UBE2K_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBE2K_MOUSE
• UniProt AC: P61087
• Protein Name: Ubiquitin-conjugating enzyme E2 K
• Gene Name: Ube2k
• Organism: Mus musculus (Mouse).
• Sequence Length: 200
• Subcellular Localization: Cytoplasm .
• Protein Description: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. Involved in stabilization of CASP12 during ER stress-mediated amyloid-beta neurotoxicity probably by inhibiting proteasome activity; in vitro ubiquitinates CASP12..
• Protein Sequence: MANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN

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
2	Acetylation	------MANIAVQRI ------CCCHHHHHH	19.01	-
14	Acetylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	22826441
14	Malonylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	26320211
18	Acetylation	REFKEVLKSEETSKN HHHHHHHHCCCCCCC	62.08	22826441
24	Ubiquitination	LKSEETSKNQIKVDL HHCCCCCCCCEEEEE	61.36	22790023
61	Ubiquitination	GRYQLEIKIPETYPF CEEEEEEECCCCCCC	42.72	22790023
72	Acetylation	TYPFNPPKVRFITKI CCCCCCCCEEEEEEE	47.50	22826441
72	Ubiquitination	TYPFNPPKVRFITKI CCCCCCCCEEEEEEE	47.50	22790023
97	Ubiquitination	AICLDILKDQWAAAM CHHHHHHHHHHHHHH	48.48	-
142	Acetylation	KQNPEMFKQTARLWA HHCHHHHHHHHHHHH	45.49	22826441
158	Phosphorylation	VYAGAPVSSPEYTKK HHCCCCCCCHHHHHH	38.83	26745281
159	Phosphorylation	YAGAPVSSPEYTKKI HCCCCCCCHHHHHHH	23.22	26745281
162	Phosphorylation	APVSSPEYTKKIENL CCCCCHHHHHHHHHH	27.52	23984901
163	Phosphorylation	PVSSPEYTKKIENLC CCCCHHHHHHHHHHH	24.97	23984901
164	Ubiquitination	VSSPEYTKKIENLCA CCCHHHHHHHHHHHH	51.34	22790023
165	Ubiquitination	SSPEYTKKIENLCAM CCHHHHHHHHHHHHC	47.67	-
165	Acetylation	SSPEYTKKIENLCAM CCHHHHHHHHHHHHC	47.67	23806337
165	Succinylation	SSPEYTKKIENLCAM CCHHHHHHHHHHHHC	47.67	23806337

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

Oops, there are no upstream regulatory protein records of UBE2K_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
14	K	Sumoylation	Sumoylation at Lys-14 impairs catalytic activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UBE2K_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANXA7_HUMAN	ANXA7	physical	26496610
PP1RA_HUMAN	PPP1R10	physical	26496610
SYQ_HUMAN	QARS	physical	26496610
UBA1_HUMAN	UBA1	physical	26496610
UBL4A_HUMAN	UBL4A	physical	26496610
NCOA2_HUMAN	NCOA2	physical	26496610
SDCG8_HUMAN	SDCCAG8	physical	26496610
PUF60_HUMAN	PUF60	physical	26496610
PDS5A_HUMAN	PDS5A	physical	26496610
CYHR1_HUMAN	CYHR1	physical	26496610
PHF20_HUMAN	PHF20	physical	26496610
RN213_HUMAN	RNF213	physical	26496610
KLF16_HUMAN	KLF16	physical	26496610
UBC_MOUSE	Ubc	physical	25471371

Drug and Disease Associations

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