RBX1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RBX1_MOUSE
• UniProt AC: P62878
• Protein Name: E3 ubiquitin-protein ligase RBX1
• Gene Name: Rbx1
• Organism: Mus musculus (Mouse).
• 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. [PubMed: 22118460 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 The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components (By similarity As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity 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 (By similarity Probably also stimulates CDC34 autoubiquitination (By similarity May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair (By similarity Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity Involved in the ubiquitination of KEAP1, ENC1 and KLHL41 (By similarity In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM (By similarity]
• Protein Sequence: MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAAAMDVD -------CCCCCCCC	5.30	-
2	Acetylation	------MAAAMDVDT ------CCCCCCCCC	12.15	-
9	Phosphorylation	AAAMDVDTPSGTNSG CCCCCCCCCCCCCCC	21.14	26643407
11	Phosphorylation	AMDVDTPSGTNSGAG CCCCCCCCCCCCCCC	61.41	28066266
13	Phosphorylation	DVDTPSGTNSGAGKK CCCCCCCCCCCCCCC	30.46	26643407
15	Phosphorylation	DTPSGTNSGAGKKRF CCCCCCCCCCCCCCE	29.83	26643407
94	S-nitrosocysteine	WLKTRQVCPLDNREW HHHHCCCCCCCCCCC	1.78	-
94	S-nitrosylation	WLKTRQVCPLDNREW HHHHCCCCCCCCCCC	1.78	21278135
105	Ubiquitination	NREWEFQKYGH---- CCCCCCCCCCC----	59.53	27667366

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RBX1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RBX1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RBX1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL3_MOUSE	Cul3	physical	19279002
KEAP1_MOUSE	Keap1	physical	19279002
UB2D1_HUMAN	UBE2D1	physical	14960280
UB2G2_MOUSE	Ube2g2	physical	22024926
UBC5_YEAST	UBC5	physical	22024926
FETUB_MOUSE	Fetub	physical	12939278
UB2E3_MOUSE	Ube2e3	physical	21343341
UB2G2_MOUSE	Ube2g2	physical	21343341
UBC5_YEAST	UBC5	physical	23707388
UB2G2_MOUSE	Ube2g2	physical	23871831
UB2D1_MOUSE	Ube2d1	physical	23871831
UB2D3_HUMAN	UBE2D3	physical	23955342
UB2R2_MOUSE	Ube2r2	physical	21245377
UB2D2_MOUSE	Ube2d2a	physical	20352047
UB2G2_MOUSE	Ube2g2	physical	22020328
UB2D3_MOUSE	Ube2d3	physical	22033112
UB2D1_HUMAN	UBE2D1	physical	28530236

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.