| UniProt ID | CDC53_YEAST | |
|---|---|---|
| UniProt AC | Q12018 | |
| Protein Name | Cell division control protein 53 | |
| Gene Name | CDC53 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 815 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes.. | |
| Protein Sequence | MSETLPRSDDLEATWNFIEPGINQILGNEKNQASTSKRVYKILSPTMYMEVYTAIYNYCVNKSRSSGHFSTDSRTGQSTILVGSEIYEKLKNYLKNYILNFKQSNSETFLQFYVKRWKRFTIGAIFLNHAFDYMNRYWVQKERSDGKRHIFDVNTLCLMTWKEVMFDPSKDVLINELLDQVTLGREGQIIQRSNISTAIKSLVALGIDPQDLKKLNLNVYIQVFEKPFLKKTQEYYTQYTNDYLEKHSVTEYIFEAHEIIKREEKAMTIYWDDHTKKPLSMALNKVLITDHIEKLENEFVVLLDARDIEKITSLYALIRRDFTLIPRMASVFENYVKKTGENEISSLLAMHKHNIMKNENANPKKLALMTAHSLSPKDYIKKLLEVHDIFSKIFNESFPDDIPLAKALDNACGAFININEFALPAGSPKSATSKTSEMLAKYSDILLKKATKPEVASDMSDEDIITIFKYLTDKDAFETHYRRLFAKRLIHGTSTSAEDEENIIQRLQAANSMEYTGKITKMFQDIRLSKILEDDFAVALKNEPDYSKAKYPDLQPFVLAENMWPFSYQEVEFKLPKELVPSHEKLKESYSQKHNGRILKWLWPLCRGELKADIGKPGRMPFNFTVTLFQMAILLLYNDADVLTLENIQEGTSLTIQHIAAAMVPFIKFKLIQQVPPGLDALVKPETQFKLSRPYKALKTNINFASGVKNDILQSLSGGGHDNHGNKLGNKRLTEDERIEKELNTERQIFLEACIVRIMKAKRNLPHTTLVNECIAQSHQRFNAKVSMVKRAIDSLIQKGYLQRGDDGESYAYLA | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MSETLPRSDDL ----CCCCCCCCCCH | 34.45 | 28889911 | |
| 30 | Ubiquitination | NQILGNEKNQASTSK HHHHCCCCCCCCCCH | 59.36 | 17644757 | |
| 65 | Phosphorylation | YCVNKSRSSGHFSTD HHCCCCCCCCCCCCC | 48.00 | 30377154 | |
| 66 | Phosphorylation | CVNKSRSSGHFSTDS HCCCCCCCCCCCCCC | 34.87 | 30377154 | |
| 73 | Phosphorylation | SGHFSTDSRTGQSTI CCCCCCCCCCCCEEE | 31.65 | 30377154 | |
| 78 | Phosphorylation | TDSRTGQSTILVGSE CCCCCCCEEEEECHH | 20.82 | 23749301 | |
| 79 | Phosphorylation | DSRTGQSTILVGSEI CCCCCCEEEEECHHH | 15.50 | 28889911 | |
| 84 | Phosphorylation | QSTILVGSEIYEKLK CEEEEECHHHHHHHH | 17.22 | 23749301 | |
| 104 | Phosphorylation | YILNFKQSNSETFLQ HHHHCCCCCCHHHHH | 42.80 | 21082442 | |
| 106 | Phosphorylation | LNFKQSNSETFLQFY HHCCCCCCHHHHHHH | 43.17 | 21082442 | |
| 108 | Phosphorylation | FKQSNSETFLQFYVK CCCCCCHHHHHHHHH | 29.48 | 21082442 | |
| 113 | Phosphorylation | SETFLQFYVKRWKRF CHHHHHHHHHHHHHH | 7.66 | 28889911 | |
| 213 | Acetylation | GIDPQDLKKLNLNVY CCCHHHHHHCCCEEE | 64.60 | 24489116 | |
| 232 | Phosphorylation | EKPFLKKTQEYYTQY CCCHHHHHHHHHHHH | 25.66 | 30377154 | |
| 235 | Phosphorylation | FLKKTQEYYTQYTND HHHHHHHHHHHHCCH | 11.29 | 30377154 | |
| 237 | Phosphorylation | KKTQEYYTQYTNDYL HHHHHHHHHHCCHHH | 17.75 | 30377154 | |
| 243 | Phosphorylation | YTQYTNDYLEKHSVT HHHHCCHHHHHCCHH | 20.87 | 30377154 | |
| 276 | Ubiquitination | IYWDDHTKKPLSMAL EEECCCCCCCHHHHH | 49.31 | 19722269 | |
| 277 | Ubiquitination | YWDDHTKKPLSMALN EECCCCCCCHHHHHH | 52.96 | 19722269 | |
| 315 | Phosphorylation | IEKITSLYALIRRDF HHHHHHHHHHHHCCC | 10.10 | 28889911 | |
| 381 | Ubiquitination | LSPKDYIKKLLEVHD CCHHHHHHHHHHHHH | 31.01 | 17644757 | |
| 382 | Ubiquitination | SPKDYIKKLLEVHDI CHHHHHHHHHHHHHH | 49.06 | 17644757 | |
| 392 | Ubiquitination | EVHDIFSKIFNESFP HHHHHHHHHHHCCCC | 40.34 | 17644757 | |
| 474 | Acetylation | IFKYLTDKDAFETHY HHHHHHCCCHHHHHH | 45.80 | 24489116 | |
| 487 | Ubiquitination | HYRRLFAKRLIHGTS HHHHHHHHHHHCCCC | 40.16 | 17644757 | |
| 512 | Phosphorylation | QRLQAANSMEYTGKI HHHHHHHCCCCCHHH | 14.31 | 24909858 | |
| 516 | Phosphorylation | AANSMEYTGKITKMF HHHCCCCCHHHHHHH | 20.77 | 24909858 | |
| 670 | Ubiquitination | MVPFIKFKLIQQVPP HCHHHHHEEHHCCCC | 39.41 | 17644757 | |
| 684 | Acetylation | PGLDALVKPETQFKL CCCCCCCCCCHHHHC | 37.68 | 24489116 | |
| 684 | Ubiquitination | PGLDALVKPETQFKL CCCCCCCCCCHHHHC | 37.68 | 17644757 | |
| 690 | Ubiquitination | VKPETQFKLSRPYKA CCCCHHHHCCCCCHH | 35.42 | 17644757 | |
| 700 | Phosphorylation | RPYKALKTNINFASG CCCHHHHCCCCCCCC | 42.03 | 19795423 | |
| 706 | Phosphorylation | KTNINFASGVKNDIL HCCCCCCCCCCHHHH | 39.73 | 19823750 | |
| 717 | Phosphorylation | NDILQSLSGGGHDNH HHHHHHHCCCCCCCC | 40.41 | 27214570 | |
| 760 | Neddylation | ACIVRIMKAKRNLPH HHHHHHHHHHHCCCC | 48.67 | - | |
| 799 | Acetylation | AIDSLIQKGYLQRGD HHHHHHHCCCCCCCC | 42.39 | 24489116 |
| 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 CDC53_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC53_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 CDC53_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
