NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1383485766|ref|NP_001349663|]
View 

serine/threonine-protein phosphatase 2A activator isoform 3 [Mus musculus]

Protein Classification

serine/threonine-protein phosphatase 2A activator( domain architecture ID 10503775)

serine/threonine-protein phosphatase 2A activator (PTPA) catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides, and acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A), modulating its activity or substrate specificity

CATH:  1.20.120.1150
EC:  5.2.1.8
Gene Ontology:  GO:0000159|GO:0003755|GO:0019888|GO:0005524
PubMed:  16885030|16380387

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTPA pfam03095
Phosphotyrosyl phosphate activator (PTPA) protein; Phosphotyrosyl phosphatase activator (PTPA) ...
 26-229 4.05e-131

Phosphotyrosyl phosphate activator (PTPA) protein; Phosphotyrosyl phosphatase activator (PTPA) proteins stimulate the phosphotyrosyl phosphatase (PTPase) activity of the dimeric form of protein phosphatase 2A (PP2A). PTPase activity in PP2A (in vitro) is relatively low when compared to the better recognized phosphoserine/ threonine protein phosphorylase activity. The specific biological role of PTPA is unknown, Basal expression of PTPA depends on the activity of a ubiquitous transcription factor, Yin Yang 1 (YY1). The tumour suppressor protein p53 can inhibit PTPA expression through an unknown mechanism that negatively controls YY1.


:

Pssm-ID: 460802  Cd Length: 293  Bit Score: 371.80  E-value: 4.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  26 PKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAY 105
Cdd:pfam03095   1 PVKRILSPEDLEKFKRSQAYADILAFILQLNEAVQGKKLSDSFPVSENVQKLLDLLDTLESLIDETPPVDQPSRFGNKAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 106 RTWYAKLDQEAENLVATVVPTHL-AAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKV 184
Cdd:pfam03095  81 RDWHDKLEERAPSLLDELLPPELlGAAINELSPYLLESFGNRTRIDYGTGHELSFLAFLLCLFKLGILTEEDERALVLRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1383485766 185 FDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLID 229
Cdd:pfam03095 161 FVRYLDLVRRLQLTYWLEPAGSHGVWGLDDYQFLPFLFGSAQLIG 205
 
Name Accession Description Interval E-value
PTPA pfam03095
Phosphotyrosyl phosphate activator (PTPA) protein; Phosphotyrosyl phosphatase activator (PTPA) ...
 26-229 4.05e-131

Phosphotyrosyl phosphate activator (PTPA) protein; Phosphotyrosyl phosphatase activator (PTPA) proteins stimulate the phosphotyrosyl phosphatase (PTPase) activity of the dimeric form of protein phosphatase 2A (PP2A). PTPase activity in PP2A (in vitro) is relatively low when compared to the better recognized phosphoserine/ threonine protein phosphorylase activity. The specific biological role of PTPA is unknown, Basal expression of PTPA depends on the activity of a ubiquitous transcription factor, Yin Yang 1 (YY1). The tumour suppressor protein p53 can inhibit PTPA expression through an unknown mechanism that negatively controls YY1.


Pssm-ID: 460802  Cd Length: 293  Bit Score: 371.80  E-value: 4.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  26 PKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAY 105
Cdd:pfam03095   1 PVKRILSPEDLEKFKRSQAYADILAFILQLNEAVQGKKLSDSFPVSENVQKLLDLLDTLESLIDETPPVDQPSRFGNKAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 106 RTWYAKLDQEAENLVATVVPTHL-AAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKV 184
Cdd:pfam03095  81 RDWHDKLEERAPSLLDELLPPELlGAAINELSPYLLESFGNRTRIDYGTGHELSFLAFLLCLFKLGILTEEDERALVLRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1383485766 185 FDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLID 229
Cdd:pfam03095 161 FVRYLDLVRRLQLTYWLEPAGSHGVWGLDDYQFLPFLFGSAQLIG 205
PTPA cd04087
Phosphotyrosyl phosphatase activator (PTPA) is also known as protein phosphatase 2A (PP2A) ...
 47-230 2.67e-113

