Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P38850

- RT107_YEAST

UniProt

P38850 - RT107_YEAST

Protein

Regulator of Ty1 transposition protein 107

Gene

RTT107

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for resumption of chromosome replication after DNA damage, specifically in S phase. Is recruited to chromatin in the presence of RTT109 and RTT101 in response to stalled replication forks and acts as a scaffold during DNA repair.2 Publications

    GO - Biological processi

    1. double-strand break repair Source: SGD
    2. negative regulation of transposition, RNA-mediated Source: SGD

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31189-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of Ty1 transposition protein 107
    Alternative name(s):
    Establishes silent chromatin protein 4
    Gene namesi
    Name:RTT107
    Synonyms:ESC4
    Ordered Locus Names:YHR154W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR154w.
    SGDiS000001197. RTT107.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Recruited to chromatin in response to replication fork stalling.

    GO - Cellular componenti

    1. Cul8-RING ubiquitin ligase complex Source: SGD
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10701070Regulator of Ty1 transposition protein 107PRO_0000097502Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei304 – 3041Phosphoserine2 Publications
    Modified residuei532 – 5321Phosphothreonine4 Publications
    Modified residuei591 – 5911Phosphoserine2 Publications
    Modified residuei593 – 5931Phosphoserine2 Publications
    Modified residuei720 – 7201Phosphoserine2 Publications
    Modified residuei800 – 8001Phosphoserine2 Publications
    Modified residuei806 – 8061Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by MEC1.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38850.
    PaxDbiP38850.
    PeptideAtlasiP38850.

    Expressioni

    Gene expression databases

    GenevestigatoriP38850.

    Interactioni

    Subunit structurei

    Forms a complex with the cullin-RING ligase (CRL) RTT101(MMS1-MMS22). Interacts with MMS22 and RTT101. Interacts with histone H2A; requires H2A to be phosphorylated (gamma-H2A). Interacts with RAD55.4 Publications

    Protein-protein interaction databases

    BioGridi36588. 353 interactions.
    DIPiDIP-6297N.
    IntActiP38850. 13 interactions.
    MINTiMINT-702893.
    STRINGi4932.YHR154W.

    Structurei

    Secondary structure

    1
    1070
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi822 – 8276
    Beta strandi837 – 8448
    Helixi851 – 8599
    Beta strandi862 – 8643
    Helixi870 – 8723
    Beta strandi876 – 8783
    Helixi886 – 8916
    Beta strandi899 – 9013
    Helixi904 – 91310
    Helixi927 – 9304
    Helixi937 – 9426
    Beta strandi945 – 9473
    Helixi949 – 9524
    Beta strandi957 – 9615
    Helixi968 – 97710
    Beta strandi982 – 9865
    Turni988 – 9903
    Helixi993 – 9953
    Beta strandi1011 – 10155
    Helixi1019 – 103214
    Beta strandi1038 – 10414
    Helixi1043 – 10519
    Beta strandi1063 – 10675

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3T7IX-ray2.30A/B820-1070[»]
    3T7JX-ray2.04A/B820-1070[»]
    3T7KX-ray2.03A/B820-1070[»]
    ProteinModelPortaliP38850.
    SMRiP38850. Positions 821-1068.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 103102BRCT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini117 – 21397BRCT 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 35293BRCT 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini369 – 45385BRCT 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini829 – 91082BRCT 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini934 – 1049116BRCT 6PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 6 BRCT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG248673.
    OMAiRINTIFA.
    OrthoDBiEOG769ZTW.

