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O75390

- CISY_HUMAN

UniProt

O75390 - CISY_HUMAN

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Protein

Citrate synthase, mitochondrial

Gene

CS

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiO75390.
CleanExiHS_CS.
ExpressionAtlasiO75390. baseline and differential.
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.
GeneTreeiENSGT00390000006813.
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

        10         20         30         40         50
MALLTAAARL LGTKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT
60 70 80 90 100
FRQQHGKTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGFSIPE
110 120 130 140 150
CQKLLPKAKG GEEPLPEGLF WLLVTGHIPT EEQVSWLSKE WAKRAALPSH
160 170 180 190 200
VVTMLDNFPT NLHPMSQLSA AVTALNSESN FARAYAQGIS RTKYWELIYE
210 220 230 240 250
DSMDLIAKLP CVAAKIYRNL YREGSGIGAI DSNLDWSHNF TNMLGYTDHQ
260 270 280 290 300
FTELTRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
310 320 330 340 350
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL
360 370 380 390 400
RKTDPRYTCQ REFALKHLPN DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN
410 420 430 440 450
VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK
460
SMSTEGLMKF VDSKSG
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00390000006813.
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

Bgeei O75390.
CleanExi HS_CS.
ExpressionAtlasi O75390. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 136 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