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P40017

- YAT2_YEAST

UniProt

P40017 - YAT2_YEAST

Protein

Carnitine O-acetyltransferase YAT2

Gene

YAT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Involved in the shutteling of acetyl-CoA in the cell.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei576 – 5761CarnitineBy similarity

    GO - Molecular functioni

    1. carnitine O-acetyltransferase activity Source: SGD

    GO - Biological processi

    1. alcohol metabolic process Source: SGD
    2. carnitine metabolic process Source: SGD
    3. fatty acid metabolic process Source: UniProtKB-KW
    4. transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    BioCyciYEAST:YER024W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carnitine O-acetyltransferase YAT2 (EC:2.3.1.7)
    Gene namesi
    Name:YAT2
    Ordered Locus Names:YER024W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER024w.
    SGDiS000000826. YAT2.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytosol Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 923922Carnitine O-acetyltransferase YAT2PRO_0000210176Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei783 – 7831Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP40017.
    PaxDbiP40017.

    Expressioni

    Gene expression databases

    GenevestigatoriP40017.

    Interactioni

    Protein-protein interaction databases

    BioGridi36758. 11 interactions.
    IntActiP40017. 1 interaction.
    MINTiMINT-4483798.
    STRINGi4932.YER024W.

    Structurei

    3D structure databases

    ProteinModelPortaliP40017.
    SMRiP40017. Positions 15-713.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni530 – 54112Coenzyme A bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG308143.
    HOGENOMiHOG000141908.
    OMAiDILPRNP.
    OrthoDBiEOG7TQV84.

    Family and domain databases

    InterProiIPR000542. Carn_acyl_trans.
    [Graphical view]
    PANTHERiPTHR22589. PTHR22589. 1 hit.
    PfamiPF00755. Carn_acyltransf. 2 hits.
    [Graphical view]
    PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P40017-1 [UniParc]FASTAAdd to Basket

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    MSSGSTIVSS DKSGRTFKHE EELPKLPLPK LCDTLQRLKE SLEPLYYADG    50
    YYQHPLDPEQ IEKLSSIIRD FEENPVSEKL QSKLQSYHDT RDCYLDELHL 100
    DINNQTSTRE IQDDVLPRNP FLVLADDALP NITQADRSAV LVHSAARFIS 150
    ALKQDLLPPD INATNGKPLS MAPFLNLFGT TRSPVFQRGE VENFDLNKPY 200
    TASDLEDPDY SSDEDDNDEP TQKDFDDRKR KHEEDIFTGN GITIKRHPDS 250
    KHILIISRGQ YYTLEVLDST NKIIYTAAEL TTIFNHIIKD SSGIEKSTAL 300
    GSLTSHSFRN WKYARKRLQK RYPNELHRID SALFVLVLDE SQEETTNDGD 350
    DTADISQMFN RTITERDKKC TSANCKRVFY GTSIINSKGH QVGSCVSRWY 400
    DKLQLVVTAD AKATVIWDSF TCDGSVVLRF TSEIYTESVL RLARDVNAGD 450
    PQFSLWPNVT QMDPETKKLM TATISADGGG PSEIDPKLVV NKIDWSFSNI 500
    LNTHVHLSET KLADLISKYD IVRASIPLGR RSAQRLGVKP DSMVQVALQI 550
    AHYALYGRMV FGLEPVSTRG FKNSRSSFIN IQSQALLELC QLFISSSIDG 600
    TDKLDKFIQT CETHNNMVKH AKSGVGYEKH FNALKYLFKF HDHFGIHLSG 650
    DESSAAKDLF ENPLVLPFSQ PELIVANCGN AATTTFGITP AVPHGFGIGY 700
    IIKDDQVDLT VTSQFRQGDR LMFMLSWVLG EIRSYWRMSR GTSHNKTGVK 750
    ISPVVDKLYE MDNAVNNPPK RNGHTVNGSR KTSSSSQVNL NRYGGFFDLE 800
    GHIDSRNISK TPSMKNLQKT FNGLTMSADN DHSSSAVSVP TEKEKLNTGH 850
    EILQIQPREV ASNGLEADDE TDIEIVAGNA DGTSSSASSA TSLNSKKRNV 900
    INSRFDIDFD RSRVGRKVAT LDQ 923
    Length:923
    Mass (Da):103,334
    Last modified:February 1, 1995 - v1
    Checksum:iB59AB881491D68A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18778 Genomic DNA. Translation: AAB64557.1.
    BK006939 Genomic DNA. Translation: DAA07677.1.
    PIRiS50482.
    RefSeqiNP_010941.1. NM_001178915.1.

    Genome annotation databases

    EnsemblFungiiYER024W; YER024W; YER024W.
    GeneIDi856745.
    KEGGisce:YER024W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18778 Genomic DNA. Translation: AAB64557.1 .
    BK006939 Genomic DNA. Translation: DAA07677.1 .
    PIRi S50482.
    RefSeqi NP_010941.1. NM_001178915.1.

    3D structure databases

    ProteinModelPortali P40017.
    SMRi P40017. Positions 15-713.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36758. 11 interactions.
    IntActi P40017. 1 interaction.
    MINTi MINT-4483798.
    STRINGi 4932.YER024W.

    Proteomic databases

    MaxQBi P40017.
    PaxDbi P40017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER024W ; YER024W ; YER024W .
    GeneIDi 856745.
    KEGGi sce:YER024W.

    Organism-specific databases

    CYGDi YER024w.
    SGDi S000000826. YAT2.

    Phylogenomic databases

    eggNOGi NOG308143.
    HOGENOMi HOG000141908.
    OMAi DILPRNP.
    OrthoDBi EOG7TQV84.

    Enzyme and pathway databases

    BioCyci YEAST:YER024W-MONOMER.

    Miscellaneous databases

    NextBioi 982885.

    Gene expression databases

    Genevestigatori P40017.

    Family and domain databases

    InterProi IPR000542. Carn_acyl_trans.
    [Graphical view ]
    PANTHERi PTHR22589. PTHR22589. 1 hit.
    Pfami PF00755. Carn_acyltransf. 2 hits.
    [Graphical view ]
    PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiYAT2_YEAST
    AccessioniPrimary (citable) accession number: P40017
    Secondary accession number(s): D3DLS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 319 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3