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Protein Page:
RBX1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

RBX1 E3 ubiquitin ligase component of multiple cullin-RING- based E3 ubiquitin-protein ligase 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. 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. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex (TCEB1 and TCEB2), CUL2 or CUL5 and VHL. Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Part of multisubunit E3 ubiquitin ligase complexes with elongin BC complex (TCEB1 and TCEB2), CUL2 and MED8; elongin BC complex (TCEB1 and TCEB2), CUL5 and MUF1. Part of multisubunit complexes with elongin BC complex (TCEB1 and TCEB2), elongin A/TCEB3 or SOCS1 or WSB1 and CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7. Probably interacts with CDC34. Interacts with COPS6. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3. Interacts with human adenovirus early E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBW7) complex. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF. Widely expressed. Belongs to the RING-box family. Note: This description may include information from UniProtKB.
Protein type: Ligase; Ubiquitin conjugating system; Ubiquitin ligase; EC 6.3.2.-
Chromosomal Location of Human Ortholog: 22q13.2
Cellular Component: Cul2-RING ubiquitin ligase complex; nucleoplasm; cullin-RING ubiquitin ligase complex; Cul5-RING ubiquitin ligase complex; VCB complex; SCF ubiquitin ligase complex; cytosol
Molecular Function: protein binding; zinc ion binding; ubiquitin protein ligase binding; protein complex binding; ubiquitin-protein ligase activity; ligase activity; NEDD8 ligase activity
Biological Process: protein monoubiquitination; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; proteasomal ubiquitin-dependent protein catabolic process; Notch signaling pathway; protein neddylation; viral reproduction; protein ubiquitination; DNA repair
Reference #:  P62877 (UniProtKB)
Alt. Names/Synonyms: BA554C12.1; MGC13357; MGC1481; Protein ZYP; RBX1; Regulator of cullins 1; RING box protein 1; RING finger protein 75; ring-box 1; RING-box protein 1; RNF75; ROC1; ZYP protein
Gene Symbols: RBX1
Molecular weight: 12,274 Da
Basal Isoelectric point: 6.49  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below


Protein Structure Not Found.

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Sites Implicated In
intracellular localization: Y106‑p

Modification Sites and Domains Show Modification Legend
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Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend

Show Multiple Sequence Alignment


SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


0 3 T9-p AAAMDVDtPsGtNsG
0 1 S11-p AMDVDtPsGtNsGAG
0 1 T13-p DVDtPsGtNsGAGKK
0 1 S15-p DtPsGtNsGAGKKRF
0 1 K105-ub NREWEFQkyGH____
1 0 Y106-p REWEFQkyGH_____


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