O75390 (CISY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Citrate synthase, mitochondrial
EC=2.3.3.1

Gene names

Name:

CS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Transferase
PTM	Acetylation Methylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from direct assay PubMed 9543345. Source: UniProtKB cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome tricarboxylic acid cycle Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Inferred from direct assay PubMed 9543345. Source: UniProtKB
Molecular_function	citrate (Si)-synthase activity Inferred from direct assay PubMed 9543345. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion
	Chain	28 – 466	439	Citrate synthase, mitochondrial		PRO_0000005471
Sites
	Active site	301	1	By similarity
	Active site	347	1	By similarity
	Active site	402	1	By similarity
Amino acid modifications
	Modified residue	76	1	N6-acetyllysine; alternate By similarity
	Modified residue	76	1	N6-succinyllysine; alternate By similarity
	Modified residue	327	1	N6-acetyllysine Ref.8
	Modified residue	375	1	N6-acetyllysine Ref.8
	Modified residue	382	1	N6-acetyllysine Ref.8
	Modified residue	393	1	N6-acetyllysine Ref.8
	Modified residue	395	1	N6,N6,N6-trimethyllysine By similarity
Experimental info
	Sequence conflict	55	1	H → R in CAE45911. Ref.4
	Sequence conflict	127	1	H → C in AAC25560. Ref.1
	Sequence conflict	183	1	R → Q in AAC25560. Ref.1
	Sequence conflict	187	1	Q → R in AAC25560. Ref.1
	Sequence conflict	203	1	M → V in AAC25560. Ref.1
	Sequence conflict	222	1	R → W in AAC25560. Ref.1
	Sequence conflict	255	1	T → M in AAC25560. Ref.1
	Sequence conflict	282	1	L → F in AAQ13428. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O75390 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 459CB29C0BA06997	FASTA	466	51,712
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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.
IPI	IPI00025366.
RefSeq	NP_004068.2. NM_004077.2.
UniGene	Hs.430606.
3D structure databases
ProteinModelPortal	O75390.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75390. 3 interactions.
MINT	MINT-1162839.
STRING	9606.ENSP00000342056.
PTM databases
PhosphoSite	O75390.
Proteomic databases
PaxDb	O75390.
PRIDE	O75390.
Protocols and materials databases
DNASU	1431.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000351328; ENSP00000342056; ENSG00000062485. ENST00000548567; ENSP00000446779; ENSG00000062485.
GeneID	1431.
KEGG	hsa:1431.
UCSC	uc001skr.1. human.
Organism-specific databases
CTD	1431.
GeneCards	GC12M056666.
HGNC	HGNC:2422. CS.
HPA	HPA038460. HPA038461.
MIM	118950. gene.
neXtProt	NX_O75390.
PharmGKB	PA26928.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0372.
HOGENOM	HOG000130831.
HOVERGEN	HBG005336.
InParanoid	O75390.
KO	K01647.
OMA	ELIYEDC.
OrthoDB	EOG4FBHSR.
PhylomeDB	O75390.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000062485-MONOMER.
Reactome	REACT_111217. Metabolism. REACT_17015. Metabolism of proteins.
UniPathway	UPA00223; UER00717.
Gene expression databases
ArrayExpress	O75390.
Bgee	O75390.
CleanEx	HS_CS.
Genevestigator	O75390.
GermOnline	ENSG00000062485. Homo sapiens.
Family and domain databases
Gene3D	1.10.580.10. 1 hit.
InterPro	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]
PANTHER	PTHR11739. PTHR11739. 1 hit.
Pfam	PF00285. Citrate_synt. 1 hit. [Graphical view]
PRINTS	PR00143. CITRTSNTHASE.
SUPFAM	SSF48256. Citrate_synthase_core. 1 hit.
TIGRFAMs	TIGR01793. cit_synth_euk. 1 hit.
PROSITE	PS00480. CITRATE_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CS. human.
GenomeRNAi	1431.
NextBio	5835.
SOURCE	Search...

Entry information

Entry name

CISY_HUMAN

Accession

Primary (citable) accession number: O75390
Secondary accession number(s): Q71UT9 , Q7KZH0, Q96FZ8, Q9BWN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.