RNA demethylase ALKBH5
Basic Information | |
---|---|
Short Name | ALKBH5 |
UNP ID | Q6P6C2 |
Organism | Homo sapiens |
Cys Site | Cys200 |
Family/Domain | 2OG-Fe(II) oxygenase superfamily,Alkb family |
Known Ligand | Ligand list |
Function Type | Nucleic acid modification |
Summary
Protein Function
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia)
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126)
Cys Function & Property
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.
- Hydrophobic property:
- SASA:
- Cys200: ? A^2
Protein Sequence
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGGC
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH
Structural Information
- Known structure with covalent ligand:
- Protein structure:
Related Pathway
- Unknown
Experimental Evidence
- Crystallography
Reference
- Aik W S, Scotti J S, Choi H, et al. Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J]. Nucleic acids research, 2014, 42(7): 4741-4754. 24489119