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Conserved domains on  [gi|1334928298|ref|NP_001346970|]
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cyclin-dependent kinase inhibitor 3 isoform 1 [Mus musculus]

Protein Classification

CDKN3 domain-containing protein( domain architecture ID 10529699)

CDKN3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 9.14e-122

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: 342.00  E-value: 9.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298   1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 1334928298 161 SISPQQAI 168
Cdd:pfam05706 161 SISPEQAI 168
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 9.14e-122

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: 342.00  E-value: 9.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298   1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 1334928298 161 SISPQQAI 168
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-191 8.06e-86

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: 250.64  E-value: 8.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  29 ISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPI 108
Cdd:cd14505     1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGsGAIQTIKQYN 187
Cdd:cd14505    81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPKQEN 159


                  ....
gi 1334928298 188 YLHE 191
Cdd:cd14505   160 FLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-196 6.78e-27

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 100.05  E-value: 6.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  62 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 141
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298 142 GGLGRSCLVAACLLLYLsdSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 196
Cdd:COG2453    89 GGIGRTGTVAAAYLVLL--GLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
104-191 1.69e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 53.13  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  104 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRSC-LVAACLLLYL----SDSISPQQAIDSLR 172
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 1334928298  173 DVRgSGAIQTIKQYNYLHE 191
Cdd:smart00404  84 SQR-PGMVQTEEQYLFLYR 101
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 65-195 2.34e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 55.32  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  65 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 138
Cdd:PTZ00393  110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1334928298 139 HCYGGLGRSCLVAACLLLYLsdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 195
Cdd:PTZ00393  176 HCVAGLGRAPVLASIVLIEF--GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 9.14e-122

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: 342.00  E-value: 9.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298   1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 1334928298 161 SISPQQAI 168
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-191 8.06e-86

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: 250.64  E-value: 8.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  29 ISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPI 108
Cdd:cd14505     1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGsGAIQTIKQYN 187
Cdd:cd14505    81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPKQEN 159


                  ....
gi 1334928298 188 YLHE 191
Cdd:cd14505   160 FLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-196 6.78e-27

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 100.05  E-value: 6.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  62 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 141
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298 142 GGLGRSCLVAACLLLYLsdSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 196
Cdd:COG2453    89 GGIGRTGTVAAAYLVLL--GLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 41-191 8.30e-17

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.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 72.77  E-value: 8.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  41 QFLGLCALPGCkfkdvrrNIQKDTEELKSYGIQDVFVFCtrgelskyrvpnLLDLYqqygivthhhpipdggtpdigscw 120
Cdd:cd14494     7 LRLIAGALPLS-------PLEADSRFLKQLGVTTIVDLT------------LAMVD------------------------ 43

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334928298 121 EIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDsISPQQAIDSLRDVRGSGAIQTIKQYNYLHE 191
Cdd:cd14494    44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGG-MSAEEAVRIVRLIRPGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 87-192 2.56e-14

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 67.30  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  87 YRVPNLlDLYQQYGIVTHHHPIPDGGTP---DIGSCWEIMEElatCLKNNRKTLIHCYGGLGRSCLVAACLLLYlSDSIS 163
Cdd:cd14504    37 EEPPPE-HSDTCPGLRYHHIPIEDYTPPtleQIDEFLDIVEE---ANAKNEAVLVHCLAGKGRTGTMLACYLVK-TGKIS 111

                          90       100
                  ....*....|....*....|....*....
gi 1334928298 164 PQQAIDSLRDVRGsGAIQTIKQYNYLHEF 192
Cdd:cd14504   112 AVDAINEIRRIRP-GSIETSEQEKFVIQF 139
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 65-192 3.41e-14

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 68.14  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  65 EELKSYGIQDVF--------VFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKT 136
Cdd:cd14506    33 EQFKEKGIKTVInlqepgehASCGPGLEPESGFSYLPEAFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKV 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1334928298 137 LIHCYGGLGRSCLVAACLLLYLSDsISPQQAIDSLRDVRgSGAIQTIKQYNYLHEF 192
Cdd:cd14506   113 AVHCHAGLGRTGVLIACYLVYALR-MSADQAIRLVRSKR-PNSIQTRGQVLCVREF 166
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 59-195 1.58e-09

