CPLM-009602

Genbank Nucleotide ID

E3 ubiquitin-protein ligase RBX1

Protein Synonyms/Alias

Protein ZYP; RING finger protein 75; RING-box protein 1; Rbx1; Regulator of cullins 1; E3 ubiquitin-protein ligase RBX1, N-terminally processed

Homo sapiens (Human)

Position	Peptide	Type	References
19	GTNSGAGKKRFEVKK	ubiquitination	[1, 2, 3]
20	TNSGAGKKRFEVKKW	ubiquitination	[1, 2, 3]
105	NREWEFQKYGH****	acetylation	[4]
105	NREWEFQKYGH****	ubiquitination	[1, 2, 3, 5, 6, 7, 8]

[1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

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. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41.

ZN_FING 53 98 RING-type.
METAL 42 42 Zinc 1.
METAL 45 45 Zinc 1.
METAL 53 53 Zinc 3.
METAL 56 56 Zinc 3.
METAL 68 68 Zinc 3.
METAL 75 75 Zinc 2.
METAL 77 77 Zinc 2.
METAL 80 80 Zinc 1.
METAL 82 82 Zinc 3.
METAL 83 83 Zinc 1.
METAL 94 94 Zinc 2.
METAL 97 97 Zinc 2.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 2 2 N-acetylalanine; in E3 ubiquitin-protein
MOD_RES 9 9 Phosphothreonine.

3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Host-virus interaction; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
GO:0005829; C:cytosol; ISS:UniProtKB.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO:0030891; C:VCB complex; IEA:Compara.
GO:0019788; F:NEDD8 ligase activity; IDA:UniProtKB.
GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO:0045116; P:protein neddylation; IDA:UniProtKB.
GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO:0016032; P:viral reproduction; TAS:Reactome.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR024766; Znf_RING_H2.