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P38850 (RT107_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of Ty1 transposition protein 107
Alternative name(s):
Establishes silent chromatin protein 4
Gene names
Name:RTT107
Synonyms:ESC4
Ordered Locus Names:YHR154W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1070 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.8

Subunit structure

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. Ref.6 Ref.8 Ref.11

Subcellular location

Nucleus. Note: Recruited to chromatin in response to replication fork stalling. Ref.3 Ref.6

Post-translational modification

Phosphorylated by MEC1. Ref.5

Miscellaneous

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

Sequence similarities

Contains 6 BRCT domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10701070Regulator of Ty1 transposition protein 107
PRO_0000097502

Regions

Domain2 – 103102BRCT 1
Domain117 – 21397BRCT 2
Domain260 – 35293BRCT 3
Domain369 – 45385BRCT 4
Domain829 – 91082BRCT 5
Domain934 – 1049116BRCT 6

Amino acid modifications

Modified residue3041Phosphoserine Ref.9
Modified residue5321Phosphothreonine Ref.7 Ref.9 Ref.10
Modified residue5911Phosphoserine Ref.9
Modified residue5931Phosphoserine Ref.9
Modified residue7201Phosphoserine Ref.10
Modified residue8001Phosphoserine Ref.9
Modified residue8061Phosphoserine Ref.9 Ref.10

Secondary structure

............................................... 1070
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38850 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 767931285BB52580

FASTA1,070123,017
        10         20         30         40         50         60 
MSTSLLFEQL NFLILVAAEA ELPIAHSTRK LLMDNSCNNC QIYELYNENL KDVKTDKDWF 

        70         80         90        100        110        120 
MNKFGPQTVH FVISNTINFP FYKIVYFDLL IPVVSHTWVQ DSVKTKRHLR TNMYSPNPFH 

       130        140        150        160        170        180 
LLRDCQVYIS KSSFNKCEYI LYSDLLHLLG GTLVNYISNR TTHVIVQSPQ DPIIATVSKL 

       190        200        210        220        230        240 
TFGSFSSSST NKHTEKPLRE WKFVYPIWIL YHFKMAKPLK GELATLCELD MQDTSEEQLF 

       250        260        270        280        290        300 
AKWEEVIGDK QTSSSQLTLH PNKTLFKNHH FAISPDLNFF TPLYWFLKGF IEDLDGKVTP 

       310        320        330        340        350        360 
LSFSDDLKSV YQAFPDIDCY IGHSANSPIL EKTKSIKPEI HVGNVSWLFY MFALQKFTPV 

       370        380        390        400        410        420 
SQCKLIHQPF HAKLFTSKEL TVAYTNYFGS QRFYIQRLVE ILGGLSTPEL TRKNTHLITK 

       430        440        450        460        470        480 
STIGKKFKVA KKWSLDPQNA IIVTNHMWLE QCYMNNSKLN PKDSRFQNFK LDDNMGWNIG 

       490        500        510        520        530        540 
QIGMDHSSLP TPKNLSMVTY DTQSISEKPP PTNDQMDQIN DNTNVLSKKD GTPISSFENS 

       550        560        570        580        590        600 
IDEKIDKLQK ISGEVAVTHS GDLERSFVSR PSRASFPVVD SKKSNLQKKD SNSDISMETE 

       610        620        630        640        650        660 
VFCEGHEKRE EKEFTKPITE YDAPKKQEIR EQSRKKNDID YKKEEEETEL QVQLGQRTKR 

       670        680        690        700        710        720 
EIKTSKKNEK EKETNECHIE VDQMTNEKQG EESTGKLIST EDVTSKKDTD KFSHLFEGLS 

       730        740        750        760        770        780 
DNDDHINDEK PAVNSKYTTP KTSQNITSGV DTPTTAQTQV FMPSSGNSRL AKTQAAKRLH 

       790        800        810        820        830        840 
TDIESLNEFQ KNFKRKRIDS EEISLSQDVE RSNNNKELAT KAEKILARFN ELPNYDLKAV 

       850        860        870        880        890        900 
CTGCFHDGFN EVDIEILNQL GIKIFDNIKE TDKLNCIFAP KILRTEKFLK SLSFEPLKFA 

       910        920        930        940        950        960 
LKPEFIIDLL KQIHSKKDKL SQININLFDY EINGINESII SKTKLPTKVF ERANIRCINL 

       970        980        990       1000       1010       1020 
VNDIPGGVDT IGSVLKAHGI EKINVLRSKK CTFEDIIPND VSKQENGGIF KYVLIVTKAS 

      1030       1040       1050       1060       1070 
QVKKFTKLIN DRDKNETILI VEWNWCVESI FHLNVDFTSK KNVLYQKKNN 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10397 Genomic DNA. Translation: AAB68978.1.
BK006934 Genomic DNA. Translation: DAA06847.1.
PIRS46755.
RefSeqNP_012024.1. NM_001179285.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T7IX-ray2.30A/B820-1070[»]
3T7JX-ray2.04A/B820-1070[»]
3T7KX-ray2.03A/B820-1070[»]
ProteinModelPortalP38850.
SMRP38850. Positions 821-1068.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36588. 162 interactions.
DIPDIP-6297N.
IntActP38850. 13 interactions.
MINTMINT-702893.
STRING4932.YHR154W.

Proteomic databases

PaxDbP38850.
PeptideAtlasP38850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR154W; YHR154W; YHR154W.
GeneID856559.
KEGGsce:YHR154W.

Organism-specific databases

CYGDYHR154w.
SGDS000001197. RTT107.

Phylogenomic databases

eggNOGNOG248673.
OMARINTIFA.
OrthoDBEOG769ZTW.

Enzyme and pathway databases

BioCycYEAST:G3O-31189-MONOMER.

Gene expression databases

GenevestigatorP38850.

Family and domain databases

Gene3D3.40.50.10190. 2 hits.
InterProIPR001357. BRCT_dom.
[Graphical view]
PfamPF00533. BRCT. 2 hits.
[Graphical view]
SMARTSM00292. BRCT. 4 hits.
[Graphical view]
SUPFAMSSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio982381.

Entry information

Entry nameRT107_YEAST
AccessionPrimary (citable) accession number: P38850
Secondary accession number(s): D3DLA3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 19, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references