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 54.53  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  59 NIQKDTEELKSYGIQDVFVFCTRgelsKYRVPNLLDLyqqyGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKT 136
Cdd:cd14500    25 NLPLYIKELKKYNVTDLVRVCEP----TYDKEPLEKA----GIKVHDWPFDDGSPPpdDVVDDW--LDLLKTRFKEEGKP 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334928298 137 L----IHCYGGLGRS-CLVAACLLLYlsdSISPQQAIDSLRDVRgSGAIqTIKQYNYLHEFRDK 195
Cdd:cd14500    95 GaciaVHCVAGLGRApVLVAIALIEL---GMKPEDAVEFIRKKR-RGAI-NSKQLQFLEKYKPK 153
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
104-191 1.69e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 53.13  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  104 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRSC-LVAACLLLYL----SDSISPQQAIDSLR 172
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 1334928298  173 DVRgSGAIQTIKQYNYLHE 191
Cdd:smart00404  84 SQR-PGMVQTEEQYLFLYR 101
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 104-191 1.69e-09

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 53.13  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  104 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRSC-LVAACLLLYL----SDSISPQQAIDSLR 172
Cdd:smart00012   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 1334928298  173 DVRgSGAIQTIKQYNYLHE 191
Cdd:smart00012  84 SQR-PGMVQTEEQYLFLYR 101
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 65-195 2.34e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 55.32  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  65 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 138
Cdd:PTZ00393  110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1334928298 139 HCYGGLGRSCLVAACLLLYLsdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 195
Cdd:PTZ00393  176 HCVAGLGRAPVLASIVLIEF--GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 62-175 3.50e-08

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 50.24  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  62 KDTEELKSYGIQdvFVFCTRGELSKYRVPNlldlyqqyGIVTHHHPIPDGGTPDIGS----CWEIMEElatCLKNNRKTL 137
Cdd:cd14498    17 QDKELLKKLGIT--HILNVAGEPPPNKFPD--------GIKYLRIPIEDSPDEDILShfeeAIEFIEE---ALKKGGKVL 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1334928298 138 IHCYGGLGRSC-LVAACLLLYLsdSISPQQAIDSLRDVR 175
Cdd:cd14498    84 VHCQAGVSRSAtIVIAYLMKKY--GWSLEEALELVKSRR 120
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
101-191 6.82e-08

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 51.51  E-value: 6.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  101 IVTHHHPI--PDGGTP-DIGSCWEIMEELATCLKNNRK-TLIHCYGGLGRS-CLVAACLLLYL---SDSISPQQAIDSLR 172
Cdd:smart00194 158 TVTHYHYTnwPDHGVPeSPESILDLIRAVRKSQSTSTGpIVVHCSAGVGRTgTFIAIDILLQQleaGKEVDIFEIVKELR 237

                           90
                   ....*....|....*....
gi 1334928298  173 DVRgSGAIQTIKQYNYLHE 191
Cdd:smart00194 238 SQR-PGMVQTEEQYIFLYR 255
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 101-191 5.51e-07

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 48.05  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 101 IVTHHHPI--PDGGTPDIGScwEIMEELA----TCLKNNRKTLIHCYGGLGRS----CLVAACLLLYLSDSISPQQAIDS 170
Cdd:cd00047   103 EVTHLHYTgwPDHGVPSSPE--DLLALVRrvrkEARKPNGPIVVHCSAGVGRTgtfiAIDILLERLEAEGEVDVFEIVKA 180

                          90       100
                  ....*....|....*....|.
gi 1334928298 171 LRDVRgSGAIQTIKQYNYLHE 191
Cdd:cd00047   181 LRKQR-PGMVQTLEQYEFIYE 200
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 96-195 7.36e-07

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 46.87  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  96 YQQYGIVTHHHPIPD-GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYlSDSISPQQAIDSLRDV 174
Cdd:cd14524    51 WKALGVEQLRLPTVDfTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQ-HKGWSPEEAQEFLRSK 129

