| Standard Name | Sis1p 1 |
|---|---|
| Systematic Name | Ynl007cp |
| ORF Classification | Verified |
| Description | Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; not functionally redundant with Ydj1p due to due to substrate specificity; has similarity to bacterial DnaJ proteins; protein abundance increases in response to DNA replication stress (2, 3, 4) |
| Name Description | SIt4 Suppressor 1 |
| Experimental Data | |
|---|---|
| Molecules/cell | 20300 5 |
| Click on image for expanded interactive view |
|---|
| Post-translational Modifications | PhosphoGRID | PhosphoPep Database |
|---|---|
| Domains/motifs | See the graphical view and list of proteins that share domains/motifs in common with Sis1p (InterPro) |
| Physical Interactions | There are 78 total physical interactions (BioGRID) |
| Homologs | PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer |
| External Sequence Databases |
EBI: UPI0000052E5F | P25294 MIPS: YNL007C NCBI: 116666768 | 116666769 | 116666770 | 122921354 | 1301824 | 134509 | 4474 | 6324321 | 9954877 | NP_014391.1 GenBank/EMBL/DDBJ: DAA10536.1 | X58460 | Z71283 |
external links for Sis1p
| Homologs | Interaction Resources | Protein databases/Other | Localization Resources |
|---|---|---|---|
| BLASTP (NCBI) | BioGRID | SCOP Superfamily | YPL+ |
| Ashbya (AGD) | BOND | GPMdb (Mass Spec.) | YeastGFP |
| Candida (CGD) | BioPIXIE | MIPS | YeastRC Public Image Repository |
| Candida (CandidaDB) | CYC2008 (complexes) | Pfam domains | |
| YGOB | Complexome | YeastRC Structure Prediction (Seattle) | |
| YOGY | DIP | ||
| GeneMANIA |
References cited on this page View Complete Literature Guide for Sis1p
| 1) | Luke MM, et al. (1991) Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J Cell Biol 114(4):623-38 |
| 2) | Lu Z and Cyr DM (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273(43):27824-30 |
| 3) | Fan CY, et al. (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15(2):761-73 |
| 4) | 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 |
| 5) | Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41 |





