Summary: Cyclin-dependent kinase inhibitor 3 (CDKN3)
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Cyclin-dependent kinase inhibitor 3 (CDKN3) Provide feedback
This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner [1,2].
Yeh CT, Lu SC, Chen TC, Peng CY, Liaw YF; , Cancer Res 2000;60:4697-4700.: Aberrant transcripts of the cyclin-dependent kinase-associated protein phosphatase in hepatocellular carcinoma. PUBMED:10987270 EPMC:10987270
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR022778
This entry represents a domain found in cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner [PUBMED:8127873], [PUBMED:10987270]. This domain is also found in MAP kinase phosphatase and esterases.
This entry contains both eukaryotic and bacterial proteins.
|Molecular function||phosphoprotein phosphatase activity (GO:0004721)|
|protein tyrosine phosphatase activity (GO:0004725)|
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This family includes tyrosine and dual specificity phosphatase enzymes.
The clan contains the following 9 members:CDKN3 DSPc DUF442 Init_tRNA_PT Myotub-related PTPlike_phytase Y_phosphatase Y_phosphatase2 Y_phosphatase3
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Curation and family details
|Seed source:||Pfam-B_5217 (release 8.0)|
|Number in seed:||2|
|Number in full:||187|
|Average length of the domain:||132.60 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||62.73 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 CDKN3 domain has been found. There are 7 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 seqence.
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