P32944 · SWE1_YEAST
- ProteinMitosis inhibitor protein kinase SWE1
- GeneSWE1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids819 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in growth, actin organization or bud formation. Inhibits the activity of B-type cyclins in replication initiation strongly for CLB2, moderately for CLB3 and CLB4, and there is no apparent inhibition for CLB5 and CLB6, correlating with the normal expression timing of those cyclins. Hyperphosphorylation and degradation of SWE1 when all checkpoint requirement are met releases CLB2-CDC28 from inhibition and allows for progression through the cell cycle. SWE1-dependent CDC28 phosphorylation is also required for pachytene arrest upon activation of the recombination checkpoint during meiosis. Also involved in the regulation of nitrogen starvation- and short chain alcohol-induced filamentous growth, or filamentous differentiation in response to slowed DNA synthesis. Can act both on serines and on tyrosines.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cellular bud neck | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein tyrosine kinase activity | |
Biological Process | cell division | |
Biological Process | G2/M transition of mitotic cell cycle | |
Biological Process | meiotic cell cycle | |
Biological Process | mitotic morphogenesis checkpoint signaling | |
Biological Process | negative regulation of G2/MI transition of meiotic cell cycle | |
Biological Process | negative regulation of mitotic spindle pole body separation | |
Biological Process | positive regulation of sphingolipid biosynthetic process | |
Biological Process | re-entry into mitotic cell cycle | |
Biological Process | regulation of cell size | |
Biological Process | regulation of meiotic nuclear division |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitosis inhibitor protein kinase SWE1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32944
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 318-328 | Impairs interaction with HSL7 and prevents bud neck localization and degradation. | ||||
Sequence: Missing | ||||||
Mutagenesis | 320 | Prevents degradation. | ||||
Sequence: L → P or Q | ||||||
Mutagenesis | 324 | Prevents degradation. | ||||
Sequence: L → S | ||||||
Mutagenesis | 327 | Prevents degradation. | ||||
Sequence: F → S | ||||||
Mutagenesis | 328 | Prevents degradation. | ||||
Sequence: K → E | ||||||
Mutagenesis | 331 | Prevents degradation. | ||||
Sequence: L → I | ||||||
Mutagenesis | 332 | Prevents degradation. | ||||
Sequence: Y → C | ||||||
Mutagenesis | 473 | Loss of catalytic activity. | ||||
Sequence: K → A or P | ||||||
Mutagenesis | 797 | Prevents degradation. | ||||
Sequence: E → K, V, or G | ||||||
Mutagenesis | 806 | Prevents degradation. | ||||
Sequence: I → T, A, or N | ||||||
Mutagenesis | 807 | Prevents degradation. | ||||
Sequence: Q → R or E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086727 | 1-819 | Mitosis inhibitor protein kinase SWE1 | |||
Sequence: MSSLDEDEEDFEMLDTENLQFMGKKMFGKQAGEDESDDFAIGGSTPTNKLKFYPYSNNKLTRSTGTLNLSLSNTALSEANSKFLGKIEEEEEEEEEGKDEESVDSRIKRWSPFHENESVTTPITKRSAEKTNSPISLKQWNQRWFPKNDARTENTSSSSSYSVAKPNQSAFTSSGLVSKMSMDTSLYPAKLRIPETPVKKSPLVEGRDHKHVHLSSSKNASSSLSVSPLNFVEDNNLQEDLLFSDSPSSKALPSIHVPTIDSSPLSEAKYHAHDRHNNQTNILSPTNSLVTNSSPQTLHSNKFKKIKRARNSVILKNRELTNSLQQFKDDLYGTDENFPPPIIISSHHSTRKNPQPYQFRGRYDNDTDEEISTPTRRKSIIGATSQTHRESRPLSLSSAIVTNTTSAETHSISSTDSSPLNSKRRLISSNKLSANPDSHLFEKFTNVHSIGKGQFSTVYQVTFAQTNKKYAIKAIKPNKYNSLKRILLEIKILNEVTNQITMDQEGKEYIIDYISSWKFQNSYYIMTELCENGNLDGFLQEQVIAKKKRLEDWRIWKIIVELSLALRFIHDSCHIVHLDLKPANVMITFEGNLKLGDFGMATHLPLEDKSFENEGDREYIAPEIISDCTYDYKADIFSLGLMIVEIAANVVLPDNGNAWHKLRSGDLSDAGRLSSTDIHSESLFSDITKVDTNDLFDFERDNISGNSNNAGTSTVHNNSNINNPNMNNGNDNNNVNTAATKNRLILHKSSKIPAWVPKFLIDGESLERIVRWMIEPNYERRPTANQILQTEECLYVEMTRNAGAIIQEDDFGPKPKFFI | ||||||
Modified residue | 36 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 45 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 56 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 63 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 70 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 74 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 102 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 105 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 111 | Phosphoserine; by CDC5, CDC28 and CLA4 | ||||
Sequence: S | ||||||
Modified residue | 118 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 121 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 124 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 127 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 131 | Phosphothreonine; by CDC5 | ||||
Sequence: T | ||||||
Modified residue | 133 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 136 | Phosphoserine; by CDC28 and CLA4 | ||||
Sequence: S | ||||||
Modified residue | 156 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 169 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 196 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 201 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 225 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 254 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 262 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 263 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 266 | Phosphoserine; by CDC28 | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphothreonine; by CDC5 | ||||
Sequence: T | ||||||
Modified residue | 284 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 294 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 312 | Phosphoserine; by CLA4 | ||||
Sequence: S | ||||||
Modified residue | 345 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 367 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 373 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 379 | Phosphoserine; by CDC5 and CLA4 | ||||
Sequence: S | ||||||
Modified residue | 384 | Phosphothreonine; by CDC28 | ||||
Sequence: T | ||||||
Modified residue | 395 | Phosphoserine; by CDC5 and CLA4 | ||||
Sequence: S | ||||||
Modified residue | 438 | Phosphoserine; by CDC5 and CLA4 | ||||
Sequence: S | ||||||
Modified residue | 610 | Phosphoserine; by CDC5 | ||||
Sequence: S | ||||||
Modified residue | 629 | Phosphothreonine; by CDC5 | ||||
Sequence: T | ||||||
Modified residue | 688 | Phosphothreonine; by CDC5 and CLA4 | ||||
Sequence: T | ||||||
Modified residue | 692 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 741 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by the SCF(MET30) complex, leading to its degradation by the proteasome.
