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185  structures 2549  species 0  interactions 30506  sequences 426  architectures

Family: DSPc (PF00782)

Summary: Dual specificity phosphatase, catalytic domain

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This is the Wikipedia entry entitled "Protein tyrosine phosphatase". More...

Protein tyrosine phosphatase Edit Wikipedia article

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Dual specificity phosphatase, catalytic domain Provide feedback

Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region [2].

Literature references

  1. Fauman EB, Saper MA; , Trends Biochem Sci 1996;21:413-417.: Structure and function of the protein tyrosine phosphatases. PUBMED:8987394 EPMC:8987394

  2. Yuvaniyama J, Denu JM, Dixon JE, Saper MA; , Science 1996;272:1328-1331.: Crystal structure of the dual specificity protein phosphatase VHR. PUBMED:8650541 EPMC:8650541

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000340

Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [ PUBMED:9818190 , PUBMED:14625689 ]. The PTP superfamily can be divided into four subfamilies [ PUBMED:12678841 ]:

  • (1) pTyr-specific phosphatases
  • (2) dual specificity phosphatases (dTyr and dSer/dThr)
  • (3) Cdc25 phosphatases (dTyr and/or dThr)
  • (4) LMW (low molecular weight) phosphatases

Based on their cellular localisation, PTPases are also classified as:

  • Receptor-like, which are transmembrane receptors that contain PTPase domains [ PUBMED:16672235 ]
  • Non-receptor (intracellular) PTPases [ PUBMED:8948575 ]

All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif [ PUBMED:9646865 ]. Functional diversity between PTPases is endowed by regulatory domains and subunits.

This entry represents dual specificity protein-tyrosine phosphatases. Ser/Thr and Tyr dual specificity phosphatases are a group of enzymes with both Ser/Thr ( EC ) and tyrosine specific protein phosphatase ( EC ) activity able to remove both the serine/threonine or tyrosine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. The crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), has been determined at 2.1 angstrom resolution [ PUBMED:8650541 ]. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region" connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.

These proteins may also have inactive phosphatase domains, and dependent on the domain composition this loss of catalytic activity has different effects on protein function. Inactive single domain phosphatases can still specifically bind substrates, and protect again dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. There is a region of higher conservation common to both classes, suggesting a new regulatory centre [ PUBMED:14739250 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Phosphatase (CL0031), which has the following description:

This family includes tyrosine and dual specificity phosphatase enzymes.

The clan contains the following 16 members:

BLH_phosphatase CDKN3 DSPc DSPn Init_tRNA_PT LMWPc Myotub-related NleF_casp_inhib PTPlike_phytase PTS_IIB Rhodanese Ssu72 Syja_N Y_phosphatase Y_phosphatase2 Y_phosphatase3


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Alignment kindly provided by SMART
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: SMART
Number in seed: 22
Number in full: 30506
Average length of the domain: 127.00 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 28.33 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 33.5 33.5
Trusted cut-off 33.5 33.5
Noise cut-off 33.4 33.4
Model length: 133
Family (HMM) version: 23
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DSPc domain has been found. There are 185 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2K3I9 View 3D Structure Click here
A0A0G2K9N1 View 3D Structure Click here
A0A0G2KB18 View 3D Structure Click here
A0A0G2KHQ4 View 3D Structure Click here
A0A0R0IF22 View 3D Structure Click here
A0A0R0JYL8 View 3D Structure Click here
A0A0R0KQX0 View 3D Structure Click here
A0A0R4I9C9 View 3D Structure Click here
A0A0R4IE73 View 3D Structure Click here
A0A0R4IS50 View 3D Structure Click here
A0A0R4IVA4 View 3D Structure Click here
A0A140LFT0 View 3D Structure Click here
A0A1D6EGX8 View 3D Structure Click here
A0A1D6EIJ0 View 3D Structure Click here
A0A1D6FVL3 View 3D Structure Click here
A0A1D6G824 View 3D Structure Click here
A0A1D6HIH3 View 3D Structure Click here
A0A1D6J5K0 View 3D Structure Click here
A0A1D6JKL8 View 3D Structure Click here
A0A1D6LHJ0 View 3D Structure Click here
A0A1D6LHJ1 View 3D Structure Click here
A0A1D6MAJ2 View 3D Structure Click here
A0A1D6MRW0 View 3D Structure Click here
A0A1D6ND14 View 3D Structure Click here
A0A1D8PDD7 View 3D Structure Click here
A0A1D8PMG3 View 3D Structure Click here
A0A1D8PQQ6 View 3D Structure Click here
A0A1D8PSH7 View 3D Structure Click here
A0A2R8PZ11 View 3D Structure Click here
A0A2R8Q350 View 3D Structure Click here
A0A2R8Q8Q6 View 3D Structure Click here
A0A2R8QCJ8 View 3D Structure Click here
A0A2R8QLM5 View 3D Structure Click here
A0A2R8QM14 View 3D Structure Click here
A0A2R8QMW0 View 3D Structure Click here
A0A2R8QPP3 View 3D Structure Click here
A0A2R8RMV8 View 3D Structure Click here
A0A2R8RXU6 View 3D Structure Click here
A0JMM1 View 3D Structure Click here
A1EC97 View 3D Structure Click here