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Q9VPC0

- KP58_DROME

UniProt

Q9VPC0 - KP58_DROME

Protein

Serine/threonine-protein kinase PITSLRE

Gene

Pitslre

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Acts as a negative regulator of the normal cell cycle progression. May function in regulating proliferation by the phosphorylation and subsequent plasma membrane targeting of galactosyltransferase By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + a protein tyrosine = ADP + protein tyrosine phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei587 – 5871ATPPROSITE-ProRule annotation
    Active sitei685 – 6851Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi564 – 5729ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    3. protein serine/threonine kinase activity Source: FlyBase

    GO - Biological processi

    1. cell adhesion Source: FlyBase
    2. mitotic cell cycle Source: FlyBase
    3. protein phosphorylation Source: FlyBase
    4. regulation of cell shape Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 1994.
    SignaLinkiQ9VPC0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PITSLRE (EC:2.7.11.22)
    Alternative name(s):
    Cell division cycle 2-like
    Gene namesi
    Name:Pitslre
    ORF Names:CG4268
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0016696. Pitslre.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 952952Serine/threonine-protein kinase PITSLREPRO_0000086160Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei439 – 4391Phosphoserine1 Publication
    Modified residuei442 – 4421Phosphoserine1 Publication
    Modified residuei447 – 4471Phosphotyrosine1 Publication
    Modified residuei449 – 4491Phosphoserine1 Publication
    Modified residuei881 – 8811Phosphoserine1 Publication
    Modified residuei886 – 8861Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9VPC0.
    PRIDEiQ9VPC0.

    Expressioni

    Tissue specificityi

    Present throughout the early embryo. In late embryos levels are highest in the CNS.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically. Highest levels in early embryogenesis (0-6 hours), low levels during later embryogenesis, moderate levels in pupae and adults.1 Publication

    Gene expression databases

    BgeeiQ9VPC0.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9VPC0. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VPC0.
    SMRiQ9VPC0. Positions 555-885.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini558 – 851294Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi51 – 566Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi92 – 14655His-richAdd
    BLAST
    Compositional biasi386 – 504119Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114964.
    InParanoidiQ9VPC0.
    KOiK08818.
    OMAiFPGEVKC.
    OrthoDBiEOG74BJS4.
    PhylomeDBiQ9VPC0.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    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.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VPC0-1 [UniParc]FASTAAdd to Basket

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    MVNSSGSEDG QLRSPNDVHY HSRGEEDEHE GDADALYIQP PQASRESGSG    50
    PRREKKKHSR ERRRHKERDD VGGAALALER DHRYDYRSRE EHYHHHQRER 100
    SSNAAAAYAK HHLGHAYHYP QPPQQQQQPL PPAPSYAAHH YHHHQHLSGA 150
    RAAPREYHSY PSGYHSGSRH GDYPMEEPTR RSSKYAESKD AESLEQDLRS 200
    RLLKKRHNYV KDYETEENYE HRVERSDRRE GGRKERERTV RSTHKQNRHD 250
    RVIELLDSPE QEHHHQHQHK SHRSKWREEV EVIRRKVPED LELLARREKL 300
    LAAERESRQR KQTAREELEA RRELLRERNE HSDALSPTTV AASVTAGLNI 350
    HVKRKSKPDN YEKEIKLKKR REDDIEVIRD DDDEESEESD SNEEVPEQDS 400
    EGSATESGSE DSYASKKKSK IKSKSQLEDD DEDLPLPDSP LSVGELYKSP 450
    KQRQRSRSVS SKSSSQSSRS SRSRSRSRSQ SSLEDEVDRQ DVGADASPSS 500
    STRSEERGMT QEQPEEKPEE KLKEKQKSLE EQIPCDDKGI PLPNYYPGVQ 550
    GCRSVEEFQC LNRIEEGTYG VVYRAKDKRT NEIVALKRLK MEKEKEGFPI 600
    TSLREINTLL KGQHPNIVTV REIVVGSNMD KIFIVMDYVE HDLKSLMETM 650
    KNRKQSFFPG EVKCLTQQLL RAVAHLHDNW ILHRDLKTSN LLLSHKGILK 700
    VGDFGLAREY GSPIKKYTSL VVTLWYRAPE LLLCSPVYST PIDVWSVGCI 750
    FAEFLQMLPL FPGKSEIDEL NRIFKELGTP NEKIWPGYTE LPAVKNMLSQ 800
    NSQFTEYPVS QLRKHFQEKT SEMGLSLLQG LLTYDPKQRL SADAALKHGF 850
    FKELPLPIDP SMFPTWPAKS ELGARKAQAS SPKPPSGGSQ FKQLGRDEPI 900
    IVGPGNKLSS GIITGNKKSH GAGGSSASTG FVLNAGITQR QLAMGPGFSL 950
    KF 952
    Length:952
    Mass (Da):108,838
    Last modified:May 1, 2000 - v1
    Checksum:i9CBDE8D459D0713D
    GO