Phosphorylated progressively by CLA4, CLB2-CDC28 and CDC5. CLA4-dependent phosphorylation occurs in late S phase, followed by phosphorylation by CLB2-CDC28 in early G2, when the levels of mitotic CLB2 increases. This phosphorylation is critical for triggering subsequent SWE1-CDC5 interaction and CDC5-dependent phosphorylation. The resulting cumulative hyperphosphorylation down-regulates SWE1 by targeting it for ubiquitin-mediated degradation. This stepwise phosphorylation is thought to be a mechanism to integrate the different checkpoint requirements before entry into mitosis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Expressed periodically during the cell cycle, with a peak in late G1. Transcriptional repression requires ZDS1. Protein accumulation is also periodic, peaking during S/G2 and declining prior to and during nuclear division of the unperturbed cell cycle. Stabilized during a checkpoint response in G2. Induced during meiosis. Induced by ethanol (at protein level).
Interaction
Subunit
Interacts with CLB2-CDC28. Partial hyperphosphorylation of SWE1 by CLB2-CDC28 stabilizes the ternary complex of SWE1 and CLB2-CDC28 and stimulates kinase activity of SWE1 in a positive feedback loop, maintaining CLB2-CDC28 in the tyrosine-phosphorylated state. Fully hyperphosphorylated SWE1 dissociates from CLB2-CDC28. Interacts with HSL7, KCC4 and MET30.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P32944 | CDC14 Q00684 | 3 | EBI-18607, EBI-4192 | |
BINARY | P32944 | CDC5 P32562 | 4 | EBI-18607, EBI-4440 | |
BINARY | P32944 | HSL7 P38274 | 4 | EBI-18607, EBI-21618 | |
BINARY | P32944 | KIN1 P13185 | 3 | EBI-18607, EBI-9716 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 86-105 | Disordered | ||||
Sequence: KIEEEEEEEEEGKDEESVDS | ||||||
Region | 117-168 | Disordered | ||||
Sequence: ESVTTPITKRSAEKTNSPISLKQWNQRWFPKNDARTENTSSSSSYSVAKPNQ | ||||||
Region | 278-297 | Disordered | ||||
Sequence: NQTNILSPTNSLVTNSSPQT | ||||||
Region | 341-395 | Disordered | ||||
Sequence: PIIISSHHSTRKNPQPYQFRGRYDNDTDEEISTPTRRKSIIGATSQTHRESRPLS | ||||||
Compositional bias | 377-395 | Polar residues | ||||
Sequence: RKSIIGATSQTHRESRPLS | ||||||
Domain | 444-794 | Protein kinase | ||||
Sequence: FTNVHSIGKGQFSTVYQVTFAQTNKKYAIKAIKPNKYNSLKRILLEIKILNEVTNQITMDQEGKEYIIDYISSWKFQNSYYIMTELCENGNLDGFLQEQVIAKKKRLEDWRIWKIIVELSLALRFIHDSCHIVHLDLKPANVMITFEGNLKLGDFGMATHLPLEDKSFENEGDREYIAPEIISDCTYDYKADIFSLGLMIVEIAANVVLPDNGNAWHKLRSGDLSDAGRLSSTDIHSESLFSDITKVDTNDLFDFERDNISGNSNNAGTSTVHNNSNINNPNMNNGNDNNNVNTAATKNRLILHKSSKIPAWVPKFLIDGESLERIVRWMIEPNYERRPTANQILQTEECL | ||||||
Region | 707-736 | Disordered | ||||
Sequence: SNNAGTSTVHNNSNINNPNMNNGNDNNNVN |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length819
- Mass (Da)92,468
- Last updated1993-10-01 v1
- ChecksumF49FE73937958A02
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 377-395 | Polar residues | ||||
Sequence: RKSIIGATSQTHRESRPLS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X73966 EMBL· GenBank· DDBJ | CAA52150.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49462 EMBL· GenBank· DDBJ | CAA89482.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006943 EMBL· GenBank· DDBJ | DAA08619.1 EMBL· GenBank· DDBJ | Genomic DNA |