NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578833691|ref|XP_006722989|]
View 

MPN domain-containing protein isoform X1 [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
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 266-421 8.60e-76

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


:

Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 235.62  E-value: 8.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691 266 KFQPFNVAVSSNVLFLLDFHSHLTRSEVVGYLGGRWDVNSQMLTVLRAFPCRSRLGDAETAAAIEEE------------- 332
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSEteireslesrgls 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691 333 ------------------DIDAQMDYQLRLQGSSNGFQPCLALLCSPYYSGNPGPESKISPFWVMPPPEQRPSDYGIPMD 394
Cdd:cd08067   81 vvgwyhshptfppnpslrDIDTQLDYQIMFKGSDSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENRPNEYGVPML 160

                        170       180
                 ....*....|....*....|....*..
gi 578833691 395 VEMAYVQDSFLTNDILHEMMLLVEFYK 421
Cdd:cd08067  161 MSYTVSQDEFLTQDVLKELRWLVEFYR 187
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 70-164 3.39e-34

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


:

Pssm-ID: 465856  Cd Length: 108  Bit Score: 123.96  E-value: 3.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691   70 LTRRAVTLRVLLKDALLEPGAGVLSIYYLGKKFLGDLQPDGRIMWqETGQTFNSPSAWATHCKKlvnpAKKSGCGWASVK 149
Cdd:pfam18755  14 RTGRRVTLQDLLEAGLLQPGEGLLSIEYKGQKHRADLLADGKIRL-EDGQIFASPSAWAKHVKR----GKKSGNGWASWK 88

                          90
                  ....*....|....*.
gi 578833691  150 Y-KGQKLDKYKATWLR 164
Cdd:pfam18755  89 YsKGKKLDDLRAELLK 104
 
Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 266-421 8.60e-76

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 235.62  E-value: 8.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691 266 KFQPFNVAVSSNVLFLLDFHSHLTRSEVVGYLGGRWDVNSQMLTVLRAFPCRSRLGDAETAAAIEEE------------- 332
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSEteireslesrgls 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691 333 ------------------DIDAQMDYQLRLQGSSNGFQPCLALLCSPYYSGNPGPESKISPFWVMPPPEQRPSDYGIPMD 394
Cdd:cd08067   81 vvgwyhshptfppnpslrDIDTQLDYQIMFKGSDSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENRPNEYGVPML 160

                        170       180
                 ....*....|....*....|....*..
gi 578833691 395 VEMAYVQDSFLTNDILHEMMLLVEFYK 421
Cdd:cd08067  161 MSYTVSQDEFLTQDVLKELRWLVEFYR 187
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 70-164 3.39e-34

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 123.96  E-value: 3.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691   70 LTRRAVTLRVLLKDALLEPGAGVLSIYYLGKKFLGDLQPDGRIMWqETGQTFNSPSAWATHCKKlvnpAKKSGCGWASVK 149
Cdd:pfam18755  14 RTGRRVTLQDLLEAGLLQPGEGLLSIEYKGQKHRADLLADGKIRL-EDGQIFASPSAWAKHVKR----GKKSGNGWASWK 88

                          90
                  ....*....|....*.
gi 578833691  150 Y-KGQKLDKYKATWLR 164
Cdd:pfam18755  89 YsKGKKLDDLRAELLK 104
 
Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 266-421 8.60e-76

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 235.62  E-value: 8.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691 266 KFQPFNVAVSSNVLFLLDFHSHLTRSEVVGYLGGRWDVNSQMLTVLRAFPCRSRLGDAETAAAIEEE------------- 332
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSEteireslesrgls 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691 333 ------------------DIDAQMDYQLRLQGSSNGFQPCLALLCSPYYSGNPGPESKISPFWVMPPPEQRPSDYGIPMD 394
Cdd:cd08067   81 vvgwyhshptfppnpslrDIDTQLDYQIMFKGSDSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENRPNEYGVPML 160

                        170       180
                 ....*....|....*....|....*..
gi 578833691 395 VEMAYVQDSFLTNDILHEMMLLVEFYK 421
Cdd:cd08067  161 MSYTVSQDEFLTQDVLKELRWLVEFYR 187
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 70-164 3.39e-34

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 123.96  E-value: 3.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578833691   70 LTRRAVTLRVLLKDALLEPGAGVLSIYYLGKKFLGDLQPDGRIMWqETGQTFNSPSAWATHCKKlvnpAKKSGCGWASVK 149
Cdd:pfam18755  14 RTGRRVTLQDLLEAGLLQPGEGLLSIEYKGQKHRADLLADGKIRL-EDGQIFASPSAWAKHVKR----GKKSGNGWASWK 88

                          90
                  ....*....|....*.
gi 578833691  150 Y-KGQKLDKYKATWLR 164
Cdd:pfam18755  89 YsKGKKLDDLRAELLK 104
 
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