Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Regulator of Ty1 transposition protein 107

Gene

RTT107

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 3041Phosphoserine1 Publication
Modified residuei532 – 5321Phosphothreonine3 Publications
Modified residuei591 – 5911Phosphoserine1 Publication
Modified residuei593 – 5931Phosphoserine1 Publication
Modified residuei720 – 7201Phosphoserine1 Publication
Modified residuei800 – 8001Phosphoserine1 Publication
Modified residuei806 – 8061Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by MEC1.1 Publication

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 – 8276Combined sources
Beta strandi837 – 8448Combined sources
Helixi851 – 8599Combined sources
Beta strandi862 – 8643Combined sources
Helixi870 – 8723Combined sources
Beta strandi876 – 8783Combined sources
Helixi886 – 8916Combined sources
Beta strandi899 – 9013Combined sources
Helixi904 – 91310Combined sources
Helixi927 – 9304Combined sources
Helixi937 – 9426Combined sources
Beta strandi945 – 9473Combined sources
Helixi949 – 9524Combined sources
Beta strandi957 – 9615Combined sources
Helixi968 – 97710Combined sources
Beta strandi982 – 9865Combined sources
Turni988 – 9903Combined sources
Helixi993 – 9953Combined sources
Beta strandi1011 – 10155Combined sources
Helixi1019 – 103214Combined sources
Beta strandi1038 – 10414Combined sources
Helixi1043 – 10519Combined sources
Beta strandi1063 – 10675Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP38850.
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

        10         20         30         40         50
MSTSLLFEQL NFLILVAAEA ELPIAHSTRK LLMDNSCNNC QIYELYNENL
60 70 80 90 100
KDVKTDKDWF MNKFGPQTVH FVISNTINFP FYKIVYFDLL IPVVSHTWVQ
110 120 130 140 150
DSVKTKRHLR TNMYSPNPFH LLRDCQVYIS KSSFNKCEYI LYSDLLHLLG
160 170 180 190 200
GTLVNYISNR TTHVIVQSPQ DPIIATVSKL TFGSFSSSST NKHTEKPLRE
210 220 230 240 250
WKFVYPIWIL YHFKMAKPLK GELATLCELD MQDTSEEQLF AKWEEVIGDK
260 270 280 290 300
QTSSSQLTLH PNKTLFKNHH FAISPDLNFF TPLYWFLKGF IEDLDGKVTP
310 320 330 340 350
LSFSDDLKSV YQAFPDIDCY IGHSANSPIL EKTKSIKPEI HVGNVSWLFY
360 370 380 390 400
MFALQKFTPV SQCKLIHQPF HAKLFTSKEL TVAYTNYFGS QRFYIQRLVE
410 420 430 440 450
ILGGLSTPEL TRKNTHLITK STIGKKFKVA KKWSLDPQNA IIVTNHMWLE
460 470 480 490 500
QCYMNNSKLN PKDSRFQNFK LDDNMGWNIG QIGMDHSSLP TPKNLSMVTY
510 520 530 540 550
DTQSISEKPP PTNDQMDQIN DNTNVLSKKD GTPISSFENS IDEKIDKLQK
560 570 580 590 600
ISGEVAVTHS GDLERSFVSR PSRASFPVVD SKKSNLQKKD SNSDISMETE
610 620 630 640 650
VFCEGHEKRE EKEFTKPITE YDAPKKQEIR EQSRKKNDID YKKEEEETEL
660 670 680 690 700
QVQLGQRTKR EIKTSKKNEK EKETNECHIE VDQMTNEKQG EESTGKLIST
710 720 730 740 750
EDVTSKKDTD KFSHLFEGLS DNDDHINDEK PAVNSKYTTP KTSQNITSGV
760 770 780 790 800
DTPTTAQTQV FMPSSGNSRL AKTQAAKRLH TDIESLNEFQ KNFKRKRIDS
810 820 830 840 850
EEISLSQDVE RSNNNKELAT KAEKILARFN ELPNYDLKAV CTGCFHDGFN
860 870 880 890 900
EVDIEILNQL GIKIFDNIKE TDKLNCIFAP KILRTEKFLK SLSFEPLKFA
910 920 930 940 950
LKPEFIIDLL KQIHSKKDKL SQININLFDY EINGINESII SKTKLPTKVF
960 970 980 990 1000
ERANIRCINL VNDIPGGVDT IGSVLKAHGI EKINVLRSKK CTFEDIIPND
1010 1020 1030 1040 1050
VSKQENGGIF KYVLIVTKAS QVKKFTKLIN DRDKNETILI VEWNWCVESI
1060 1070
FHLNVDFTSK KNVLYQKKNN
Length:1,070
Mass (Da):123,017
Last modified:February 1, 1995 - v1
Checksum:i767931285BB52580
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
U10397 Genomic DNA. Translation: AAB68978.1.
BK006934 Genomic DNA. Translation: DAA06847.1.
PIRiS46755.
RefSeqiNP_012024.1. NM_001179285.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP38850.
PaxDbiP38850.
PeptideAtlasiP38850.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYHR154w.
SGDiS000001197. RTT107.

Phylogenomic databases

eggNOGiNOG248673.
InParanoidiP38850.
OMAiRINTIFA.
OrthoDBiEOG769ZTW.

Enzyme and pathway databases

BioCyciYEAST:G3O-31189-MONOMER.

Miscellaneous databases

NextBioi982381.

Gene expression databases

GenevestigatoriP38850.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.