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Conserved domains on  [gi|1907105538|ref|XP_036014748|]
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cyclin-dependent kinase inhibitor 3 isoform X1 [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1-139 3.65e-98

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member pfam05706:

Pssm-ID: 475123  Cd Length: 168  Bit Score: 282.30  E-value: 3.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105538   1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105538  81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIQ 139
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIH 139
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-139 3.65e-98

Cyclin-dependent kinase inhibitor 3 (CDKN3); 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.


Pssm-ID: 399018  Cd Length: 168  Bit Score: 282.30  E-value: 3.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105538   1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105538  81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIQ 139
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIH 139
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-138 2.68e-51

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 163.20  E-value: 2.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105538  29 ISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPI 108
Cdd:cd14505     1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907105538 109 PDGGTPD-IGSCWEIMEELATCLKNNRKTLI 138
Cdd:cd14505    81 PDGGVPSdIAQWQELLEELLSALENGKKVLI 111
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-138 1.85e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.43  E-value: 1.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907105538  62 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLI 138
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLV 85
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-139 3.65e-98

Cyclin-dependent kinase inhibitor 3 (CDKN3); 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.


Pssm-ID: 399018  Cd Length: 168  Bit Score: 282.30  E-value: 3.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105538   1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105538  81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIQ 139
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIH 139
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-138 2.68e-51

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 163.20  E-value: 2.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105538  29 ISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPI 108
Cdd:cd14505     1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907105538 109 PDGGTPD-IGSCWEIMEELATCLKNNRKTLI 138
Cdd:cd14505    81 PDGGVPSdIAQWQELLEELLSALENGKKVLI 111
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-138 1.85e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.43  E-value: 1.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907105538  62 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLI 138
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLV 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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