RPH1/YER169W Protein Information Help

Standard Name Rph1p
Systematic Name Yer169wp
ORF Classification Verified
Description JmjC domain-containing histone demethylase; specifically demethylates H3K36 tri- and dimethyl modification states; associates with actively transcribed (RNA polymerase II) regions in vivo and specifically targets H3K36 in its trimethylation state as its substrate; transcriptional repressor of PHR1; Rph1p phosphorylation during DNA damage is under control of the MEC1-RAD53 pathway; RPH1 has a paralog, GIS1, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6)
Name Description Regulator of PHR1 1
Gene Product KDM4 7
Experimental Data
Molecules/cell 2230 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 796
Molecular Weight (Da) 90,211
Isoelectric Point (pI) 9.84

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 Rph1p (InterPro)
Physical Interactions There are 8 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000013ACD1 | P39956
MIPS: YER169W
NCBI: 315364635 | 315364636 | 603410 | 6321017 | 731532 | NP_011096.1
GenBank/EMBL/DDBJ: DAA07831.1 | U18922
Amino Acid Sequence (or in FASTA format)
 
       1  MTKLIAPSEI VGGVPVFKPT YEQFEDFYAY CKAINKYGMK SGVVKVIPPK
      51  EWKDKLDLPY SAETLQKIKI KSPIQQHISG NKGLFMVQNV EKNKTYNIIQ
     101  WKDLSKDYVP PEDPKARRNS RKGSVSKSTK LKLKNFESSF NIDDFEQFRT
     151  EYTIDLSDFQ NTERLKFLEE YYWKTLNFTT PMYGADTPGS IFPEGLNVWN
     201  VAKLPNILDH METKVPGVND SYLYAGLWKA SFSWHLEDQD LYSINYIHFG
     251  APKQWYSIPQ EDRFKFYKFM QEQFPEEAKN CPEFLRHKMF LASPKLLQEN
     301  GIRCNEIVHH EGEFMITYPY GYHAGFNYGY NLAESVNFAL EEWLPIGKKA
     351  GKCHCISDSV EIDVKKLAKS WRDNNKESKG TPPLNQLPNP AMPLLHRPTL
     401  KEMESSSLRS TSPDVGHFSN FKSKSSGVSS PLLSRMKDYS NIVEPTLEDP
     451  TLKLKRISSF QEQPLNKLLK RETSQTAMLT DHEDNIVAMS LTSMANSAAS
     501  SPRLPLSRLN SSNELSNAQP LLDMTNNTLA FPRPNGPSGL NPLLYISNKN
     551  ISGISHSAPH SPVNPNISLI KRVKSPNIVT LNISRESSRS PIALNYEARQ
     601  QHSQQHSFST PSTVSNLSTS VLGPLSDTND IKTPHPERPN HKTANRILKK
     651  ESPVETSKSN LILSKVASTR QEDSFTSRND DLDKEQGSSP LNSKFAPEEI
     701  VLSGKNKIYI CKECQRKFSS GHHLTRHKKS VHSGEKPHSC PKCGKRFKRR
     751  DHVLQHLNKK IPCISNETTV DAPIMNPTVQ PQDGKAAINQ QSTPLN*

external links for Rph1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
YGOB BioPIXIE MIPS YeastRC Public Image Repository
YOGY CYC2008 (complexes) Pfam domains

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Rph1p
1) Jang YK, et al.  (1999) RPH1 and GIS1 are damage-responsive repressors of PHR1. Mol Cell Biol 19(11):7630-8
2) Kim EM, et al.  (2002) Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase. Nucleic Acids Res 30(3):643-8
3) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
4) Tu S, et al.  (2007) Identification of histone demethylases in Saccharomyces cerevisiae. J Biol Chem 282(19):14262-71
5) Klose RJ, et al.  (2007) Demethylation of histone H3K36 and H3K9 by Rph1: a vestige of an H3K9 methylation system in Saccharomyces cerevisiae? Mol Cell Biol 27(11):3951-61
6) Kwon DW and Ahn SH  (2011) Role of yeast JmjC-domain containing histone demethylases in actively transcribed regions. Biochem Biophys Res Commun 410(3):614-9
7) Allis CD, et al.  (2007) New nomenclature for chromatin-modifying enzymes. Cell 131(4):633-6
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41