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P43612

- SA155_YEAST

UniProt

P43612 - SA155_YEAST

Protein

SIT4-associating protein SAP155

Gene

SAP155

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 4 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Positive regulator of protein phosphatase SIT4. Involved in directing expression of TOR-repressed genes and in dephosphorylation of NPR1 in response to nutrient starvation. Negatively modulates K+ efflux of the cell by the Na+-K+/H+ antiporter NHA1.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: SGD

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30487-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SIT4-associating protein SAP155
    Gene namesi
    Name:SAP155
    Ordered Locus Names:YFR040W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VI

    Organism-specific databases

    CYGDiYFR040w.
    SGDiS000001936. SAP155.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10021002SIT4-associating protein SAP155PRO_0000097561Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581Phosphoserine2 Publications
    Modified residuei255 – 2551Phosphoserine2 Publications
    Modified residuei613 – 6131Phosphothreonine2 Publications
    Modified residuei618 – 6181Phosphothreonine2 Publications

    Post-translational modificationi

    Hyperphosphorylated in the absence of SIT4.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP43612.
    PaxDbiP43612.
    PeptideAtlasiP43612.

    Expressioni

    Gene expression databases

    GenevestigatoriP43612.

    Interactioni

    Subunit structurei

    Associates with the SIT4 protein phosphatase catalytic subunit in a cell-cycle-dependent manner.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SIT4P206048EBI-16370,EBI-13707

    Protein-protein interaction databases

    BioGridi31198. 150 interactions.
    DIPiDIP-5852N.
    IntActiP43612. 32 interactions.
    MINTiMINT-632146.
    STRINGi4932.YFR040W.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi938 – 99760Asn-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SAPS family.Curated

    Phylogenomic databases

    eggNOGiNOG301298.
    GeneTreeiENSGT00390000009899.
    HOGENOMiHOG000142084.
    KOiK15457.
    OMAiNNFWHNV.
    OrthoDBiEOG7647CP.

    Family and domain databases

    InterProiIPR007587. SAPS.
    [Graphical view]
    PANTHERiPTHR12634. PTHR12634. 1 hit.
    PfamiPF04499. SAPS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P43612-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFWPFGQNL NHSNINKILD EYFHVLHELE RINPSVGKAI PAIFNNVQER     50
    GTSDSLDSIP EEYSHGDEVK TARGDQKSRF EKDDQQERYE KEEEERSMNS 100
    SESSTTSFSS GSTSKTDLDE EDISNATAPM MVTTKNLDNS FIERMLVETE 150
    LLNELSRQNK TLLDFICFGF FFDKKTNKKV NNMEYLVDQL MECISKIKTA 200
    TTVDLNNLID YQEQQQLDDS SQEDVYVESD TEQEEEKEDD NNSNNKKRRK 250
    RGSSSFGNDD INNNDDDDDA NEDDESAYLT KATIISEIFS LDIWLISESL 300
    VKNQSYLNKI WSIINQPNFN SENSPLVPIF LKINQNLLLT RQDQYLNFIR 350
    TERSFVDDML KHVDISLLMD FFLKIISTDK IESPTGIIEL VYDQNLISKC 400
    LSFLNNKESP ADIQACVGDF LKALIAISAN APLDDISIGP NSLTRQLASP 450
    ESIAKLVDIM INQRGAALNT TVSIVIELIR KNNSDYDQVN LLTTTIKTHP 500
    PSNRDPIYLG YLLRKFSNHL SDFFQIILDI ENDANIPLHE NQLHEKFKPL 550
    GFERFKVVEL IAELLHCSNM GLMNSKRAER IARRRDKVRS QLSHHLQDAL 600
    NDLSIEEKEQ LKTKHSPTRD TDHDLKNNNG KIDNDNNDND DESDYGDEID 650
    ESFEIPYINM KQNIKLRTDP TVGDLFKIKL YDTRIVSKIM ELFLTHPWNN 700
    FWHNVIFDII QQIFNGRMDF SYNSFLVLSL FNLKSSYQFM TDIVISDEKG 750
    TDVSRFSPVI RDPNFDFKIT TDFILRGYQD SYKFYELRKM NLGYMGHIVL 800
    IAEEVVKFSK LYKVELISPD IQVILQTEEW QYYSEEVLNE TRMMYSKILG 850
    GGSYIDDGNG NIIPQLPDNT TVLTPNGDAS NNNEILDSDT GSSNGTSGGG 900
    QLINVESLEE QLSLSTESDL HNKLREMLIN RAQEDVDNKN TENGVFILGP 950
    PEDKNSNSNI NNTNHNSNNS NNNDNNDNND NDNDNTRNYN EDADNDNDYD 1000
    HE 1002
    Length:1,002
    Mass (Da):115,002
    Last modified:September 21, 2011 - v4
    Checksum:i50CDC17130333022
    GO

    Sequence cautioni

    The sequence BAA09279.1 differs from that shown. Reason: Frameshift at position 74.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti663 – 6631N → T(PubMed:8686379)Curated
    Sequence conflicti663 – 6631N → T in BAA09279. (PubMed:7670463)Curated
    Sequence conflicti668 – 6681T → G in CAC42243. (PubMed:11779790)Curated
    Sequence conflicti674 – 69017DLFKI…VSKIM → TYSKSNYMIRDCFQNN AA sequence (PubMed:8649382)CuratedAdd
    BLAST
    Sequence conflicti815 – 82410ELISPDIQVI → DYISRYSSN in AAC49303. (PubMed:8649382)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50560 Genomic DNA. Translation: AAC49303.1.
    AJ318331 Genomic DNA. Translation: CAC42243.1.
    D50617 Genomic DNA. Translation: BAA09279.1. Frameshift.
    BK006940 Genomic DNA. Translation: DAA12483.2.
    RefSeqiNP_116698.3. NM_001180005.2.

    Genome annotation databases

    EnsemblFungiiYFR040W; YFR040W; YFR040W.
    GeneIDi850601.
    KEGGisce:YFR040W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50560 Genomic DNA. Translation: AAC49303.1 .
    AJ318331 Genomic DNA. Translation: CAC42243.1 .
    D50617 Genomic DNA. Translation: BAA09279.1 . Frameshift.
    BK006940 Genomic DNA. Translation: DAA12483.2 .
    RefSeqi NP_116698.3. NM_001180005.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31198. 150 interactions.
    DIPi DIP-5852N.
    IntActi P43612. 32 interactions.
    MINTi MINT-632146.
    STRINGi 4932.YFR040W.

    Proteomic databases

    MaxQBi P43612.
    PaxDbi P43612.
    PeptideAtlasi P43612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YFR040W ; YFR040W ; YFR040W .
    GeneIDi 850601.
    KEGGi sce:YFR040W.

    Organism-specific databases

    CYGDi YFR040w.
    SGDi S000001936. SAP155.

    Phylogenomic databases

    eggNOGi NOG301298.
    GeneTreei ENSGT00390000009899.
    HOGENOMi HOG000142084.
    KOi K15457.
    OMAi NNFWHNV.
    OrthoDBi EOG7647CP.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30487-MONOMER.

    Miscellaneous databases

    NextBioi 966469.

    Gene expression databases

    Genevestigatori P43612.

    Family and domain databases

    InterProi IPR007587. SAPS.
    [Graphical view ]
    PANTHERi PTHR12634. PTHR12634. 1 hit.
    Pfami PF04499. SAPS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The SAPs, a new family of proteins, associate and function positively with the SIT4 phosphatase."
      Luke M.M., della Seta F., di Como C.J., Sugimoto H., Kobayashi R., Arndt K.T.
      Mol. Cell. Biol. 16:2744-2755(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SIT4, PHOSPHORYLATION.
    2. "Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin."
      Jablonowski D., Butler A.R., Fichtner L., Gardiner D., Schaffrath R., Stark M.J.R.
      Genetics 159:1479-1489(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF FRAMESHIFT.
    3. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
      Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
      Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 663.
      Strain: ATCC 204508 / S288c.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors."
      Rohde J.R., Campbell S., Zurita-Martinez S.A., Cutler N.S., Ashe M., Cardenas M.E.
      Mol. Cell. Biol. 24:8332-8341(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p."
      Manlandro C.M.A., Haydon D.H., Rosenwald A.G.
      Eukaryot. Cell 4:1041-1049(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613 AND THR-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSA155_YEAST
    AccessioniPrimary (citable) accession number: P43612
    Secondary accession number(s): D6VTS3, Q96VG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 5960 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 VI
      Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

    External Data

    Dasty 3