    Family and domain databases

    Gene3Di3.40.50.10190. 2 hits.
    InterProiIPR001357. BRCT_dom.
    [Graphical view]
    PfamiPF00533. BRCT. 2 hits.
    [Graphical view]
    SMARTiSM00292. BRCT. 4 hits.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 2 hits.
    PROSITEiPS50172. BRCT. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38850-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTSLLFEQL NFLILVAAEA ELPIAHSTRK LLMDNSCNNC QIYELYNENL     50
    KDVKTDKDWF MNKFGPQTVH FVISNTINFP FYKIVYFDLL IPVVSHTWVQ 100
    DSVKTKRHLR TNMYSPNPFH LLRDCQVYIS KSSFNKCEYI LYSDLLHLLG 150
    GTLVNYISNR TTHVIVQSPQ DPIIATVSKL TFGSFSSSST NKHTEKPLRE 200
    WKFVYPIWIL YHFKMAKPLK GELATLCELD MQDTSEEQLF AKWEEVIGDK 250
    QTSSSQLTLH PNKTLFKNHH FAISPDLNFF TPLYWFLKGF IEDLDGKVTP 300
    LSFSDDLKSV YQAFPDIDCY IGHSANSPIL EKTKSIKPEI HVGNVSWLFY 350
    MFALQKFTPV SQCKLIHQPF HAKLFTSKEL TVAYTNYFGS QRFYIQRLVE 400
    ILGGLSTPEL TRKNTHLITK STIGKKFKVA KKWSLDPQNA IIVTNHMWLE 450
    QCYMNNSKLN PKDSRFQNFK LDDNMGWNIG QIGMDHSSLP TPKNLSMVTY 500
    DTQSISEKPP PTNDQMDQIN DNTNVLSKKD GTPISSFENS IDEKIDKLQK 550
    ISGEVAVTHS GDLERSFVSR PSRASFPVVD SKKSNLQKKD SNSDISMETE 600
    VFCEGHEKRE EKEFTKPITE YDAPKKQEIR EQSRKKNDID YKKEEEETEL 650
    QVQLGQRTKR EIKTSKKNEK EKETNECHIE VDQMTNEKQG EESTGKLIST 700
    EDVTSKKDTD KFSHLFEGLS DNDDHINDEK PAVNSKYTTP KTSQNITSGV 750
    DTPTTAQTQV FMPSSGNSRL AKTQAAKRLH TDIESLNEFQ KNFKRKRIDS 800
    EEISLSQDVE RSNNNKELAT KAEKILARFN ELPNYDLKAV CTGCFHDGFN 850
    EVDIEILNQL GIKIFDNIKE TDKLNCIFAP KILRTEKFLK SLSFEPLKFA 900
    LKPEFIIDLL KQIHSKKDKL SQININLFDY EINGINESII SKTKLPTKVF 950
    ERANIRCINL VNDIPGGVDT IGSVLKAHGI EKINVLRSKK CTFEDIIPND 1000
    VSKQENGGIF KYVLIVTKAS QVKKFTKLIN DRDKNETILI VEWNWCVESI 1050
    FHLNVDFTSK KNVLYQKKNN 1070
    Length:1,070
    Mass (Da):123,017
    Last modified:February 1, 1995 - v1
    Checksum:i767931285BB52580
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10397 Genomic DNA. Translation: AAB68978.1.
    BK006934 Genomic DNA. Translation: DAA06847.1.
    PIRiS46755.
    RefSeqiNP_012024.1. NM_001179285.1.

    Genome annotation databases

    EnsemblFungiiYHR154W; YHR154W; YHR154W.
    GeneIDi856559.
    KEGGisce:YHR154W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10397 Genomic DNA. Translation: AAB68978.1 .
    BK006934 Genomic DNA. Translation: DAA06847.1 .
    PIRi S46755.
    RefSeqi NP_012024.1. NM_001179285.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3T7I X-ray 2.30 A/B 820-1070 [» ]
    3T7J X-ray 2.04 A/B 820-1070 [» ]
    3T7K X-ray 2.03 A/B 820-1070 [» ]
    ProteinModelPortali P38850.
    SMRi P38850. Positions 821-1068.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36588. 353 interactions.
    DIPi DIP-6297N.
    IntActi P38850. 13 interactions.
    MINTi MINT-702893.
    STRINGi 4932.YHR154W.

    Proteomic databases

    MaxQBi P38850.
    PaxDbi P38850.
    PeptideAtlasi P38850.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR154W ; YHR154W ; YHR154W .
    GeneIDi 856559.
    KEGGi sce:YHR154W.

    Organism-specific databases

    CYGDi YHR154w.
    SGDi S000001197. RTT107.

    Phylogenomic databases

    eggNOGi NOG248673.
    OMAi RINTIFA.
    OrthoDBi EOG769ZTW.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31189-MONOMER.

    Miscellaneous databases

    NextBioi 982381.

    Gene expression databases

    Genevestigatori P38850.

    Family and domain databases

    Gene3Di 3.40.50.10190. 2 hits.
    InterProi IPR001357. BRCT_dom.
    [Graphical view ]
    Pfami PF00533. BRCT. 2 hits.
    [Graphical view ]
    SMARTi SM00292. BRCT. 4 hits.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 2 hits.
    PROSITEi PS50172. BRCT. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage."
      Rouse J.
      EMBO J. 23:1188-1197(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY MEC1.
    6. "Esc4/Rtt107 and the control of recombination during replication."
      Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.
      DNA Repair 5:618-628(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD55 AND MMS22, SUBCELLULAR LOCATION.
    7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase."
      Roberts T.M., Zaidi I.W., Vaisica J.A., Peter M., Brown G.W.
      Mol. Biol. Cell 19:171-180(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RTT101.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; THR-532; SER-591; SER-593; SER-800 AND SER-806, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532; SER-720 AND SER-806, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage response and transcriptional silencing."
      Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C., Kamura T.
      J. Biol. Chem. 285:9858-9867(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MMS22, IDENTIFICATION IN A COMPLEX WITH RTT101 AND MMS1.
    12. "Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals critical role in interaction with phosphorylated histone H2A during DNA damage repair."
      Li X., Liu K., Li F., Wang J., Huang H., Wu J., Shi Y.
      J. Biol. Chem. 287:9137-9146(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 820-1070 IN COMPLEX WITH HTA1.

    Entry informationi

    Entry nameiRT107_YEAST
    AccessioniPrimary (citable) accession number: P38850
    Secondary accession number(s): D3DLA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1380 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3