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Q92398

- SPM1_SCHPO

UniProt

Q92398 - SPM1_SCHPO

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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

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

Mg2+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. MAP kinase activity involved in cell wall organization or biogenesis Source: PomBase
  4. protein kinase activity Source: PomBase

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular sodium ion homeostasis Source: PomBase
  3. MAPK cascade Source: PomBase
  4. MAPK cascade involved in cell wall organization or biogenesis Source: PomBase
  5. positive regulation of calcium ion transport into cytosol Source: PomBase
  6. positive regulation of calcium-mediated signaling Source: PomBase
  7. positive regulation of sequence-specific DNA binding transcription factor activity Source: PomBase
  8. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

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.
ReactomeiREACT_231661. ERKs are inactivated.
REACT_260281. ERK/MAPK targets.
REACT_269633. Signalling to ERK5.

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
Complete GO annotation...

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.
InParanoidiQ92398.
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.
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

        10         20         30         40         50
MDRRHRVYRV FNQEMYVEPN FKVVKELGQG AYGIVCAARN VASKDQEAVA
60 70 80 90 100
IKKITNVFSK SILTKRALRE IKLLIHFRNH RNITCIYDLD IINPYNFNEV
110 120 130 140 150
YIYEELMEAD LNAIIKSGQP LTDAHFQSFI YQILCGLKYI HSANVIHRDL
160 170 180 190 200
KPGNLLVNAD CELKICDFGL ARGCSENPEE NPGFMTEYVA TRWYRAPEIM
210 220 230 240 250
LSFSSYHKGI DVWSVGCILA ELLGGTPLFK GKDFVHQLNL ILHQLGTPDE
260 270 280 290 300
ETLSHISSSR AQEYVRSLPK QRPIPFETNF PKANPLALDL LAKLLAFDPN
310 320 330 340 350
RRISVDDALE HPYLAVWHDP SDEPVCDSVF DFSFEYIEDA NELRRVILDE
360 370 380 390 400
VLNFRQKVRR RSHPTNPTVN IPQPAQTVPS NDNGSFNVSS SSSSQTSNKK
410 420
RHDHSYNETA AIDHKSDDNR HN
Length:422
Mass (Da):48,262
Last modified:February 1, 1997 - v1
Checksum:iFD02521E64E8BF82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q92398.
KOi K04464.
OMAi FMPKKPF.
OrthoDBi EOG7K3TWD.
PhylomeDBi Q92398.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 5615.
Reactomei REACT_231661. ERKs are inactivated.
REACT_260281. ERK/MAPK targets.
REACT_269633. Signalling to ERK5.

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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 134 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