RAD17
entrez
5884
canonical
uniprot
O75943
canonical
ensembl
ENSG00000152942
resolver
ensembl
ENSG00000276618
resolver
ensp
ENSP00000282891
resolver
ensp
ENSP00000303134
resolver
ensp
ENSP00000311227
resolver
ensp
ENSP00000346271
resolver
ensp
ENSP00000346938
resolver
ensp
ENSP00000350725
resolver
ensp
ENSP00000355226
resolver
ensp
ENSP00000370151
resolver
ensp
ENSP00000477962
resolver
ensp
ENSP00000477996
resolver
ensp
ENSP00000478167
resolver
ensp
ENSP00000479160
resolver
ensp
ENSP00000482371
resolver
ensp
ENSP00000482775
resolver
ensp
ENSP00000483115
resolver
ensp
ENSP00000484854
resolver
ensp
ENSP00000580415
resolver
ensp
ENSP00000580416
resolver
ensp
ENSP00000580427
resolver
ensp
ENSP00000580432
resolver
ensp
ENSP00000580434
resolver
ensp
ENSP00000580435
resolver
ensp
ENSP00000580437
resolver
ensp
ENSP00000596187
resolver
enst
ENST00000610770
resolver
enst
ENST00000611523
resolver
enst
ENST00000612044
resolver
enst
ENST00000616158
resolver
enst
ENST00000616488
resolver
enst
ENST00000616759
resolver
enst
ENST00000620889
resolver
genesymbol
RAD17
resolver
genesymbol_syn
R24L
resolver
hgnc
HGNC:9807
resolver
uniprot
A0A0G2JP78
resolver
uniprot
A8K8X2
resolver
uniprot
D3DWA5
resolver
uniprot
O75714
resolver
uniprot
Q7Z3S4
resolver
uniprot
Q9UNK7
resolver
uniprot
Q9UNR7
resolver
uniprot
Q9UNR8
resolver
uniprot
Q9UPF5
resolver
uniprot_entry
A0A0G2JP78_HUMAN
resolver
uniprot_entry
RAD17_HUMAN
resolver
uniprot_sec
A8K8X2
resolver
uniprot_sec
D3DWA5
resolver
uniprot_sec
O75714
resolver
uniprot_sec
Q7Z3S4
resolver
uniprot_sec
Q9UNK7
resolver
uniprot_sec
Q9UNR7
resolver
uniprot_sec
Q9UNR8
resolver
uniprot_sec
Q9UPF5
resolver
amino_acid_sequence
MSKTFLRPKVSSTKVTDWVDPSFDDFLECSGVSTITATSLGVNNSSHRRKNGPSTLESSRFPARKRGNLSSLEQIYGLENSKEYLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQGGSILLITGPPGCGKTTTLKILSKEHGIQVQEWINPVLPDFQKDDFKGMFNTESSFHMFPYQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRCPLIFIISDSLSGDNNQRLLFPKEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLELLCQGCSGDIRSAINSLQFSSSKGENNLRPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKILYCKRASLTELDSPRLPSHLSEYERDTLLVEPEEVVEMSHMPGDLFNLYLHQNYIDFFMEIDDIVRASEFLSFADILSGDWNTRSLLREYSTSIATRGVMHSNKARGYAHCQGGGSSFRPLHKPQWFLINKKYRENCLAAKALFPDFCLPALCLQTQLLPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSAEESLGEPTQATVPETWSLPLSQNSASELPASQPQPFSAQGDMEENIIIEDYESDGT
uniprot
proteins
function
FUNCTION: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage (PubMed:10208430, PubMed:11418864, PubMed:11687627, PubMed:11799063, PubMed:12672690, PubMed:14624239, PubMed:15235112). Has a weak ATPase activity required for binding to chromatin (PubMed:10208430, PubMed:11418864, PubMed:11687627, PubMed:11799063, PubMed:12672690, PubMed:14624239, PubMed:15235112). Participates in the recruitment of the 9-1-1 (RAD1-RAD9-HUS1) complex and RHNO1 onto chromatin, and in CHEK1 activation (PubMed:21659603). Involved in homologous recombination by mediating recruitment of the MRN complex to DNA damage sites (PubMed:24534091). May also serve as a sensor of DNA replication progression (PubMed:12578958, PubMed:14500819, PubMed:15538388). {ECO:0000269|PubMed:10208430, ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12578958, ECO:0000269|PubMed:12672690, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14624239, ECO:0000269|PubMed:15235112, ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:24534091}.