                          90       100
                  ....*....|....*....|.
gi 1334928298 175 RGSGAIQTiKQYNYLHEFRDK 195
Cdd:cd14524   130 RPHILLRL-SQREVLEEFYRK 149
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 83-193 9.11e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 46.94  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  83 ELSKYRVPNLL---------DLYQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTL----IHCYGGLGRS 147
Cdd:PTZ00242   35 ELQRYNVTHLVrvcgptydaELLEKNGIEVHDWPFDDGAPPpkAVIDNW--LRLLDQEFAKQSTPPetiaVHCVAGLGRA 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1334928298 148 -CLVAACLLLYlsDSISPQQAIDSLRDVRgSGAIQtIKQYNYLHEFR 193
Cdd:PTZ00242  113 pILVALALVEY--GGMEPLDAVGFVREKR-KGAIN-QTQLQFLKKYK 155
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
102-191 2.66e-06

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 46.47  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 102 VTHHHPI--PDGGTP-DIGSCWEIMEELATCLKNNRKT--LIHCYGGLGRS-CLVAACLLLYL---SDSISPQQAIDSLR 172
Cdd:pfam00102 133 VKHFHYTgwPDHGVPeSPNSLLDLLRKVRKSSLDGRSGpiVVHCSAGIGRTgTFIAIDIALQQleaEGEVDIFQIVKELR 212

                          90
                  ....*....|....*....
gi 1334928298 173 DVRGsGAIQTIKQYNYLHE 191
Cdd:pfam00102 213 SQRP-GMVQTLEQYIFLYD 230
PRK12361 PRK12361
hypothetical protein; Provisional
 131-195 5.88e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 46.15  E-value: 5.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298 131 KNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTiKQYNYLHEFRDK 195
Cdd:PRK12361  173 RANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIRKTARLNK-RQLRALEKMLEQ 236
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
113-177 1.03e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.81  E-value: 1.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298  113 TPDIGSCWEIMEElatCLKNNRKTLIHCYGGLGRSCLVAACLLLYlSDSISPQQAIDSLRDVRGS 177
Cdd:smart00195  61 SPYFPEAVEFIED---AESKGGKVLVHCQAGVSRSATLIIAYLMK-TRNMSLNDAYDFVKDRRPI 121
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 86-169 1.38e-05

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 43.72  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  86 KYRVPNL----LDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLK--NNRKTLIHCYGGLGRSCLVAACLLLYLS 159
Cdd:cd14497    42 HYMIFNLseeeYDDDSKFEGRVLHYGFPDHHPPPLGLLLEIVDDIDSWLSedPNNVAVVHCKAGKGRTGTVICAYLLYYG 121

                          90
                  ....*....|
gi 1334928298 160 DSISPQQAID 169
Cdd:cd14497   122 QYSTADEALE 131
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 123-175 2.16e-05

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 42.65  E-value: 2.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1334928298 123 MEELAtclKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVR 175
Cdd:cd14527    69 IEELR---AQGGPVLVHCALGYGRSATVVAAWLLAYGRAKSVAEAEALIRAAR 118
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 65-195 3.26e-05

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 42.70  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  65 EELKSYGIQDVFVFCtrgELSKYRVPnlldlYQQYGIVTHHHPIPDGGTP--DIGSCWEIMEELATCLKNNRKTLIHCYG 142
Cdd:cd18535    31 EDLKKYGATTVVRVC---EVTYDKTP-----LEKDGITVVDWPFDDGAPPpgKVVEDWLSLLKTKFCEDPGCCVAVHCVA 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1334928298 143 GLGRSCLVAACLLlyLSDSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDK 195
Cdd:cd18535   103 GLGRAPVLVALAL--IESGMKYEDAIQFIRQKR-RGAINS-KQLTYLEKYRPK 151
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 58-158 3.90e-05

