Conserved Protein Domain Family
PHD1_KDM5A

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cd15602: PHD1_KDM5A 
PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A)
KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.
Statistics
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PSSM-Id: 277075
Aligned: 3 rows
Threshold Bit Score: 115.047
Created: 12-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 CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structure evidence that human KDM5D (2E6R) binds two Zn2+ ions through its first PHD finger
  • Comment:The PHD zinc finger is characterized as Cys4HisCys3.
  • Citation:PMID 7583761
  • Citation:PMID 7701562

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #  #           #  #    #  #              #  #   
P29375        295 VCMFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAE 343  human
XP_002941946  321 ICLFCARGDCEDKLLLCDGCDDSYHTFCLIPPLSEVPKGDWRCPKCVAE 369  western clawed frog
EOB07246      239 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAE 287  mallard

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