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Conserved domains on  [gi|2222466704|gb|KAI2554809|]
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euchromatic histone lysine methyltransferase 1, partial [Homo sapiens]

Protein Classification

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 ...
 237-367 1.38e-72

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: 223.04  E-value: 1.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222466704 237 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 315
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2222466704 316 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 367
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
 
Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 237-367 1.38e-72

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: 223.04  E-value: 1.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222466704 237 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 315
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2222466704 316 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 367
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
 
Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 237-367 1.38e-72

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: 223.04  E-value: 1.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222466704 237 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 315
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2222466704 316 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 367
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
RING-HC_PCGF2 cd16734
RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, ...
 308-371 8.43e-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: 34.96  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222466704 308 HQCCPGCG-YFCTAGNFMECQpessisHRFHKDCASRVNNAS-YCPHCGEESSKAKEVTIAKADTT 371
Cdd:cd16734    14 HLMCALCGgYFIDAATIVECL------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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