RAD1/YPL022W Protein Information Help

Standard Name Rad1p
Systematic Name Ypl022wp
Alias Lpb9p
ORF Classification Verified
Description Single-stranded DNA endonuclease (with Rad10p), cleaves single-stranded DNA during nucleotide excision repair and double-strand break repair; subunit of Nucleotide Excision Repair Factor 1 (NEF1); homolog of human XPF protein (1, 2, 3)
Name Description RADiation sensitive
Experimental Data
Molecules/cell 1400 4
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,100
Molecular Weight (Da) 126,369
Isoelectric Point (pI) 5.21

Click on image for expanded interactive view
pbrowse

Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Rad1p (InterPro)
Physical Interactions There are 78 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052FC5 | P06777
MIPS: YPL022W
NCBI: 1039455 | 131810 | 172318 | 172325 | 6325235 | NP_015303.1
GenBank/EMBL/DDBJ: DAA11406.1 | K02070 | M15435 | U36624
Amino Acid Sequence (or in FASTA format)
 
       1  MSQLFYQGDS DDELQEELTR QTTQASQSSK IKNEDEPDDS NHLNEVENED
      51  SKVLDDDAVL YPLIPNEPDD IETSKPNIND IRPVDIQLTL PLPFQQKVVE
     101  NSLITEDALI IMGKGLGLLD IVANLLHVLA TPTSINGQLK RALVLVLNAK
     151  PIDNVRIKEA LEELSWFSNT GKDDDDTAVE SDDELFERPF NVVTADSLSI
     201  EKRRKLYISG GILSITSRIL IVDLLSGIVH PNRVTGMLVL NADSLRHNSN
     251  ESFILEIYRS KNTWGFIKAF SEAPETFVME FSPLRTKMKE LRLKNVLLWP
     301  RFRVEVSSCL NATNKTSHNK VIEVKVSLTN SMSQIQFGLM ECLKKCIAEL
     351  SRKNPELALD WWNMENVLDI NFIRSIDSVM VPNWHRISYE SKQLVKDIRF
     401  LRHLLKMLVT SDAVDFFGEI QLSLDANKPS VSRKYSESPW LLVDEAQLVI
     451  SYAKKRIFYK NEYTLEENPK WEQLIHILHD ISHERMTNHL QGPTLVACSD
     501  NLTCLELAKV LNASNKKRGV RQVLLNKLKW YRKQREETKK LVKEVQSQDT
     551  FPENATLNVS STFSKEQVTT KRRRTRGASQ VAAVEKLRNA GTNVDMEVVF
     601  EDHKLSEEIK KGSGDDLDDG QEENAANDSK IFEIQEQENE ILIDDGDAEF
     651  DNGELEYVGD LPQHITTHFN KDLWAEHCNE YEYVDRQDEI LISTFKSLND
     701  NCSLQEMMPS YIIMFEPDIS FIRQIEVYKA IVKDLQPKVY FMYYGESIEE
     751  QSHLTAIKRE KDAFTKLIRE NANLSHHFET NEDLSHYKNL AERKLKLSKL
     801  RKSNTRNAGG QQGFHNLTQD VVIVDTREFN ASLPGLLYRY GIRVIPCMLT
     851  VGDYVITPDI CLERKSISDL IGSLQNNRLA NQCKKMLKYY AYPTLLIEFD
     901  EGQSFSLEPF SERRNYKNKD ISTVHPISSK LSQDEIQLKL AKLVLRFPTL
     951  KIIWSSSPLQ TVNIILELKL GREQPDPSNA VILGTNKVRS DFNSTAKGLK
    1001  DGDNESKFKR LLNVPGVSKI DYFNLRKKIK SFNKLQKLSW NEINELINDE
    1051  DLTDRIYYFL RTEKEEQEQE STDENLESPG KTTDDNALHD HHNDVPEAPV
    1101  *

external links for Rad1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Rad1p
1) Prakash S and Prakash L  (2000) Nucleotide excision repair in yeast. Mutat Res 451(1-2):13-24
2) Symington LS  (2002) Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair. Microbiol Mol Biol Rev 66(4):630-70, table of contents
3) de Laat WL, et al.  (1999) Molecular mechanism of nucleotide excision repair. Genes Dev 13(7):768-85
4) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41