| UniProt ID | CDC13_YEAST | |
|---|---|---|
| UniProt AC | P32797 | |
| Protein Name | Cell division control protein 13 | |
| Gene Name | CDC13 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 924 | |
| Subcellular Localization | Chromosome, telomere. | |
| Protein Description | Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.. | |
| Protein Sequence | MDTLEEPECPPHKNRIFVSSSKDFEGYPSKAIVPVQFVALLTSIHLTETKCLLGFSNFERRGDQSQEDQYLIKLKFKDRGSERLARITISLLCQYFDIELPDLDSDSGASPTVILRDIHLERLCFSSCKALYVSKHGNYTLFLEDIKPLDLVSVISTISTKSTNSSKHSSSELISECDLNNSLVDIFNNLIEMNRDEKNRFKFVKLIHYDIELKKFVQDQQKVLSQKSKAAAINPFFVPNRLGIPYIESQNEFNSQLMTLNVDEPTTDISNMGEEMHDSADPIEDSDSSTTSSTGKYFSSKSYIQSQTPERKTSVPNNWHDDDSGSKRKRKLSFHSPNASSIRKAISYEQLSLASVGSVERLEGKIVGMNPPQFASINEFKYCTLKLYFTQLLPNVPDKVLVPGVNCIEIVIPTRERICELFGVLNCQSDKISDILLLEKPDRISVEVERILWDNDKTASPGMAVWSLKNISTDTQAQAQVQVPAQSSASIDPSRTRMSKMARKDPTIEFCQLGLDTFETKYITMFGMLVSCSFDKPAFISFVFSDFTKNDIVQNYLYDRYLIDYENKLELNEGFKAIMYKNQFETFDSKLRKIFNNGLRDLQNGRDENLSQYGIVCKMNIKVKMYNGKLNAIVRECEPVPHSQISSIASPSQCEHLRLFYQRAFKRIGESAISRYFEEYRRFFPIHRNGSHLAKLRFDEVKHEPKKSPTTPALAEHIPDLNADVSSFDVKFTDISSLLDSSARLPRPQQTHKSNTLYSCEGRIIAIEYHASDLCFHITNELPLLQTRGLAPERVLQLHIITSKNFAYFFNRSSAYLQRQPLEEKYTQLAQFLGHSFKFNITSSLTLFPDTTVALQIWCPIECTFRELQQQLAHPKVAAAPDSGSLDCAINATVNPLRLLAAQNGVTVKKEEDNDDDAGAVPTS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MDTLEEPECP -----CCCCCCCCCC | 34.47 | 30377154 | |
| 139 | Phosphorylation | YVSKHGNYTLFLEDI EEECCCCEEEEECCC | 14.93 | 27017623 | |
| 140 | Phosphorylation | VSKHGNYTLFLEDIK EECCCCEEEEECCCC | 18.29 | 27017623 | |
| 153 | Phosphorylation | IKPLDLVSVISTIST CCCCCEEEEEEEEEC | 22.49 | 27017623 | |
| 156 | Phosphorylation | LDLVSVISTISTKST CCEEEEEEEEECCCC | 19.96 | 27017623 | |
| 157 | Phosphorylation | DLVSVISTISTKSTN CEEEEEEEEECCCCC | 14.07 | 27017623 | |
| 159 | Phosphorylation | VSVISTISTKSTNSS EEEEEEEECCCCCCC | 29.85 | 27017623 | |
| 225 | Phosphorylation | QDQQKVLSQKSKAAA HHHHHHHHHHHHHHH | 38.25 | 17108359 | |
| 249 | Phosphorylation | LGIPYIESQNEFNSQ CCCCCCCCCCCCCCC | 28.84 | 17108359 | |
| 255 | Phosphorylation | ESQNEFNSQLMTLNV CCCCCCCCCEEECCC | 29.97 | 20837994 | |
| 306 | Phosphorylation | SSKSYIQSQTPERKT CCHHHHCCCCCCCCC | 26.85 | 21551504 | |
| 308 | Phosphorylation | KSYIQSQTPERKTSV HHHHCCCCCCCCCCC | 32.15 | 21551504 | |
| 314 | Phosphorylation | QTPERKTSVPNNWHD CCCCCCCCCCCCCCC | 38.32 | 21440633 | |
| 324 | Phosphorylation | NNWHDDDSGSKRKRK CCCCCCCCCCHHHEE | 52.54 | 20377248 | |
| 326 | Phosphorylation | WHDDDSGSKRKRKLS CCCCCCCCHHHEEEE | 32.99 | 21440633 | |
| 333 | Phosphorylation | SKRKRKLSFHSPNAS CHHHEEEECCCCCHH | 24.77 | 10898792 | |
| 336 | Phosphorylation | KRKLSFHSPNASSIR HEEEECCCCCHHHHH | 20.17 | 19823750 | |
| 340 | Phosphorylation | SFHSPNASSIRKAIS ECCCCCHHHHHHHCC | 32.70 | 28889911 | |
| 341 | Phosphorylation | FHSPNASSIRKAISY CCCCCHHHHHHHCCH | 24.81 | 19823750 | |
| 524 | Phosphorylation | TFETKYITMFGMLVS HHHHCEEEHHHHHHH | 11.89 | 30377154 | |
| 533 | Phosphorylation | FGMLVSCSFDKPAFI HHHHHHCCCCCCCEE | 29.04 | 30377154 | |
| 626 | Phosphorylation | MNIKVKMYNGKLNAI EEEEEEEECCEECEE | 18.29 | 21551504 | |
| 674 | Phosphorylation | RIGESAISRYFEEYR HHCHHHHHHHHHHHH | 22.20 | 24930733 | |
| 733 | Phosphorylation | SSFDVKFTDISSLLD HHCCCEECCHHHHHC | 27.06 | 28889911 | |
| 736 | Phosphorylation | DVKFTDISSLLDSSA CCEECCHHHHHCCCC | 20.10 | 28889911 | |
| 737 | Phosphorylation | VKFTDISSLLDSSAR CEECCHHHHHCCCCC | 33.03 | 28889911 | |
| 741 | Phosphorylation | DISSLLDSSARLPRP CHHHHHCCCCCCCCC | 26.35 | 28889911 | |
| 909 | Sumoylation | AQNGVTVKKEEDNDD HHCCCEEECCCCCCC | 45.14 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC13_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 CDC13_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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-306 AND THR-308, 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 SER-306 AND THR-308, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-336, ANDMASS SPECTROMETRY. | |
