P40048 · PTP3_YEAST
- ProteinTyrosine-protein phosphatase 3
- GenePTP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids928 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Major phosphatase responsible for tyrosine dephosphorylation of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has important roles, along with MSG5, in the inactivation of FUS3 following pheromone stimulation.
Miscellaneous
Present with 768 molecules/cell in log phase SD medium.
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 804 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | cellular hyperosmotic response | |
Biological Process | cytoplasmic sequestering of protein | |
Biological Process | fungal-type cell wall organization or biogenesis | |
Biological Process | negative regulation of cell wall integrity MAPK cascade | |
Biological Process | pheromone response MAPK cascade | |
Biological Process | regulation of sporulation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein phosphatase 3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40048
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094857 | 1-928 | Tyrosine-protein phosphatase 3 | |||
Sequence: MKDSVDCPSILPTDRTSVLSETSTLVGSSSHVYSRHAPMNSYHNSMNSNIYHSPKASSPLVSYKTSSPVLLKRATAPVLPSFKPKEQRYNKPQGCSLITAVELGKIIETLPDEKVLLLDVRPFTEHAKSIITNSIHVCLPSTLLRRKNFTFSKLLDNLTPSEQSVLKSKLAIDNLRIIIYDSTANQTESSVSLPCYGIASKLIEFDTNVKKTVSILMCGFPQFKILFPDHINTNTFNSDCISSAEPKSPKTNLMNSLHNTAPHMTATTPLSSPQMNLKLKVPDDSRSDHSNFSSSPSPRNVLSDSPMSSSSPISALFKFQLPAPQTNINQMFKFSQNEEIMGLETYLSAVNIKEEHERWYNNDSAKKSLQNFQFPKNQNSLEKDTNKDKLGFQIRYENLSKNYEKEVIDSVIPEWFQHLMSIPKIELVSQFQKLDFLEKRRLNHSVSFRKKENSFILEKPSSYPEQLTSTSSSTIMPPKFPDVNKVQKRSHSQPIFTQYSKYKSMLSLESDSDSESDDVIISSGVELGAKNRYKDIFPYEHSRVILKKGLQSSKGIKHSHSTSDGGILDNYINANYLSLPRFSVEQNSSFQTTTTTTRRVRYIATQAPMPSTVHDFYTCILNNGVPLVLSLTNDFENGIEKCYRYWQEGNYNGIHVKLLEKKILKMPSTTSMRKNTMGTQNSSLYSAGVQGNSSNYSTDNDNDNDNNNNNNNNSNIAVTAAACDDDDDDDDDAILIRKILLTYHDQEKPYELLQIQVKNWPDLGTLLNPISILQAINVKNHIIDTLFARNYYQNDQLPTILVHCSAGCGRTGTLCTIDSILSNFEMFEMLQKEFVKLKYPAKLFDPISWTINIFRKQRISMVQNINQFIFIYDCLLFYFRLRLDDITERTDGDGSNKDNISLSALIEQIEKLEILQTFVDDKLKELPQ | ||||||
Modified residue | 75 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 248 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 297 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 368 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 111-232 | Rhodanese | ||||
Sequence: PDEKVLLLDVRPFTEHAKSIITNSIHVCLPSTLLRRKNFTFSKLLDNLTPSEQSVLKSKLAIDNLRIIIYDSTANQTESSVSLPCYGIASKLIEFDTNVKKTVSILMCGFPQFKILFPDHIN | ||||||
Compositional bias | 247-275 | Polar residues | ||||
Sequence: KSPKTNLMNSLHNTAPHMTATTPLSSPQM | ||||||
Region | 247-307 | Disordered | ||||
Sequence: KSPKTNLMNSLHNTAPHMTATTPLSSPQMNLKLKVPDDSRSDHSNFSSSPSPRNVLSDSPM | ||||||
Compositional bias | 288-307 | Polar residues | ||||
Sequence: DHSNFSSSPSPRNVLSDSPM | ||||||
Region | 467-487 | Disordered | ||||
Sequence: LTSTSSSTIMPPKFPDVNKVQ | ||||||
Domain | 502-878 | Tyrosine-protein phosphatase | ||||
Sequence: YKSMLSLESDSDSESDDVIISSGVELGAKNRYKDIFPYEHSRVILKKGLQSSKGIKHSHSTSDGGILDNYINANYLSLPRFSVEQNSSFQTTTTTTRRVRYIATQAPMPSTVHDFYTCILNNGVPLVLSLTNDFENGIEKCYRYWQEGNYNGIHVKLLEKKILKMPSTTSMRKNTMGTQNSSLYSAGVQGNSSNYSTDNDNDNDNNNNNNNNSNIAVTAAACDDDDDDDDDAILIRKILLTYHDQEKPYELLQIQVKNWPDLGTLLNPISILQAINVKNHIIDTLFARNYYQNDQLPTILVHCSAGCGRTGTLCTIDSILSNFEMFEMLQKEFVKLKYPAKLFDPISWTINIFRKQRISMVQNINQFIFIYDCLLFY | ||||||
Region | 672-713 | Disordered | ||||
Sequence: MRKNTMGTQNSSLYSAGVQGNSSNYSTDNDNDNDNNNNNNNN |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length928
- Mass (Da)105,224
- Last updated2011-09-21 v2
- Checksum9BB710EDAF7E3940
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 247-275 | Polar residues | ||||
Sequence: KSPKTNLMNSLHNTAPHMTATTPLSSPQM | ||||||
Compositional bias | 288-307 | Polar residues | ||||
Sequence: DHSNFSSSPSPRNVLSDSPM | ||||||
Sequence conflict | 717 | in Ref. 1; AAB70811 and 2; AAB64614 | ||||
Sequence: A → P | ||||||
Sequence conflict | 738 | in Ref. 1; AAB70811 and 2; AAB64614 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 857 | in Ref. 1; AAB70811 and 2; AAB64614 | ||||
Sequence: Q → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF006304 EMBL· GenBank· DDBJ | AAB70811.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18814 EMBL· GenBank· DDBJ | AAB64614.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07735.2 EMBL· GenBank· DDBJ | Genomic DNA |