2E6R,2MIQ,2MNY


Conserved Protein Domain Family
PHD1_KDM5A_like

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cd15515: PHD1_KDM5A_like 
Click on image for an interactive view with Cn3D
PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar proteins
The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A 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. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me2 and H3K4me3), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. This family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent H3K4me3 demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.
Statistics
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PSSM-Id: 276990
Aligned: 9 rows
Threshold Bit Score: 73.9659
Created: 9-Aug-2013
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteputative
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
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:
  • Structure:2E6R; Human KDM5D 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          #  #           #  #    #  #              #  #
2E6R_A         18 ICQVCSRGdedDKLLFCDGCDDNYHIFCLLPPLPEIPRGIWRCPKC 63   human
2MIQ_A         40 ICHICNRGdveESMLLCDGCDDSYHTFCLLPPLTSIPKGEWLCPRC 85   fruit fly
2MNY_A          6 VCLLCGSGndeDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 51   human
XP_002111443  285 ACMLCGLGdneEFLLLCDGCDDSYHTYCLIPPLQSIPPGDWRCPKC 330  Trichoplax adhaerens
P29375        295 VCMFCGRGnneDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKC 340  human
XP_002153783   76 RCNVCEFGdeeHCMLLCDSCDSSYHSFCLIPPLQSVPPGDWRCPKC 121  green hydra
XP_002120014  107 NCKMCSKDsneSLLLLCDGCDDSYHTFCLIPPLPNVPTGEWRCPKC 152  vase tunicate
XP_005649478  991 GCAACWSNddhRNILLCDGCDLEFHHYCVVPPLPDIPSGEWFCPAC 1036 Coccomyxa subellipsoidea C-169
ESO07518      277 KCQSCERGdddDVLLLCDGCDEAYHTFCLIPPLSKIPPGDWLCPRC 322  Helobdella robusta

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