UniProt ID | SKP1_YEAST | |
---|---|---|
UniProt AC | P52286 | |
Protein Name | Suppressor of kinetochore protein 1 | |
Gene Name | SKP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 194 | |
Subcellular Localization | Cytoplasm . Nucleus . Chromosome, centromere, kinetochore . | |
Protein Description | Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52.. | |
Protein Sequence | MVTSNVVLVSGEGERFTVDKKIAERSLLLKNYLNDMHDSNLQNNSDSESDSDSETNHKSKDNNNGDDDDEDDDEIVMPVPNVRSSVLQKVIEWAEHHRDSNFPDEDDDDSRKSAPVDSWDREFLKVDQEMLYEIILAANYLNIKPLLDAGCKVVAEMIRGRSPEEIRRTFNIVNDFTPEEEAAIRRENEWAEDR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MVTSNVVLVS -----CCCCCEEEEE | 17.18 | 28889911 | |
4 | Phosphorylation | ----MVTSNVVLVSG ----CCCCCEEEEEC | 19.06 | 28889911 | |
32 | Phosphorylation | RSLLLKNYLNDMHDS HHHHHHHHHHHHHHH | 12.80 | 22890988 | |
39 | Phosphorylation | YLNDMHDSNLQNNSD HHHHHHHHCCCCCCC | 25.43 | 22890988 | |
45 | Phosphorylation | DSNLQNNSDSESDSD HHCCCCCCCCCCCCC | 50.49 | 19823750 | |
47 | Phosphorylation | NLQNNSDSESDSDSE CCCCCCCCCCCCCCC | 38.53 | 19823750 | |
49 | Phosphorylation | QNNSDSESDSDSETN CCCCCCCCCCCCCCC | 46.49 | 19823750 | |
51 | Phosphorylation | NSDSESDSDSETNHK CCCCCCCCCCCCCCC | 52.92 | 22890988 | |
53 | Phosphorylation | DSESDSDSETNHKSK CCCCCCCCCCCCCCC | 50.72 | 22890988 | |
55 | Phosphorylation | ESDSDSETNHKSKDN CCCCCCCCCCCCCCC | 46.72 | 22890988 | |
59 | Phosphorylation | DSETNHKSKDNNNGD CCCCCCCCCCCCCCC | 37.38 | 28889911 | |
60 | Ubiquitination | SETNHKSKDNNNGDD CCCCCCCCCCCCCCC | 70.09 | 23749301 | |
110 | Phosphorylation | PDEDDDDSRKSAPVD CCCCCCCHHHCCCCC | 48.91 | 19795423 | |
112 | Ubiquitination | EDDDDSRKSAPVDSW CCCCCHHHCCCCCHH | 55.72 | 24961812 | |
113 | Phosphorylation | DDDDSRKSAPVDSWD CCCCHHHCCCCCHHC | 36.37 | 22369663 | |
162 | Phosphorylation | AEMIRGRSPEEIRRT HHHHCCCCHHHHHHH | 39.21 | 29136822 | |
169 | Phosphorylation | SPEEIRRTFNIVNDF CHHHHHHHHHHHCCC | 15.93 | 22369663 | |
177 | Phosphorylation | FNIVNDFTPEEEAAI HHHHCCCCHHHHHHH | 32.43 | 22369663 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SKP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SKP1_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SKP1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-177, AND MASSSPECTROMETRY. |