Excision repair cross-complementing rodent repair deficiency, complementation group 2

Summary

Excision repair cross-complementing rodent repair deficiency, complementation group 2 is a protein^[1].

Key Facts

• Excision repair cross-complementing rodent repair deficiency, complementation group 2's instance of is recorded as protein^[2].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's subclass of is recorded as protein^[3].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's UniProt protein ID is recorded as O08811^[4].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as P-loop containing nucleoside triphosphate hydrolase^[5].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as RAD3/XPD family^[6].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as ATP-dependent helicase, C-terminal domain, protein family^[7].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as Helical and beta-bridge domain, protein family^[8].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as DEAD2, protein family^[9].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type, protein family^[10].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as Helicase-like, DEXD box c2 type, protein family^[11].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's part of is recorded as DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site, protein family^[12].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's has part is recorded as DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site^[13].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's has part is recorded as Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type^[14].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's has part is recorded as Helical and beta-bridge domain^[15].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's has part is recorded as ATP-dependent helicase, C-terminal^[16].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's has part is recorded as DEAD2^[17].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's has part is recorded as Helicase-like, DEXD box c2 type^[18].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's RefSeq protein ID is recorded as NP_031975^[19].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's RefSeq protein ID is recorded as NP_001350910^[20].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's molecular function is recorded as DNA binding^[21].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's molecular function is recorded as nucleotide binding^[22].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's molecular function is recorded as protein kinase activity^[23].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's molecular function is recorded as ATP-dependent activity, acting on DNA^[24].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's molecular function is recorded as 4 iron, 4 sulfur cluster binding^[25].
• Excision repair cross-complementing rodent repair deficiency, complementation group 2's molecular function is recorded as helicase activity^[26].