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Conserved domains on  [gi|755571540|ref|NP_001291725|]
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dual specificity protein phosphatase 18 isoform b [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 19-55 1.64e-15

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 cd14573:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 158  Bit Score: 67.89  E-value: 1.64e-15
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755571540  19 GLSQITKSLYISNGVAANNKLMLSSNQITMVINVSVE 55
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLE 37
 
Name Accession Description Interval E-value
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 19-55 1.64e-15

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 67.89  E-value: 1.64e-15
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755571540  19 GLSQITKSLYISNGVAANNKLMLSSNQITMVINVSVE 55
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLE 37
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
21-70 5.23e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 34.18  E-value: 5.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 755571540    21 SQITKSLYISNGVAANNKLMLSSNQITMVINVSVERGDEAGPYFAALCCW 70
Cdd:smart00195   2 SEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVP 51
 
Name Accession Description Interval E-value
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 19-55 1.64e-15

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 67.89  E-value: 1.64e-15
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755571540  19 GLSQITKSLYISNGVAANNKLMLSSNQITMVINVSVE 55
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLE 37
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 20-58 2.94e-07

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 45.62  E-value: 2.94e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755571540  20 LSQITKSLYISNGVAANNKLMLSSNqITMVINVSVERGD 58
Cdd:cd14514    1 ISQITPHLFLSGASAATPPLLLSRG-ITCIINATTELPD 38
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 16-83 4.84e-07

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 45.63  E-value: 4.84e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755571540  16 SVSGLSQITKSLYISNGVAANNKLMLSSNQITMVINVSVERGDEAGPYFaalccwcEPLSCPVPRLPH 83
Cdd:cd14572    4 DLGGIAQITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQF-------EYVKVPLADMPH 64
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 21-62 5.47e-06

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: 42.53  E-value: 5.47e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755571540  21 SQITKSLYISNGVAANNKLMLSSNQITMVINVSVERGDEAGP 62
Cdd:cd14498    2 SEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFP 43
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
21-70 5.23e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 34.18  E-value: 5.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 755571540    21 SQITKSLYISNGVAANNKLMLSSNQITMVINVSVERGDEAGPYFAALCCW 70
Cdd:smart00195   2 SEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVP 51
 
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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