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Q9CZU6 (CISY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Citrate synthase, mitochondrial

EC=2.3.3.1
Gene names
Name:Cs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length464 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 By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 464437Citrate synthase, mitochondrial
PRO_0000005472

Sites

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

Amino acid modifications

Modified residue571N6-succinyllysine Ref.5
Modified residue761N6-acetyllysine; alternate By similarity
Modified residue761N6-succinyllysine; alternate By similarity
Modified residue1031N6-succinyllysine Ref.5
Modified residue1931N6-succinyllysine Ref.5
Modified residue3211N6-acetyllysine; alternate Ref.6
Modified residue3211N6-succinyllysine; alternate Ref.5
Modified residue3271N6-acetyllysine; alternate Ref.6
Modified residue3271N6-succinyllysine; alternate Ref.5
Modified residue3751N6-acetyllysine; alternate Ref.6
Modified residue3751N6-succinyllysine; alternate Ref.5
Modified residue3821N6-acetyllysine Ref.6
Modified residue3931N6-acetyllysine; alternate Ref.6
Modified residue3931N6-succinyllysine; alternate Ref.5
Modified residue3951N6,N6,N6-trimethyllysine By similarity
Modified residue4501N6-succinyllysine Ref.5
Modified residue4591N6-acetyllysine; alternate Ref.6
Modified residue4591N6-succinyllysine; alternate Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9CZU6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 710639871C31EED5

FASTA46451,737
        10         20         30         40         50         60 
MALLTAATRL LGAKNSSCLV LAARHASASS TNLKDVLSNL IPKEQARIKT FKQQHGKTVV 

        70         80         90        100        110        120 
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKMLPKAKG GEEPLPEGLF 

       130        140        150        160        170        180 
WLLVTGQMPT EEQVSWLSRE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN 

       190        200        210        220        230        240 
FARAYAEGMN RAKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSRLDWSHNF 

       250        260        270        280        290        300 
TNMLGYTDPQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL 

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

       370        380        390        400        410        420 
REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY 

       430        440        450        460 
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_080720.1. NM_026444.3.
UniGeneMm.58836.

3D structure databases

ProteinModelPortalQ9CZU6.
SMRQ9CZU6. Positions 28-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198926. 1 interaction.
IntActQ9CZU6. 7 interactions.
MINTMINT-1844265.

Chemistry

ChEMBLCHEMBL2176798.

PTM databases

PhosphoSiteQ9CZU6.

Proteomic databases

PaxDbQ9CZU6.
PRIDEQ9CZU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005826; ENSMUSP00000005826; ENSMUSG00000005683.
GeneID12974.
KEGGmmu:12974.
UCSCuc007hmj.1. mouse.

Organism-specific databases

CTD1431.
MGIMGI:88529. Cs.

Phylogenomic databases

eggNOGCOG0372.
GeneTreeENSGT00390000006813.
HOGENOMHOG000130831.
HOVERGENHBG005336.
InParanoidQ9CZU6.
KOK01647.
OMAELIYEDC.
OrthoDBEOG73BVCB.
PhylomeDBQ9CZU6.
TreeFamTF300398.

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Gene expression databases

ArrayExpressQ9CZU6.
BgeeQ9CZU6.
CleanExMM_CS.
GenevestigatorQ9CZU6.

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. mouse.
NextBio282742.
PROQ9CZU6.
SOURCESearch...

Entry information

Entry nameCISY_MOUSE
AccessionPrimary (citable) accession number: Q9CZU6
Secondary accession number(s): Q3UDP3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot