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P25389

- KCC4_YEAST

UniProt

P25389 - KCC4_YEAST

Protein

Probable serine/threonine-protein kinase KCC4

Gene

KCC4

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 139 (01 Oct 2014)
      Sequence version 3 (27 Jun 2003)
      Previous versions | rss
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    Functioni

    Involved in regulation of bud growth during cell cycle and in septin organization. Plays a role in cell wall synthesis.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501ATPPROSITE-ProRule annotation
    Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidic acid binding Source: UniProtKB
    3. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    4. phosphatidylserine binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase activity Source: SGD
    7. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. budding cell bud growth Source: SGD
    2. cytokinesis checkpoint Source: SGD
    3. protein phosphorylation Source: SGD
    4. regulation of cell shape Source: UniProtKB-KW
    5. septin ring assembly Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29286-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable serine/threonine-protein kinase KCC4 (EC:2.7.11.1)
    Gene namesi
    Name:KCC4
    Ordered Locus Names:YCL024W
    ORF Names:YCL24W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCL024w.
    SGDiS000000529. KCC4.

    Subcellular locationi

    Bud neck 2 Publications

    GO - Cellular componenti

    1. cellular bud neck Source: SGD
    2. cellular bud neck septin collar Source: SGD
    3. incipient cellular bud site Source: SGD
    4. plasma membrane Source: UniProtKB
    5. septin ring Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10371037Probable serine/threonine-protein kinase KCC4PRO_0000086109Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei396 – 3961Phosphoserine1 Publication
    Modified residuei675 – 6751Phosphoserine1 Publication
    Modified residuei707 – 7071Phosphoserine1 Publication
    Modified residuei777 – 7771Phosphoserine1 Publication
    Modified residuei822 – 8221Phosphoserine1 Publication
    Modified residuei825 – 8251Phosphoserine1 Publication
    Modified residuei871 – 8711Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25389.
    PaxDbiP25389.
    PRIDEiP25389.

    Expressioni

    Gene expression databases

    GenevestigatoriP25389.

    Interactioni

    Subunit structurei

    Interacts with septin proteins, primarily with CDC11. Interacts with SWE1 and NAP1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NAP1P252936EBI-9607,EBI-11850

    Protein-protein interaction databases

    BioGridi30960. 85 interactions.
    DIPiDIP-1779N.
    IntActiP25389. 14 interactions.
    MINTiMINT-397998.

