CMR1/YDL156W Protein Information

Standard Name	Cmr1p 1, 2
Systematic Name	Ydl156wp
ORF Classification	Verified
Description	DNA-binding protein with preference for UV-damaged DNA; protein sequence contains three WD domains (WD-40 repeat); green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and nucleus; potential regulatory target of Mbp1p, which binds to the promoter region; co-localizes with Hos2p in nuclear foci in response to DNA damage by MMS (2, 3, 4, 5, 6)
Name Description	Changed Mutation Rate 1

Experimental Data
Molecules/cell	3810 7

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	522
Molecular Weight (Da)	59,155
Isoelectric Point (pI)	7.26

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Cmr1p (InterPro)
Physical Interactions	There are 317 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00000531D4 \| Q12510 MIPS: YDL156W NCBI: 1321948 \| 1431247 \| 6320045 \| 74676615 \| NP_010125.1 \| NM_001180216.1 GenBank/EMBL/DDBJ: DAA11704.1 \| X97751 \| Z74204

Amino Acid Sequence (or in FASTA format)
1 MPELTEFQKK RLENIKRNND LLKKLHLSGV ASQIKHEAGV LEKSRAPAKK 51 KQKTTNTRAT KSASPTLPTR RSRRLRGESA DDVKGIPNVN DNQLLKMGSP 101 DGQDKNFIDA IKEKPVIGDV KLSDLIKDED ESALLEKFKR FNNGNFSSGD 151 FFEEIKKRQG DVTGMDEFDL DLYDVFQPNE IKITYERISA TYFHPAMEKK 201 LIIAGDTSGT VGFWNVRDEP LADSEEDRME EPDITRVKLF TKNVGRIDCF 251 PADTSKILLT SYDGSIRSVH LNNLQSEEVL TLKNEYDDSL GISDCQFSYE 301 NPNVLFLTTL GGEFTTFDTR VKKSEYNLRR LADKKIGSMA INPMRPYEIA 351 TGSLDRTLKI WDTRNLVKKP EWSQYEDYPS HEIVSTYDSR LSVSAVSYSP 401 TDGTLVCNGY DDTIRLFDVK SRDHLSAKLE PKLTIQHNCQ TGRWTSILKA 451 RFKPNKNVFA IANMKRAIDI YNSEGQQLAH LPTATVPAVI SWHPLRNWIA 501 GGNSSGKIFL FTDDSGTIKQ EE*

Amino Acid Sequence (or in FASTA format)

       1  MPELTEFQKK RLENIKRNND LLKKLHLSGV ASQIKHEAGV LEKSRAPAKK
      51  KQKTTNTRAT KSASPTLPTR RSRRLRGESA DDVKGIPNVN DNQLLKMGSP
     101  DGQDKNFIDA IKEKPVIGDV KLSDLIKDED ESALLEKFKR FNNGNFSSGD
     151  FFEEIKKRQG DVTGMDEFDL DLYDVFQPNE IKITYERISA TYFHPAMEKK
     201  LIIAGDTSGT VGFWNVRDEP LADSEEDRME EPDITRVKLF TKNVGRIDCF
     251  PADTSKILLT SYDGSIRSVH LNNLQSEEVL TLKNEYDDSL GISDCQFSYE
     301  NPNVLFLTTL GGEFTTFDTR VKKSEYNLRR LADKKIGSMA INPMRPYEIA
     351  TGSLDRTLKI WDTRNLVKKP EWSQYEDYPS HEIVSTYDSR LSVSAVSYSP
     401  TDGTLVCNGY DDTIRLFDVK SRDHLSAKLE PKLTIQHNCQ TGRWTSILKA
     451  RFKPNKNVFA IANMKRAIDI YNSEGQQLAH LPTATVPAVI SWHPLRNWIA
     501  GGNSSGKIFL FTDDSGTIKQ EE*

external links for Cmr1p

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 Cmr1p

1)	Offman J (2008) personal communication
2)	Choi DH, et al. (2012) Saccharomyces cerevisiae Cmr1 protein preferentially binds to UV-damaged DNA in vitro. J Microbiol 50(1):112-8
3)	Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
4)	Hellauer K, et al. (2005) Large-scale analysis of genes that alter sensitivity to the anticancer drug tirapazamine in Saccharomyces cerevisiae. Mol Pharmacol 68(5):1365-75
5)	Brohee S, et al. (2011) Unraveling networks of co-regulated genes on the sole basis of genome sequences. Nucleic Acids Res 39(15):6340-58
6)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
7)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41