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Conserved domains on  [gi|1110938025|ref|XP_019213254|]
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protein phosphatase 1 regulatory subunit 1B isoform X2 [Oreochromis niloticus]

Protein Classification

DARPP-32 domain-containing protein( domain architecture ID 10526785)

DARPP-32 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DARPP-32 pfam05395
Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein ...
12-147 8.82e-64

Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein phosphatase inhibitor 1 (IPP-1) and dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32) proteins. Protein phosphatase inhibitor-1 is involved in signal transduction and is an endogenous inhibitor of protein phosphatase-1. It has been demonstrated that DARPP-32, if phosphorylated, can inhibit protein-phosphatase-1. DARPP-32 has a key role in many neurotransmitter pathways throughout the brain and has been shown to be involved in controlling receptors, ion channels and other physiological factors including the brain's response to drugs of abuse, such as cocaine, opiates and nicotine. DARPP-32 is reciprocally regulated by the two neurotransmitters that are most often implicated in schizophrenia - dopamine and glutamate. Dopamine activates DARPP-32 through the D1 receptor pathway and disables DARPP-32 through the D2 receptor. Glutamate, acting through the N-methyl-d-aspartate receptor, renders DARPP-32 inactive. A mutant form of DARPP-32 has been linked with gastric cancers.


:

Pssm-ID: 428454  Cd Length: 136  Bit Score: 193.13  E-value: 8.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110938025  12 EPKERKKIQFAVPANaPTNLDPRQVEMIRRRRPTPATLFRVADQSSPEDDQSTHQWVVGENGVLKPKRVNPNVYQPPSLK 91
Cdd:pfam05395   1 EPKERKKIQFAVPAP-PSQLDPRQVEMIRRRRPTPATLFRVSDQSSPEDEQSSHQWVVGENGILKPKRRNPCVYTPPSLK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1110938025  92 AVQKMAEAHMQKLGVYPPLEDPCEGEEDEDYLKGEEG-EDAAPTKAADRQETAATEQ 147
Cdd:pfam05395  80 AVQRMAEAHMQKLGVYPNLEDPPEGQEEEDELGEPEGnEDSPPTSGEEGEEEESEEE 136
 
Name Accession Description Interval E-value
DARPP-32 pfam05395
Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein ...
12-147 8.82e-64

Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein phosphatase inhibitor 1 (IPP-1) and dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32) proteins. Protein phosphatase inhibitor-1 is involved in signal transduction and is an endogenous inhibitor of protein phosphatase-1. It has been demonstrated that DARPP-32, if phosphorylated, can inhibit protein-phosphatase-1. DARPP-32 has a key role in many neurotransmitter pathways throughout the brain and has been shown to be involved in controlling receptors, ion channels and other physiological factors including the brain's response to drugs of abuse, such as cocaine, opiates and nicotine. DARPP-32 is reciprocally regulated by the two neurotransmitters that are most often implicated in schizophrenia - dopamine and glutamate. Dopamine activates DARPP-32 through the D1 receptor pathway and disables DARPP-32 through the D2 receptor. Glutamate, acting through the N-methyl-d-aspartate receptor, renders DARPP-32 inactive. A mutant form of DARPP-32 has been linked with gastric cancers.


Pssm-ID: 428454  Cd Length: 136  Bit Score: 193.13  E-value: 8.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110938025  12 EPKERKKIQFAVPANaPTNLDPRQVEMIRRRRPTPATLFRVADQSSPEDDQSTHQWVVGENGVLKPKRVNPNVYQPPSLK 91
Cdd:pfam05395   1 EPKERKKIQFAVPAP-PSQLDPRQVEMIRRRRPTPATLFRVSDQSSPEDEQSSHQWVVGENGILKPKRRNPCVYTPPSLK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1110938025  92 AVQKMAEAHMQKLGVYPPLEDPCEGEEDEDYLKGEEG-EDAAPTKAADRQETAATEQ 147
Cdd:pfam05395  80 AVQRMAEAHMQKLGVYPNLEDPPEGQEEEDELGEPEGnEDSPPTSGEEGEEEESEEE 136
 
Name Accession Description Interval E-value
DARPP-32 pfam05395
Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein ...
12-147 8.82e-64

Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein phosphatase inhibitor 1 (IPP-1) and dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32) proteins. Protein phosphatase inhibitor-1 is involved in signal transduction and is an endogenous inhibitor of protein phosphatase-1. It has been demonstrated that DARPP-32, if phosphorylated, can inhibit protein-phosphatase-1. DARPP-32 has a key role in many neurotransmitter pathways throughout the brain and has been shown to be involved in controlling receptors, ion channels and other physiological factors including the brain's response to drugs of abuse, such as cocaine, opiates and nicotine. DARPP-32 is reciprocally regulated by the two neurotransmitters that are most often implicated in schizophrenia - dopamine and glutamate. Dopamine activates DARPP-32 through the D1 receptor pathway and disables DARPP-32 through the D2 receptor. Glutamate, acting through the N-methyl-d-aspartate receptor, renders DARPP-32 inactive. A mutant form of DARPP-32 has been linked with gastric cancers.


Pssm-ID: 428454  Cd Length: 136  Bit Score: 193.13  E-value: 8.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110938025  12 EPKERKKIQFAVPANaPTNLDPRQVEMIRRRRPTPATLFRVADQSSPEDDQSTHQWVVGENGVLKPKRVNPNVYQPPSLK 91
Cdd:pfam05395   1 EPKERKKIQFAVPAP-PSQLDPRQVEMIRRRRPTPATLFRVSDQSSPEDEQSSHQWVVGENGILKPKRRNPCVYTPPSLK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1110938025  92 AVQKMAEAHMQKLGVYPPLEDPCEGEEDEDYLKGEEG-EDAAPTKAADRQETAATEQ 147
Cdd:pfam05395  80 AVQRMAEAHMQKLGVYPNLEDPPEGQEEEDELGEPEGnEDSPPTSGEEGEEEESEEE 136
 
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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