| UniProt ID | CUL8_YEAST | |
|---|---|---|
| UniProt AC | P47050 | |
| Protein Name | Cullin-8 | |
| Gene Name | RTT101 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 842 | |
| Subcellular Localization | Cytoplasm . Nucleus . Recruited to chromatin in response to replication fork stalling. | |
| Protein Description | Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The CRL associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the CRL depends on the type of the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition. RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is also involved in the non-functional rRNA decay (NRD) of 25S rRNA through the selective, ubiquitination-dependent degradation of nonfunctional ribosomal particles. Ubiquitinates the FACT (facilitiates chromatin transcription) complex subunit SPT16 in an MMS1-independent manner. Involved in regulation of Ty1 transposition and protects the genome from Ty1 integration upstream of tRNA genes.. | |
| Protein Sequence | MINESVSKREGFHESISRETSASNALGLYNKFNDERNPRYRTMIAELHEFFHLTLAETITETDVKELECNKEKAAKFRKLMPKMLNNCRELTQRKSYIPYNSEFNGNDEKQKKFQLLHQHQIVLSFQEFCDELAKLIIDAHVLSFLTRCDYSYEIIPKNWTSFYKLFQYVMGAVGPIISYVPVNYPMIRKELGFETLTIFQYYDSKLFECMKSHFGREFSTLVSATIHHYIHMFPITNTMLEKEVPMLRIMSNCNFSIEGLSPKDFYMKTLRQYYCEESNLRPRLETFKNFKVLLTRNALLASLFSPEWVSDANDLFISHLLLNKKSISEYIEIGKDTYDEEKERYFKTETHFSLLMFRNAFEAKNMLSKFKEFCDDAVSEKLKAAYGSNHDTERLFDEVVQLANVDHLKIYSDSIEYHLCNLLGSTSKAIEQYVKYFESHLFIIVRKIKTTKKDLPRDMKIKYLNENLPILRLKFVNLPTFPNFFERSIFRKTILQSDQNSSFIKDILPVYKDSLMELFKQRIITNVSQEDEMRYRDQYQPYLSQFFQPVEVMADLRIKYASFLSFYENIEAAVKFGKTYNENNSKSFFPLIFDRERIPKVFQQSNEVKKNFVLPQEMDDTWNQFLRNYHEQNKVEDSDASKKELYPMWNLHHCEVESPYIIQDGTNLIFELTLFQTCVLTLFNESDHLTLQVISEQTKLAYKDLALVLKSFCNYKILTRDIDNTYSINESFKPDMKKVKNGKLRVVLPRTASLQSSNTGGERTSSAHHEGSNSQWTQELLKACITRSVKSERNGLDYDHLFETVKQQIKGFSVGEFKDALAKLLRDKFITRDESTATYKY | |
| 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 |
|---|---|---|---|---|---|
| 21 | Phosphorylation | ESISRETSASNALGL HHHHCHHCHHHHHHH | 25.58 | 30377154 | |
| 23 | Phosphorylation | ISRETSASNALGLYN HHCHHCHHHHHHHHH | 23.54 | 28889911 | |
| 606 | Phosphorylation | IPKVFQQSNEVKKNF HCHHHHCCCCHHHCC | 24.95 | 30377154 | |
| 639 | Phosphorylation | EQNKVEDSDASKKEL HHCCCCCCCCHHHHH | 22.90 | 27717283 | |
| 642 | Phosphorylation | KVEDSDASKKELYPM CCCCCCCHHHHHCCC | 49.61 | 27717283 | |
| 732 | Phosphorylation | NTYSINESFKPDMKK CCCCCCCCCCCCHHH | 33.80 | 30377154 | |
| 752 | Phosphorylation | LRVVLPRTASLQSSN EEEEEECCCCCCCCC | 20.75 | 25752575 | |
| 754 | Phosphorylation | VVLPRTASLQSSNTG EEEECCCCCCCCCCC | 26.74 | 30377154 | |
| 760 | Phosphorylation | ASLQSSNTGGERTSS CCCCCCCCCCCCCCC | 48.81 | 28889911 | |
| 775 | Phosphorylation | AHHEGSNSQWTQELL CCCCCCCCHHHHHHH | 28.88 | 27017623 | |
| 791 | Neddylation | ACITRSVKSERNGLD HHHHHHHHHHHCCCC | 48.09 | - | |
| 791 | Ubiquitination | ACITRSVKSERNGLD HHHHHHHHHHHCCCC | 48.09 | 24961812 | |
| 819 | Acetylation | GFSVGEFKDALAKLL CCCHHHHHHHHHHHH | 37.48 | 24489116 | |
| 839 | Phosphorylation | TRDESTATYKY---- CCCCCCCCCCC---- | 22.19 | 27017623 |
| 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 CUL8_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CUL8_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 CUL8_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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