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P40017 (YAT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. 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:
Carnitine O-acetyltransferase YAT2

EC=2.3.1.7
Gene names
Name:YAT2
Ordered Locus Names:YER024W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length923 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the shutteling of acetyl-CoA in the cell. Ref.3

Catalytic activity

Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.

Subcellular location

Cytoplasm Ref.4 Ref.6.

Miscellaneous

Present with 319 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 923922Carnitine O-acetyltransferase YAT2
PRO_0000210176

Regions

Region530 – 54112Coenzyme A binding By similarity

Sites

Binding site5761Carnitine By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue7831Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P40017 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B59AB881491D68A7

FASTA923103,334
        10         20         30         40         50         60 
MSSGSTIVSS DKSGRTFKHE EELPKLPLPK LCDTLQRLKE SLEPLYYADG YYQHPLDPEQ 

        70         80         90        100        110        120 
IEKLSSIIRD FEENPVSEKL QSKLQSYHDT RDCYLDELHL DINNQTSTRE IQDDVLPRNP 

       130        140        150        160        170        180 
FLVLADDALP NITQADRSAV LVHSAARFIS ALKQDLLPPD INATNGKPLS MAPFLNLFGT 

       190        200        210        220        230        240 
TRSPVFQRGE VENFDLNKPY TASDLEDPDY SSDEDDNDEP TQKDFDDRKR KHEEDIFTGN 

       250        260        270        280        290        300 
GITIKRHPDS KHILIISRGQ YYTLEVLDST NKIIYTAAEL TTIFNHIIKD SSGIEKSTAL 

       310        320        330        340        350        360 
GSLTSHSFRN WKYARKRLQK RYPNELHRID SALFVLVLDE SQEETTNDGD DTADISQMFN 

       370        380        390        400        410        420 
RTITERDKKC TSANCKRVFY GTSIINSKGH QVGSCVSRWY DKLQLVVTAD AKATVIWDSF 

       430        440        450        460        470        480 
TCDGSVVLRF TSEIYTESVL RLARDVNAGD PQFSLWPNVT QMDPETKKLM TATISADGGG 

       490        500        510        520        530        540 
PSEIDPKLVV NKIDWSFSNI LNTHVHLSET KLADLISKYD IVRASIPLGR RSAQRLGVKP 

       550        560        570        580        590        600 
DSMVQVALQI AHYALYGRMV FGLEPVSTRG FKNSRSSFIN IQSQALLELC QLFISSSIDG 

       610        620        630        640        650        660 
TDKLDKFIQT CETHNNMVKH AKSGVGYEKH FNALKYLFKF HDHFGIHLSG DESSAAKDLF 

       670        680        690        700        710        720 
ENPLVLPFSQ PELIVANCGN AATTTFGITP AVPHGFGIGY IIKDDQVDLT VTSQFRQGDR 

       730        740        750        760        770        780 
LMFMLSWVLG EIRSYWRMSR GTSHNKTGVK ISPVVDKLYE MDNAVNNPPK RNGHTVNGSR 

       790        800        810        820        830        840 
KTSSSSQVNL NRYGGFFDLE GHIDSRNISK TPSMKNLQKT FNGLTMSADN DHSSSAVSVP 

       850        860        870        880        890        900 
TEKEKLNTGH EILQIQPREV ASNGLEADDE TDIEIVAGNA DGTSSSASSA TSLNSKKRNV 

       910        920 
INSRFDIDFD RSRVGRKVAT LDQ 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Carnitine-dependent metabolic activities in Saccharomyces cerevisiae: three carnitine acetyltransferases are essential in a carnitine-dependent strain."
Swiegers J.H., Dippenaar N., Pretorius I.S., Bauer F.F.
Yeast 18:585-595(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Carnitine and carnitine acetyltransferases in the yeast Saccharomyces cerevisiae: a role for carnitine in stress protection."
Franken J., Kroppenstedt S., Swiegers J.H., Bauer F.F.
Curr. Genet. 53:347-360(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"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-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18778 Genomic DNA. Translation: AAB64557.1.
BK006939 Genomic DNA. Translation: DAA07677.1.
PIRS50482.
RefSeqNP_010941.1. NM_001178915.1.

3D structure databases

ProteinModelPortalP40017.
SMRP40017. Positions 15-713.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36758. 11 interactions.
IntActP40017. 1 interaction.
MINTMINT-4483798.
STRING4932.YER024W.

Proteomic databases

MaxQBP40017.
PaxDbP40017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER024W; YER024W; YER024W.
GeneID856745.
KEGGsce:YER024W.

Organism-specific databases

CYGDYER024w.
SGDS000000826. YAT2.

Phylogenomic databases

eggNOGNOG308143.
HOGENOMHOG000141908.
OMADILPRNP.
OrthoDBEOG7TQV84.

Enzyme and pathway databases

BioCycYEAST:YER024W-MONOMER.

Gene expression databases

GenevestigatorP40017.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. PTHR22589. 1 hit.
PfamPF00755. Carn_acyltransf. 2 hits.
[Graphical view]
PROSITEPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982885.

Entry information

Entry nameYAT2_YEAST
AccessionPrimary (citable) accession number: P40017
Secondary accession number(s): D3DLS3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families