Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P32801

- ELM1_YEAST

UniProt

P32801 - ELM1_YEAST

Protein

Serine/threonine-protein kinase ELM1

Gene

ELM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Important role in G1 events required for bud emergence and septin organization. Coordinates cell growth and cell division at G2/M, essential for efficient cytokinesis and for regulation of SWE1.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171ATPPROSITE-ProRule annotation
    Active sitei259 – 2591Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi94 – 1029ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein serine/threonine kinase activity Source: SGD

    GO - Biological processi

    1. axial cellular bud site selection Source: SGD
    2. budding cell bud growth Source: SGD
    3. cell morphogenesis Source: SGD
    4. cytokinesis checkpoint Source: SGD
    5. glucose metabolic process Source: SGD
    6. positive regulation of protein autophosphorylation Source: SGD
    7. protein autophosphorylation Source: SGD
    8. protein phosphorylation Source: SGD
    9. pseudohyphal growth Source: SGD
    10. response to drug Source: SGD
    11. response to osmotic stress Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31849-MONOMER.
    BRENDAi2.7.10.2. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase ELM1 (EC:2.7.11.1)
    Gene namesi
    Name:ELM1
    Ordered Locus Names:YKL048C
    ORF Names:YKL261
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL048c.
    SGDiS000001531. ELM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cellular bud neck contractile ring Source: SGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi200 – 2001T → G: Allows selective inhibition in vivo. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 640640Serine/threonine-protein kinase ELM1PRO_0000085951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521Phosphoserine1 Publication
    Modified residuei516 – 5161Phosphoserine1 Publication
    Modified residuei519 – 5191Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32801.
    PaxDbiP32801.
    PeptideAtlasiP32801.
    PRIDEiP32801.

    Expressioni

    Gene expression databases

    GenevestigatoriP32801.

    Interactioni

    Protein-protein interaction databases

    BioGridi34085. 392 interactions.
    DIPiDIP-2731N.
    IntActiP32801. 5 interactions.
    MINTiMINT-691352.
    STRINGi4932.YKL048C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32801.
    SMRiP32801. Positions 80-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini88 – 420333Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000066096.
    KOiK00924.
    OMAiELPFFGE.
    OrthoDBiEOG7TQVBC.

    Family and domain databases

    InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24347. PTHR24347. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32801-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPRQLIPTL IPEWAPLSQQ SCIREDELDS PPITPTSQTS SFGSSFSQQK    50
    PTYSTIIGEN IHTILDEIRP YVKKITVSDQ DKKTINQYTL GVSAGSGQFG 100
    YVRKAYSSTL GKVVAVKIIP KKPWNAQQYS VNQVMRQIQL WKSKGKITTN 150
    MSGNEAMRLM NIEKCRWEIF AASRLRNNVH IVRLIECLDS PFSESIWIVT 200
    NWCSLGELQW KRDDDEDILP QWKKIVISNC SVSTFAKKIL EDMTKGLEYL 250
    HSQGCIHRDI KPSNILLDEE EKVAKLSDFG SCIFTPQSLP FSDANFEDCF 300
    QRELNKIVGT PAFIAPELCH LGNSKRDFVT DGFKLDIWSL GVTLYCLLYN 350
    ELPFFGENEF ETYHKIIEVS LSSKINGNTL NDLVIKRLLE KDVTLRISIQ 400
    DLVKVLSRDQ PIDSRNHSQI SSSSVNPVRN EGPVRRFFGR LLTKKGKKKT 450
    SGKGKDKVLV SATSKVTPSI HIDEEPDKEC FSTTVLRSSP DSSDYCSSLG 500
    EEAIQVTDFL DTFCRSNESL PNLTVNNDKQ NSDMKTDRSE SSSHSSLKIP 550
    TPIKAMIRLK SSPKENGNRT HINCSQDKPS SPLMDRTVGK RTVNNSGARK 600
    LAHSSNILNF KAYINSEDSD IRETVEDVKT YLNFADNGQI 640
    Length:640
    Mass (Da):72,150
    Last modified:June 1, 1994 - v2
    Checksum:i33C3A7E188DF12C4
    GO

    Sequence cautioni

    The sequence AAA02892.1 differs from that shown. Reason: Frameshift at position 539.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti390 – 3901E → Y in AAA02892. (PubMed:8395007)Curated
    Sequence conflicti484 – 4852TV → SD in AAA02892. (PubMed:8395007)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81258 Unassigned DNA. Translation: AAA02892.1. Frameshift.
    X71621 Genomic DNA. No translation available.
    Z28048 Genomic DNA. Translation: CAA81883.1.
    BK006944 Genomic DNA. Translation: DAA09109.1.
    PIRiS37869.
    RefSeqiNP_012876.1. NM_001179614.1.

    Genome annotation databases

    EnsemblFungiiYKL048C; YKL048C; YKL048C.
    GeneIDi853818.
    KEGGisce:YKL048C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81258 Unassigned DNA. Translation: AAA02892.1 . Frameshift.
    X71621 Genomic DNA. No translation available.
    Z28048 Genomic DNA. Translation: CAA81883.1 .
    BK006944 Genomic DNA. Translation: DAA09109.1 .
    PIRi S37869.
    RefSeqi NP_012876.1. NM_001179614.1.

    3D structure databases

    ProteinModelPortali P32801.
    SMRi P32801. Positions 80-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34085. 392 interactions.
    DIPi DIP-2731N.
    IntActi P32801. 5 interactions.
    MINTi MINT-691352.
    STRINGi 4932.YKL048C.

    Proteomic databases

    MaxQBi P32801.
    PaxDbi P32801.
    PeptideAtlasi P32801.
    PRIDEi P32801.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL048C ; YKL048C ; YKL048C .
    GeneIDi 853818.
    KEGGi sce:YKL048C.

    Organism-specific databases

    CYGDi YKL048c.
    SGDi S000001531. ELM1.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000066096.
    KOi K00924.
    OMAi ELPFFGE.
    OrthoDBi EOG7TQVBC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31849-MONOMER.
    BRENDAi 2.7.10.2. 984.

    Miscellaneous databases

    NextBioi 974996.
    PROi P32801.

    Gene expression databases

    Genevestigatori P32801.

    Family and domain databases

    InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24347. PTHR24347. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of dimorphism in Saccharomyces cerevisiae: involvement of the novel protein kinase homolog Elm1p and protein phosphatase 2A."
      Blacketer M.J., Koehler C.M., Coats S.G., Myers A.M., Madaule P.
      Mol. Cell. Biol. 13:5567-5581(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, FUNCTION.
    2. "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a new gene encoding a putative histone and seven new open reading frames."
      Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.
      Yeast 9:1379-1384(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [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. "Specific inhibition of Elm1 kinase activity reveals functions required for early G1 events."
      Sreenivasan A., Bishop A.C., Shokat K.M., Kellogg D.R.
      Mol. Cell. Biol. 23:6327-6337(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-200.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "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-152 AND SER-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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-516 AND SER-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiELM1_YEAST
    AccessioniPrimary (citable) accession number: P32801
    Secondary accession number(s): D6VXN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 139 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 149 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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3