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Conserved domains on  [gi|1002623453|ref|NP_001307612|]
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tyrosine-protein phosphatase non-receptor type 20 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc super family cl33376
Protein tyrosine phosphatase, catalytic domain;
159-197 6.92e-05

Protein tyrosine phosphatase, catalytic domain;


The actual alignment was detected with superfamily member smart00194:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 42.65  E-value: 6.92e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002623453  159 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPFQH 197
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDH 41
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
159-197 6.92e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 42.65  E-value: 6.92e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002623453  159 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPFQH 197
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDH 41
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 159-197 4.62e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 40.43  E-value: 4.62e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1002623453 159 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPFQH 197
Cdd:cd14543     5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQ 43
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
159-197 6.92e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 42.65  E-value: 6.92e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002623453  159 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPFQH 197
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDH 41
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 159-197 4.62e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 40.43  E-value: 4.62e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1002623453 159 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPFQH 197
Cdd:cd14543     5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQ 43
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 176-197 8.10e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 36.45  E-value: 8.10e-03
                          10        20
                  ....*....|....*....|..
gi 1002623453 176 NSGNQPSNREKNRYRDILPFQH 197
Cdd:cd14604    50 ATGEKEENVKKNRYKDILPFDH 71
 
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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