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Conserved domains on  [gi|1054487231|ref|NP_001317102|]
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cyclin-dependent kinase inhibitor 3 isoform 3 [Homo sapiens]

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 5.93e-118

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: 331.99  E-value: 5.93e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231   1 MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 1054487231 161 TISPEQAI 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 5.93e-118

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: 331.99  E-value: 5.93e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231   1 MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 1054487231 161 TISPEQAI 168
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-184 2.62e-82

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: 241.40  E-value: 2.62e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  29 ISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPI 108
Cdd:cd14505     1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054487231 109 ADGGTPD-IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGsGAIQTIK 184
Cdd:cd14505    81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPK 156
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-182 2.13e-21

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 85.41  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  62 KDTEELKSCGIQDIFVFCTRGELskyrvpnLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCY 141
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1054487231 142 GGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAIQT 182
Cdd:COG2453    89 GGIGRTGTVAAAYLVLLG--LSAEEALARVRAAR-PGAVET 126
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
104-183 1.65e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 42.35  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  104 HHHPIADGGTPD----IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSC-LVAACLLLYL----SDTISPEQAIDSLRDL 174
Cdd:smart00404   6 HYTGWPDHGVPEspdsILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELRSQ 85


                   ....*....
gi 1054487231  175 RgSGAIQTI 183
Cdd:smart00404  86 R-PGMVQTE 93
PRK12361 PRK12361
hypothetical protein; Provisional
 107-177 6.03e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.07  E-value: 6.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054487231 107 PIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGS 177
Cdd:PRK12361  149 PILDHSVPTLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIRKT 219
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 5.93e-118

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: 331.99  E-value: 5.93e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231   1 MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 1054487231 161 TISPEQAI 168
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-184 2.62e-82

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: 241.40  E-value: 2.62e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  29 ISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPI 108
Cdd:cd14505     1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054487231 109 ADGGTPD-IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGsGAIQTIK 184
Cdd:cd14505    81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPK 156
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-182 2.13e-21

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 85.41  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  62 KDTEELKSCGIQDIFVFCTRGELskyrvpnLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCY 141
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1054487231 142 GGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAIQT 182
Cdd:COG2453    89 GGIGRTGTVAAAYLVLLG--LSAEEALARVRAAR-PGAVET 126
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 41-186 2.96e-16

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: 71.23  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  41 QFLGLCALPGCkfkdvrrNVQKDTEELKSCGIQDIFVFCTrgelskyrvpnlldlyqqcgiithhhpiadggtpdiASCC 120
Cdd:cd14494     7 LRLIAGALPLS-------PLEADSRFLKQLGVTTIVDLTL------------------------------------AMVD 43

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054487231 121 EIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDtISPEQAIDSLRDLRGSGAIQTIKDL 186
Cdd:cd14494    44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGG-MSAEEAVRIVRLIRPGGIPQTIEQL 108
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 87-184 7.76e-12

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: 60.37  E-value: 7.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  87 YRVPNLlDLYQQCGIITHHHPIADGGTP---DIASCCEIMEElttCLKNYRKTLIHCYGGLGRSCLVAACLLLYlSDTIS 163
Cdd:cd14504    37 EEPPPE-HSDTCPGLRYHHIPIEDYTPPtleQIDEFLDIVEE---ANAKNEAVLVHCLAGKGRTGTMLACYLVK-TGKIS 111

                          90       100
                  ....*....|....*....|.
gi 1054487231 164 PEQAIDSLRDLRGsGAIQTIK 184
Cdd:cd14504   112 AVDAINEIRRIRP-GSIETSE 131
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 65-182 3.36e-11

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: 60.06  E-value: 3.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  65 EELKSCGIQDIF--------VFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKT 136
Cdd:cd14506    33 EQFKEKGIKTVInlqepgehASCGPGLEPESGFSYLPEAFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKV 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1054487231 137 LIHCYGGLGRSCLVAACLLLYLSDtISPEQAIDSLRDLRgSGAIQT 182
Cdd:cd14506   113 AVHCHAGLGRTGVLIACYLVYALR-MSADQAIRLVRSKR-PNSIQT 156
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 62-175 1.03e-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: 51.78  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  62 KDTEELKSCGIQdiFVFCTRGELSKYRVPnlldlyqqcGIITHHH-PIADGGTPDIAS----CCEIMEElttCLKNYRKT 136
Cdd:cd14498    17 QDKELLKKLGIT--HILNVAGEPPPNKFP---------DGIKYLRiPIEDSPDEDILShfeeAIEFIEE---ALKKGGKV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1054487231 137 LIHCYGGLGRSC-LVAACLLLYLSdtISPEQAIDSLRDLR 175
Cdd:cd14498    83 LVHCQAGVSRSAtIVIAYLMKKYG--WSLEEALELVKSRR 120
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 96-175 1.66e-06

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: 46.10  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  96 YQQCGIITHHHPIAD-GGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYlSDTISPEQAIDSLRDL 174
Cdd:cd14524    51 WKALGVEQLRLPTVDfTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQ-HKGWSPEEAQEFLRSK 129


                  .
gi 1054487231 175 R 175
Cdd:cd14524   130 R 130
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 83-180 4.59e-06

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: 44.90  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  83 ELSKYRVPNLL---------DLYQQCGIITHHHPIADGGTPDIasccEIMEE----LTTCLKNYRKTL----IHCYGGLG 145
Cdd:cd14500    32 ELKKYNVTDLVrvceptydkEPLEKAGIKVHDWPFDDGSPPPD----DVVDDwldlLKTRFKEEGKPGaciaVHCVAGLG 107

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1054487231 146 RS-CLVAACLLLYlsdTISPEQAIDSLRDLRgSGAI 180
Cdd:cd14500   108 RApVLVAIALIEL---GMKPEDAVEFIRKKR-RGAI 139
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
104-183 1.65e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 42.35  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  104 HHHPIADGGTPD----IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSC-LVAACLLLYL----SDTISPEQAIDSLRDL 174
Cdd:smart00404   6 HYTGWPDHGVPEspdsILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELRSQ 85


                   ....*....
gi 1054487231  175 RgSGAIQTI 183
Cdd:smart00404  86 R-PGMVQTE 93
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 104-183 1.65e-05

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: 42.35  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  104 HHHPIADGGTPD----IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSC-LVAACLLLYL----SDTISPEQAIDSLRDL 174
Cdd:smart00012   6 HYTGWPDHGVPEspdsILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELRSQ 85


                   ....*....
gi 1054487231  175 RgSGAIQTI 183
Cdd:smart00012  86 R-PGMVQTE 93
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 107-175 5.64e-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: 41.49  E-value: 5.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054487231 107 PIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLR 175
Cdd:cd14527    50 PLLDLVAPTPEQLERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWLLAYGRAKSVAEAEALIRAAR 118
PRK12361 PRK12361
hypothetical protein; Provisional
 107-177 6.03e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.07  E-value: 6.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054487231 107 PIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGS 177
Cdd:PRK12361  149 PILDHSVPTLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIRKT 219
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 83-180 1.65e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 40.39  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  83 ELSKYRVPNLL---------DLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTL----IHCYGGLGRS-C 148
Cdd:PTZ00242   35 ELQRYNVTHLVrvcgptydaELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQSTPPetiaVHCVAGLGRApI 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1054487231 149 LVAACLLLYlsDTISPEQAIDSLRDLRgSGAI 180
Cdd:PTZ00242  115 LVALALVEY--GGMEPLDAVGFVREKR-KGAI 143
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
74-183 3.15e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 40.34  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231   74 DIFVFCTRGELSKYRVPNLLDL-YQQCG---IITHHHPIA--DGGTPDIASCC-EIMEELTTCLKNYRK-TLIHCYGGLG 145
Cdd:smart00194 127 DITVTLKSVEKVDDYTIRTLEVtNTGCSetrTVTHYHYTNwpDHGVPESPESIlDLIRAVRKSQSTSTGpIVVHCSAGVG 206