Phosphotyrosyl phosphatase activator (PTPA) is also known as protein phosphatase 2A (PP2A) phosphatase activator. PTPA is an essential, well conserved protein that stimulates the tyrosyl phosphatase activity of PP2A. It also reactivates the serine/threonine phosphatase activity of an inactive form of PP2A. Together, PTPA and PP2A constitute an ATPase. It has been suggested that PTPA alters the relative specificity of PP2A from phosphoserine/phosphothreonine substrates to phosphotyrosine substrates in an ATP-hydrolysis-dependent manner. Basal expression of PTPA is controlled by the transcription factor Yin Yang1 (YY1). PTPA has been suggested to play a role in the insertion of metals to the PP2A catalytic subunit (PP2Ac) active site, to act as a chaperone, and more recently, to have peptidyl prolyl cis/trans isomerase activity that specifically targets human PP2Ac.


Pssm-ID: 239754  Cd Length: 266  Bit Score: 325.64  E-value: 2.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  47 DYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDQEAENLVATVVPT 126
Cdd:cd04087     1 DIIAFIQDLSESVQGKPLSDEIPVSENIEKLVEILDQLDALIDETPPIDQPSRFGNKAFRTWHDKLEEELPSLLEELLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 127 HLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKVFDRYLEVMRKLQKTYRMEPAGS 206
Cdd:cd04087    81 ELDEAVNELSYYLLESFGNSTRIDYGTGHELNFLAFLCCLFKLGILTEEDYGAIVLRVFNRYLELVRRLQLTYRLEPAGS 160

                         170       180
                  ....*....|....*....|....
gi 1383485766 207 QGVWGLDDFQFLPFIWGSSQLIDE 230
Cdd:cd04087   161 HGVWGLDDYQFLPFIFGSAQLINH 184
LAG1 COG5057
Phosphotyrosyl phosphatase activator [Cell division and chromosome partitioning / Signal ...
 23-231 1.93e-71

Phosphotyrosyl phosphatase activator [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227390  Cd Length: 353  Bit Score: 222.41  E-value: 1.93e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  23 FIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTfDYKV--SEAIEKLVALLDTLDRWIDETPPVDQPSRF 100
Cdd:COG5057     9 FSTPVKRILDMKDMKDFVESEAYARIYNFILDLDESIKGCSDS-DYHSeqSSSVNHMMNVLDRIKEITQETPPIPGPQRF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 101 GNKAYRTWYAKLDQEAENLVATVVPTHLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAI 180
Cdd:COG5057    88 GNPAFRTWHDKLYDTYPQILQEMLPSEYHEAVPELQYYLRNSFGNSIRIDYGTGHELNFMCYLYALYCLGIFGIADYGAL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1383485766 181 VFKVFDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDED 231
Cdd:COG5057   168 VFTIFVKYLEIMRLLITKYTLEPAGSHGVWGLDDYFFLPFLFGSSQLCNHK 218
 
Name Accession Description Interval E-value
PTPA pfam03095
Phosphotyrosyl phosphate activator (PTPA) protein; Phosphotyrosyl phosphatase activator (PTPA) ...
 26-229 4.05e-131

Phosphotyrosyl phosphate activator (PTPA) protein; Phosphotyrosyl phosphatase activator (PTPA) proteins stimulate the phosphotyrosyl phosphatase (PTPase) activity of the dimeric form of protein phosphatase 2A (PP2A). PTPase activity in PP2A (in vitro) is relatively low when compared to the better recognized phosphoserine/ threonine protein phosphorylase activity. The specific biological role of PTPA is unknown, Basal expression of PTPA depends on the activity of a ubiquitous transcription factor, Yin Yang 1 (YY1). The tumour suppressor protein p53 can inhibit PTPA expression through an unknown mechanism that negatively controls YY1.


