| UniProt ID | CDH1_YEAST | |
|---|---|---|
| UniProt AC | P53197 | |
| Protein Name | APC/C activator protein CDH1 | |
| Gene Name | CDH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 566 | |
| Subcellular Localization | Cytoplasm . Nucleus . Nuclear import and export are mediated by the importin PSE1 and the exportin MSN5. | |
| Protein Description | Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). During telophase and in the subsequent G1 phase of the cell cycle, recognizes and binds proteins containing a destruction box (D-box) and an additional degradation signal termed the KEN box including ASE1, CDC20, the B-type cyclins CLB2 and CLB3, the polo-like kinase CDC5 and HSL1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1. Probably is the target of a BUB2-dependent spindle checkpoint pathway.. | |
| Protein Sequence | MSTNLNPFMNNTPSSSPLKGSESKRVSKRPISSSSSASLLSSPSRRSRPSTVYGDRYIPSRTDIDFNSIVSISSMASVPALNPSSTEDQVEYQKERQAHETYNTLLKNELFGEMLSKDTVGSESSIDRIKNTRPSTRGNVHAENTTRHGYELERVSTPPPEAAGLEEFSPHSTPVTPRRLFTSQQDEITRPSSNSVRGASLLTYQQRKGRRLSAASLLQSQFFDSMSPVRPDSKQLLLSPGKQFRQIAKVPYRVLDAPSLADDFYYSLIDWSSTDVLAVALGKSIFLTDNNTGDVVHLCDTENEYTSLSWIGAGSHLAVGQANGLVEIYDVMKRKCIRTLSGHIDRVACLSWNNHVLTSGSRDHRILHRDVRMPDPFFETIESHTQEVCGLKWNVADNKLASGGNDNVVHVYEGTSKSPILTFDEHKAAVKAMAWSPHKRGVLATGGGTADRRLKIWNVNTSIKMSDIDSGSQICNMVWSKNTNELVTSHGYSKYNLTLWDCNSMDPIAILKGHSFRVLHLTLSNDGTTVVSGAGDETLRYWKLFDKPKAKVQPNSLIFDAFNQIR | |
| 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 |
|---|---|---|---|---|---|
| 12 | Phosphorylation | LNPFMNNTPSSSPLK CCHHCCCCCCCCCCC | 21.39 | 15467459 | |
| 14 | Phosphorylation | PFMNNTPSSSPLKGS HHCCCCCCCCCCCCC | 41.22 | 15467459 | |
| 15 | Phosphorylation | FMNNTPSSSPLKGSE HCCCCCCCCCCCCCC | 36.86 | 15467459 | |
| 16 | Phosphorylation | MNNTPSSSPLKGSES CCCCCCCCCCCCCCC | 38.29 | 15467459 | |
| 21 | Phosphorylation | SSSPLKGSESKRVSK CCCCCCCCCCCCCCC | 36.79 | 15467459 | |
| 23 | Phosphorylation | SPLKGSESKRVSKRP CCCCCCCCCCCCCCC | 27.71 | 15467459 | |
| 32 | Phosphorylation | RVSKRPISSSSSASL CCCCCCCCCCCCCHH | 27.18 | 28889911 | |
| 33 | Phosphorylation | VSKRPISSSSSASLL CCCCCCCCCCCCHHH | 34.65 | 27017623 | |
| 35 | Phosphorylation | KRPISSSSSASLLSS CCCCCCCCCCHHHCC | 31.69 | 27017623 | |
| 36 | Phosphorylation | RPISSSSSASLLSSP CCCCCCCCCHHHCCC | 24.67 | 15467459 | |
| 38 | Phosphorylation | ISSSSSASLLSSPSR CCCCCCCHHHCCCCC | 31.61 | 15467459 | |
| 41 | Phosphorylation | SSSASLLSSPSRRSR CCCCHHHCCCCCCCC | 45.56 | 27017623 | |
| 42 | Phosphorylation | SSASLLSSPSRRSRP CCCHHHCCCCCCCCC | 27.19 | 23749301 | |
| 44 | Phosphorylation | ASLLSSPSRRSRPST CHHHCCCCCCCCCCC | 42.12 | 28889911 | |
| 47 | Phosphorylation | LSSPSRRSRPSTVYG HCCCCCCCCCCCCCC | 47.64 | 15467459 | |
| 50 | Phosphorylation | PSRRSRPSTVYGDRY CCCCCCCCCCCCCCC | 29.42 | 28889911 | |
| 51 | Phosphorylation | SRRSRPSTVYGDRYI CCCCCCCCCCCCCCC | 22.04 | 28889911 | |
