NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370473865|ref|XP_024307037|]
View 

putative Polycomb group protein ASXL3 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 179-304 1.25e-39

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


:

Pssm-ID: 464041  Cd Length: 129  Bit Score: 143.97  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1370473865  257 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 304
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 super family cl16478
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2135-2190 3.22e-20

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


The actual alignment was detected with superfamily member pfam13922:

Pssm-ID: 316444  Cd Length: 68  Bit Score: 86.49  E-value: 3.22e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473865 2135 QNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2190
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 498-770 3.84e-03

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  498 SDTEHKESETAVETSTPKIKTGSSSLEGQF-PNEGIAIDMELQSDPEEQLSENACISET--------SFSSESPEGACTS 568
Cdd:pfam03154   89 SDTEEPERATAKKSKTQEISRPNSPSEGEGeSSDGRSVNDEGSSDPKDIDQDNRSTSPSipspqdneSDSDSSAQQQILQ 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  569 LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTdkynqrnstdenfhASLMSEISPISTSPEISEASLMSNLPLTSEA 648
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSA--------------PSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  649 SPVSNLPLTSETSPMSDLPLTSETSSVSSmlltsettfvSSLPLPSETSPIsnssinERMAHQQRKSPSVSEEPLSPQkd 728
Cdd:pfam03154  235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSP----------QPLPQPSLHGQM------PPMPHSLQTGPSHMQHPVPPQ-- 296

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1370473865  729 essatakPLGENLTSQQKNLSNTPEPIIMSSSSIAPEAFPSE 770
Cdd:pfam03154  297 -------PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ 331
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 179-304 1.25e-39

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 143.97  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1370473865  257 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 304
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2135-2190 3.22e-20

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 86.49  E-value: 3.22e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473865 2135 QNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2190
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 498-770 3.84e-03

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: 42.45  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  498 SDTEHKESETAVETSTPKIKTGSSSLEGQF-PNEGIAIDMELQSDPEEQLSENACISET--------SFSSESPEGACTS 568
Cdd:pfam03154   89 SDTEEPERATAKKSKTQEISRPNSPSEGEGeSSDGRSVNDEGSSDPKDIDQDNRSTSPSipspqdneSDSDSSAQQQILQ 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  569 LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTdkynqrnstdenfhASLMSEISPISTSPEISEASLMSNLPLTSEA 648
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSA--------------PSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  649 SPVSNLPLTSETSPMSDLPLTSETSSVSSmlltsettfvSSLPLPSETSPIsnssinERMAHQQRKSPSVSEEPLSPQkd 728
Cdd:pfam03154  235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSP----------QPLPQPSLHGQM------PPMPHSLQTGPSHMQHPVPPQ-- 296

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1370473865  729 essatakPLGENLTSQQKNLSNTPEPIIMSSSSIAPEAFPSE 770
Cdd:pfam03154  297 -------PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ 331
 
Name Accession Description Interval E-value
ASXH pfam13919
Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The ...
 179-304 1.25e-39

Asx homology domain; A conserved alpha helical domain with a characteriztic LXXLL motif. The LXXLL motif is detected in diverse transcription factors, coactivators and corepressors and is implicated in mediating interactions between them. The ASXH domain is found in animals, fungi and plants and is predicted to play a role in mediating contact between transcription factors and chromatin-associated complexes. In Drosophila Asx and Human ASXL1, the ASXH domain is predicted to mediate interactions with the Calypso and BAP1 deubiquitinases (DUBs) which further belong to the UCHL5/UCH37 clade of DUBs.


Pssm-ID: 464041  Cd Length: 129  Bit Score: 143.97  E-value: 1.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  179 KSGLGHLKWTKAEDIDIETPGSILVNTNLRALINKHTFASLPQHFQQYLLLLLPEVDRQMGSDG-ILRLSTSAL-NNEFF 256
Cdd:pfam13919    1 KSRKAQKKGKWEAEILLTSPKSPLVNADLRALLNKAAWDCLPPEEQQELLSLLPDVDHILDPDTdDSRPALPSLrNNEFF 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1370473865  257 AYAAQGWKQRLAEGEFTPEMQLRIRQEIEKEK-KTEPWKEKFFERFYGE 304
Cdd:pfam13919   81 RHACARFQEDLAEGRFDPELRQAWKAEEKREAgKFDPWKEKEFEEFWGQ 129
PHD_3 pfam13922
PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional ...
 2135-2190 3.22e-20

PHD domain of transcriptional enhancer, Asx; This is the DNA-binding domain on the additional sex combs-like 1 proteins. The Asx protein acts as an enhancer of trithorax and polycomb in displaying bidirectional homoeotic phenotypes in Drosophila, suggesting that it is required for maintenance of both activation and silencing of Hox genes. Asx is required for normal adult haematopoiesis and its function depends on its cellular context.


Pssm-ID: 316444  Cd Length: 68  Bit Score: 86.49  E-value: 3.22e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473865 2135 QNAQMPVQNFADSSNADELELKCSCRLKAMIVCKGCGAFCHDDCIGPSKLCVACLV 2190
Cdd:pfam13922   13 QLAHQSGENTPPGNEATHTANKCACRLNAMVICQQCGAFCHDDCIGASKLCVSCVI 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 498-770 3.84e-03

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: 42.45  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  498 SDTEHKESETAVETSTPKIKTGSSSLEGQF-PNEGIAIDMELQSDPEEQLSENACISET--------SFSSESPEGACTS 568
Cdd:pfam03154   89 SDTEEPERATAKKSKTQEISRPNSPSEGEGeSSDGRSVNDEGSSDPKDIDQDNRSTSPSipspqdneSDSDSSAQQQILQ 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  569 LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTdkynqrnstdenfhASLMSEISPISTSPEISEASLMSNLPLTSEA 648
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSA--------------PSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  649 SPVSNLPLTSETSPMSDLPLTSETSSVSSmlltsettfvSSLPLPSETSPIsnssinERMAHQQRKSPSVSEEPLSPQkd 728
Cdd:pfam03154  235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSP----------QPLPQPSLHGQM------PPMPHSLQTGPSHMQHPVPPQ-- 296

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1370473865  729 essatakPLGENLTSQQKNLSNTPEPIIMSSSSIAPEAFPSE 770
Cdd:pfam03154  297 -------PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ 331
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 559-801 7.75e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.44  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  559 SESPEGACTS--LPSPGGETQSTSEESCTPASLETTFCSEVSSTENTDKYNQRNSTDenfhASLMSEISPISTSPEISEA 636
Cdd:pfam05109  422 SKAPESTTTSptLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTP----AGTTSGASPVTPSPSPRDN 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  637 SLMSNLP-LTSEASPVSNlPLTSETSPMSDLPLTSETSSVSSMLLTSETTFVSSlPLPSETSP---ISNSSINERMAHQQ 712
Cdd:pfam05109  498 GTESKAPdMTSPTSAVTT-PTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTT-PTPNATSPtpaVTTPTPNATIPTLG 575

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473865  713 RKSPSVSEEPLSPqkdesSATAKPLGEnlTSQQKNLSN------TPEPIIMSSSSIAPEAFPSEDlHNKTLSQQTCKSHv 786
Cdd:pfam05109  576 KTSPTSAVTTPTP-----NATSPTVGE--TSPQANTTNhtlggtSSTPVVTSPPKNATSAVTTGQ-HNITSSSTSSMSL- 646

                          250
                   ....*....|....*
gi 1370473865  787 dtekpYPASIPELAS 801
Cdd:pfam05109  647 -----RPSSISETLS 656
 
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