| Id: | acc1566 |
| Group: | 2sens |
| Protein: | cullin |
| Gene Symbol: | CUL1 |
| Protein Id: | Q13616 |
| Protein Name: | CUL1_HUMAN |
| PTM: | neddylation |
| Site: | unclear |
| Site Sequence: | |
| Disease Category: | Cancer |
| Disease: | Breast Cancer |
| Disease Subtype: | |
| Disease Cellline: | MCF7 |
| Disease Info: | |
| Drug: | MLN4924 |
| Drug Info: | "MLN4924 (Pevonedistat) is a potent and selective NEDD8-activating enzyme (NAE) inhibitor with an IC50 of 4.7 nM, primarily investigated for its anticancer activity by blocking cullin-RING ubiquitin ligase (CRL)-mediated protein degradation." |
| Effect: | modulate |
| Effect Info: | "MLN4924, a Cullin Neddylation inhibitor, inactivates CRLs, leading to the accumulation of CRL substrates and inhibiting the growth of tumor cells in vitro and in vivo." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 23151137 |
| Sentence Index: | 23151137_8-9 |
| Sentence: | "In this review, we will introduce the UPS and CRL E3s and discuss the biological processes regulated by each of eight CRLs through substrate degradation. We will further discuss how cullin neddylation controls CRL activity, and how CRLs are being validated as the attractive cancer targets by abrogating the RING component through genetic means and by inhibiting cullin neddylation via MLN4924, a small molecule indirect inhibitor of CRLs, currently in several Phase I clinical trials." |
Sequence & Structure:
MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRHWVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA
Select PDB:
No data.
Protein Tractability:
source: Open TargetsPTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMD| Residue | Position | State | Disease | Class | PMID |
|---|---|---|---|---|---|
| - | - | U | Breast cancer | Neddylation | 38126621 |
| - | - | U | Pleural mesothelioma | Neddylation | 35197103 |
| - | - | U | Hepatocellular carcinoma | Neddylation | 35713976 |
State Note: Based on the distinct PTM states in diseases, PTMD classified all disease-associated PTMs into six classes, including whether the up-regulation (U) or down-regulation (D) of PTM levels, the absence (A) or presence (P) of PTMs, and the creation (C) or disruption (N) of PTM sites are associated with diseases.
PTM-Drug Perturbation Response:
source: DecryptMNo data.
Function score:
source: funscoRNo data.
