UB2L3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UB2L3_MOUSE
• UniProt AC: P68037
• Protein Name: Ubiquitin-conjugating enzyme E2 L3
• Gene Name: Ube2l3
• Organism: Mus musculus (Mouse).
• Sequence Length: 154
• Subcellular Localization: Nucleus . Cytoplasm .
• Protein Description: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis..
• Protein Sequence: MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD

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
9	Acetylation	AASRRLMKELEEIRK HHHHHHHHHHHHHHH	64.83	-
9	Malonylation	AASRRLMKELEEIRK HHHHHHHHHHHHHHH	64.83	26320211
20	Ubiquitination	EIRKCGMKNFRNIQV HHHHHCCCCCCCCCC	37.91	-
64	Ubiquitination	FPAEYPFKPPKITFK CCCCCCCCCCEEEEE	56.77	22790023
64	Acetylation	FPAEYPFKPPKITFK CCCCCCCCCCEEEEE	56.77	23236377
67	Ubiquitination	EYPFKPPKITFKTKI CCCCCCCEEEEEEEE	64.01	22790023
73	Ubiquitination	PKITFKTKIYHPNID CEEEEEEEECCCCCC	41.69	-
73	Malonylation	PKITFKTKIYHPNID CEEEEEEEECCCCCC	41.69	26320211
82	Ubiquitination	YHPNIDEKGQVCLPV CCCCCCCCCCEEEEE	51.39	22790023
82	Acetylation	YHPNIDEKGQVCLPV CCCCCCCCCCEEEEE	51.39	23806337
86	S-nitrosocysteine	IDEKGQVCLPVISAE CCCCCCEEEEEEECC	2.46	-
86	S-nitrosylation	IDEKGQVCLPVISAE CCCCCCEEEEEEECC	2.46	21278135
86	Glutathionylation	IDEKGQVCLPVISAE CCCCCCEEEEEEECC	2.46	24333276
96	Acetylation	VISAENWKPATKTDQ EEECCCCCCCCCHHH	36.03	22826441
96	Ubiquitination	VISAENWKPATKTDQ EEECCCCCCCCCHHH	36.03	22790023
131	Ubiquitination	DLAEEYSKDRKKFCK HHHHHHHHHHHHHHH	61.73	22790023
131	Acetylation	DLAEEYSKDRKKFCK HHHHHHHHHHHHHHH	61.73	22826441
134	Acetylation	EEYSKDRKKFCKNAE HHHHHHHHHHHHCHH	61.40	8275677
135	Acetylation	EYSKDRKKFCKNAEE HHHHHHHHHHHCHHH	57.81	8276417
138	Malonylation	KDRKKFCKNAEEFTK HHHHHHHHCHHHHHH	63.43	26320211
138	Ubiquitination	KDRKKFCKNAEEFTK HHHHHHHHCHHHHHH	63.43	-
138	Acetylation	KDRKKFCKNAEEFTK HHHHHHHHCHHHHHH	63.43	22826441
145	Acetylation	KNAEEFTKKYGEKRP HCHHHHHHHHCCCCC	49.68	22826441
147	Phosphorylation	AEEFTKKYGEKRPVD HHHHHHHHCCCCCCC	31.88	25367039

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

Oops, there are no upstream regulatory protein records of UB2L3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UB2L3_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 UB2L3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RNF37_HUMAN	UBOX5	physical	11274149
HOIL1_MOUSE	Rbck1	physical	10431818
ARI2_MOUSE	Arih2	physical	10431818
R144A_HUMAN	RNF144A	physical	10431818
RN216_MOUSE	Rnf216	physical	10431818
ARI1_MOUSE	Arih1	physical	10431818
RN19A_MOUSE	Rnf19a	physical	10431818
R144A_MOUSE	Rnf144a	physical	10431818
RNF37_MOUSE	Ubox5	physical	10431818
ARI1_DROME	ari-1	physical	10880484
R144A_HUMAN	RNF144A	physical	11722579
HOIL1_MOUSE	Rbck1	physical	11722579
ARI2_MOUSE	Arih2	physical	11722579

Drug and Disease Associations

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