HIS1/YER055C Summary 
| Standard Name | HIS1 1, 2 |
|---|---|
| Systematic Name | YER055C |
| Feature Type | ORF, Verified |
| Description | ATP phosphoribosyltransferase, a hexameric enzyme, catalyzes the first step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control (3, 4, 5 and see Summary Paragraph) |
| Name Description | HIStidine 2 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
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| Genetic position: 49 cM |
Gene Ontology Annotations All HIS1 GO evidence and references
| View Computational GO annotations for HIS1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
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| Pathways |
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Mutant phenotypes All HIS1 Phenotype evidence and references
| Classical genetics | |
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| unspecified | |
| Large-scale survey | |
| null |
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| Resources |
interactions All HIS1 Interaction evidence and references
| 10 total interaction(s) for 10 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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Expression Summary
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| Resources |
Protein Information All HIS1 Protein evidence and references
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Genetic position: 49 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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Analyze Sequence
| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000857 |
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SUMMARY PARAGRAPH for HIS1
HIS1 encodes ATP phosphoribosyltransferase, which catalyzes the first step in histidine biosynthesis (5). The biosynthesis of histidine has been most extensively studied in Salmonella typhimurium and E. coli. The reactions and enzymes involved in histidine biosynthesis have been identified in many organisms, and are thoroughly reviewed in Alifano et al. (5). Mutations in HIS1, as well as in genes encoding other histidine biosynthetic enzymes, cause histidine auxotrophy and sensitivity to copper, cobalt, and nickel salts (4). Transcription of HIS1 is regulated by general amino acid control, in which the transcription factor Gcn4p plays a key role (reviewed in 6). The transcription factors Bas1p and Bas2p also activate HIS1 transcription (7).
Last updated: 1999-11-10 
References cited on this page View Complete Literature Guide for HIS1
| 1) | Savage, E. (1979) A comparative analysis of recombination at the his1 locus among five related diploid strains of Saccharomyces cerevisiae. Ph.D Thesis |
| 2) | Korch CT and Snow R (1973) Allelic Complementation in the First Gene for Histidine Biosynthesis in SACCHAROMYCES CEREVISIAE. I. Characteristics of Mutants and Genetic Mapping of Alleles. Genetics 74(2):287-305 |
| 3) | Hinnebusch AG and Fink GR (1983) Repeated DNA sequences upstream from HIS1 also occur at several other co-regulated genes in Saccharomyces cerevisiae. J Biol Chem 258(8):5238-47 |
| 4) | Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 |
| 5) | Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 |
| 6) | Hinnebusch A (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press |
| 7) | Denis V, et al. (1998) Role of the myb-like protein bas1p in Saccharomyces cerevisiae: a proteome analysis. Mol Microbiol 30(3):557-66 |
