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Protein

Regulator of Ty1 transposition protein 103

Gene

RTT103

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

Functioni

Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • RNA polymerase II core binding Source: SGD

GO - Biological processi

  • DNA damage response, detection of DNA damage Source: SGD
  • mRNA 3'-end processing Source: SGD
  • negative regulation of transposition, RNA-mediated Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29853-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of Ty1 transposition protein 103
Gene namesi
Name:RTT103
Ordered Locus Names:YDR289C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR289C.
SGDiS000002697. RTT103.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: SGD
  • site of double-strand break Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Regulator of Ty1 transposition protein 103PRO_0000268707Add
BLAST

Proteomic databases

MaxQBiQ05543.

PTM databases

iPTMnetiQ05543.

Interactioni

Subunit structurei

Interacts with PCF11, RAI1, RAT1, RPO21 AND RBP2.1 Publication

GO - Molecular functioni

  • RNA polymerase II core binding Source: SGD

Protein-protein interaction databases

BioGridi32342. 307 interactions.
DIPiDIP-2583N.
IntActiQ05543. 5 interactions.
MINTiMINT-425860.

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Helixi19 – 3012Combined sources
Helixi33 – 353Combined sources
Helixi36 – 4712Combined sources
Beta strandi49 – 524Combined sources
Helixi54 – 7118Combined sources
Helixi72 – 743Combined sources
Helixi78 – 858Combined sources
Helixi87 – 9711Combined sources
Helixi100 – 11617Combined sources
Helixi121 – 13111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KM4NMR-A1-131[»]
2L0INMR-A3-131[»]
ProteinModelPortaliQ05543.
SMRiQ05543. Positions 3-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05543.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 135135CIDPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 29630Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the UPF0400 (RTT103) family.Curated
Contains 1 CID domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00400000022016.
HOGENOMiHOG000141975.
InParanoidiQ05543.
KOiK15559.
OMAiASESCKG.
OrthoDBiEOG7H79C2.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR006903. RNA_pol_II-bd.
[Graphical view]
PfamiPF04818. CTD_bind. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFSSEQFTT KLNTLEDSQE SISSASKWLL LQYRDAPKVA EMWKEYMLRP
60 70 80 90 100
SVNTRRKLLG LYLMNHVVQQ AKGQKIIQFQ DSFGKVAAEV LGRINQEFPR
110 120 130 140 150
DLKKKLSRVV NILKERNIFS KQVVNDIERS LKTESSPVEA LVLPQKLKDF
160 170 180 190 200
AKDYEKLVKM HHNVCAMKMR FDKSSDELDP SSSVYEENFK TISKIGNMAK
210 220 230 240 250
DIINESILKR ESGIHKLQST LDDEKRHLDE EQNMLSEIEF VLSAKDPSRL
260 270 280 290 300
NKNVDEDNII PTYEVGDGDD DDDDGDNDDD DDDDDDDKNY DDRSNDSNYG
310 320 330 340 350
VTNISTTDKK NEVVEKTDSE HKNSTHNPSD NQFGMKRTHD MIGHDDANDI
360 370 380 390 400
PEKKVHLDSK TSEDGTFNSE DGHYELDIEG HVGAQTDEGV ENSGGVSSSI

QDLLSKLAN
Length:409
Mass (Da):46,488
Last modified:November 1, 1996 - v1
Checksum:i08D37739466E3010
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51031 Genomic DNA. Translation: AAB64467.1.
AY557793 Genomic DNA. Translation: AAS56119.1.
BK006938 Genomic DNA. Translation: DAA12129.1.
PIRiS70119.
RefSeqiNP_010575.1. NM_001180597.1.

Genome annotation databases

EnsemblFungiiYDR289C; YDR289C; YDR289C.
GeneIDi851884.
KEGGisce:YDR289C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51031 Genomic DNA. Translation: AAB64467.1.
AY557793 Genomic DNA. Translation: AAS56119.1.
BK006938 Genomic DNA. Translation: DAA12129.1.
PIRiS70119.
RefSeqiNP_010575.1. NM_001180597.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KM4NMR-A1-131[»]
2L0INMR-A3-131[»]
ProteinModelPortaliQ05543.
SMRiQ05543. Positions 3-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32342. 307 interactions.
DIPiDIP-2583N.
IntActiQ05543. 5 interactions.
MINTiMINT-425860.

PTM databases

iPTMnetiQ05543.

Proteomic databases

MaxQBiQ05543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR289C; YDR289C; YDR289C.
GeneIDi851884.
KEGGisce:YDR289C.

Organism-specific databases

EuPathDBiFungiDB:YDR289C.
SGDiS000002697. RTT103.

Phylogenomic databases

GeneTreeiENSGT00400000022016.
HOGENOMiHOG000141975.
InParanoidiQ05543.
KOiK15559.
OMAiASESCKG.
OrthoDBiEOG7H79C2.

Enzyme and pathway databases

BioCyciYEAST:G3O-29853-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ05543.
PROiQ05543.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR006903. RNA_pol_II-bd.
[Graphical view]
PfamiPF04818. CTD_bind. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance."
    Scholes D.T., Banerjee M., Bowen B., Curcio M.J.
    Genetics 159:1449-1465(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II."
    Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F., Buratowski S.
    Nature 432:517-522(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCF11; RAI1; RAT1; RPO21 AND RBP2.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT103_YEAST
AccessioniPrimary (citable) accession number: Q05543
Secondary accession number(s): D6VSR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 108 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 3930 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. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.