| 68 | Phosphorylation | RTDIDFNSIVSISSM CCCCCCCCCEEHHHH | 25.10 | 25371407 | |
| 71 | Phosphorylation | IDFNSIVSISSMASV CCCCCCEEHHHHCCC | 18.32 | 27017623 | |
| 73 | Phosphorylation | FNSIVSISSMASVPA CCCCEEHHHHCCCCC | 13.42 | 27017623 | |
| 74 | Phosphorylation | NSIVSISSMASVPAL CCCEEHHHHCCCCCC | 19.39 | 27017623 | |
| 77 | Phosphorylation | VSISSMASVPALNPS EEHHHHCCCCCCCCC | 21.71 | 25371407 | |
| 85 | Phosphorylation | VPALNPSSTEDQVEY CCCCCCCCCHHHHHH | 36.75 | 27017623 | |
| 92 | Phosphorylation | STEDQVEYQKERQAH CCHHHHHHHHHHHHH | 26.48 | 27017623 | |
| 122 | Phosphorylation | LSKDTVGSESSIDRI HCCCCCCCHHHHHHH | 29.93 | 28889911 | |
| 125 | Phosphorylation | DTVGSESSIDRIKNT CCCCCHHHHHHHHCC | 25.18 | 19853567 | |
| 136 | Phosphorylation | IKNTRPSTRGNVHAE HHCCCCCCCCCCCEE | 45.32 | 28889911 | |
| 150 | Phosphorylation | ENTTRHGYELERVST ECCCCCCEEEEEECC | 15.94 | 21440633 | |
| 156 | Phosphorylation | GYELERVSTPPPEAA CEEEEEECCCCCCCC | 41.22 | 22369663 | |
| 157 | Phosphorylation | YELERVSTPPPEAAG EEEEEECCCCCCCCC | 36.64 | 22369663 | |
| 169 | Phosphorylation | AAGLEEFSPHSTPVT CCCCCCCCCCCCCCC | 25.61 | 22369663 | |
| 172 | Phosphorylation | LEEFSPHSTPVTPRR CCCCCCCCCCCCHHH | 37.48 | 22369663 | |
| 173 | Phosphorylation | EEFSPHSTPVTPRRL CCCCCCCCCCCHHHC | 20.81 | 22369663 | |
| 176 | Phosphorylation | SPHSTPVTPRRLFTS CCCCCCCCHHHCCCC | 16.57 | 22369663 | |
| 189 | Phosphorylation | TSQQDEITRPSSNSV CCCCCCCCCCCCCCC | 34.18 | 15467459 | |
| 192 | Phosphorylation | QDEITRPSSNSVRGA CCCCCCCCCCCCCCC | 38.57 | 15467459 | |
| 193 | Phosphorylation | DEITRPSSNSVRGAS CCCCCCCCCCCCCCH | 35.49 | 15467459 | |
| 195 | Phosphorylation | ITRPSSNSVRGASLL CCCCCCCCCCCCHHH | 18.35 | 27017623 | |
| 213 | Phosphorylation | QRKGRRLSAASLLQS HHHCCCCCHHHHHHH | 21.70 | 21440633 | |
| 216 | Phosphorylation | GRRLSAASLLQSQFF CCCCCHHHHHHHHHH | 29.36 | 22369663 | |
| 220 | Phosphorylation | SAASLLQSQFFDSMS CHHHHHHHHHHHCCC | 28.99 | 22369663 | |
| 225 | Phosphorylation | LQSQFFDSMSPVRPD HHHHHHHCCCCCCCC | 18.92 | 22369663 | |
| 227 | Phosphorylation | SQFFDSMSPVRPDSK HHHHHCCCCCCCCCC | 24.97 | 22369663 | |
| 233 | Phosphorylation | MSPVRPDSKQLLLSP CCCCCCCCCCCCCCC | 25.61 | 22369663 | |
| 239 | Phosphorylation | DSKQLLLSPGKQFRQ CCCCCCCCCCHHHHH | 31.41 | 25752575 | |
| 259 | Phosphorylation | YRVLDAPSLADDFYY CEECCCHHHCCCHHH | 37.60 | 19853567 | |
| 418 | Phosphorylation | VYEGTSKSPILTFDE EEECCCCCCCEEHHH | 19.55 | 28889911 | |
| 436 | Phosphorylation | AVKAMAWSPHKRGVL HHHHHHCCCCCCCEE | 13.95 | 15467459 | |
| 556 | Phosphorylation | KAKVQPNSLIFDAFN CCCCCCCCCHHHHHH | 29.53 | 15467459 |
| 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 CDH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDH1_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 CDH1_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-156 AND THR-157, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND MASSSPECTROMETRY. | |
