| Standard Name | SAP155 1 |
|---|---|
| Systematic Name | YFR040W |
| Feature Type | ORF, Verified |
| Description | Protein required for function of the Sit4p protein phosphatase; forms a complex with Sit4p; member of a family of similar proteins including Sap4p, Sap185p, and Sap190p; protein abundance increases in response to DNA replication stress; SAP155 has a paralog, SAP4, that arose from the whole genome duplication (1, 2, 3) |
| Name Description | Sit4 Associated Protein 1 |
| Chromosomal Location | |
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Gene Ontology Annotations All SAP155 GO evidence and references
| View Computational GO annotations for SAP155 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
Mutant phenotypes All SAP155 Phenotype evidence and references
interactions All SAP155 Interaction evidence and references
| 199 total interaction(s) for 150 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 SAP155 Protein evidence and references
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
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| Last Update | Coordinates: 2011-02-03 | Sequence: 2011-02-03 | ||||||||||||
| 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 | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000001936 |
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References cited on this page View Complete Literature Guide for SAP155
| 1) | Luke MM, et al. (1996) The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase. Mol Cell Biol 16(6):2744-55 |
| 2) | Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 |
| 3) | Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 |




