTDHQ FTELTRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL 

       310        320        330        340        350        360 
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYTCQ 

       370        380        390        400        410        420 
REFALKHLPN DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY 

       430        440        450        460 
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTEGLMKF VDSKSG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Wikipedia

Citrate synthase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_004068.2. NM_004077.2.
UniGeneHs.743252.

3D structure databases

ProteinModelPortalO75390.
SMRO75390. Positions 28-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107818. 15 interactions.
IntActO75390. 4 interactions.
MINTMINT-1162839.
STRING9606.ENSP00000342056.

PTM databases

PhosphoSiteO75390.

Proteomic databases

PaxDbO75390.
PRIDEO75390.

Protocols and materials databases

DNASU1431.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351328; ENSP00000342056; ENSG00000062485.
ENST00000548567; ENSP00000446779; ENSG00000062485.
GeneID1431.
KEGGhsa:1431.
UCSCuc001skr.1. human.

Organism-specific databases

CTD1431.
GeneCardsGC12M056666.
HGNCHGNC:2422. CS.
HPAHPA038460.
HPA038461.
MIM118950. gene.
neXtProtNX_O75390.
PharmGKBPA26928.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000130831.
HOVERGENHBG005336.
InParanoidO75390.
KOK01647.
OMAELIYEDC.
PhylomeDBO75390.
TreeFamTF300398.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000062485-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00223; UER00717.

Gene expression databases

ArrayExpressO75390.
BgeeO75390.
CleanExHS_CS.
GenevestigatorO75390.

Family and domain databases

Gene3D1.10.580.10. 1 hit.
InterProIPR016142. 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]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01793. cit_synth_euk. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCS. human.
GenomeRNAi1431.
NextBio5835.
PROO75390.
SOURCESearch...

Entry information

Entry nameCISY_HUMAN
AccessionPrimary (citable) accession number: O75390
Secondary accession number(s): Q71UT9 expand/collapse secondary AC list , Q7KZH0, Q96FZ8, Q9BWN8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM