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P08459

- SPS2_YEAST

UniProt

P08459 - SPS2_YEAST

Protein

Sporulation-specific protein 2

Gene

SPS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in middle stages of meiosis. Redundant with SPS22 for the organization of the beta-glucan layer of the spore wall.3 Publications

    GO - Biological processi

    1. ascospore formation Source: SGD
    2. ascospore wall assembly Source: SGD
    3. meiotic nuclear division Source: UniProtKB-KW

    Keywords - Biological processi

    Meiosis, Sporulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30038-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sporulation-specific protein 2
    Gene namesi
    Name:SPS2
    Ordered Locus Names:YDR522C
    ORF Names:D9719.26
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR522c.
    SGDiS000002930. SPS2.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. fungal-type cell wall Source: SGD
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5656Sequence AnalysisAdd
    BLAST
    Chaini57 – 475419Sporulation-specific protein 2PRO_0000033195Add
    BLAST
    Propeptidei476 – 50227Removed in mature formSequence AnalysisPRO_0000277471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
    Lipidationi475 – 4751GPI-anchor amidated asparagineSequence Analysis

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP08459.

    Expressioni

    Gene expression databases

    GenevestigatoriP08459.

    Interactioni

    Protein-protein interaction databases

    BioGridi32572. 42 interactions.
    DIPiDIP-7764N.
    IntActiP08459. 3 interactions.
    STRINGi4932.YDR522C.

    Structurei

    3D structure databases

    ProteinModelPortaliP08459.
    SMRiP08459. Positions 216-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SPS2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG309463.
    GeneTreeiENSGT00530000065410.
    HOGENOMiHOG000057088.
    OMAiGLMIANN.
    OrthoDBiEOG75XGWQ.

    Sequencei

    Sequence statusi: Complete.

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

    P08459-1 [UniParc]FASTAAdd to Basket

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    MPIWKTQTFF TSISVIQIVN KETKVSTKKE KDSMLNQLNT ILRFLFLFLQ    50
    LIKSSAAVEP NGGPNILDHN IMLVNTNATI PKKEQTDFEV ISPTKQTQVD 100
    EDCKKGLYHI ENAGNLIELQ AKCWKVVGNI EISSNYSGSL IDLGLIREIE 150
    GDLIIKNNKH IFRIQGYNLE SLGKLELDSL TSFVSLDFPA LKEVETVDWR 200
    VLPILSSVVI NGNIKKIKNI IISDTALTSI DYFNNVKKVD IFNINNNRFL 250
    ENLFASLESV TKQLTVHSNA KELELDLSNL HTVENMTIKD VSEIKLAKLS 300
    SVNSSLEFIE NQFSSLELPL LAKVQGTLGL IDNKNLKKLN FSNATDIQGG 350
    LMIANNTELA KIDFFPKLRQ IGGAIYFEGS FDKIDLPELK LVKGSAYIKS 400
    SSEELNCEEF TSPKAGRSII RGGKIECTSG MKSKMLNVDE EGNVLGKQET 450
    DNDNGKKEKG KNGAKSQGSS KKMENSAPKN IFIDAFKMSV YAVFTVLFSI 500
    IF 502
    Length:502
    Mass (Da):55,939
    Last modified:October 1, 1996 - v2
    Checksum:i11F9EFB11CD4D59C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti203 – 2031P → L in AAA35080. (PubMed:9169867)Curated
    Sequence conflicti210 – 2101I → S in AAA35080. (PubMed:9169867)Curated
    Sequence conflicti324 – 3241V → G in AAA35080. (PubMed:9169867)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33057 Genomic DNA. Translation: AAB64962.1.
    M13629 Genomic DNA. Translation: AAA35080.1.
    BK006938 Genomic DNA. Translation: DAA12352.1.
    PIRiS69578.
    RefSeqiNP_010810.1. NM_001180830.1.

    Genome annotation databases

    EnsemblFungiiYDR522C; YDR522C; YDR522C.
    GeneIDi852134.
    KEGGisce:YDR522C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33057 Genomic DNA. Translation: AAB64962.1 .
    M13629 Genomic DNA. Translation: AAA35080.1 .
    BK006938 Genomic DNA. Translation: DAA12352.1 .
    PIRi S69578.
    RefSeqi NP_010810.1. NM_001180830.1.

    3D structure databases

    ProteinModelPortali P08459.
    SMRi P08459. Positions 216-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32572. 42 interactions.
    DIPi DIP-7764N.
    IntActi P08459. 3 interactions.
    STRINGi 4932.YDR522C.

    Proteomic databases

    PaxDbi P08459.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR522C ; YDR522C ; YDR522C .
    GeneIDi 852134.
    KEGGi sce:YDR522C.

    Organism-specific databases

    CYGDi YDR522c.
    SGDi S000002930. SPS2.

    Phylogenomic databases

    eggNOGi NOG309463.
    GeneTreei ENSGT00530000065410.
    HOGENOMi HOG000057088.
    OMAi GLMIANN.
    OrthoDBi EOG75XGWQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30038-MONOMER.

    Miscellaneous databases

    NextBioi 970537.

    Gene expression databases

    Genevestigatori P08459.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Characterization and mutational analysis of a cluster of three genes expressed preferentially during sporulation of Saccharomyces cerevisiae."
      Percival-Smith A., Segall J.
      Mol. Cell. Biol. 6:2443-2451(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-502.
    4. "Increased copy number of the 5' end of the SPS2 gene inhibits sporulation of Saccharomyces cerevisiae."
      Percival-Smith A., Segall J.
      Mol. Cell. Biol. 7:2484-2490(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Stimulation of later functions of the yeast meiotic protein kinase Ime2p by the IDS2 gene product."
      Sia R.A., Mitchell A.P.
      Mol. Cell. Biol. 15:5279-5287(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Morphogenetic pathway of spore wall assembly in Saccharomyces cerevisiae."
      Coluccio A., Bogengruber E., Conrad M.N., Dresser M.E., Briza P., Neiman A.M.
      Eukaryot. Cell 3:1464-1475(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiSPS2_YEAST
    AccessioniPrimary (citable) accession number: P08459
    Secondary accession number(s): D6VTE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 238 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3