RAD26/YJR035W Protein Information Help

Standard Name Rad26p 1
Systematic Name Yjr035wp
ORF Classification Verified
Description Protein involved in transcription-coupled nucleotide excision repair of UV-induced DNA lesions; recruitment to DNA lesions is dependent on an elongating RNA polymerase II; homolog of human CSB protein (2, 3)
Name Description RADiation sensitive
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,085
Molecular Weight (Da) 124,527
Isoelectric Point (pI) 7.47

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Rad26p (InterPro)
Physical Interactions There are 38 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000133021 | P40352
MIPS: YJR035W
NCBI: 1015683 | 506419 | 550429 | 6322495 | 730465 | NP_012569.1
GenBank/EMBL/DDBJ: DAA08824.1 | L26910 | X81635 | Z49535
External Classifications EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
EC: 3.6.4.12 [DNA helicase]
Amino Acid Sequence (or in FASTA format)
 
       1  MEDKEQQDNA KLENNESLKD LGVNVLSQSS LEEKIANDVT NFSNLQSLQQ
      51  EETRLERSKT ALQRYVNKKN HLTRKLNNTT RISVKQNLRD QIKNLQSDDI
     101  ERVLKDIDDI QSRIKELKEQ VDQGAENKGS KEGLQRPGET EKEFLIRTGK
     151  ITAFGHKAGF SLDTANREYA KNDEQKDEDF EMATEQMVEN LTDEDDNLSD
     201  QDYQMSGKES EDDEEEENDD KILKELEDLR FRGQPGEAKD DGDELYYQER
     251  LKKWVKQRSC GSQRSSDLPE WRRPHPNIPD AKLNSQFKIP GEIYSLLFNY
     301  QKTCVQWLYE LYQQNCGGII GDEMGLGKTI QVIAFIAALH HSGLLTGPVL
     351  IVCPATVMKQ WCNEFQHWWP PLRTVILHSM GSGMASDQKF KMDENDLENL
     401  IMNSKPSDFS YEDWKNSTRT KKALESSYHL DKLIDKVVTD GHILITTYVG
     451  LRIHSDKLLK VKWQYAVLDE GHKIRNPDSE ISLTCKKLKT HNRIILSGTP
     501  IQNNLTELWS LFDFIFPGKL GTLPVFQQQF VIPINIGGYA NATNIQVQTG
     551  YKCAVALRDL ISPYLLRRVK ADVAKDLPQK KEMVLFCKLT KYQRSKYLEF
     601  LHSSDLNQIQ NGKRNVLFGI DILRKICNHP DLLDRDTKRH NPDYGDPKRS
     651  GKMQVVKQLL LLWHKQGYKA LLFTQSRQML DILEEFISTK DPDLSHLNYL
     701  RMDGTTNIKG RQSLVDRFNN ESFDVFLLTT RVGGLGVNLT GANRIIIFDP
     751  DWNPSTDMQA RERAWRIGQK REVSIYRLMV GGSIEEKIYH RQIFKQFLTN
     801  RILTDPKQKR FFKIHELHDL FSLGGENGYS TEELNEEVQK HTENLKNSKS
     851  EESDDFEQLV NLSGVSKLES FYNGKEKKEN SKTEDDRLIE GLLGGESNLE
     901  TVMSHDSVVN SHAGSSSSNI ITKEASRVAI EAVNALRKSR KKITKQYEIG
     951  TPTWTGRFGK AGKIRKRDPL KNKLTGSAAI LGNITKSQKE ASKEARQENY
    1001  DDGITFARSK EINSNTKTLE NIRAYLQKQN NFFSSSVSIL NSIGVSLSDK
    1051  EDVIKVRALL KTIAQFDKER KGWVLDEEFR NNNAS*

external links for Rad26p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Rad26p
1) van Gool AJ, et al.  (1994) RAD26, the functional S. cerevisiae homolog of the Cockayne syndrome B gene ERCC6. EMBO J 13(22):5361-9
2) Lee SK, et al.  (2002) Yeast RAD26, a homolog of the human CSB gene, functions independently of nucleotide excision repair and base excision repair in promoting transcription through damaged bases. Mol Cell Biol 22(12):4383-9
3) Malik S, et al.  (2010) Rad26p, a transcription-coupled repair factor, is recruited to the site of DNA lesion in an elongating RNA polymerase II-dependent manner in vivo. Nucleic Acids Res 38(5):1461-77