    Structurei

    Secondary structure

    1
    1037
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi921 – 9244
    Helixi925 – 9273
    Beta strandi930 – 9334
    Beta strandi938 – 9425
    Helixi944 – 95613
    Helixi959 – 9613
    Beta strandi963 – 9697
    Turni970 – 9734
    Beta strandi974 – 9796
    Beta strandi984 – 9863
    Beta strandi990 – 9989
    Beta strandi1004 – 101310
    Helixi1015 – 103117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OSMX-ray1.70A917-1037[»]
    3OSTX-ray1.69A917-1037[»]
    ProteinModelPortaliP25389.
    SMRiP25389. Positions 18-361, 918-1036.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25389.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 285265Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi388 – 499112Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117372.
    HOGENOMiHOG000057100.
    KOiK08286.
    OrthoDBiEOG793BK1.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25389-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVANTETHS AAKPSSTIGP WKLGETLGFG STGKVQLAQH ERTGHRTAVK     50
    VISKSIFNNN GNHSNDDSVL PYNIEREIVI MKLLSHPNVL SLYDVWETNN 100
    NLYLILEYAE KGELFNLLVD HGPLPEREAI NCFRQIIIGI SYCHALGIVH 150
    RDLKPENLLL DSFYNIKIAD FGMAALQTDA DLLETSCGSP HYAAPEIVSG 200
    LPYEGFASDV WSCGVILFAL LTGRLPFDEE NGNVRDLLLK VQKGQFEMPN 250
    DTEISRDAQD LIGKILVVDP RQRIKIRDIL SHPLLKKYQT IKDSKSIKDL 300
    PRENTYLYPL ADSNNHTSAS IDDSILQNLV VLWHGRHADD IVSKLKENGT 350
    NKEKILYALL YRFKLDSVRG SNKKNRNKIK KTKKNKRSST LSSSSSLLLN 400
    NRSIQSTPRR RTSKRHSREF SSSRKRSSFL LSSNPTDSSP IPLRSSKRIT 450
    HINVASANTQ ATPSGVPNPH KRNSKKRSSK RLSYMPNTKR SSLTSKSLSN 500
    FTNLIDDDDW EYIEKDAKRT SSNFATLIDE IFEPEKFELA KREKAELQRK 550
    VQEAKRQSVN AQKINEDEFG SEVSDGMKEL KKINDKVSSP LINYEFSQQE 600
    LLQDIDTLLT NRYQLSSYTR PISRLDPGLT PVTETLPNNL KEKTALLQDT 650
    EKKIIETIRR SKFLGSLLNV RGGLSPGKSE LAPIEESPIV STTPLIYNDR 700
    MEPRRISDVE VPHFTRKSKH FTTANNRRSV LSLYAKDSIK DLNEFLIKED 750
    PDLPPQGSTD NESRSEDPEI AESITDSRNI QYDEDDSKDG DNVNNDNILS 800
    DFPQGVGISQ EYDMKDKNPN QSPISKSAEP TLVVKLPSLS SFQGKNASGL 850
    GLYQREPSKV TLPSLTSNNS SVGENIEDGA EKGTESEKIA ASLSDDDLKE 900
    DNDKKDNDTV NAPTTVKKPP NSVLLKKFSK GKILELEIHA KIPEKRLYEG 950
    LHKLLEGWKQ YGLKNLVFNI TNMIITGKLV NDSILFLRST LFEIMVLPNG 1000
    DGRSLIKFNK KTGSTKTLTK LATEIQIILQ KEGVLDK 1037
    Length:1,037
    Mass (Da):116,475
    Last modified:June 27, 2003 - v3
    Checksum:i2F5FF36DA8C5B1A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAC42961.1.
    BK006937 Genomic DNA. Translation: DAA07461.1.
    PIRiS74283.
    RefSeqiNP_009907.2. NM_001178670.1.

    Genome annotation databases

    EnsemblFungiiYCL024W; YCL024W; YCL024W.
    GeneIDi850334.
    KEGGisce:YCL024W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAC42961.1 .
    BK006937 Genomic DNA. Translation: DAA07461.1 .
    PIRi S74283.
    RefSeqi NP_009907.2. NM_001178670.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OSM X-ray 1.70 A 917-1037 [» ]
    3OST X-ray 1.69 A 917-1037 [» ]
    ProteinModelPortali P25389.
    SMRi P25389. Positions 18-361, 918-1036.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 30960. 85 interactions.
    DIPi DIP-1779N.
    IntActi P25389. 14 interactions.
    MINTi MINT-397998.

    Proteomic databases

    MaxQBi P25389.
    PaxDbi P25389.
    PRIDEi P25389.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCL024W ; YCL024W ; YCL024W .
    GeneIDi 850334.
    KEGGi sce:YCL024W.

    Organism-specific databases

    CYGDi YCL024w.
    SGDi S000000529. KCC4.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117372.
    HOGENOMi HOG000057100.
    KOi K08286.
    OrthoDBi EOG793BK1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29286-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P25389.
    NextBioi 965772.
    PROi P25389.

    Gene expression databases

    Genevestigatori P25389.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast."
      Barral Y., Parra M., Bidlingmaier S., Snyder M.
      Genes Dev. 13:176-187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    2. "The Saccharomyces cerevisiae bud-neck proteins Kcc4 and Gin4 have distinct but partially-overlapping cellular functions."
      Okuzaki D., Watanabe T., Tanaka S., Nojima H.
      Genes Genet. Syst. 78:113-126(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH SWE1.
    3. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Gromadka R.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. Valles G., Volckaerts G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Kcc4 associates with septin proteins of Saccharomyces cerevisiae."
      Okuzaki D., Nojima H.
      FEBS Lett. 489:197-201(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPTIN PROTEINS, SUBCELLULAR LOCATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
      Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
      Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "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-675; SER-822 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-396; SER-707; SER-777 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKCC4_YEAST
    AccessioniPrimary (citable) accession number: P25389
    Secondary accession number(s): D6VQZ2, P87005, Q8NKJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: June 27, 2003
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 538 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3