Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA repair protein RAD16

Gene

RAD16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Involved in differential repair of DNA after UV damage. Will repair preferentially the MAT-alpha locus compared with the HML-alpha locus.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 2178ATPPROSITE-ProRule annotation
Zinc fingeri537 – 58145RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular protein localization Source: SGD
  • nucleotide-excision repair, DNA damage recognition Source: SGD
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29074-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD16 (EC:3.6.4.-)
Alternative name(s):
ATP-dependent helicase RAD16
Gene namesi
Name:RAD16
Ordered Locus Names:YBR114W
ORF Names:YBR0909
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR114W.
SGDiS000000318. RAD16.

Subcellular locationi

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: SGD
  • nucleotide-excision repair factor 4 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790DNA repair protein RAD16PRO_0000056132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei109 – 1091PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP31244.

PTM databases

iPTMnetiP31244.

Interactioni

Subunit structurei

Component of the global genome repair (GGR) complex composed of at least ABF1, RAD7 and RAD16.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD7P067794EBI-14645,EBI-14780

Protein-protein interaction databases

BioGridi32817. 70 interactions.
DIPiDIP-697N.
IntActiP31244. 26 interactions.
MINTiMINT-616306.

Structurei

3D structure databases

ProteinModelPortaliP31244.
SMRiP31244. Positions 157-520, 535-595, 603-761.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 371175Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini623 – 777155Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi322 – 3254DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 136Poly-Arg
Compositional biasi65 – 706Poly-Asp
Compositional biasi125 – 1295Poly-Lys

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri537 – 58145RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00830000128384.
HOGENOMiHOG000179829.
InParanoidiP31244.
KOiK15083.
OMAiFFNHFML.
OrthoDBiEOG7HMS90.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEGGFIRRR RTRSTKKSVN YNELSDDDTA VKNSKTLQLK GNSENVNDSQ
60 70 80 90 100
DEEYRDDATL VKSPDDDDKD FIIDLTGSDK ERTATDENTH AIKNDNDEII
110 120 130 140 150
EIKEERDVSD DDEPLTKKRK TTARKKKKKT STKKKSPKVT PYERNTLRLY
160 170 180 190 200
EHHPELRNVF TDLKNAPPYV PQRSKQPDGM TIKLLPFQLE GLHWLISQEE
210 220 230 240 250
SIYAGGVLAD EMGMGKTIQT IALLMNDLTK SPSLVVAPTV ALMQWKNEIE
260 270 280 290 300
QHTKGQLKIY IYHGASRTTD IKDLQGYDVV LTTYAVLESV FRKQNYGFRR
310 320 330 340 350
KNGLFKQPSV LHNIDFYRVI LDEAHNIKDR QSNTARAVNN LKTQKRWCLS
360 370 380 390 400
GTPLQNRIGE MYSLIRFLNI NPFTKYFCTK CDCASKDWKF TDRMHCDHCS
410 420 430 440 450
HVIMQHTNFF NHFMLKNIQK FGVEGPGLES FNNIQTLLKN IMLRRTKVER
460 470 480 490 500
ADDLGLPPRI VTVRRDFFNE EEKDLYRSLY TDSKRKYNSF VEEGVVLNNY
510 520 530 540 550
ANIFTLITRM RQLADHPDLV LKRLNNFPGD DIGVVICQLC NDEAEEPIES
560 570 580 590 600
KCHHKFCRLC IKEYVESFME NNNKLTCPVC HIGLSIDLSQ PALEVDLDSF
610 620 630 640 650
KKQSIVSRLN MSGKWQSSTK IEALVEELYK LRSNKRTIKS IVFSQFTSML
660 670 680 690 700
DLVEWRLKRA GFQTVKLQGS MSPTQRDETI KYFMNNIQCE VFLVSLKAGG
710 720 730 740 750
VALNLCEASQ VFILDPWWNP SVEWQSGDRV HRIGQYRPVK ITRFCIEDSI
760 770 780 790
EARIIELQEK KANMIHATIN QDEAAISRLT PADLQFLFNN
Length:790
Mass (Da):91,430
Last modified:July 1, 1993 - v1
Checksum:i954317B5E85C6306
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86929 Genomic DNA. Translation: AAA34931.1.
X66247 Genomic DNA. Translation: CAA46974.1.
X78993 Genomic DNA. Translation: CAA55616.1.
Z35983 Genomic DNA. Translation: CAA85071.1.
M83553 Genomic DNA. Translation: AAA34930.1.
BK006936 Genomic DNA. Translation: DAA07233.1.
PIRiS25366.
RefSeqiNP_009672.1. NM_001178462.1.

Genome annotation databases

EnsemblFungiiYBR114W; YBR114W; YBR114W.
GeneIDi852411.
KEGGisce:YBR114W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86929 Genomic DNA. Translation: AAA34931.1.
X66247 Genomic DNA. Translation: CAA46974.1.
X78993 Genomic DNA. Translation: CAA55616.1.
Z35983 Genomic DNA. Translation: CAA85071.1.
M83553 Genomic DNA. Translation: AAA34930.1.
BK006936 Genomic DNA. Translation: DAA07233.1.
PIRiS25366.
RefSeqiNP_009672.1. NM_001178462.1.

3D structure databases

ProteinModelPortaliP31244.
SMRiP31244. Positions 157-520, 535-595, 603-761.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32817. 70 interactions.
DIPiDIP-697N.
IntActiP31244. 26 interactions.
MINTiMINT-616306.

PTM databases

iPTMnetiP31244.

Proteomic databases

MaxQBiP31244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR114W; YBR114W; YBR114W.
GeneIDi852411.
KEGGisce:YBR114W.

Organism-specific databases

EuPathDBiFungiDB:YBR114W.
SGDiS000000318. RAD16.

Phylogenomic databases

GeneTreeiENSGT00830000128384.
HOGENOMiHOG000179829.
InParanoidiP31244.
KOiK15083.
OMAiFFNHFML.
OrthoDBiEOG7HMS90.

Enzyme and pathway databases

BioCyciYEAST:G3O-29074-MONOMER.

Miscellaneous databases

NextBioi971261.
PROiP31244.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of RAD16, a gene involved in differential repair in Saccharomyces cerevisiae."
    Bang D.D., Verhage R., Goosen N., Brouwer J., de Putte P.
    Nucleic Acids Res. 20:3925-3931(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins."
    Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
    Yeast 8:397-408(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Identification of RAD16, a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation."
    Schild D., Glassner B.J., Mortimer R.K., Carlson M., Laurent B.C.
    Yeast 8:385-395(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-790.
  6. "Yeast autonomously replicating sequence binding factor is involved in nucleotide excision repair."
    Reed S.H., Akiyama M., Stillman B., Friedberg E.C.
    Genes Dev. 13:3052-3058(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE GGR COMPLEX, FUNCTION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "The yeast Rad7/Rad16/Abf1 complex generates superhelical torsion in DNA that is required for nucleotide excision repair."
    Yu S., Owen-Hughes T., Friedberg E.C., Waters R., Reed S.H.
    DNA Repair 3:277-287(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE GGR COMPLEX.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAD16_YEAST
AccessioniPrimary (citable) accession number: P31244
Secondary accession number(s): D6VQB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.