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Protein Overview: RTT107

General Information:
Name(s) found: RTT107 / YHR154W [SGD]
Description(s) found:
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  • gi|731729|sp|P38850.1|RT107_YEAST RecName: Full=Regulator of Ty1 transposition protein 107 [NCBI NR]
  • gi|6321948|ref|NP_012024.1| Protein implicated in Mms22-dependent DNA repair during S phase, DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 t [NCBI NR]
  • pir||S46755 hypothetical protein YHR154w - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|500651|gb|AAB68978.1| Yhr154wp [Saccharomyces cerevisiae] [NCBI NR]
  • (P38850) Hypothetical 123.0 kDa protein in SPO16-REC104 intergenic region [Swiss-Prot]
  • Regulator of Ty1 transposition protein 107 OS=Saccharomyces cerevisiae GN=RTT107 PE=1 SV=1 [Swiss-Prot]
  • RTT107 Establishes Silent Chromatin [mips]
  • Protein implicated in Mms22-dependent DNA repair during S phase, DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 transposition [SGD]
  • ESC4, Chr VIII from 402967-406179 [yeast_orfs2]
  • Chr VIII from 402967-406179 [yeastorf3.fasta]
  • RTT107 SGDID:S0001197, Chr VIII from 402967-406179, Verified ORF [yeastflysequest.fasta]
  • RTT107 SGDID:S0001197, Chr VIII from 402968-406180, Verified ORF [10112005cervSGD.fasta]
  • Regulator of Ty1 Transposition; Establishes Silent Chromatin; involved in silencing [Saccharomyces cerevisiae]gi|731729|sp|P38850|YHV4_YEAST Hypothetical 123.0 kDa protein in SPO16-REC104 intergenic regiongi|626668|pir||S46755 hypothetical protein YHR15 [nrdb_11152004_Chlamydomonas]
  • RTT107 SGDID:S000001197, Chr VIII from 402969-406181, Verified ORF, "Protein that interacts with Mms22p and is implicated in Mms22-dependent DNA repair during S phase, damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; has four BRCT doma [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • RTT107 SGDID:S000001197, Chr VIII from 402969-406181, Verified ORF, "Protein implicated in Mms22-dependent DNA repair during S phase, DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT d [yeast-contam.fasta]
  • Regulator of Ty1 transposition protein 107 [nr-271106-contam.fasta]
  • Yhr154wp [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Protein implicated in Mms22-dependent DNA repair during S phase, DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 transposition; Rtt107p [Sacch [nr-271106-contam.fasta]
  • RTT107 SGDID:S000001197, Chr VIII from 402969-406181, Verified ORF, "Protein implicated in Mms22-dependent DNA repair during S phase, DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 transposition" [yeast-bovrabprots.fasta]
  • [chemostatdb.fasta]
  • Regulator of Ty1 transposition protein 107 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RTT107 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • RTT107 SGDID:S000001197, Chr VIII from 402966-406178, Genome Release 64-1-1, Verified ORF, "Protein implicated in Mms22-dependent DNA repair during S phase; involved in recruiting the SMC5/6 complex to double-strand breaks; DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 transposition" [yeast-030211-contam.fasta]
  • RTT107 SGDID:S000001197, Chr VIII from 402966-406178, Genome Release 64-2-1, Verified ORF, "Protein implicated in Mms22-dependent DNA repair during S phase; involved in recruiting the SMC5/6 complex to double-strand breaks; DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 transposition; relative distribution to nuclear foci increases upon DNA replication stress" [20141208_orf_trans.fasta]
  • YHR154W SGDID:S000001197, Chr VIII from 402966-406178, Genome Release 64-1-1, Verified ORF, "Protein implicated in Mms22-dependent DNA repair during S phase; involved in recruiting the SMC5/6 complex to double-strand breaks; DNA damage induces phosphorylation by Mec1p at one or more SQ/TQ motifs; interacts with Mms22p and Slx4p; has four BRCT domains; has a role in regulation of Ty1 transposition" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 1070 amino acids