uniprot
proteins
mass_dalton
77055
uniprot
proteins
mutagenesis
MUTAGEN 18..23; /note="WVDPSF->AADPSA: Strongly reduced interaction with RAD1."; /evidence="ECO:0000269|PubMed:36841485"; MUTAGEN 143; /note="K->E: Impairs phosphorylation on S-656. Abolishes interaction with the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3."; /evidence="ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:15235112"; MUTAGEN 143; /note="K->G: Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3."; /evidence="ECO:0000269|PubMed:10884395, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:15235112"; MUTAGEN 191; /note="S->A: No effect on phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11687627"; MUTAGEN 633; /note="T->A: Impaired phosphorylation by ATM and interaction with NBN."; /evidence="ECO:0000269|PubMed:24534091"; MUTAGEN 646; /note="S->A: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RAD17, RFC3, RFC4, ATM or ATR; when associated with A-656."; /evidence="ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:15235112, ECO:0000269|PubMed:24534091"; MUTAGEN 646; /note="S->D: Abolishes interaction with RAD1; when associated with D-656."; /evidence="ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:15235112"; MUTAGEN 656; /note="S->A: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RAD17, RFC3, RFC4, ATM or ATR; when associated with A-646."; /evidence="ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:15235112, ECO:0000269|PubMed:24534091"; MUTAGEN 656; /note="S->D: Abolishes interaction with RAD1; when associated with D-646."; /evidence="ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:15235112
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-646 and Ser-656 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling (PubMed:11418864, PubMed:14500819, PubMed:14871926). Phosphorylation is mediated by ATR upon UV or replication arrest, whereas it may be mediated both by ATR and ATM upon ionizing radiation (PubMed:11418864, PubMed:11799063). Phosphorylation on both sites is required for interaction with RAD1 but dispensable for interaction with RFC3 or RFC4 (PubMed:11687627). Phosphorylation at Thr-633 by ATM in response to DNA damage promotes interaction with NBN and recruitment of the MRN complex to DNA damage sites (PubMed:24534091). {ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:24534091}.
uniprot
proteins
protein_family
Rad17/RAD24 family
uniprot
proteins
pubmed
10208430
uniprot
proteins
pubmed
10232579
uniprot
proteins
pubmed
10480350
uniprot
proteins
pubmed
10593953
uniprot
proteins
pubmed
10884395
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11418864
uniprot
proteins
pubmed
11572977
uniprot
proteins
pubmed
11602352
uniprot
proteins
pubmed
11687627
uniprot
proteins
pubmed
11715513
uniprot
proteins
pubmed
11799063
uniprot
proteins
pubmed
12400013
uniprot
proteins
pubmed
12578958
uniprot
proteins
pubmed
12672690
uniprot
proteins
pubmed
14500819
uniprot
proteins
pubmed
14611806
uniprot
proteins
pubmed
14624239
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14871926
uniprot
proteins
pubmed
15235112
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15538388
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21659603
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24534091
uniprot
proteins
pubmed
36841485
uniprot
proteins
pubmed
9660800
uniprot
proteins
pubmed
9878245
uniprot
proteins
pubmed
9933569
uniprot
proteins
sequence_length
681
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10232579, ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12400013}. Chromosome {ECO:0000269|PubMed:24534091}. Note=Phosphorylated form redistributes to discrete nuclear foci upon DNA damage (PubMed:11799063). Localizes to DNA double-strand breaks (DSBs) (PubMed:24534091). {ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:24534091}.
uniprot
proteins