Conserved Protein Domain Family
PHD5_NSD1

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cd15659: PHD5_NSD1 
PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1)
NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.
Statistics
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PSSM-Id: 277129
Aligned: 4 rows
Threshold Bit Score: 97.3207
Created: 13-Aug-2013
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Zn binding siteputative
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C C H C C HClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structure evidence that human NSD3 (4GND) binds two Zn2+ ions through its PHD finger
  • Comment:The PHD zinc finger is typically characterized as Cys4HisCys3, for this PHD zinc finger the motif is Cys4HisCys2His.
  • Citation:PMID 7583761
  • Citation:PMID 7701562

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #  #        #    #    #  #            #  #
Q96L73       2120 ECFSCGDAGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 2162 human
EMP30944       51 ECFSCGDGGQLVSCKKTGCPKVYHADCLNLTKRPAGKWECPWH 93   green seaturtle
XP_683890    1802 ECFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844 zebrafish
XP_002936997 1936 ECFSCGDGGQLVSCKKPGCPKVYHAECLKLTRRPAGKWECPWH 1978 western clawed frog

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