P40048 · PTP3_YEAST

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

Features

Showing features for active site.

1928100200300400500600700800900
TypeIDPosition(s)Description
Active site804Phosphocysteine intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionprotein tyrosine phosphatase activity
Biological Processcellular hyperosmotic response
Biological Processcytoplasmic sequestering of protein
Biological Processfungal-type cell wall organization or biogenesis
Biological Processnegative regulation of cell wall integrity MAPK cascade
Biological Processpheromone response MAPK cascade
Biological Processregulation of sporulation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tyrosine-protein phosphatase 3
  • EC number
  • Alternative names
    • Protein-tyrosine phosphatase 3 (PTPase 3)

Gene names

    • Name
      PTP3
    • Ordered locus names
      YER075C

Organism names

Accessions

  • Primary accession
    P40048
  • Secondary accessions
    • D3DLY1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000948571-928Tyrosine-protein phosphatase 3
Modified residue75Phosphothreonine
Modified residue248Phosphoserine
Modified residue297Phosphoserine
Modified residue368Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with HOG1.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain111-232Rhodanese
Compositional bias247-275Polar residues
Region247-307Disordered
Compositional bias288-307Polar residues
Region467-487Disordered
Domain502-878Tyrosine-protein phosphatase
Region672-713Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    928
  • Mass (Da)
    105,224
  • Last updated
    2011-09-21 v2
  • Checksum
    9BB710EDAF7E3940
MKDSVDCPSILPTDRTSVLSETSTLVGSSSHVYSRHAPMNSYHNSMNSNIYHSPKASSPLVSYKTSSPVLLKRATAPVLPSFKPKEQRYNKPQGCSLITAVELGKIIETLPDEKVLLLDVRPFTEHAKSIITNSIHVCLPSTLLRRKNFTFSKLLDNLTPSEQSVLKSKLAIDNLRIIIYDSTANQTESSVSLPCYGIASKLIEFDTNVKKTVSILMCGFPQFKILFPDHINTNTFNSDCISSAEPKSPKTNLMNSLHNTAPHMTATTPLSSPQMNLKLKVPDDSRSDHSNFSSSPSPRNVLSDSPMSSSSPISALFKFQLPAPQTNINQMFKFSQNEEIMGLETYLSAVNIKEEHERWYNNDSAKKSLQNFQFPKNQNSLEKDTNKDKLGFQIRYENLSKNYEKEVIDSVIPEWFQHLMSIPKIELVSQFQKLDFLEKRRLNHSVSFRKKENSFILEKPSSYPEQLTSTSSSTIMPPKFPDVNKVQKRSHSQPIFTQYSKYKSMLSLESDSDSESDDVIISSGVELGAKNRYKDIFPYEHSRVILKKGLQSSKGIKHSHSTSDGGILDNYINANYLSLPRFSVEQNSSFQTTTTTTRRVRYIATQAPMPSTVHDFYTCILNNGVPLVLSLTNDFENGIEKCYRYWQEGNYNGIHVKLLEKKILKMPSTTSMRKNTMGTQNSSLYSAGVQGNSSNYSTDNDNDNDNNNNNNNNSNIAVTAAACDDDDDDDDDAILIRKILLTYHDQEKPYELLQIQVKNWPDLGTLLNPISILQAINVKNHIIDTLFARNYYQNDQLPTILVHCSAGCGRTGTLCTIDSILSNFEMFEMLQKEFVKLKYPAKLFDPISWTINIFRKQRISMVQNINQFIFIYDCLLFYFRLRLDDITERTDGDGSNKDNISLSALIEQIEKLEILQTFVDDKLKELPQ

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias247-275Polar residues
Compositional bias288-307Polar residues
Sequence conflict717in Ref. 1; AAB70811 and 2; AAB64614
Sequence conflict738in Ref. 1; AAB70811 and 2; AAB64614
Sequence conflict857in Ref. 1; AAB70811 and 2; AAB64614

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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