P87050 · CDR2_SCHPO

Function

function

Acts as a mitotic inducer. In G2 it negatively regulates wee1, a mitotic inhibitor. Also has a role in cytokinesis where it required for proper septum formation.

Catalytic activity

Features

Showing features for binding site, active site.

1775100200300400500600700
TypeIDPosition(s)Description
Binding site16-24ATP (UniProtKB | ChEBI)
Binding site39ATP (UniProtKB | ChEBI)
Active site133Proton acceptor

GO annotations

AspectTerm
Cellular ComponentCdr2 medial cortical node complex
Cellular Componentcytoplasm
Cellular Componentmedial cortex
Cellular Componentmedial cortical node
Cellular Componentmitotic spindle pole body
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionprotein-membrane adaptor activity
Molecular Functionsignaling adaptor activity
Biological Processcell division
Biological Processmitotic G2 cell size control checkpoint signaling
Biological Processpositive regulation of G2/M transition of mitotic cell cycle
Biological Processpositive regulation of protein localization to medial cortical node
Biological Processprotein phosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Mitosis inducer protein kinase cdr2
  • EC number

Gene names

    • Name
      cdr2
    • ORF names
      SPAC57A10.02

Organism names

Accessions

  • Primary accession
    P87050

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000858451-775Mitosis inducer protein kinase cdr2
Modified residue309Phosphoserine
Modified residue311Phosphoserine
Modified residue476Phosphoserine
Modified residue587Phosphoserine
Modified residue632Phosphoserine

Post-translational modification

Autophosphorylated.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with blt1 and mid1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P87050pom1 Q096902EBI-4319869, EBI-4319163

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain10-262Protein kinase
Compositional bias549-593Polar residues
Region549-620Disordered
Compositional bias600-618Polar residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    775
  • Mass (Da)
    85,972
  • Last updated
    1997-07-01 v1
  • Checksum
    2EE2EECABC8A4FAC
MSTISEVGPWELGLSLGSGGPNSSRLAKHRETGQLAVVKPIVGWSELTSSQQARIEGELVLLRLIEHPNVLQLIDVISAQEQLFVVVEYMPGGELFDCMLRKGSFTEQDTAKFLWQILCGLEYCHKLHICHRDLKPENLYLDAHGSIKIGEFGMASIQQPGKLLQTSCGSPHYASPEIIMGRSYDGCASDIWSCGIIFFALLTGKLPFDDDNIRSLLLKVCQGQFEMPSNISPQAQHLLYRMLDVDSSTRITMEQIREHPFLSCFVHPNISIPIISAPIQPIDPLIVQHLSLVFRCSDDPMPLYEKLASQSPLVEKTLYTLLSRHLHPPSSAAVDRNRAVVDDLLGTAASNGQQMDEEEIEQAINIPTLAPYPISYAAESVPRPATSASPFLTPVTTSGTFNYSFNATNPQSILQRPATTSSAVPQLPKSVTPGLAYPHDSSMLSSNYRPPSALSPRNFNVSINDPEVQLSRRATSLDMSNDFRMNENDPSIVGNLAASNFPTGMGPPRKRVTSRMSEHTGNRVVSFPRGSAFNPRVTRFNVGNEQFSNNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDSLNVPKHRRRQSLFSPSSTKKKLSGSPFQPKRSFLRRLFSSEPSCKCVYASLVASELEHEILEVLRRWQLLGIGIADIIYDSVSASISARIKRQNSLNLKPVRFRISVLAEFFGSQAVFVLESGSSTTFDHLATEFQLIFEDKGFLDNLELSYFQASASRPVSRMSVSSSPFAVFRQRQSVQS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias549-593Polar residues
Compositional bias600-618Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329670
EMBL· GenBank· DDBJ
CAB08165.1
EMBL· GenBank· DDBJ
Genomic DNA
AF092508
EMBL· GenBank· DDBJ
AAC72832.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp