NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767944956|ref|XP_011513469|]
View 

ETS translocation variant 1 isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
29-347 7.66e-172

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: 487.31  E-value: 7.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956   29 ESQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDnDEQFVPDYQAESLAFHGLP-LKIKKEPH 107
Cdd:pfam04621  15 GSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEAQVPD-DEQFVPDFQSENLAFHGPPpAKIKREPQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  108 SPCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP-------------------N 168
Cdd:pfam04621  94 SPSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplqrqpsplplmrqsP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  169 STHTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDP 248
Cdd:pfam04621 170 PFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVPYPPQGFKQEYHDP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  249 VYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQFYDDTCVVPEKFDG 328
Cdd:pfam04621 247 LYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLFYDDTCVVPEKLEG 325
                         330
                  ....*....|....*....
gi 767944956  329 DIKQEPGMYREGPTYQRRG 347
Cdd:pfam04621 326 KVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
348-432 2.34e-49

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


:

Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.98  E-value: 2.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956   348 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 426
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 767944956   427 KFVCDP 432
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 ...
29-347 7.66e-172

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: 487.31  E-value: 7.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956   29 ESQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDnDEQFVPDYQAESLAFHGLP-LKIKKEPH 107
Cdd:pfam04621  15 GSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEAQVPD-DEQFVPDFQSENLAFHGPPpAKIKREPQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  108 SPCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP-------------------N 168
Cdd:pfam04621  94 SPSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplqrqpsplplmrqsP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  169 STHTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDP 248
Cdd:pfam04621 170 PFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVPYPPQGFKQEYHDP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  249 VYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQFYDDTCVVPEKFDG 328
Cdd:pfam04621 247 LYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLFYDDTCVVPEKLEG 325
                         330
                  ....*....|....*....
gi 767944956  329 DIKQEPGMYREGPTYQRRG 347
Cdd:pfam04621 326 KVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
348-432 2.34e-49

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


Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.98  E-value: 2.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956   348 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 426
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 767944956   427 KFVCDP 432
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
350-428 2.38e-44

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 150.34  E-value: 2.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  350 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 428
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
135-284 1.42e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  135 VSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSthtPKPDRAFPAHLPPSQSIPDSSYPMDHRFRrqlSEPCNSFPPL 214
Cdd:PHA03247 2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSPSPAANEPDPHPPPT---VPPPERPRDD 2655
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767944956  215 PTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehntmVGSAASQSFPPPLMIKQEPRDFAYDSEVP 284
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 ...
29-347 7.66e-172

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: 487.31  E-value: 7.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956   29 ESQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDnDEQFVPDYQAESLAFHGLP-LKIKKEPH 107
Cdd:pfam04621  15 GSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEAQVPD-DEQFVPDFQSENLAFHGPPpAKIKREPQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  108 SPCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP-------------------N 168
Cdd:pfam04621  94 SPSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplqrqpsplplmrqsP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  169 STHTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDP 248
Cdd:pfam04621 170 PFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVPYPPQGFKQEYHDP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  249 VYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQFYDDTCVVPEKFDG 328
Cdd:pfam04621 247 LYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLFYDDTCVVPEKLEG 325
                         330
                  ....*....|....*....
gi 767944956  329 DIKQEPGMYREGPTYQRRG 347
Cdd:pfam04621 326 KVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
348-432 2.34e-49

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


Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.98  E-value: 2.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956   348 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 426
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 767944956   427 KFVCDP 432
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
350-428 2.38e-44

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 150.34  E-value: 2.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  350 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 428
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
135-284 1.42e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  135 VSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSthtPKPDRAFPAHLPPSQSIPDSSYPMDHRFRrqlSEPCNSFPPL 214
Cdd:PHA03247 2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSPSPAANEPDPHPPPT---VPPPERPRDD 2655
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767944956  215 PTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehntmVGSAASQSFPPPLMIKQEPRDFAYDSEVP 284
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------VGSLTSLADPPPPPPTPEPAPHALVSATP 2720
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
102-284 3.08e-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: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  102 IKKEPHSPCSEISSACSQEQPfkfsygekclynvsAYDQKPQVGMRPSN-PPTPSSTPVSPLHHASPNSTHTP------- 173
Cdd:pfam03154 355 IKPPPTTPIPQLPNPQSHKHP--------------PHLSGPSPFQMNSNlPPPPALKPLSSLSTHHPPSAHPPplqlmpq 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  174 ----KPDRAFPAHLPPSQSIP--DSSYPMDHRFRRQLSEPcnSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHD 247
Cdd:pfam03154 421 sqqlPPPPAQPPVLTQSQSLPppAASHPPTSGLHQVPSQS--PFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767944956  248 PVYEHNTMVGSAASQSfpPPLMIKQEPRDFAYDSEVP 284
Cdd:pfam03154 499 SVSSSGPVPAAVSCPL--PPVQIKEEALDEAEEPESP 533
PHA03247 PHA03247
large tegument protein UL36; Provisional
148-238 3.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944956  148 PSNPPTPSSTPVSPLHHASPNSTHTP-----KPDRAFPAHLPPSQSIPDSSYPMDHRFRR----QLSEPCNSFP------ 212
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPPPSLPlggsvAPGGDVRRRPPSRSPAAKPAAPARPPVRRlarpAVSRSTESFAlppdqp 2905
                          90       100
                  ....*....|....*....|....*..
gi 767944956  213 -PLPTMPREGRPMYQRQMSEPNIPFPP 238
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH