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Conserved domains on  [gi|1370509635|ref|XP_024302444|]
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ETS translocation variant 1 isoform X3 [Homo sapiens]

Protein Classification

ETS translocation variant( domain architecture ID 12054215)

ETS translocation variant (ETV) is a transcriptional activator that binds to consensus DNA sequences, such as human ETV1 that binds to the pentanucleotide 5'-CGGA[AT]-3'

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ETS_PEA3_N pfam04621
PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 ...
29-329 8.09e-156

PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 transcription factors is implicated in transactivation and in inhibition of DNA binding. Transactivation is potentiated by activation of the Ras/MAP kinase and protein kinase A signalling cascades. The N terminal region contains conserved MAP kinase phosphorylation sites.


:

Pssm-ID: 461371  Cd Length: 344  Bit Score: 445.71  E-value: 8.09e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  29 ESQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE-----------------VAFHGLP-LKIKKEPHS 90
Cdd:pfam04621  15 GSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEaqvpddeqfvpdfqsenLAFHGPPpAKIKREPQS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  91 PCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP-------------------NS 151
Cdd:pfam04621  95 PSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplqrqpsplplmrqsPP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 152 THTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPV 231
Cdd:pfam04621 171 FAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVPYPPQGFKQEYHDPL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 232 YEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQFYDDTCVVPEKFDGD 311
Cdd:pfam04621 248 YEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLFYDDTCVVPEKLEGK 326
                         330
                  ....*....|....*...
gi 1370509635 312 IKQEPGMYREGPTYQRRG 329
Cdd:pfam04621 327 VKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
330-414 2.09e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


:

Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.59  E-value: 2.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  330 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 408
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 1370509635  409 KFVCDP 414
Cdd:smart00413  81 KFVKNP 86
 
Name Accession Description Interval E-value
ETS_PEA3_N pfam04621
PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 ...
29-329 8.09e-156

PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 transcription factors is implicated in transactivation and in inhibition of DNA binding. Transactivation is potentiated by activation of the Ras/MAP kinase and protein kinase A signalling cascades. The N terminal region contains conserved MAP kinase phosphorylation sites.


Pssm-ID: 461371  Cd Length: 344  Bit Score: 445.71  E-value: 8.09e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  29 ESQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE-----------------VAFHGLP-LKIKKEPHS 90
Cdd:pfam04621  15 GSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEaqvpddeqfvpdfqsenLAFHGPPpAKIKREPQS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  91 PCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP-------------------NS 151
Cdd:pfam04621  95 PSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplqrqpsplplmrqsPP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 152 THTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPV 231
Cdd:pfam04621 171 FAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVPYPPQGFKQEYHDPL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 232 YEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQFYDDTCVVPEKFDGD 311
Cdd:pfam04621 248 YEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLFYDDTCVVPEKLEGK 326
                         330
                  ....*....|....*...
gi 1370509635 312 IKQEPGMYREGPTYQRRG 329
Cdd:pfam04621 327 VKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
330-414 2.09e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.59  E-value: 2.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  330 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 408
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 1370509635  409 KFVCDP 414
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
332-410 2.88e-44

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 149.95  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 332 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 410
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
117-266 1.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  117 VSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSthtPKPDRAFPAHLPPSQSIPDSSYPMDHRFRrqlSEPCNSFPPL 196
Cdd:PHA03247  2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSPSPAANEPDPHPPPT---VPPPERPRDD 2655
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370509635  197 PTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehntmVGSAASQSFPPPLMIKQEPRDFAYDSEVP 266
Cdd:PHA03247  2656 PAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------VGSLTSLADPPPPPPTPEPAPHALVSATP 2720
 
Name Accession Description Interval E-value
ETS_PEA3_N pfam04621
PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 ...
29-329 8.09e-156

PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 transcription factors is implicated in transactivation and in inhibition of DNA binding. Transactivation is potentiated by activation of the Ras/MAP kinase and protein kinase A signalling cascades. The N terminal region contains conserved MAP kinase phosphorylation sites.


Pssm-ID: 461371  Cd Length: 344  Bit Score: 445.71  E-value: 8.09e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  29 ESQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE-----------------VAFHGLP-LKIKKEPHS 90
Cdd:pfam04621  15 GSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEaqvpddeqfvpdfqsenLAFHGPPpAKIKREPQS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  91 PCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP-------------------NS 151
Cdd:pfam04621  95 PSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplqrqpsplplmrqsPP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 152 THTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPV 231
Cdd:pfam04621 171 FAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVPYPPQGFKQEYHDPL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 232 YEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQFYDDTCVVPEKFDGD 311
Cdd:pfam04621 248 YEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLFYDDTCVVPEKLEGK 326
                         330
                  ....*....|....*...
gi 1370509635 312 IKQEPGMYREGPTYQRRG 329
Cdd:pfam04621 327 VKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
330-414 2.09e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.59  E-value: 2.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  330 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 408
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 1370509635  409 KFVCDP 414
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
332-410 2.88e-44

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 149.95  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 332 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 410
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
117-266 1.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  117 VSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSthtPKPDRAFPAHLPPSQSIPDSSYPMDHRFRrqlSEPCNSFPPL 196
Cdd:PHA03247  2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSPSPAANEPDPHPPPT---VPPPERPRDD 2655
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370509635  197 PTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehntmVGSAASQSFPPPLMIKQEPRDFAYDSEVP 266
Cdd:PHA03247  2656 PAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------VGSLTSLADPPPPPPTPEPAPHALVSATP 2720
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
84-266 2.75e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  84 IKKEPHSPCSEISSACSQEQPfkfsygekclynvsAYDQKPQVGMRPSN-PPTPSSTPVSPLHHASPNSTHTP------- 155
Cdd:pfam03154 355 IKPPPTTPIPQLPNPQSHKHP--------------PHLSGPSPFQMNSNlPPPPALKPLSSLSTHHPPSAHPPplqlmpq 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635 156 ----KPDRAFPAHLPPSQSIP--DSSYPMDHRFRRQLSEPcnSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHD 229
Cdd:pfam03154 421 sqqlPPPPAQPPVLTQSQSLPppAASHPPTSGLHQVPSQS--PFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370509635 230 PVYEHNTMVGSAASQSfpPPLMIKQEPRDFAYDSEVP 266
Cdd:pfam03154 499 SVSSSGPVPAAVSCPL--PPVQIKEEALDEAEEPESP 533
PHA03247 PHA03247
large tegument protein UL36; Provisional
130-220 2.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509635  130 PSNPPTPSSTPVSPLHHASPNSTHTP-----KPDRAFPAHLPPSQSIPDSSYPMDHRFRR----QLSEPCNSFP------ 194
Cdd:PHA03247  2826 GPLPPPTSAQPTAPPPPPGPPPPSLPlggsvAPGGDVRRRPPSRSPAAKPAAPARPPVRRlarpAVSRSTESFAlppdqp 2905
                           90       100
                   ....*....|....*....|....*..
gi 1370509635  195 -PLPTMPREGRPMYQRQMSEPNIPFPP 220
Cdd:PHA03247  2906 eRPPQPQAPPPPQPQPQPPPPPQPQPP 2932
 
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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