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Conserved domains on  [gi|1207734412|ref|NP_001339479|]
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tyrosine-protein phosphatase non-receptor type 20 isoform 25 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 51-72 1.07e-08

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


The actual alignment was detected with superfamily member cd14538:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 207  Bit Score: 49.29  E-value: 1.07e-08
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14538   173 FDIQDIVKDLREQRQGMIQTKD 194
 
Name Accession Description Interval E-value
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 51-72 1.07e-08

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 49.29  E-value: 1.07e-08
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14538   173 FDIQDIVKDLREQRQGMIQTKD 194
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
51-72 1.57e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 40.72  E-value: 1.57e-05
                           10        20
                   ....*....|....*....|..
gi 1207734412   51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:smart00194 227 VDIFEIVKELRSQRPGMVQTEE 248
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
51-72 1.48e-04

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 37.99  E-value: 1.48e-04
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:pfam00102 202 VDIFQIVKELRSQRPGMVQTLE 223
 
Name Accession Description Interval E-value
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 51-72 1.07e-08

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 49.29  E-value: 1.07e-08
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14538   173 FDIQDIVKDLREQRQGMIQTKD 194
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 51-72 2.75e-08

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 48.20  E-value: 2.75e-08
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14596   172 FNIKDIVREMRQQRYGMIQTKD 193
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
51-72 1.57e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 40.72  E-value: 1.57e-05
                           10        20
                   ....*....|....*....|..
gi 1207734412   51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:smart00194 227 VDIFEIVKELRSQRPGMVQTEE 248
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 51-72 9.02e-05

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: 38.81  E-value: 9.02e-05
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd00047   172 VDVFEIVKALRKQRPGMVQTLE 193
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
51-72 1.48e-04

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 37.99  E-value: 1.48e-04
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:pfam00102 202 VDIFQIVKELRSQRPGMVQTLE 223
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 51-72 1.52e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 38.17  E-value: 1.52e-04
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14542   174 FSLFDLVREMRKQRPAMVQTKE 195
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 35-70 1.87e-04

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 37.61  E-value: 1.87e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1207734412  35 MRRLQGHHRLSPLYFLFN--IMDIVAQMREQRSGMVQT 70
Cdd:cd18533   166 LDELKRGLSDSQDLEDSEdpVYEIVNQLRKQRMSMVQT 203
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
51-72 7.45e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 35.03  E-value: 7.45e-04
                           10        20
                   ....*....|....*....|..
gi 1207734412   51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:smart00404  73 VDIFDTVKELRSQRPGMVQTEE 94
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 51-72 7.45e-04

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: 35.03  E-value: 7.45e-04
                           10        20
                   ....*....|....*....|..
gi 1207734412   51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:smart00012  73 VDIFDTVKELRSQRPGMVQTEE 94
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 51-72 8.72e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 35.96  E-value: 8.72e-04
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14597   200 FDISDIVRTMRLQRHGMVQTED 221
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 51-72 1.43e-03

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: 35.57  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|..
gi 1207734412  51 FNIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14603   232 FSIFDVVLEMRKQRPAAVQTEE 253
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 52-72 1.70e-03

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: 35.06  E-value: 1.70e-03
                          10        20
                  ....*....|....*....|.
gi 1207734412  52 NIMDIVAQMREQRSGMVQTKE 72
Cdd:cd14547   197 DVLGIVCQLRLDRGGMVQTAE 217
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 54-78 6.90e-03

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 33.57  E-value: 6.90e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1207734412  54 MDIVA---QMREQRSGMVQTKE-----LSSVAE 78
Cdd:cd14546   173 IDIAAtleHLRDQRPGMVKTKDqfefvLTAVAE 205
 
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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