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Q92398

- SPM1_SCHPO

UniProt

Q92398 - SPM1_SCHPO

Protein

Mitogen-activated protein kinase spm1

Gene

spm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Regulates cell integrity and functions coordinately with the protein kinase C pathway (pck1 and pck2). Involved the regulation of wall architecture, cell shape, cytokinesis in exponential and stationary phase, and metabolism of ions.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation by skh1/pek1.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521ATPPROSITE-ProRule annotation
    Active sitei149 – 1491Proton 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. MAP kinase activity Source: PomBase
    3. protein binding Source: PomBase
    4. protein serine/threonine kinase activity Source: PomBase

    GO - Biological processi

    1. activation of bipolar cell growth Source: PomBase
    2. cellular sodium ion homeostasis Source: PomBase
    3. fungal-type cell wall organization or biogenesis Source: PomBase
    4. MAPK cascade Source: PomBase
    5. mitotic cytokinesis Source: PomBase
    6. positive regulation of calcium ion transport into cytosol Source: PomBase
    7. positive regulation of calcium-mediated signaling Source: PomBase
    8. regulation of cell shape Source: PomBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell shape

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 5615.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase spm1 (EC:2.7.11.24)
    Short name:
    MAP kinase spm1
    Alternative name(s):
    MAP kinase pmk1
    Gene namesi
    Name:spm1
    Synonyms:pmk1
    ORF Names:SPBC119.08
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC119.08.

    Subcellular locationi

    GO - Cellular componenti

    1. cell division site Source: PomBase
    2. cytoplasm Source: PomBase
    3. cytosol Source: PomBase
    4. mitotic spindle pole body Source: PomBase
    5. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422Mitogen-activated protein kinase spm1PRO_0000186341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei186 – 1861Phosphothreonine1 Publication
    Modified residuei188 – 1881Phosphotyrosine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-186 and Tyr-188, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92398.
    PaxDbiQ92398.

    Interactioni

    Protein-protein interaction databases

    BioGridi276464. 128 interactions.
    MINTiMINT-4701538.
    STRINGi4896.SPBC119.08-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 314294Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi186 – 1883TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi389 – 3946Poly-Ser

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    KOiK04464.
    OMAiFMPKKPF.
    OrthoDBiEOG7K3TWD.
    PhylomeDBiQ92398.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    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.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92398-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRRHRVYRV FNQEMYVEPN FKVVKELGQG AYGIVCAARN VASKDQEAVA    50
    IKKITNVFSK SILTKRALRE IKLLIHFRNH RNITCIYDLD IINPYNFNEV 100
    YIYEELMEAD LNAIIKSGQP LTDAHFQSFI YQILCGLKYI HSANVIHRDL 150
    KPGNLLVNAD CELKICDFGL ARGCSENPEE NPGFMTEYVA TRWYRAPEIM 200
    LSFSSYHKGI DVWSVGCILA ELLGGTPLFK GKDFVHQLNL ILHQLGTPDE 250
    ETLSHISSSR AQEYVRSLPK QRPIPFETNF PKANPLALDL LAKLLAFDPN 300
    RRISVDDALE HPYLAVWHDP SDEPVCDSVF DFSFEYIEDA NELRRVILDE 350
    VLNFRQKVRR RSHPTNPTVN IPQPAQTVPS NDNGSFNVSS SSSSQTSNKK 400
    RHDHSYNETA AIDHKSDDNR HN 422
    Length:422
    Mass (Da):48,262
    Last modified:February 1, 1997 - v1
    Checksum:iFD02521E64E8BF82
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98243 Genomic DNA. Translation: CAA66899.1.
    U65405 Genomic DNA. Translation: AAC49707.1.
    CU329671 Genomic DNA. Translation: CAA17923.1.
    PIRiT39306.
    RefSeqiNP_595289.1. NM_001021196.2.

    Genome annotation databases

    EnsemblFungiiSPBC119.08.1; SPBC119.08.1:pep; SPBC119.08.
    GeneIDi2539920.
    KEGGispo:SPBC119.08.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98243 Genomic DNA. Translation: CAA66899.1 .
    U65405 Genomic DNA. Translation: AAC49707.1 .
    CU329671 Genomic DNA. Translation: CAA17923.1 .
    PIRi T39306.
    RefSeqi NP_595289.1. NM_001021196.2.

    3D structure databases

    ProteinModelPortali Q92398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276464. 128 interactions.
    MINTi MINT-4701538.
    STRINGi 4896.SPBC119.08-1.

    Proteomic databases

    MaxQBi Q92398.
    PaxDbi Q92398.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC119.08.1 ; SPBC119.08.1:pep ; SPBC119.08 .
    GeneIDi 2539920.
    KEGGi spo:SPBC119.08.

    Organism-specific databases

    PomBasei SPBC119.08.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    KOi K04464.
    OMAi FMPKKPF.
    OrthoDBi EOG7K3TWD.
    PhylomeDBi Q92398.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 5615.

    Miscellaneous databases

    NextBioi 20801063.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    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 PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway."
      Toda T., Dhut S., Superti-Furga G., Gotoh G., Nishida E., Sugiura R., Kuno T.
      Mol. Cell. Biol. 16:6752-6764(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Spm1, a stress-activated MAP kinase that regulates morphogenesis in S.pombe."
      Zaitsevskaya-Carter T., Cooper J.A.
      EMBO J. 16:1318-1331(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186 AND TYR-188, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSPM1_SCHPO
    AccessioniPrimary (citable) accession number: Q92398
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3