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Protein

Citrate synthase, mitochondrial

Gene

Cs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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: MGI
  3. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_249033. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:88529. Cs.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. mitochondrial matrix Source: UniProtKB
  3. mitochondrion Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 464437Citrate synthase, mitochondrialPRO_0000005472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571N6-succinyllysine1 Publication
Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
Modified residuei103 – 1031N6-succinyllysine1 Publication
Modified residuei193 – 1931N6-succinyllysine1 Publication
Modified residuei321 – 3211N6-acetyllysine; alternate1 Publication
Modified residuei321 – 3211N6-succinyllysine; alternate1 Publication
Modified residuei327 – 3271N6-acetyllysine; alternate1 Publication
Modified residuei327 – 3271N6-succinyllysine; alternate1 Publication
Modified residuei375 – 3751N6-acetyllysine; alternate1 Publication
Modified residuei375 – 3751N6-succinyllysine; alternate1 Publication
Modified residuei382 – 3821N6-acetyllysine1 Publication
Modified residuei393 – 3931N6-acetyllysine; alternate1 Publication
Modified residuei393 – 3931N6-succinyllysine; alternate1 Publication
Modified residuei395 – 3951N6,N6,N6-trimethyllysineBy similarity
Modified residuei450 – 4501N6-succinyllysine1 Publication
Modified residuei459 – 4591N6-acetyllysine; alternate1 Publication
Modified residuei459 – 4591N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiQ9CZU6.
PaxDbiQ9CZU6.
PRIDEiQ9CZU6.

PTM databases

PhosphoSiteiQ9CZU6.

Expressioni

Gene expression databases

BgeeiQ9CZU6.
CleanExiMM_CS.
ExpressionAtlasiQ9CZU6. baseline and differential.
GenevestigatoriQ9CZU6.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi198926. 1 interaction.
IntActiQ9CZU6. 7 interactions.
MINTiMINT-1844265.

Structurei

3D structure databases

ProteinModelPortaliQ9CZU6.
SMRiQ9CZU6. 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.
InParanoidiQ9CZU6.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG73BVCB.
PhylomeDBiQ9CZU6.
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.

Q9CZU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLTAATRL LGAKNSSCLV LAARHASASS TNLKDVLSNL IPKEQARIKT
60 70 80 90 100
FKQQHGKTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE
110 120 130 140 150
CQKMLPKAKG GEEPLPEGLF WLLVTGQMPT EEQVSWLSRE WAKRAALPSH
160 170 180 190 200
VVTMLDNFPT NLHPMSQLSA AITALNSESN FARAYAEGMN RAKYWELIYE
210 220 230 240 250
DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSRLDWSHNF TNMLGYTDPQ
260 270 280 290 300
FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
310 320 330 340 350
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL
360 370 380 390 400
RKTDPRYSCQ REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN
410 420 430 440 450
VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK
460
SMSTDGLMKF VDSK
Length:464
Mass (Da):51,737
Last modified:June 1, 2001 - v1
Checksum:i710639871C31EED5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB056479 mRNA. Translation: BAB63945.1.
AK012151 mRNA. Translation: BAB28063.1.
AK145643 mRNA. Translation: BAE26560.1.
AK149990 mRNA. Translation: BAE29218.1.
AK163273 mRNA. Translation: BAE37268.1.
AK166814 mRNA. Translation: BAE39041.1.
AK167125 mRNA. Translation: BAE39273.1.
BC013554 mRNA. Translation: AAH13554.1.
BC029754 mRNA. Translation: AAH29754.1.
CCDSiCCDS24273.1.
RefSeqiNP_080720.1. NM_026444.3.
UniGeneiMm.58836.

Genome annotation databases

EnsembliENSMUST00000005826; ENSMUSP00000005826; ENSMUSG00000005683.
GeneIDi12974.
KEGGimmu:12974.
UCSCiuc007hmj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB056479 mRNA. Translation: BAB63945.1.
AK012151 mRNA. Translation: BAB28063.1.
AK145643 mRNA. Translation: BAE26560.1.
AK149990 mRNA. Translation: BAE29218.1.
AK163273 mRNA. Translation: BAE37268.1.
AK166814 mRNA. Translation: BAE39041.1.
AK167125 mRNA. Translation: BAE39273.1.
BC013554 mRNA. Translation: AAH13554.1.
BC029754 mRNA. Translation: AAH29754.1.
CCDSiCCDS24273.1.
RefSeqiNP_080720.1. NM_026444.3.
UniGeneiMm.58836.

3D structure databases

ProteinModelPortaliQ9CZU6.
SMRiQ9CZU6. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198926. 1 interaction.
IntActiQ9CZU6. 7 interactions.
MINTiMINT-1844265.

Chemistry

ChEMBLiCHEMBL2176798.

PTM databases

PhosphoSiteiQ9CZU6.

Proteomic databases

MaxQBiQ9CZU6.
PaxDbiQ9CZU6.
PRIDEiQ9CZU6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005826; ENSMUSP00000005826; ENSMUSG00000005683.
GeneIDi12974.
KEGGimmu:12974.
UCSCiuc007hmj.1. mouse.

Organism-specific databases

CTDi1431.
MGIiMGI:88529. Cs.

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00390000006813.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiQ9CZU6.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG73BVCB.
PhylomeDBiQ9CZU6.
TreeFamiTF300398.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
ReactomeiREACT_249033. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiCs. mouse.
NextBioi282742.
PROiQ9CZU6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZU6.
CleanExiMM_CS.
ExpressionAtlasiQ9CZU6. baseline and differential.
GenevestigatoriQ9CZU6.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Sone H., Shimano H., Yamada N.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Egg.
  3. "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].
    Strain: FVB/N and FVB/N-3.
    Tissue: Kidney and Mammary tumor.
  4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 35-43; 58-73; 77-92; 223-256; 328-351; 376-393 AND 429-450, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-103; LYS-193; LYS-321; LYS-327; LYS-375; LYS-393; LYS-450 AND LYS-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321; LYS-327; LYS-375; LYS-382; LYS-393 AND LYS-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCISY_MOUSE
AccessioniPrimary (citable) accession number: Q9CZU6
Secondary accession number(s): Q3UDP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 112 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.