UB2R1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UB2R1_MOUSE
• UniProt AC: Q8CFI2
• Protein Name: Ubiquitin-conjugating enzyme E2 R1
• Gene Name: Cdc34
• Organism: Mus musculus (Mouse).
• Sequence Length: 235
• Subcellular Localization: Cytoplasm . Nucleus . The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase.
• Protein Description: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin..
• Protein Sequence: MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEADSCFGDEEDDSGTEES

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
11	Ubiquitination	PLVPSSQKALLLELK CCCCHHHHHHHHHHC	42.84	22790023
63	Ubiquitination	GYFKARLKFPIDYPY CEEEEEEECCCCCCC	43.47	22790023
93	Glutathionylation	IYETGDVCISILHPP CCCCCCEEEEEECCC	2.10	24333276
193	Ubiquitination	TLAEYCVKTKAPAPD HHHHHHHHCCCCCCC	40.52	-
203	Phosphorylation	APAPDEGSDLFYDDY CCCCCCCCCCCCCCC	29.15	-
221	Phosphorylation	GEVEEADSCFGDEED CCEEECHHCCCCCCC	20.56	25338131
230	Phosphorylation	FGDEEDDSGTEES-- CCCCCCCCCCCCC--	60.99	25338131
232	Phosphorylation	DEEDDSGTEES---- CCCCCCCCCCC----	40.30	-
235	Phosphorylation	DDSGTEES------- CCCCCCCC-------	39.01	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
203	S	Phosphorylation	Kinase	CK2	-	Uniprot
221	S	Phosphorylation	Kinase	CK2	-	Uniprot
230	S	Phosphorylation	Kinase	CK2	-	Uniprot
232	T	Phosphorylation	Kinase	CK2	-	Uniprot
235	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UB2R1_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 UB2R1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_MOUSE	Ubc	physical	25471371

Drug and Disease Associations

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