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P31244 (RAD16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA repair protein RAD16

EC=3.6.4.-
Alternative name(s):
ATP-dependent helicase RAD16
Gene names
Name:RAD16
Ordered Locus Names:YBR114W
ORF Names:YBR0909
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length790 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 compaired with the HML-alpha locus. Ref.6 Ref.9

Subunit structure

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

Subcellular location

Nucleus.

Miscellaneous

Present with 358 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 RING-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD7P067794EBI-14645,EBI-14780

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 790790DNA repair protein RAD16
PRO_0000056132

Regions

Domain197 – 371175Helicase ATP-binding
Domain623 – 777155Helicase C-terminal
Nucleotide binding210 – 2178ATP Potential
Zinc finger537 – 58145RING-type
Motif322 – 3254DEAH box
Compositional bias8 – 136Poly-Arg
Compositional bias65 – 706Poly-Asp
Compositional bias125 – 1295Poly-Lys

Amino acid modifications

Modified residue251Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12
Modified residue491Phosphoserine Ref.11 Ref.12
Modified residue1091Phosphoserine Ref.10 Ref.12

Sequences

Sequence LengthMass (Da)Tools
P31244 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 954317B5E85C6306

FASTA79091,430
        10         20         30         40         50         60 
MQEGGFIRRR RTRSTKKSVN YNELSDDDTA VKNSKTLQLK GNSENVNDSQ DEEYRDDATL 

        70         80         90        100        110        120 
VKSPDDDDKD FIIDLTGSDK ERTATDENTH AIKNDNDEII EIKEERDVSD DDEPLTKKRK 

       130        140        150        160        170        180 
TTARKKKKKT STKKKSPKVT PYERNTLRLY EHHPELRNVF TDLKNAPPYV PQRSKQPDGM 

       190        200        210        220        230        240 
TIKLLPFQLE GLHWLISQEE SIYAGGVLAD EMGMGKTIQT IALLMNDLTK SPSLVVAPTV 

       250        260        270        280        290        300 
ALMQWKNEIE QHTKGQLKIY IYHGASRTTD IKDLQGYDVV LTTYAVLESV FRKQNYGFRR 

       310        320        330        340        350        360 
KNGLFKQPSV LHNIDFYRVI LDEAHNIKDR QSNTARAVNN LKTQKRWCLS GTPLQNRIGE 

       370        380        390        400        410        420 
MYSLIRFLNI NPFTKYFCTK CDCASKDWKF TDRMHCDHCS HVIMQHTNFF NHFMLKNIQK 

       430        440        450        460        470        480 
FGVEGPGLES FNNIQTLLKN IMLRRTKVER ADDLGLPPRI VTVRRDFFNE EEKDLYRSLY 

       490        500        510        520        530        540 
TDSKRKYNSF VEEGVVLNNY ANIFTLITRM RQLADHPDLV LKRLNNFPGD DIGVVICQLC 

       550        560        570        580        590        600 
NDEAEEPIES KCHHKFCRLC IKEYVESFME NNNKLTCPVC HIGLSIDLSQ PALEVDLDSF 

       610        620        630        640        650        660 
KKQSIVSRLN MSGKWQSSTK IEALVEELYK LRSNKRTIKS IVFSQFTSML DLVEWRLKRA 

       670        680        690        700        710        720 
GFQTVKLQGS MSPTQRDETI KYFMNNIQCE VFLVSLKAGG VALNLCEASQ VFILDPWWNP 

       730        740        750        760        770        780 
SVEWQSGDRV HRIGQYRPVK ITRFCIEDSI EARIIELQEK KANMIHATIN QDEAAISRLT 

       790 
PADLQFLFNN 

« Hide

References

« Hide 'large scale' references
[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: 1508678] [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: 1626431] [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. expand/collapse author list , 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: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 1626430] [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: 10601031] [Abstract]
Cited for: IDENTIFICATION IN THE GGR COMPLEX, FUNCTION.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY.
Strain: SUB592.
[9]"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: 15177043] [Abstract]
Cited for: FUNCTION OF THE GGR COMPLEX.
[10]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, MASS SPECTROMETRY.
Strain: ADR376.
[11]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-49, MASS SPECTROMETRY.
[12]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-49 AND SER-109, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS25366.
RefSeqNP_009672.1. NM_001178462.1.

3D structure databases

ProteinModelPortalP31244.
SMRP31244. Positions 171-789.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-697N.
IntActP31244. 36 interactions.
MINTMINT-616306.
STRINGP31244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR114W; YBR114W; YBR114W.
GeneID852411.
KEGGsce:YBR114W.
NMPDRfig|4932.3.peg.373.

Organism-specific databases

CYGDYBR114w.
SGDS000000318. RAD16.

Phylogenomic databases

eggNOGfuNOG05094.
GeneTreeEFGT00050000000148.
HOGENOMHBG522881.
OMAPIESKCH.
OrthoDBEOG4Q5CXS.

Gene expression databases

ArrayExpressP31244.
GenevestigatorP31244.
GermOnlineYBR114W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR014001. DEAD-like_helicase.
IPR001650. Helicase_C.
IPR000330. SNF2_N.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KOK15083.
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00690. DEAH_ATP_HELICASE. False negative.
PS51192. 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]
ProtoNetSearch...

Other

NextBio971261.

Entry information

Entry nameRAD16_YEAST
AccessionPrimary (citable) accession number: P31244
Secondary accession number(s): D6VQB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: January 25, 2012
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

SIMILARITY comments

Index of protein domains and families