UniProt ID | RBX2_HUMAN | |
---|---|---|
UniProt AC | Q9UBF6 | |
Protein Name | RING-box protein 2 | |
Gene Name | RNF7 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 113 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. [PubMed: 10851089 CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (By similarity Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents.] | |
Protein Sequence | MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MADVEDGEE ------CCCCCCCCE | 29.56 | 19413330 | |
10 | Phosphorylation | DVEDGEETCALASHS CCCCCCEEEEEEECC | 9.97 | 16874460 | |
15 | Phosphorylation | EETCALASHSGSSGS CEEEEEEECCCCCCC | 21.02 | 27251275 | |
17 | Phosphorylation | TCALASHSGSSGSKS EEEEEECCCCCCCCC | 37.56 | 25159151 | |
19 | Phosphorylation | ALASHSGSSGSKSGG EEEECCCCCCCCCCC | 34.24 | 25159151 | |
20 | Phosphorylation | LASHSGSSGSKSGGD EEECCCCCCCCCCCC | 51.08 | 25159151 | |
22 | Phosphorylation | SHSGSSGSKSGGDKM ECCCCCCCCCCCCCC | 26.12 | 25627689 | |
23 | Ubiquitination | HSGSSGSKSGGDKMF CCCCCCCCCCCCCCE | 57.56 | - | |
28 | Acetylation | GSKSGGDKMFSLKKW CCCCCCCCCEEECCC | 45.15 | 23954790 | |
28 | Ubiquitination | GSKSGGDKMFSLKKW CCCCCCCCCEEECCC | 45.15 | 29967540 | |
31 | O-linked_Glycosylation | SGGDKMFSLKKWNAV CCCCCCEEECCCCEE | 35.46 | 30379171 | |
31 | Phosphorylation | SGGDKMFSLKKWNAV CCCCCCEEECCCCEE | 35.46 | - | |
58 | Sulfoxidation | AICRVQVMDACLRCQ EEEEHHHHHHHHHHC | 1.19 | 21406390 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
10 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
10 | T | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
10 | T | Phosphorylation | Kinase | CK2 | - | Uniprot |
10 | T | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
- | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:25216516 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RBX2_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 RBX2_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
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, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Phosphorylation of threonine 10 on CKBBP1/SAG/ROC2/Rbx2 by proteinkinase CKII promotes the degradation of IkappaBalpha and p27Kip1."; Kim Y.-S., Lee J.-Y., Son M.-Y., Park W., Bae Y.-S.; J. Biol. Chem. 278:28462-28469(2003). Cited for: PHOSPHORYLATION AT THR-10 BY CK2. |