Pssm-ID: 460802  Cd Length: 293  Bit Score: 371.80  E-value: 4.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  26 PKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAY 105
Cdd:pfam03095   1 PVKRILSPEDLEKFKRSQAYADILAFILQLNEAVQGKKLSDSFPVSENVQKLLDLLDTLESLIDETPPVDQPSRFGNKAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 106 RTWYAKLDQEAENLVATVVPTHL-AAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKV 184
Cdd:pfam03095  81 RDWHDKLEERAPSLLDELLPPELlGAAINELSPYLLESFGNRTRIDYGTGHELSFLAFLLCLFKLGILTEEDERALVLRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1383485766 185 FDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLID 229
Cdd:pfam03095 161 FVRYLDLVRRLQLTYWLEPAGSHGVWGLDDYQFLPFLFGSAQLIG 205
PTPA cd04087
Phosphotyrosyl phosphatase activator (PTPA) is also known as protein phosphatase 2A (PP2A) ...
 47-230 2.67e-113

Phosphotyrosyl phosphatase activator (PTPA) is also known as protein phosphatase 2A (PP2A) phosphatase activator. PTPA is an essential, well conserved protein that stimulates the tyrosyl phosphatase activity of PP2A. It also reactivates the serine/threonine phosphatase activity of an inactive form of PP2A. Together, PTPA and PP2A constitute an ATPase. It has been suggested that PTPA alters the relative specificity of PP2A from phosphoserine/phosphothreonine substrates to phosphotyrosine substrates in an ATP-hydrolysis-dependent manner. Basal expression of PTPA is controlled by the transcription factor Yin Yang1 (YY1). PTPA has been suggested to play a role in the insertion of metals to the PP2A catalytic subunit (PP2Ac) active site, to act as a chaperone, and more recently, to have peptidyl prolyl cis/trans isomerase activity that specifically targets human PP2Ac.


Pssm-ID: 239754  Cd Length: 266  Bit Score: 325.64  E-value: 2.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  47 DYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDQEAENLVATVVPT 126
Cdd:cd04087     1 DIIAFIQDLSESVQGKPLSDEIPVSENIEKLVEILDQLDALIDETPPIDQPSRFGNKAFRTWHDKLEEELPSLLEELLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 127 HLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKVFDRYLEVMRKLQKTYRMEPAGS 206
Cdd:cd04087    81 ELDEAVNELSYYLLESFGNSTRIDYGTGHELNFLAFLCCLFKLGILTEEDYGAIVLRVFNRYLELVRRLQLTYRLEPAGS 160

                         170       180
                  ....*....|....*....|....
gi 1383485766 207 QGVWGLDDFQFLPFIWGSSQLIDE 230
Cdd:cd04087   161 HGVWGLDDYQFLPFIFGSAQLINH 184
LAG1 COG5057
Phosphotyrosyl phosphatase activator [Cell division and chromosome partitioning / Signal ...
 23-231 1.93e-71

Phosphotyrosyl phosphatase activator [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227390  Cd Length: 353  Bit Score: 222.41  E-value: 1.93e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766  23 FIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTfDYKV--SEAIEKLVALLDTLDRWIDETPPVDQPSRF 100
Cdd:COG5057     9 FSTPVKRILDMKDMKDFVESEAYARIYNFILDLDESIKGCSDS-DYHSeqSSSVNHMMNVLDRIKEITQETPPIPGPQRF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383485766 101 GNKAYRTWYAKLDQEAENLVATVVPTHLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAI 180
Cdd:COG5057    88 GNPAFRTWHDKLYDTYPQILQEMLPSEYHEAVPELQYYLRNSFGNSIRIDYGTGHELNFMCYLYALYCLGIFGIADYGAL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1383485766 181 VFKVFDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDED 231
Cdd:COG5057   168 VFTIFVKYLEIMRLLITKYTLEPAGSHGVWGLDDYFFLPFLFGSSQLCNHK 218
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH