UniProt ID | RBX1_HUMAN | |
---|---|---|
UniProt AC | P62877 | |
Protein Name | E3 ubiquitin-protein ligase RBX1 | |
Gene Name | RBX1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 108 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets. [PubMed: 27565346 The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM.] | |
Protein Sequence | MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MAAAMDVD -------CCCCCCCC | 5.30 | 20068231 | |
2 | Acetylation | ------MAAAMDVDT ------CCCCCCCCC | 12.15 | 20068231 | |
5 | Sulfoxidation | ---MAAAMDVDTPSG ---CCCCCCCCCCCC | 4.41 | 28465586 | |
9 | Phosphorylation | AAAMDVDTPSGTNSG CCCCCCCCCCCCCCC | 21.14 | 29255136 | |
11 | Phosphorylation | AMDVDTPSGTNSGAG CCCCCCCCCCCCCCC | 61.41 | 29255136 | |
13 | Phosphorylation | DVDTPSGTNSGAGKK CCCCCCCCCCCCCCC | 30.46 | 29255136 | |
15 | Phosphorylation | DTPSGTNSGAGKKRF CCCCCCCCCCCCCCE | 29.83 | 29255136 | |
19 | Acetylation | GTNSGAGKKRFEVKK CCCCCCCCCCEEECC | 40.00 | 25953088 | |
19 | Ubiquitination | GTNSGAGKKRFEVKK CCCCCCCCCCEEECC | 40.00 | 33845483 | |
20 | Ubiquitination | TNSGAGKKRFEVKKW CCCCCCCCCEEECCH | 62.49 | 22505724 | |
90 | Phosphorylation | CISRWLKTRQVCPLD HHHHHHHHCCCCCCC | 24.94 | 30266825 | |
99 | Methylation | QVCPLDNREWEFQKY CCCCCCCCCCCCCCC | 50.50 | 115490943 | |
105 | Acetylation | NREWEFQKYGH---- CCCCCCCCCCC---- | 59.53 | 23236377 | |
105 | Ubiquitination | NREWEFQKYGH---- CCCCCCCCCCC---- | 59.53 | 23000965 | |
106 | Phosphorylation | REWEFQKYGH----- CCCCCCCCCC----- | 15.06 | 22448038 |
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 RBX1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RBX1_HUMAN !! |
* 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 RBX1_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY. |