    Sequence cautioni

    The sequence AAM75018.1 differs from that shown. Reason: Intron retention.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691D → E in CAA67863. (PubMed:8930898)Curated
    Sequence conflicti223 – 2231V → A in CAA67863. (PubMed:8930898)Curated
    Sequence conflicti283 – 2831I → S in CAA67863. (PubMed:8930898)Curated
    Sequence conflicti492 – 4921V → A in CAA67863. (PubMed:8930898)Curated
    Sequence conflicti584 – 5841V → E(PubMed:1378625)Curated
    Sequence conflicti603 – 6031L → R(PubMed:1378625)Curated
    Sequence conflicti612 – 6121G → GG(PubMed:1378625)Curated
    Sequence conflicti670 – 6701Missing(PubMed:1378625)Curated
    Sequence conflicti680 – 6801Missing(PubMed:1378625)Curated
    Sequence conflicti717 – 7171Missing(PubMed:1378625)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99513 mRNA. Translation: CAA67863.1.
    AE014296 Genomic DNA. Translation: AAF51635.1.
    AE014296 Genomic DNA. Translation: AAN12141.1.
    BT016092 mRNA. Translation: AAV36977.1.
    AY128425 mRNA. Translation: AAM75018.1. Sequence problems.
    RefSeqiNP_001246851.1. NM_001259922.2.
    NP_001246852.1. NM_001259923.2.
    NP_001262122.1. NM_001275193.1.
    NP_649251.2. NM_140994.4.
    NP_730563.1. NM_168869.3.
    UniGeneiDm.1019.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078247; FBpp0077905; FBgn0016696.
    FBtr0078250; FBpp0077908; FBgn0016696.
    GeneIDi40292.
    KEGGidme:Dmel_CG4268.
    UCSCiCG4268-RC. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99513 mRNA. Translation: CAA67863.1 .
    AE014296 Genomic DNA. Translation: AAF51635.1 .
    AE014296 Genomic DNA. Translation: AAN12141.1 .
    BT016092 mRNA. Translation: AAV36977.1 .
    AY128425 mRNA. Translation: AAM75018.1 . Sequence problems.
    RefSeqi NP_001246851.1. NM_001259922.2.
    NP_001246852.1. NM_001259923.2.
    NP_001262122.1. NM_001275193.1.
    NP_649251.2. NM_140994.4.
    NP_730563.1. NM_168869.3.
    UniGenei Dm.1019.

    3D structure databases

    ProteinModelPortali Q9VPC0.
    SMRi Q9VPC0. Positions 555-885.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9VPC0. 2 interactions.

    Proteomic databases

    PaxDbi Q9VPC0.
    PRIDEi Q9VPC0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078247 ; FBpp0077905 ; FBgn0016696 .
    FBtr0078250 ; FBpp0077908 ; FBgn0016696 .
    GeneIDi 40292.
    KEGGi dme:Dmel_CG4268.
    UCSCi CG4268-RC. d. melanogaster.

    Organism-specific databases

    CTDi 40292.
    FlyBasei FBgn0016696. Pitslre.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114964.
    InParanoidi Q9VPC0.
    KOi K08818.
    OMAi FPGEVKC.
    OrthoDBi EOG74BJS4.
    PhylomeDBi Q9VPC0.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 1994.
    SignaLinki Q9VPC0.

    Miscellaneous databases

    GenomeRNAii 40292.
    NextBioi 818015.
    PROi Q9VPC0.

    Gene expression databases

    Bgeei Q9VPC0.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    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 PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel members of the cdc2-related kinase family in Drosophila: cdk4/6, cdk5, PFTAIRE, and PITSLRE kinase."
      Sauer K., Weigmann K., Sigrist S., Lehner C.F.
      Mol. Biol. Cell 7:1759-1769(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Embryo.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-952.
      Strain: Berkeley.
      Tissue: Head.
    6. "Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase."
      Biggs W.H. III, Zipursky S.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 571-722.
      Tissue: Imaginal disk.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-442; TYR-447; SER-449; SER-881 AND SER-886, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiKP58_DROME
    AccessioniPrimary (citable) accession number: Q9VPC0
    Secondary accession number(s): Q5U100
    , Q8MQR7, Q94889, Q9TXB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3