Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P08679

- CISY2_YEAST

UniProt

P08679 - CISY2_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Citrate synthase, peroxisomal

Gene

CIT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 sitei293 – 2931PROSITE-ProRule annotation
Active sitei339 – 3391PROSITE-ProRule annotation
Active sitei394 – 3941PROSITE-ProRule annotation

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: SGD

GO - Biological processi

  1. citrate metabolic process Source: SGD
  2. glutamate biosynthetic process Source: SGD
  3. glyoxylate cycle Source: SGD
  4. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciYEAST:YCR005C-MONOMER.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, peroxisomal (EC:2.3.3.16)
Gene namesi
Name:CIT2
Ordered Locus Names:YCR005C
ORF Names:YCR043, YCR5C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCR005c.
SGDiS000000598. CIT2.

Subcellular locationi

GO - Cellular componenti

  1. peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Citrate synthase, peroxisomalPRO_0000169984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine1 Publication
Cross-linki354 – 354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki385 – 385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP08679.
PaxDbiP08679.
PeptideAtlasiP08679.

Expressioni

Gene expression databases

GenevestigatoriP08679.

Interactioni

Protein-protein interaction databases

BioGridi30983. 47 interactions.
DIPiDIP-1259N.
IntActiP08679. 2 interactions.
MINTiMINT-403455.
STRINGi4932.YCR005C.

Structurei

3D structure databases

ProteinModelPortaliP08679.
SMRiP08679. Positions 26-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi458 – 4603Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00760000120118.
HOGENOMiHOG000130831.
InParanoidiP08679.
KOiK01647.
OMAiSCKSRIT.
OrthoDBiEOG7WQ82G.

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.

P08679-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVPYLNSNR NVASYLQSNS SQEKTLKERF SEIYPIHAQD VRQFVKEHGK
60 70 80 90 100
TKISDVLLEQ VYGGMRGIPG SVWEGSVLDP EDGIRFRGRT IADIQKDLPK
110 120 130 140 150
AKGSSQPLPE ALFWLLLTGE VPTQAQVENL SADLMSRSEL PSHVVQLLDN
160 170 180 190 200
LPKDLHPMAQ FSIAVTALES ESKFAKAYAQ GISKQDYWSY TFEDSLDLLG
210 220 230 240 250
KLPVIAAKIY RNVFKDGKMG EVDPNADYAK NLVNLIGSKD EDFVDLMRLY
260 270 280 290 300
LTIHSDHEGG NVSAHTSHLV GSALSSPYLS LASGLNGLAG PLHGRANQEV
310 320 330 340 350
LEWLFALKEE VNDDYSKDTI EKYLWDTLNS GRVIPGYGHA VLRKTDPRYM
360 370 380 390 400
AQRKFAMDHF PDYELFKLVS SIYEVAPGVL TEHGKTKNPW PNVDAHSGVL
410 420 430 440 450
LQYYGLKESS FYTVLFGVSR AFGILAQLIT DRAIGASIER PKSYSTEKYK
460
ELVKNIESKL
Length:460
Mass (Da):51,413
Last modified:January 1, 1988 - v1
Checksum:iAB2F66AD9A9399EF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11113 Genomic DNA. Translation: CAA77442.1.
M14686 Genomic DNA. Translation: AAA34497.1.
X59720 Genomic DNA. Translation: CAA42342.1.
AY692837 Genomic DNA. Translation: AAT92856.1.
M54982 Genomic DNA. Translation: AAA34498.1.
BK006937 Genomic DNA. Translation: DAA07484.1.
PIRiA25393. YKBYC.
RefSeqiNP_009931.1. NM_001178718.1.

Genome annotation databases

EnsemblFungiiYCR005C; YCR005C; YCR005C.
GeneIDi850361.
KEGGisce:YCR005C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11113 Genomic DNA. Translation: CAA77442.1 .
M14686 Genomic DNA. Translation: AAA34497.1 .
X59720 Genomic DNA. Translation: CAA42342.1 .
AY692837 Genomic DNA. Translation: AAT92856.1 .
M54982 Genomic DNA. Translation: AAA34498.1 .
BK006937 Genomic DNA. Translation: DAA07484.1 .
PIRi A25393. YKBYC.
RefSeqi NP_009931.1. NM_001178718.1.

3D structure databases

ProteinModelPortali P08679.
SMRi P08679. Positions 26-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30983. 47 interactions.
DIPi DIP-1259N.
IntActi P08679. 2 interactions.
MINTi MINT-403455.
STRINGi 4932.YCR005C.

Chemistry

ChEMBLi CHEMBL1741170.

Proteomic databases

MaxQBi P08679.
PaxDbi P08679.
PeptideAtlasi P08679.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCR005C ; YCR005C ; YCR005C .
GeneIDi 850361.
KEGGi sce:YCR005C.

Organism-specific databases

CYGDi YCR005c.
SGDi S000000598. CIT2.

Phylogenomic databases

eggNOGi COG0372.
GeneTreei ENSGT00760000120118.
HOGENOMi HOG000130831.
InParanoidi P08679.
KOi K01647.
OMAi SCKSRIT.
OrthoDBi EOG7WQ82G.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
BioCyci YEAST:YCR005C-MONOMER.

Miscellaneous databases

NextBioi 965839.

Gene expression databases

Genevestigatori P08679.

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. "Mitochondrial and nonmitochondrial citrate synthases in Saccharomyces cerevisiae are encoded by distinct homologous genes."
    Rosenkrantz M., Alam T., Kim K.-S., Clark B.J., Srere P.A., Guarente L.P.
    Mol. Cell. Biol. 6:4509-4515(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequence of a 10.8kb fragment to the right of the chromosome III centromere of Saccharomyces cerevisiae."
    Biteau N., Fremaux C., Hebrard S., Menara A., Aigle M., Crouzet M.
    Yeast 8:61-70(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Intramitochondrial functions regulate nonmitochondrial citrate synthase (CIT2) expression in Saccharomyces cerevisiae."
    Liao X., Small W.C., Srere P.A., Butow R.A.
    Mol. Cell. Biol. 11:38-46(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-354 AND LYS-385.
    Strain: SUB592.
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCISY2_YEAST
AccessioniPrimary (citable) accession number: P08679
Secondary accession number(s): D6VR15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Present with 2310 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3