RAD16_YEAST
ID RAD16_YEAST Reviewed; 790 AA.
AC P31244; D6VQB3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=DNA repair protein RAD16;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase RAD16;
GN Name=RAD16; OrderedLocusNames=YBR114W; ORFNames=YBR0909;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1508678; DOI=10.1093/nar/20.15.3925;
RA Bang D.D., Verhage R., Goosen N., Brouwer J., de Putte P.;
RT "Molecular cloning of RAD16, a gene involved in differential repair in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 20:3925-3931(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1626431; DOI=10.1002/yea.320080507;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Molecular analysis of yeast chromosome II between CMD1 and LYS2: the
RT excision repair gene RAD16 located in this region belongs to a novel group
RT of double-finger proteins.";
RL Yeast 8:397-408(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-790.
RX PubMed=1626430; DOI=10.1002/yea.320080506;
RA Schild D., Glassner B.J., Mortimer R.K., Carlson M., Laurent B.C.;
RT "Identification of RAD16, a yeast excision repair gene homologous to the
RT recombinational repair gene RAD54 and to the SNF2 gene involved in
RT transcriptional activation.";
RL Yeast 8:385-395(1992).
RN [6]
RP IDENTIFICATION IN THE GGR COMPLEX, AND FUNCTION.
RX PubMed=10601031; DOI=10.1101/gad.13.23.3052;
RA Reed S.H., Akiyama M., Stillman B., Friedberg E.C.;
RT "Yeast autonomously replicating sequence binding factor is involved in
RT nucleotide excision repair.";
RL Genes Dev. 13:3052-3058(1999).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION OF THE GGR COMPLEX.
RX PubMed=15177043; DOI=10.1016/j.dnarep.2003.11.004;
RA Yu S., Owen-Hughes T., Friedberg E.C., Waters R., Reed S.H.;
RT "The yeast Rad7/Rad16/Abf1 complex generates superhelical torsion in DNA
RT that is required for nucleotide excision repair.";
RL DNA Repair 3:277-287(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the global genome repair (GGR) complex which
CC promotes global genome nucleotide excision repair (GG-NER) which
CC removes DNA damage from nontranscribing DNA. Involved in differential
CC repair of DNA after UV damage. Will repair preferentially the MAT-alpha
CC locus compared with the HML-alpha locus. {ECO:0000269|PubMed:10601031,
CC ECO:0000269|PubMed:15177043}.
CC -!- SUBUNIT: Component of the global genome repair (GGR) complex composed
CC of at least ABF1, RAD7 and RAD16. {ECO:0000269|PubMed:10601031}.
CC -!- INTERACTION:
CC P31244; P06779: RAD7; NbExp=5; IntAct=EBI-14645, EBI-14780;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; M86929; AAA34931.1; -; Genomic_DNA.
DR EMBL; X66247; CAA46974.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55616.1; -; Genomic_DNA.
DR EMBL; Z35983; CAA85071.1; -; Genomic_DNA.
DR EMBL; M83553; AAA34930.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07233.1; -; Genomic_DNA.
DR PIR; S25366; S25366.
DR RefSeq; NP_009672.1; NM_001178462.1.
DR AlphaFoldDB; P31244; -.
DR SMR; P31244; -.
DR BioGRID; 32817; 115.
DR ComplexPortal; CPX-1191; Global genome repair CUL3/RAD7/RAD16/ELC1 ubiquitin ligase complex.
DR ComplexPortal; CPX-1709; Nucleotide excision repair factor 4 complex.
DR DIP; DIP-697N; -.
DR IntAct; P31244; 44.
DR MINT; P31244; -.
DR STRING; 4932.YBR114W; -.
DR iPTMnet; P31244; -.
DR MaxQB; P31244; -.
DR PaxDb; P31244; -.
DR PRIDE; P31244; -.
DR EnsemblFungi; YBR114W_mRNA; YBR114W; YBR114W.
DR GeneID; 852411; -.
DR KEGG; sce:YBR114W; -.
DR SGD; S000000318; RAD16.
DR VEuPathDB; FungiDB:YBR114W; -.
DR eggNOG; KOG1002; Eukaryota.
DR HOGENOM; CLU_000315_2_1_1; -.
DR InParanoid; P31244; -.
DR OMA; TIQHFMN; -.
DR BioCyc; YEAST:G3O-29074-MON; -.
DR PRO; PR:P31244; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P31244; protein.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:SGD.
DR GO; GO:0008104; P:protein localization; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR GO; GO:0009411; P:response to UV; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..790
FT /note="DNA repair protein RAD16"
FT /id="PRO_0000056132"
FT DOMAIN 197..371
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 623..777
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 537..581
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 322..325
FT /note="DEAH box"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 790 AA; 91430 MW; 954317B5E85C6306 CRC64;
MQEGGFIRRR RTRSTKKSVN YNELSDDDTA VKNSKTLQLK GNSENVNDSQ DEEYRDDATL
VKSPDDDDKD FIIDLTGSDK ERTATDENTH AIKNDNDEII EIKEERDVSD DDEPLTKKRK
TTARKKKKKT STKKKSPKVT PYERNTLRLY EHHPELRNVF TDLKNAPPYV PQRSKQPDGM
TIKLLPFQLE GLHWLISQEE SIYAGGVLAD EMGMGKTIQT IALLMNDLTK SPSLVVAPTV
ALMQWKNEIE QHTKGQLKIY IYHGASRTTD IKDLQGYDVV LTTYAVLESV FRKQNYGFRR
KNGLFKQPSV LHNIDFYRVI LDEAHNIKDR QSNTARAVNN LKTQKRWCLS GTPLQNRIGE
MYSLIRFLNI NPFTKYFCTK CDCASKDWKF TDRMHCDHCS HVIMQHTNFF NHFMLKNIQK
FGVEGPGLES FNNIQTLLKN IMLRRTKVER ADDLGLPPRI VTVRRDFFNE EEKDLYRSLY
TDSKRKYNSF VEEGVVLNNY ANIFTLITRM RQLADHPDLV LKRLNNFPGD DIGVVICQLC
NDEAEEPIES KCHHKFCRLC IKEYVESFME NNNKLTCPVC HIGLSIDLSQ PALEVDLDSF
KKQSIVSRLN MSGKWQSSTK IEALVEELYK LRSNKRTIKS IVFSQFTSML DLVEWRLKRA
GFQTVKLQGS MSPTQRDETI KYFMNNIQCE VFLVSLKAGG VALNLCEASQ VFILDPWWNP
SVEWQSGDRV HRIGQYRPVK ITRFCIEDSI EARIIELQEK KANMIHATIN QDEAAISRLT
PADLQFLFNN
