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Q0QEL7

- CISY_MESAU

UniProt

Q0QEL7 - CISY_MESAU

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Protein
Citrate synthase, mitochondrial
Gene
CS
Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741 By similarityBy similarity
Active sitei120 – 1201 By similarityBy similarity
Active sitei175 – 1751 By similarityBy similarity

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Mitochondrion matrix By similarity By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›213›213Citrate synthase, mitochondrial
PRO_0000394310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941N6-acetyllysine; alternate By similarity
Modified residuei94 – 941N6-succinyllysine; alternate By similarity
Modified residuei100 – 1001N6-acetyllysine; alternate By similarityBy similarity
Modified residuei100 – 1001N6-succinyllysine; alternate By similarity
Modified residuei148 – 1481N6-acetyllysine; alternate By similarityBy similarity
Modified residuei148 – 1481N6-succinyllysine; alternate By similarity
Modified residuei155 – 1551N6-acetyllysine By similarityBy similarity
Modified residuei166 – 1661N6-acetyllysine; alternate By similarityBy similarity
Modified residuei166 – 1661N6-succinyllysine; alternate By similarity
Modified residuei168 – 1681N6,N6,N6-trimethyllysine By similarityBy similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PRIDEiQ0QEL7.

Interactioni

Subunit structurei

Homodimer By similarity.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Phylogenomic databases

HOVERGENiHBG005336.

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.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q0QEL7-1 [UniParc]FASTAAdd to Basket

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GAIDSKLDWS HNFTNMLGYT EPQFTELMRL YLTIHSDHEG GNVSAHTSHL    50
VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLVWLTQLQK EVGKDVSDEK 100
LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY SCQREFALKH LPNDPLFKLV 150
AQLYKIVPNI LLEQGKAKNP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS 200
RALGVLAQLI WSR 213
Length:213
Mass (Da):23,884
Last modified:September 5, 2006 - v1
Checksum:iF423CBF73DF89D63
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei213 – 2131

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ403127 mRNA. Translation: ABD77260.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ403127 mRNA. Translation: ABD77260.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q0QEL7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005336.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

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.
[Graphical view ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
    Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
    Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCISY_MESAU
AccessioniPrimary (citable) accession number: Q0QEL7
Secondary accession number(s): P86224
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 39 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.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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