Modomics - A Database of RNA Modifications

ID Card:

Full name: YTH N6-methyladenosine RNA binding protein 1
Synonym: FLJ20391
GI: 28380041
UniProt: Q9BYJ9
Structures: | 4RCI | 4RCJ |
Alpha Fold Predicted Structure: AF-Q9BYJ9-F1


PDB Structures:


4RCI

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

N(6)-Methyladenosine (m(6)A) is the most abundant internal modification in RNA and is specifically recognized by YT521-B homology (YTH) domain-containing proteins. Recently we reported that YTHDC1 prefers guanosine and disfavors adenosine at the position preceding the m(6)A nucleotide in RNA and preferentially binds to the GG(m(6)A)C sequence. Now we systematically characterized the binding affinities of the YTH domains of three other human proteins and yeast YTH domain protein Pho92 and determined the crystal structures of the YTH domains of human YTHDF1 and yeast Pho92 in complex with a 5-mer m(6)A RNA, respectively. Our binding and structural data revealed that the YTH domain used a conserved aromatic cage to recognize m(6)A. Nevertheless, none of these YTH domains, except YTHDC1, display sequence selectivity at the position preceding the m(6)A modification. Structural comparison of these different YTH domains revealed that among those, only YTHDC1 harbors a distinctly selective binding pocket for the nucleotide preceding the m(6)A nucleotide.

Download RCSB-PDB Structures:

Pdb Files   4RCI.pdb   4RCJ.pdb  
Pdbx/mmCIF Files   4RCI.cif   4RCJ.cif  


Protein sequence:

MSATSVDTQRTKGQDNKVQNGSLHQKDTVHDNDFEPYLTGQSNQSNSYPSMSDPYLSSYYPPSIGFPYSLNEAPWSTAGDPPIPYLTTYGQLSNGDHHFMHDAVFGQPGGLGNNIYQHRFNFFPENPAFSAWGTSGSQGQQTQSSAYGSSYTYPPSSLGGTVVDGQPGFHSDTLSKAPGMNSLEQGMVGLKIGDVSSSAVKTVGSVVSSVALTGVLSGNGGTNVNMPVSKPTSWAAIASKPAKPQPKMKTKSGPVMGGGLPPPPIKHNMDIGTWDNKGPVPKAPVPQQAPSPQAAPQPQQVAQPLPAQPPALAQPQYQSPQQPPQTRWVAPRNRNAAFGQSGGAGSDSNSPGNVQPNSAPSVESHPVLEKLKAAHSYNPKEFEWNLKSGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDSAFRCMSSKGPVYLLFSVNGSGHFCGVAEMKSPVDYGTSAGVWSQDKWKGKFDVQWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIISSYKHTTSIFDDFAHYEKRQEEEEVVRKERQSRNKQ

Comments:





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M S A T S V D T Q R T K G Q D N K V Q N G S L H Q K D T V H D N D F E P Y L T G Q S N Q S N S Y P S M S D P Y L S S Y Y P P S I G F P Y S L N E A P W S T A G D P P I P Y L T T Y G Q L S N G D H H F M H D A V F G Q P G G L G N N I Y Q H R F N F F P E N P A F S A W G T S G S Q G Q Q T Q S S A Y G S S Y T Y P P S S L G G T V V D G Q P G F H S D T L S K A P G M N S L E Q G M V G L K I G D V S S S A V K T V G S V V S S V A L T G V L S G N G G T N V N M P V S K P T S W A A I A S K P A K P Q P K M K T K S G P V M G G G L P P P P I K H N M D I G T W D N K G P V P K A P V P Q Q A P S P Q A A P Q P Q Q V A Q P L P A Q P P A L A Q P Q Y Q S P Q Q P P Q T R W V A P R N R N A A F G Q S G G A G S D S N S P G N V Q P N S A P S V E S H P V L E K L K A A H S Y N P K E F E W N L K S G R V F I I K S Y S E D D I H R S I K Y S I W C S T E H G N K R L D S A F R C M S S K G P V Y L L F S V N G S G H F C G V A E M K S P V D Y G T S A G V W S Q D K W K G K F D V Q W I F V K D V P N N Q L R H I R L E N N D N K P V T N S R D T Q E V P L E K A K Q V L K I I S S Y K H T T S I F D D F A H Y E K R Q E E E E V V R K E R Q S R N K Q

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-Q9BYJ9-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9BYJ9-F1.cif  
DSSP Secondary Structures   Q9BYJ9.dssp  





Diseases connected to this enzyme:

Description Reaction Disease Name
Decreased m6A levels are identified in ocular melanoma samples, indicating poor prognosis, and changes in global m6A modification are highly associated with tumor progression. Mechanistically, YTHDF1 promotes the translation of methylated mRNA of HINT2, a tumor suppressor in ocular melanoma. A:m6A
Melanoma
Mutations found in m6A regulatory genes are associated with lower OS and EFS rates in patients with AML ( Acute myeloid Leukemia) and presence of p53 mutations. A:m6A
Leukemia
YTHDF1 was found to be upregulated in HCC and to play an important role in regulating HCC cell cycle progression and metabolism. A:m6A
Hepatocellular carcinoma
The overexpressed YTHDF1, associated to DNA copy number gain, recognizes and promotes the translation of m6A-modified FZD9 and Wnt6 mRNAs, leading to an aberrant activation of Wnt/b-catenin signaling and ultimately affecting the tumorigenicity and stem cell-like activity in CRC. Epigenetic regulation by YTHDF1 plays an important role in cancer progression processes in CRC. In another study, it was demonstrated that YTHDF1 overexpression is promoted by c-Myc and is associated to CRC cells proliferation and chemoresistence. A:m6A
Colorectal cancer
m6A-related targets were altered at protein level; overexpression of the enzymes was associated with poor prognosis on overal survival; YTHDF3 is considered independent prognosis factor for OS and relapse free survival. A:m6A
Breast cancer

Publications:

Title Authors Journal Details PubMed Id DOI