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 42.18  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  58 RNIQkDTEELKSYGIQDVFVFCTRGELSKYRV--PNLLDLYQQYGIVTHHHPIPDGGTPD----IGSCWEIMEELatcLK 131
Cdd:cd14526    17 QNPE-DVDRLKKEGVTAVLNLQTDSDMEYWGVdiDSIRKACKESGIRYVRLPIRDFDTEDlrqkLPQAVALLYRL---LK 92

                          90       100
                  ....*....|....*....|....*..
gi 1334928298 132 NNRKTLIHCYGGLGRSCLVaACLLLYL 158
Cdd:cd14526    93 NGGTVYVHCTAGLGRAPAT-VIAYLYW 118
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 60-196 6.02e-05

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 41.91  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  60 IQKDTEELKSYGIQDVFVFCTrgelSKYRVPnlldLYQQYGIVTHHHPIPDGGTP--DIGSCW------EIMEELATCLK 131
Cdd:cd18536    27 LNKFTEELKKYGVTTLVRVCD----ATYDKA----PVEKEGIQVLDWPFDDGAPPpnQIVDDWlnllktKFREEPGCCVA 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298 132 nnrktlIHCYGGLGRSCLVAACLLLYLsdSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDKL 196
Cdd:cd18536    99 ------VHCVAGLGRAPVLVALALIEC--GMKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 153
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 109-190 8.38e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 42.12  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTPDIGSCWEIMEELATCLKNNRKT--LIHCYGGLGRS---CLVAACLLLYLSDSISPQ----QAIDSLRDVRGSgA 179
Cdd:cd14603   170 PDHGIPDSPDCMLAMIELARRLQGSGPEplCVHCSAGCGRTgviCTVDYVRQLLLTQRIPPDfsifDVVLEMRKQRPA-A 248

                          90
                  ....*....|.
gi 1334928298 180 IQTIKQYNYLH 190
Cdd:cd14603   249 VQTEEQYEFLY 259
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 61-199 8.40e-05

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 41.21  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  61 QKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLyqqyGIVTHHHPIPDGGTPDIGscwEIMEELATCLKNNRK-TLIH 139
Cdd:cd14529    23 DEDRALLKKLGIKTVIDLRGADERAASEEAAAKID----GVKYVNLPLSATRPTESD---VQSFLLIMDLKLAPGpVLIH 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298 140 CYGGLGRSCLVAA-CLLLYlsdSISPQQAIDSLRdvRGSGAIQTIKQYNYLHE----FRDKLAAY 199
Cdd:cd14529    96 CKHGKDRTGLVSAlYRIVY---GGSKEEANEDYR--LSNRHLEGLRSGIALDSkggvKGRYLAAY 155
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 54-191 1.14e-04

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 41.62  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  54 KDVRRNIQKDTEELKSYGIQdvfvfcTRGELSKYRVPnlldlyqqygiVTHHHPIPDGGTpdIGScwEIMEELATCLKNN 133
Cdd:cd14559    89 KKTGKDELVDGLKADMYNLK------ITDGNKTITIP-----------VVHVTNWPDHTA--ISS--EGLKELADLVNKS 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 134 RKT---------------------LIHCYGGLGRS-CLVAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHE 191
Cdd:cd14559   148 AEEkrnfykskgssaindknkllpVIHCRAGVGRTgQLAAAMELNKSPNNLSVEDIVSDMRTSRNGKMVQKDEQLDTLKE 227
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 126-177 1.20e-04

Dual specificity phosphatase, catalytic domain; 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.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 40.32  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1334928298 126 LATCLKNNRKTLIHCYGGLGRS-CLVAACLLLYLSDSISpqQAIDSLRDVRGS 177
Cdd:pfam00782  62 IDDARQKGGKVLVHCQAGISRSaTLIIAYLMKTRNLSLN--EAYSFVKERRPG 112
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 109-190 2.67e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 40.59  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTPDigsCWEIMEELATCLKNNRKT-------LIHCYGGLGRS-CLVAA---CLLLYLSDSISPQQAIDSLRDVRGs 177
Cdd:cd14612   153 PDHQTPE---SAGPLLRLVAEVEESRQTaaspgpiVVHCSAGIGRTgCFIATsigCQQLKDTGKVDILGIVCQLRLDRG- 228

                          90
                  ....*....|...
gi 1334928298 178 GAIQTIKQYNYLH 190
Cdd:cd14612   229 GMIQTSEQYQFLH 241
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 109-190 2.94e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 40.52  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTP-DIGSCWEIMEEL---------ATCLKN-NRKTLIHCYGGLGRSCLVAAC-LLLYLSDS---ISPQQAIDSLRD 173
Cdd:cd14540   117 PDHGCPeDVSGFLDFLEEInsvrrhtnqDVAGHNrNPPTLVHCSAGVGRTGVVILAdLMLYCLDHneeLDIPRVLALLRH 196

                          90
                  ....*....|....*..
gi 1334928298 174 VRGSgAIQTIKQYNYLH 190
Cdd:cd14540   197 QRML-LVQTLAQYKFVY 212
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 60-196 3.56e-04

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 39.67  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  60 IQKDTEELKSYGIQDVFVFCTrgelSKYRVpnllDLYQQYGIVTHHHPIPDGGTPD--IGSCW------EIMEELATCLK 131
Cdd:cd18537    30 LNKFIEELKKYGVTTVVRVCE----ATYDT----TLVEKEGIQVLDWPFDDGAPPSnqIVDDWlnllkvKFREEPGCCIA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928298 132 nnrktlIHCYGGLGRSCLVAAclLLYLSDSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDKL 196
Cdd:cd18537   102 ------VHCVAGLGRAPVLVA--LALIECGMKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 156
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 109-190 9.04e-04

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 38.92  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTPDigsCWEIMEELATCLKNNRKT-------LIHCYGGLGRS-CLVAAclllylsdSISPQQ-----AIDSLRDV- 174
Cdd:cd14547   135 PDHKTPE---AAQPLLSLVQEVEEARQTephrgpiVVHCSAGIGRTgCFIAT--------SIGCQQlreegVVDVLGIVc 203

                          90       100
                  ....*....|....*....|.
gi 1334928298 175 -----RGsGAIQTIKQYNYLH 190
Cdd:cd14547   204 qlrldRG-GMVQTAEQYEFVH 223
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 72-169 1.20e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.95  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298  72 IQDVFVFCTRGELSKYRVPNLLDLYQQ-----YGIVTHHhPIPDGGTPDIGSCWEIMEELATCLKNNRKTL--IHCYGGL 144
Cdd:cd14509    27 IDDVQRFLETKHKGHYKVYNLCSERSYdpskfNGRVAEY-PFDDHNPPPLELIKPFCEDVDEWLKEDEKNVaaVHCKAGK 105

                          90       100
                  ....*....|....*....|....*
gi 1334928298 145 GRSCLVAACLLLYLSDSISPQQAID 169
Cdd:cd14509   106 GRTGVMICCYLLYLGKFPSAKEALD 130
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 102-190 2.33e-03

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 38.00  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 102 VTHHH--PIPDGGTPDIGSCW----EIMEELATCLKNNRKTLIHCYGGLGRSCLVAAclLLYLSDSISPQQAID------ 169
Cdd:cd14618   129 VKHLHytAWPDHGIPESTSSLmafrELVREHVQATKGKGPTLVHCSAGVGRSGTFIA--LDRLLRQLKEEKVVDvfntvy 206

                          90       100
                  ....*....|....*....|.
gi 1334928298 170 SLRDVRGSgAIQTIKQYNYLH 190
Cdd:cd14618   207 ILRMHRYL-MIQTLSQYIFLH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 109-190 5.69e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 36.76  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928298 109 PDGGTPD-----IGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLVAACLllyLSDSISPQQAIDSLRDV------RG 176
Cdd:cd14613   163 PDQKTPDnapplLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTgCFIATSI---CCKQLRNEGVVDILRTTcqlrldRG 239

                          90
                  ....*....|....
gi 1334928298 177 sGAIQTIKQYNYLH 190
Cdd:cd14613   240 -GMIQTCEQYQFVH 252
 
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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