UniProt ID | CTF18_YEAST | |
---|---|---|
UniProt AC | P49956 | |
Protein Name | Chromosome transmission fidelity protein 18 | |
Gene Name | CTF18 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 741 | |
Subcellular Localization | Nucleus . | |
Protein Description | Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.. | |
Protein Sequence | MVDTAPYIGSLGRSSLFDTGDIEQAPGNNAIGINEEDIHAFVSSTGETVQLKKKPAKLATGNISLYTNPDTVWRSDDTYGININYLLDKIEASGDDRTNAQKTSPITGKIGSDTLWVEKWRPKKFLDLVGNEKTNRRMLGWLRQWTPAVFKEQLPKLPTEKEVSDMELDPLKRPPKKILLLHGPPGIGKTSVAHVIAKQSGFSVSEINASDERAGPMVKEKIYNLLFNHTFDTNPVCLVADEIDGSIESGFIRILVDIMQSDIKATNKLLYGQPDKKDKKRKKKRSKLLTRPIICICNNLYAPSLEKLKPFCEIIAVKRPSDTTLLERLNLICHKENMNIPIKAINDLIDLAQGDVRNCINNLQFLASNVDSRDSSASDKPACAKNTWASSNKDSPISWFKIVNQLFRKDPHRDIKEQFYELLNQVELNGNSDRILQGCFNIFPYVKYSDNGIRKPANISDWLFFHDLMYQSMYAHNGELLRYSALVPLVFFQTFGDIANKDDIRMKNSEYEQRELKRANSDIVSLIMRHISVQSPLMASFTDRKSLIFEILPYLDSMISSDFNKIRNLKLKQAIMEELVQLLKSFQLNLIQNRSEGFDVRGGLTIDPPIDEVVLLNPKHINEVQHKRANNLSSLLAKIEENRAKKRHIDQVTEDRLQSQEMHSKKVKTGLNSSSSTIDFFKNQYGLLKQTQELEETQKTIGSDETNQADDCNQTVKIWVKYNEGFSNAVRKNVTWNNLWE | |
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 |
---|---|---|---|---|---|
103 | Phosphorylation | DRTNAQKTSPITGKI CCCCCCCCCCCCCCC | 27.88 | 21440633 | |
104 | Phosphorylation | RTNAQKTSPITGKIG CCCCCCCCCCCCCCC | 22.72 | 20377248 | |
266 | Phosphorylation | MQSDIKATNKLLYGQ HHHCHHHHHHHHCCC | 28.08 | 27017623 | |
659 | Phosphorylation | VTEDRLQSQEMHSKK HHHHHHHHHHHHHHH | 32.47 | 28889911 | |
664 | Phosphorylation | LQSQEMHSKKVKTGL HHHHHHHHHHCCCCC | 32.63 | 30377154 | |
669 | Phosphorylation | MHSKKVKTGLNSSSS HHHHHCCCCCCCCHH | 50.30 | 21126336 | |
673 | Phosphorylation | KVKTGLNSSSSTIDF HCCCCCCCCHHHHHH | 36.32 | 30377154 | |
674 | Phosphorylation | VKTGLNSSSSTIDFF CCCCCCCCHHHHHHH | 27.51 | 28889911 | |
675 | Phosphorylation | KTGLNSSSSTIDFFK CCCCCCCHHHHHHHH | 31.18 | 25521595 | |
676 | Phosphorylation | TGLNSSSSTIDFFKN CCCCCCHHHHHHHHH | 31.18 | 28152593 | |
677 | Phosphorylation | GLNSSSSTIDFFKNQ CCCCCHHHHHHHHHH | 26.89 | 20377248 | |
703 | Phosphorylation | ETQKTIGSDETNQAD HHHHHHCCCCCCCCC | 28.55 | 23749301 |
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 CTF18_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CTF18_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 CTF18_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-104; SER-659; SER-674AND THR-677, AND MASS SPECTROMETRY. |