Reviewed,
UniProtKB/Swiss-Prot P38165 (RTG3_YEAST)
Last modified
November 24, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Retrograde regulation protein 3 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 486 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Transcription factor that regulates CIT2 gene expression. Binds to two identical sites oriented as inverted repeats 28 bp apart in a regulatory upstream activation sequence element (UASR) in the CIT2 promoter. The core binding site is 5'-GGTCAC-3'. |
| Subunit structure | Binds DNA as a heterodimer with RTG1. |
| Subcellular location | Nucleus Probable. |
| Miscellaneous | Present with 1050 molecules/cell in log phase SD medium. Ref.4 |
| Sequence similarities | Contains 1 basic helix-loop-helix (bHLH) domain. |
| Sequence caution | The sequence CAA55992.1 differs from that shown. Reason: Frameshift at position 310. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Ligand | DNA-binding |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | mitochondrial signaling pathway Ref.1 Inferred from direct assay. Source: SGD regulation of transcriptionInferred from electronic annotation. Source: UniProtKB-KW transcription initiation from RNA polymerase II promoterInferred from direct assay. Source: SGD |
| Cellular component | cytoplasm Inferred from direct assay. Source: SGD nucleusInferred from direct assay. Source: SGD |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct sequence-specific DNA bindingInferred from direct assay. Source: SGD specific RNA polymerase II transcription factor activity Ref.1Inferred from direct assay. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 486 | 486 | Retrograde regulation protein 3 | PRO_0000127434 | |||||
Regions | |||||||||
| Domain | 299 – 345 | 47 | Helix-loop-helix motif | ||||||
| DNA binding | 283 – 298 | 16 | Basic motif | ||||||
Amino acid modifications | |||||||||
| Modified residue | 72 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 113 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 123 | 1 | Phosphoserine Ref.7 Ref.5 | ||||||
| Modified residue | 126 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 135 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 140 | 1 | Phosphotyrosine Ref.7 | ||||||
| Modified residue | 142 | 1 | Phosphoserine Ref.7 Ref.5 | ||||||
| Modified residue | 150 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 221 | 1 | Phosphotyrosine Ref.7 | ||||||
| Modified residue | 222 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 227 | 1 | Phosphoserine Ref.7 Ref.6 | ||||||
| Modified residue | 236 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 279 | 1 | Phosphoserine Ref.7 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A basic helix-loop-helix-leucine zipper transcription complex in yeast functions in a signaling pathway from mitochondria to the nucleus." Jia Y., Rothermel B., Thornton J., Butow R.A. Mol. Cell. Biol. 17:1110-1117(1997) [PubMed: 9032238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88. |
| [2] | "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K.EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [5] | "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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-142, MASS SPECTROMETRY. |
| [6] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, MASS SPECTROMETRY. |
| [7] | "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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-113; SER-123; SER-126; SER-135; TYR-140; SER-142; THR-150; TYR-221; SER-222; SER-227; SER-236 AND SER-279, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U46012 Genomic DNA. Translation: AAA86842.1. X79489 Genomic DNA. Translation: CAA55992.1. Frameshift. Z35864 Genomic DNA. Translation: CAA84929.1. Z35865 Genomic DNA. Translation: CAA84931.1. | |
| PIR | S74319. |
| RefSeq | NP_009447.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:2501N. |
| IntAct | P38165. 8 interactions. |
| STRING | P38165. |
Genome annotation databases | |
| Ensembl | YBL103C; YBL103C; YBL103C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 852171. |
| KEGG | sce:YBL103C. |
| NMPDR | fig|4932.3.peg.132. |
Organism-specific databases | |
| CYGD | YBL103c. |
| SGD | S000000199. RTG3. |
Phylogenomic databases | |
| OMA | ENSEERI |
| OrthoDB | EOG9XPRZ0 |
Gene expression databases | |
| ArrayExpress | P38165. |
| Genevestigator | P38165. |
| GermOnline | YBL103C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001092. HLH_basic. IPR011598. HLH_DNA_bd. [Graphical view] |
| Gene3D | G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit. |
| Pfam | PF00010. HLH. 1 hit. [Graphical view] |
| SMART | SM00353. HLH. 1 hit. [Graphical view] |
| PROSITE | PS50888. HLH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 970620. |
Entry information
| Entry name | RTG3_YEAST | ||||||||
| Accession | Primary (citable) accession number: P38165 Secondary accession number(s): P89494 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome II Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names |

Clusters with


