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Conserved domains on  [gi|224465235|ref|NP_001138999|]
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histone-lysine N-methyltransferase EHMT1 isoform 2 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 15337343)

ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions, such as myotrophin that promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 514-644 4.52e-71

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


:

Pssm-ID: 411018  Cd Length: 133  Bit Score: 229.20  E-value: 4.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465235 514 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 592
Cdd:cd20905    1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 593 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 644
Cdd:cd20905   81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
742-798 1.14e-05

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224465235  742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQFCRL 798
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLEHADV 55
 
Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 514-644 4.52e-71

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 229.20  E-value: 4.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465235 514 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 592
Cdd:cd20905    1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 593 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 644
Cdd:cd20905   81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
742-798 1.14e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224465235  742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQFCRL 798
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLEHADV 55
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
742-794 4.59e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 4.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQ 794
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHLAAANGNLEIVKLLLE 174
 
Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 514-644 4.52e-71

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 229.20  E-value: 4.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465235 514 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 592
Cdd:cd20905    1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 593 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 644
Cdd:cd20905   81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
742-798 1.14e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224465235  742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQFCRL 798
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLEHADV 55
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
742-794 4.59e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 4.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQ 794
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHLAAANGNLEIVKLLLE 174
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
742-794 4.93e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 4.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 742 LYFSARQGELQKVLLMLVDGIDPNFKMEhqNKRSPLHAAAEAGHVDICHMLVQ 794
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDK--DGETPLHLAAYNGNLEIVKLLLE 141
Ank_2 pfam12796
Ankyrin repeats (3 copies);
742-794 7.15e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224465235  742 LYFSARQGELQKVLLmLVDGIDPNFKMehqNKRSPLHAAAEAGHVDICHMLVQ 794
Cdd:pfam12796  34 LHLAAKNGHLEIVKL-LLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLE 82
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
742-794 2.10e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.09  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224465235 742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQ 794
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHLAAENGHLEIVKLLLE 207
RING-HC_PCGF2 cd16734
RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, ...
 578-648 4.57e-03

RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, also known as DNA-binding protein Mel-18, RING finger protein 110 (RNF110), or zinc finger protein 144 (ZNF144), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF2 uniquely regulates PRC1 to specify mesoderm cell fate in embryonic stem cells. It is required for PRC1 stability and maintenance of gene repression in embryonic stem cells (ESCs) and essential for ESC differentiation into early cardiac-mesoderm precursors. PCGF2 also plays a significant role in the angiogenic function of endothelial cells (ECs) by regulating endothelial gene expression. Furthermore, PCGF2 is a SUMO-dependent regulator of hormone receptors. It facilitates the deSUMOylation process by inhibiting PCGF4/BMI1-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1). It is also a novel negative regulator of breast cancer stem cells (CSCs) that inhibits the stem cell population and in vitro and in vivo self-renewal through the inactivation of Wnt-mediated Notch signaling. PCGF2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438392 [Multi-domain]  Cd Length: 80  Bit Score: 36.89  E-value: 4.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224465235 578 HRGRMVK------HQCCPGCG-YFCTAGNFMECQpessisHRFHKDCASRVNNAS-YCPHCGEESSKAKEVTIAKADTT 648
Cdd:cd16734    1 HRTTRIKitelnpHLMCALCGgYFIDAATIVECL------HSFCKTCIVRYLETNkYCPMCDVQVHKTRPLLSIRSDKT 73
 
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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