Rad4p YER162C
fungal protein found in Saccharomyces cerevisiae S288c
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Rad4p YER162C
Summary
Rad4p YER162C is a protein[1].
Key Facts
- Rad4p YER162C's instance of is recorded as protein[2].
- Rad4p YER162C's subclass of is recorded as protein[3].
- Rad4p YER162C's UniProt protein ID is recorded as P14736[4].
- Rad4p YER162C's part of is recorded as DNA repair protein Rad4[5].
- Rad4p YER162C's part of is recorded as Transglutaminase-like superfamily[6].
- Rad4p YER162C's part of is recorded as Papain-like cysteine peptidase superfamily[7].
- Rad4p YER162C's part of is recorded as Rad4 beta-hairpin domain 1, protein family[8].
- Rad4p YER162C's part of is recorded as Rad4 beta-hairpin domain 3, protein family[9].
- Rad4p YER162C's part of is recorded as Rad4/PNGase transglutaminase-like fold, protein family[10].
- Rad4p YER162C's part of is recorded as Rad4 beta-hairpin domain 2, protein family[11].
- Rad4p YER162C's has part is recorded as Rad4 beta-hairpin domain 2[12].
- Rad4p YER162C's has part is recorded as Rad4/PNGase transglutaminase-like fold[13].
- Rad4p YER162C's has part is recorded as Rad4 beta-hairpin domain 3[14].
- Rad4p YER162C's has part is recorded as Rad4 beta-hairpin domain 1[15].
- Rad4p YER162C's RefSeq protein ID is recorded as NP_011089[16].
- Rad4p YER162C's molecular function is recorded as single-strand break-containing DNA binding[17].
- Rad4p YER162C's molecular function is recorded as DNA binding[18].
- Rad4p YER162C's molecular function is recorded as single-stranded DNA binding[19].
- Rad4p YER162C's molecular function is recorded as damaged DNA binding[20].
- Rad4p YER162C's molecular function is recorded as protein binding[21].
- Rad4p YER162C's molecular function is recorded as damaged DNA binding[22].
- Rad4p YER162C's cell component is recorded as nucleotide-excision repair factor 2 complex[23].
- Rad4p YER162C's cell component is recorded as nucleus[24].
- Rad4p YER162C's cell component is recorded as XPC complex[25].
- Rad4p YER162C's cell component is recorded as cytosol[26].