P87050 · CDR2_SCHPO
- ProteinMitosis inducer protein kinase cdr2
- Genecdr2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids775 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Cdr2 medial cortical node complex | |
Cellular Component | cytoplasm | |
Cellular Component | medial cortex | |
Cellular Component | medial cortical node | |
Cellular Component | mitotic spindle pole body | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein-membrane adaptor activity | |
Molecular Function | signaling adaptor activity | |
Biological Process | cell division | |
Biological Process | mitotic G2 cell size control checkpoint signaling | |
Biological Process | positive regulation of G2/M transition of mitotic cell cycle | |
Biological Process | positive regulation of protein localization to medial cortical node | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitosis inducer protein kinase cdr2
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP87050
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000085845 | 1-775 | Mitosis inducer protein kinase cdr2 | |||
Sequence: MSTISEVGPWELGLSLGSGGPNSSRLAKHRETGQLAVVKPIVGWSELTSSQQARIEGELVLLRLIEHPNVLQLIDVISAQEQLFVVVEYMPGGELFDCMLRKGSFTEQDTAKFLWQILCGLEYCHKLHICHRDLKPENLYLDAHGSIKIGEFGMASIQQPGKLLQTSCGSPHYASPEIIMGRSYDGCASDIWSCGIIFFALLTGKLPFDDDNIRSLLLKVCQGQFEMPSNISPQAQHLLYRMLDVDSSTRITMEQIREHPFLSCFVHPNISIPIISAPIQPIDPLIVQHLSLVFRCSDDPMPLYEKLASQSPLVEKTLYTLLSRHLHPPSSAAVDRNRAVVDDLLGTAASNGQQMDEEEIEQAINIPTLAPYPISYAAESVPRPATSASPFLTPVTTSGTFNYSFNATNPQSILQRPATTSSAVPQLPKSVTPGLAYPHDSSMLSSNYRPPSALSPRNFNVSINDPEVQLSRRATSLDMSNDFRMNENDPSIVGNLAASNFPTGMGPPRKRVTSRMSEHTGNRVVSFPRGSAFNPRVTRFNVGNEQFSNNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDSLNVPKHRRRQSLFSPSSTKKKLSGSPFQPKRSFLRRLFSSEPSCKCVYASLVASELEHEILEVLRRWQLLGIGIADIIYDSVSASISARIKRQNSLNLKPVRFRISVLAEFFGSQAVFVLESGSSTTFDHLATEFQLIFEDKGFLDNLELSYFQASASRPVSRMSVSSSPFAVFRQRQSVQS | ||||||
Modified residue | 309 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 311 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 476 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 587 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 632 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with blt1 and mid1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P87050 | pom1 Q09690 | 2 | EBI-4319869, EBI-4319163 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-262 | Protein kinase | ||||
Sequence: WELGLSLGSGGPNSSRLAKHRETGQLAVVKPIVGWSELTSSQQARIEGELVLLRLIEHPNVLQLIDVISAQEQLFVVVEYMPGGELFDCMLRKGSFTEQDTAKFLWQILCGLEYCHKLHICHRDLKPENLYLDAHGSIKIGEFGMASIQQPGKLLQTSCGSPHYASPEIIMGRSYDGCASDIWSCGIIFFALLTGKLPFDDDNIRSLLLKVCQGQFEMPSNISPQAQHLLYRMLDVDSSTRITMEQIREHPFL | ||||||
Compositional bias | 549-593 | Polar residues | ||||
Sequence: NNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDS | ||||||
Region | 549-620 | Disordered | ||||
Sequence: NNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDSLNVPKHRRRQSLFSPSSTKKKLSGSPF | ||||||
Compositional bias | 600-618 | Polar residues | ||||
Sequence: RRRQSLFSPSSTKKKLSGS |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length775
- Mass (Da)85,972
- Last updated1997-07-01 v1
- Checksum2EE2EECABC8A4FAC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 549-593 | Polar residues | ||||
Sequence: NNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDS | ||||||
Compositional bias | 600-618 | Polar residues | ||||
Sequence: RRRQSLFSPSSTKKKLSGS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329670 EMBL· GenBank· DDBJ | CAB08165.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF092508 EMBL· GenBank· DDBJ | AAC72832.1 EMBL· GenBank· DDBJ | Genomic DNA |