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1054487231  146 RS-CLVAACLLLYL---SDTISPEQAIDSLRDLRgSGAIQTI 183
Cdd:smart00194 207 RTgTFIAIDILLQQleaGKEVDIFEIVKELRSQR-PGMVQTE 247
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
113-177 3.54e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.19  E-value: 3.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054487231  113 TPDIASCCEIMEElttCLKNYRKTLIHCYGGLGRS-CLVAACLLLYLSdtISPEQAIDSLRDLRGS 177
Cdd:smart00195  61 SPYFPEAVEFIED---AESKGGKVLVHCQAGVSRSaTLIIAYLMKTRN--MSLNDAYDFVKDRRPI 121
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 65-180 3.93e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 39.92  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  65 EELKSCGIQDIFVFCTR----GELskyrvpnlldlyQQCGIITHHHPIADGGTP--DIAScceimEELTTC---LKNYRK 135
Cdd:PTZ00393  110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVS-----NWLTIVnnvIKNNRA 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1054487231 136 TLIHCYGGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAI 180
Cdd:PTZ00393  173 VAVHCVAGLGRAPVLASIVLIEFG--MDPIDAIVFIRDRR-KGAI 214
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 137-169 1.58e-03

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: 37.56  E-value: 1.58e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1054487231 137 LIHCYGGLGRSCLVAACLLLYLSDTISPEQAID 169
Cdd:cd14497    99 VVHCKAGKGRTGTVICAYLLYYGQYSTADEALE 131
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 61-172 2.80e-03

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: 36.97  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  61 QKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLyqqcGIITHHHPIaDGGTPDIA---SCCEIMEELTtclkNYRKTL 137
Cdd:cd14529    23 DEDRALLKKLGIKTVIDLRGADERAASEEAAAKID----GVKYVNLPL-SATRPTESdvqSFLLIMDLKL----APGPVL 93

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1054487231 138 IHCYGGLGRSCLVAA-CLLLYlsdTISPEQAIDSLR 172
Cdd:cd14529    94 IHCKHGKDRTGLVSAlYRIVY---GGSKEEANEDYR 126
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 116-169 3.28e-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: 36.80  E-value: 3.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054487231 116 IASCCEIMEE-LTTCLKNYrkTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAID 169
Cdd:cd14509    78 IKPFCEDVDEwLKEDEKNV--AAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALD 130
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 128-177 4.38e-03

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: 35.70  E-value: 4.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054487231 128 TCLKNYRKTLIHCYGGLGRS-CLVAACLLLYLSdtISPEQAIDSLRDLRGS 177
Cdd:pfam00782  64 DARQKGGKVLVHCQAGISRSaTLIIAYLMKTRN--LSLNEAYSFVKERRPG 112
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 58-175 5.29e-03

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: 36.02  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231  58 RNVQkDTEELKSCGIQDIFVFCTRGELSKYRV--PNLLDLYQQCGIITHHHPIADGGTPD----IASCCEIMEELttcLK 131
Cdd:cd14526    17 QNPE-DVDRLKKEGVTAVLNLQTDSDMEYWGVdiDSIRKACKESGIRYVRLPIRDFDTEDlrqkLPQAVALLYRL---LK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1054487231 132 NYRKTLIHCYGGLGRSCLVaACLLLYLSDTISPEQAIDSLRDLR 175
Cdd:cd14526    93 NGGTVYVHCTAGLGRAPAT-VIAYLYWVLGYSLDEAYYLLTSKR 135
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 101-182 5.41e-03

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: 36.49  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054487231 101 IITHHHPIA--DGGTPDiaSCCEIMEELTTCLKNYRK----TLIHCYGGLGRS----CLVAACLLLYLSDTISPEQAIDS 170
Cdd:cd00047   103 EVTHLHYTGwpDHGVPS--SPEDLLALVRRVRKEARKpngpIVVHCSAGVGRTgtfiAIDILLERLEAEGEVDVFEIVKA 180

                          90
                  ....*....|..
gi 1054487231 171 LRDLRgSGAIQT 182
Cdd:cd00047   181 LRKQR-PGMVQT 191
 
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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