!!

Powering down the Pfam website
On October 5th, we will start redirecting the traffic from Pfam (pfam.xfam.org) to InterPro (www.ebi.ac.uk/interpro). The Pfam website will be available at pfam-legacy.xfam.org until January 2023, when it will be decommissioned. You can read more about the sunset period in our blog post.

Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
3314  structures 2018  species 0  interactions 212672  sequences 6511  architectures

Family: PK_Tyr_Ser-Thr (PF07714)

Summary: Protein tyrosine and serine/threonine kinase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Receptor tyrosine kinase". More...

Receptor tyrosine kinase Edit Wikipedia article

The Receptor Tyrosine Kinase (RTK) family of cell surface receptors shows a high affinity to numerous growth signals. Although numerous intracellular signaling pathways are shared following activation of the receptors by ligand, the responses may be tightly regulated by ligand-receptor specificity or through variations in responses to specific receptors – the one receptor may induce differing results following stimulation depending on the cell type in which the receptor is expressed.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Tyrosine kinase". More...

Tyrosine kinase Edit Wikipedia article

A tyrosine kinase is an enzyme that can transfer a phosphate group to a tyrosine residue in a protein. This is an important function in signal transduction to regulate enzyme activity.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Protein tyrosine and serine/threonine kinase Provide feedback

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.

Literature references

  1. Hanks SK, Quinn AM, Hunter T;, Science. 1988;241:42-52.: The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. PUBMED:3291115 EPMC:3291115

  2. Hanks SK, Quinn AM; , Methods Enzymol 1991;200:38-62.: Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. PUBMED:1956325 EPMC:1956325

  3. Hanks SK, Hunter T; , FASEB J 1995;9:576-596.: Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. PUBMED:7768349 EPMC:7768349

  4. Hunter T, Plowman GD; , Trends Biochem Sci 1997;22:18-22.: The protein kinases of budding yeast: six score and more. PUBMED:9020587 EPMC:9020587


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001245

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [ PUBMED:3291115 ]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function is evolutionarily conserved from Escherichia coli to human [ PUBMED:12471243 ]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [ PUBMED:12368087 ]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [ PUBMED:15078142 ], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [ PUBMED:15320712 ].

This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include catalytic domain of dual specificity kinases.

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...

Loading domain graphics...

Pfam Clan

This family is a member of clan PKinase (CL0016), which has the following description:

This superfamily includes the Serine/Threonine- and Tyrosine- protein kinases as well as related kinases that act on non-protein substrates.

The clan contains the following 40 members:

ABC1 AceK_kinase Act-Frag_cataly Alpha_kinase APH APH_6_hur Choline_kinase CotH DUF1679 DUF2252 DUF4135 DUF5898 EcKL Fam20C Fructosamin_kin FTA2 Haspin_kinase HipA_C Ins_P5_2-kin IPK IucA_IucC Kdo Kinase-like Kinase-PolyVal KIND Pan3_PK PI3_PI4_kinase PIP49_C PIP5K PK_Tyr_Ser-Thr Pkinase Pkinase_fungal Pox_ser-thr_kin RIO1 Seadorna_VP7 TCAD9 UL97 WaaY YrbL-PhoP_reg YukC

Alignments

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...

View options

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.

  Seed
(118)
Full
(212672)
Representative proteomes UniProt
(328726)
RP15
(37940)
RP35
(96298)
RP55
(175423)
RP75
(224916)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(118)
Full
(212672)
Representative proteomes UniProt
(328726)
RP15
(37940)
RP35
(96298)
RP55
(175423)
RP75
(224916)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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.

  Seed
(118)
Full
(212672)
Representative proteomes UniProt
(328726)
RP15
(37940)
RP35
(96298)
RP55
(175423)
RP75
(224916)
Raw Stockholm Download     Download   Download        
Gzipped Download     Download   Download        

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

HMM logo

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...

Trees

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: Unknown
Previous IDs: Pkinase_Tyr;
Type: Domain
Sequence Ontology: SO:0000417
Author: Studholme DJ
Number in seed: 118
Number in full: 212672
Average length of the domain: 234.3 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 34.58 %

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 23.1 23.1
Trusted cut-off 23.1 23.1
Noise cut-off 23.0 23.0
Model length: 259
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

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

Selections

Generate a FASTA-format file

Clear selection

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...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Structures

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 PK_Tyr_Ser-Thr domain has been found. There are 3314 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.

Loading structure mapping...

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
A0A044QUD1 View 3D Structure Click here
A0A044QX42 View 3D Structure Click here
A0A044QXE5 View 3D Structure Click here
A0A044R6Z3 View 3D Structure Click here
A0A044R7E2 View 3D Structure Click here
A0A044R7H0 View 3D Structure Click here
A0A044RAI2 View 3D Structure Click here
A0A044RBD4 View 3D Structure Click here
A0A044RJ14 View 3D Structure Click here
A0A044RJH9 View 3D Structure Click here
A0A044RM31 View 3D Structure Click here
A0A044S1R5 View 3D Structure Click here
A0A044SEN6 View 3D Structure Click here
A0A044SK90 View 3D Structure Click here
A0A044SLK7 View 3D Structure Click here
A0A044SSA9 View 3D Structure Click here
A0A044SSB7 View 3D Structure Click here
A0A044SUG6 View 3D Structure Click here
A0A044SXD4 View 3D Structure Click here
A0A044SZ66 View 3D Structure Click here
A0A044T2J4 View 3D Structure Click here
A0A044TAS9 View 3D Structure Click here
A0A044TBE7 View 3D Structure Click here
A0A044TDE5 View 3D Structure Click here
A0A044TPB0 View 3D Structure Click here
A0A044TV08 View 3D Structure Click here
A0A044TYG1 View 3D Structure Click here
A0A044UE07 View 3D Structure Click here
A0A044UIH6 View 3D Structure Click here
A0A044UP09 View 3D Structure Click here
A0A044UUJ7 View 3D Structure Click here
A0A044UX42 View 3D Structure Click here
A0A044UYX2 View 3D Structure Click here
A0A044V0E0 View 3D Structure Click here
A0A044V3J5 View 3D Structure Click here
A0A044V7E8 View 3D Structure Click here
A0A044V7G0 View 3D Structure Click here
A0A044V7H8 View 3D Structure Click here
A0A044V9F0 View 3D Structure Click here
A0A044VAP5 View 3D Structure Click here