| UniProt ID | CUL4_ARATH | |
|---|---|---|
| UniProt AC | Q8LGH4 | |
| Protein Name | Cullin-4 | |
| Gene Name | CUL4 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 792 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the CUL4-RBX1-CDD (COP10-DDB1a-DET1) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Participates in the CDD complex to light-mediated control of development. May repress photomorphogenesis through enhancing COP1 E3 ubiquitin-protein ligase activity. Acts together with the CUL4-DDB1-COP1-SPA E3 ubiquitin-protein ligase complexes in the repression of photomorphogenesis and flowering time. Component ot the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein ligase complex which mediates ubiquitination and subsequent degradation of AKIN10. Component of the CUL4-RBX1-DDB1-DWA1/DWA2 E3 ubiquitin-protein ligase complex that acts as negative regulator in abscisic acid (ABA) signaling and may target ABI5 for degradation.. | |
| Protein Sequence | MSLPTKRSTFSAASASDDSSYSSPPMKKAKNDLHHSPQHPNTADKVVGFHMEEDPTPAAANLSRKKATLPQPTKKFVIKLNKAKPTLPTNFEENTWEKLQSAIRAIFLKKKISFDLESLYQAVDNLCLHKLDGKLYDQIEKECEEHISAALQSLVGQNTDLTVFLSRVEKCWQDFCDQMLMIRSIALTLDRKYVIQNPNVRSLWEMGLQLFRKHLSLAPEVEQRTVKGLLSMIEKERLAEAVNRTLLSHLLKMFTALGIYMESFEKPFLEGTSEFYAAEGMKYMQQSDVPEYLKHVEGRLHEENERCILYIDAVTRKPLITTVERQLLERHILVVLEKGFTTLMDGRRTEDLQRMQTLFSRVNALESLRQALSSYVRKTGQKIVMDEEKDKDMVQSLLDFKASLDIIWEESFYKNESFGNTIKDSFEHLINLRQNRPAELIAKFLDEKLRAGNKGTSEEELESVLEKVLVLFRFIQGKDVFEAFYKKDLAKRLLLGKSASIDAEKSMISKLKTECGSQFTNKLEGMFKDIELSKEINESFKQSSQARTKLPSGIEMSVHVLTTGYWPTYPPMDVKLPHELNVYQDIFKEFYLSKYSGRRLMWQNSLGHCVLKADFSKGKKELAVSLFQAVVLMLFNDAMKLSFEDIKDSTSIEDKELRRTLQSLACGKVRVLQKNPKGRDVEDGDEFEFNDEFAAPLYRIKVNAIQMKETVEENTSTTERVFQDRQYQIDAAIVRIMKTRKVLSHTLLITELFQQLKFPIKPADLKKRIESLIDREYLEREKSNPQIYNYLA | |
| 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 |
|---|---|---|---|---|---|
| 36 | Phosphorylation | AKNDLHHSPQHPNTA HCCCCCCCCCCCCHH | 18.60 | 23776212 | |
| 42 | Phosphorylation | HSPQHPNTADKVVGF CCCCCCCHHHHEEEE | 40.46 | 23776212 | |
| 248 | Phosphorylation | AVNRTLLSHLLKMFT HHHHHHHHHHHHHHH | 18.40 | 19880383 | |
| 417 | Phosphorylation | ESFYKNESFGNTIKD HHHCCCCCCCHHHHH | 48.09 | 25368622 | |
| 421 | Phosphorylation | KNESFGNTIKDSFEH CCCCCCHHHHHHHHH | 29.77 | 25368622 | |
| 425 | Phosphorylation | FGNTIKDSFEHLINL CCHHHHHHHHHHHHH | 27.77 | 25368622 |
| 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 CUL4_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CUL4_ARATH !! | ||||||
* 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 CUL4_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| COP10_ARATH | FUS9 | physical | 16844902 | |
| CSN3_ARATH | COP13 | physical | 16844902 | |
| CSN4_ARATH | COP8 | physical | 16844902 | |
| COP1_ARATH | COP1 | physical | 16844902 | |
| DDB1A_ARATH | DDB1A | physical | 16792691 | |
| RBX1A_ARATH | RBX1 | physical | 16792691 | |
| DET1_ARATH | DET1 | physical | 16792691 | |
| PRL1_ARATH | PRL1 | physical | 18223036 | |
| DET1_ARATH | DET1 | physical | 20061554 | |
| COP1_ARATH | COP1 | physical | 20061554 | |
| DDB1A_ARATH | DDB1A | physical | 20061554 | |
| MSI1_ARATH | MSI1 | physical | 21240189 | |
| DCAF1_ARATH | DCAF1 | physical | 18552200 | |
| DDB1B_ARATH | DDB1B | physical | 24067658 | |
| COP1_ARATH | COP1 | physical | 24067658 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASSSPECTROMETRY. | |