    Gene Ontology:
    Cellular Component: nucleus [IDALink to PubMed article]
    Biological Process: negative regulation of transposition, DNA-mediated [IMPLink to PubMed article]
    double-strand break repair [IMPLink to PubMed article]
    Molecular Function: molecular_function [ND]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MSTSLLFEQL NFLILVAAEA ELPIAHSTRK LLMDNSCNNC QIYELYNENL KDVKTDKDWF  60
   61 MNKFGPQTVH FVISNTINFP FYKIVYFDLL IPVVSHTWVQ DSVKTKRHLR TNMYSPNPFH 120
  121 LLRDCQVYIS KSSFNKCEYI LYSDLLHLLG GTLVNYISNR TTHVIVQSPQ DPIIATVSKL 180
  181 TFGSFSSSST NKHTEKPLRE WKFVYPIWIL YHFKMAKPLK GELATLCELD MQDTSEEQLF 240
  241 AKWEEVIGDK QTSSSQLTLH PNKTLFKNHH FAISPDLNFF TPLYWFLKGF IEDLDGKVTP 300
  301 LSFSDDLKSV YQAFPDIDCY IGHSANSPIL EKTKSIKPEI HVGNVSWLFY MFALQKFTPV 360
  361 SQCKLIHQPF HAKLFTSKEL TVAYTNYFGS QRFYIQRLVE ILGGLSTPEL TRKNTHLITK 420
  421 STIGKKFKVA KKWSLDPQNA IIVTNHMWLE QCYMNNSKLN PKDSRFQNFK LDDNMGWNIG 480
  481 QIGMDHSSLP TPKNLSMVTY DTQSISEKPP PTNDQMDQIN DNTNVLSKKD GTPISSFENS 540
  541 IDEKIDKLQK ISGEVAVTHS GDLERSFVSR PSRASFPVVD SKKSNLQKKD SNSDISMETE 600
  601 VFCEGHEKRE EKEFTKPITE YDAPKKQEIR EQSRKKNDID YKKEEEETEL QVQLGQRTKR 660
  661 EIKTSKKNEK EKETNECHIE VDQMTNEKQG EESTGKLIST EDVTSKKDTD KFSHLFEGLS 720
  721 DNDDHINDEK PAVNSKYTTP KTSQNITSGV DTPTTAQTQV FMPSSGNSRL AKTQAAKRLH 780
  781 TDIESLNEFQ KNFKRKRIDS EEISLSQDVE RSNNNKELAT KAEKILARFN ELPNYDLKAV 840
  841 CTGCFHDGFN EVDIEILNQL GIKIFDNIKE TDKLNCIFAP KILRTEKFLK SLSFEPLKFA 900
  901 LKPEFIIDLL KQIHSKKDKL SQININLFDY EINGINESII SKTKLPTKVF ERANIRCINL 960
  961 VNDIPGGVDT IGSVLKAHGI EKINVLRSKK CTFEDIIPND VSKQENGGIF KYVLIVTKAS1020
 1021 QVKKFTKLIN DRDKNETILI VEWNWCVESI FHLNVDFTSK KNVLYQKKNN

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Krogan NJ, et al. (2006) DBP10 RTT107
    View Details Ho Y, et al. (2002) GDH2 MMS22 RTT101 RTT107

    Mass Spectrometry Data

    The following runs contain data for this protein:

      BAIT COMMENTS PUBLICATION
    View Run MLP2 #12 Mitotic Prep1-TiO2 Flowthrough Keck JM, et al. (2011)
    View Run MLP2 #02 Alpha Factor Prep1-TiO2 enriched, new search criteria Keck JM, et al. (2011)

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

    New Feature: Upload Your Own Microscopy Data

      PROTEIN(S) PUBLICATION
    View Data RTT107 Huh WK, et al. (2003)

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..119] ORFEUS 8.32 Breast cancer associated protein, BRCA1
    2 View Details [120..260] ORFEUS 8.32 Breast cancer associated protein, BRCA1
    3 View Details [261..359] deduced N/A No confident structure predictions are available.
    4 View Details [360..452] ORFEUS 7.91 NAD+-dependent DNA ligase, domain 3; NAD+-dependent DNA ligase; Adenylation domain of NAD+-dependent DNA ligase
    5 View Details [453..747] PSI-BLAST 32.39794 Heavy meromyosin subfragment
    6 View Details [748..834] PSI-BLAST 4.30103 Tropomyosin
    7 View Details [835..1070] MSA 2.803997 View MSA. No confident structure predictions are available.

    Functions predicted (by domain):

    # Gene Ontology predictions
    1 No functions predicted.
    2
    Term Confidence Notes
  • damaged DNA binding
    		•  2.78264840479873 bayes_pls_golite062009
  • binding
    		•  2.39904249850929 bayes_pls_golite062009
  • nucleic acid binding
    		•  2.01217461524277 bayes_pls_golite062009
  • DNA binding
    		•  1.94626538619156 bayes_pls_golite062009
  • transcription regulator activity
    		•  1.6615655042871 bayes_pls_golite062009
  • protein binding
    		•  1.25126059595954 bayes_pls_golite062009
  • sequence-specific DNA binding
    		•  0.87932139868144 bayes_pls_golite062009
  • telomeric DNA binding
    		•  0.53051501110858 bayes_pls_golite062009
  • structure-specific DNA binding
    		•  0.436014478237905 bayes_pls_golite062009
  • transcription activator activity
    		•  0.355931500039388 bayes_pls_golite062009
  • ligase activity
    		•  0.334005199756535 bayes_pls_golite062009
  • transcription factor binding
    		•  0.27424353108553 bayes_pls_golite062009
  • transcription repressor activity
    		•  0.210876161781476 bayes_pls_golite062009
  • catalytic activity
    		•  0.17721113579921 bayes_pls_golite062009
  • double-stranded DNA binding
    		•  0.163902958036495 bayes_pls_golite062009
    3 No functions predicted.
    4 No functions predicted.
    5 No functions predicted.
    6 No functions predicted.
    7 No functions predicted.


    Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076


    Philius Transmembrane Prediction:

    [View Details]
    Source: Reynolds et al. 2008. Manuscript submitted Philius confidence legend
    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle