dbPTM

UB2L3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2L3_HUMAN
UniProt AC	P68036
Protein Name	Ubiquitin-conjugating enzyme E2 L3
Gene Name	UBE2L3
Organism	Homo sapiens (Human).
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	AASRRLMKELEEIRK HHHHHHHHHHHHHHH	64.83	21890473
9	Malonylation	AASRRLMKELEEIRK HHHHHHHHHHHHHHH	64.83	26320211
9	Acetylation	AASRRLMKELEEIRK HHHHHHHHHHHHHHH	64.83	21791702
20	Acetylation	EIRKCGMKNFRNIQV HHHHHCCCCCCCCCC	37.91	23749302
20	Ubiquitination	EIRKCGMKNFRNIQV HHHHHCCCCCCCCCC	37.91	21906983
32	Ubiquitination	IQVDEANLLTWQGLI CCCCCHHHCEECCEE	6.09	21890473
41	Ubiquitination	TWQGLIVPDNPPYDK EECCEECCCCCCCCC	28.77	21890473
48	Ubiquitination	PDNPPYDKGAFRIEI CCCCCCCCCCEEEEE	46.42	21906983
50	Ubiquitination	NPPYDKGAFRIEINF CCCCCCCCEEEEEEC	9.04	21890473
61	Phosphorylation	EINFPAEYPFKPPKI EEECCCCCCCCCCEE	18.97	28152594
64	Acetylation	FPAEYPFKPPKITFK CCCCCCCCCCEEEEE	56.77	23236377
64	Ubiquitination	FPAEYPFKPPKITFK CCCCCCCCCCEEEEE	56.77	21890473
64	Ubiquitination	FPAEYPFKPPKITFK CCCCCCCCCCEEEEE	56.77	21906983
67	Ubiquitination	EYPFKPPKITFKTKI CCCCCCCEEEEEEEE	64.01	21906983
68	Ubiquitination	YPFKPPKITFKTKIY CCCCCCEEEEEEEEC	7.26	21890473
71	Ubiquitination	KPPKITFKTKIYHPN CCCEEEEEEEECCCC	40.01	21906983
73	Acetylation	PKITFKTKIYHPNID CEEEEEEEECCCCCC	41.69	26051181
73	Ubiquitination	PKITFKTKIYHPNID CEEEEEEEECCCCCC	41.69	21890473
73	Malonylation	PKITFKTKIYHPNID CEEEEEEEECCCCCC	41.69	26320211
75	Phosphorylation	ITFKTKIYHPNIDEK EEEEEEECCCCCCCC	16.87	28152594
82	Acetylation	YHPNIDEKGQVCLPV CCCCCCCCCCEEEEE	51.39	23954790
82	Malonylation	YHPNIDEKGQVCLPV CCCCCCCCCCEEEEE	51.39	26320211
82	Ubiquitination	YHPNIDEKGQVCLPV CCCCCCCCCCEEEEE	51.39	21890473
86	S-nitrosylation	IDEKGQVCLPVISAE CCCCCCEEEEEEECC	2.46	22178444
86	S-nitrosocysteine	IDEKGQVCLPVISAE CCCCCCEEEEEEECC	2.46	-
96	Ubiquitination	VISAENWKPATKTDQ EEECCCCCCCCCHHH	36.03	21906983
96	Acetylation	VISAENWKPATKTDQ EEECCCCCCCCCHHH	36.03	25953088
99	Ubiquitination	AENWKPATKTDQVIQ CCCCCCCCCHHHHHH	42.90	19608861
99	Acetylation	AENWKPATKTDQVIQ CCCCCCCCCHHHHHH	42.90	19608861
100	Ubiquitination	ENWKPATKTDQVIQS CCCCCCCCHHHHHHH	52.81	21906983
106	Acetylation	TKTDQVIQSLIALVN CCHHHHHHHHHHHHC	33.07	19608861
122	Ubiquitination	PQPEHPLRADLAEEY CCCCCCCCHHHHHHH	30.42	21890473
129	Phosphorylation	RADLAEEYSKDRKKF CHHHHHHHHHHHHHH	16.72	28152594
130	Phosphorylation	ADLAEEYSKDRKKFC HHHHHHHHHHHHHHH	31.21	28152594
131	Ubiquitination	DLAEEYSKDRKKFCK HHHHHHHHHHHHHHH	61.73	19608861
131	Acetylation	DLAEEYSKDRKKFCK HHHHHHHHHHHHHHH	61.73	19608861
131	Ubiquitination	DLAEEYSKDRKKFCK HHHHHHHHHHHHHHH	61.73	21890473
131	Malonylation	DLAEEYSKDRKKFCK HHHHHHHHHHHHHHH	61.73	26320211
138	Ubiquitination	KDRKKFCKNAEEFTK HHHHHHHHCHHHHHH	63.43	19608861
138	Acetylation	KDRKKFCKNAEEFTK HHHHHHHHCHHHHHH	63.43	21791702
138	Malonylation	KDRKKFCKNAEEFTK HHHHHHHHCHHHHHH	63.43	26320211
140	Ubiquitination	RKKFCKNAEEFTKKY HHHHHHCHHHHHHHH	11.82	21890473
145	Acetylation	KNAEEFTKKYGEKRP HCHHHHHHHHCCCCC	49.68	23749302
145	Ubiquitination	KNAEEFTKKYGEKRP HCHHHHHHHHCCCCC	49.68	-
145	Succinylation	KNAEEFTKKYGEKRP HCHHHHHHHHCCCCC	49.68	23954790
145	2-Hydroxyisobutyrylation	KNAEEFTKKYGEKRP HCHHHHHHHHCCCCC	49.68	-
147	Phosphorylation	AEEFTKKYGEKRPVD HHHHHHHHCCCCCCC	31.88	28152594
150	Acetylation	FTKKYGEKRPVD--- HHHHHCCCCCCC---	58.60	25953088
150	Ubiquitination	FTKKYGEKRPVD--- HHHHHCCCCCCC---	58.60	-
154	Ubiquitination	YGEKRPVD------- HCCCCCCC-------	56.33	21890473
158	Ubiquitination	RPVD----------- CCCC-----------		21890473
189	Acetylation	------------------------------------------ ------------------------------------------		19608861
189	Ubiquitination	------------------------------------------ ------------------------------------------		19608861
196	Acetylation	------------------------------------------------- -------------------------------------------------		19608861

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF5	Q99942	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2L3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of UB2L3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEDD4_HUMAN	NEDD4	physical	9990509
UBE3A_HUMAN	UBE3A	physical	9990509
ARI1_HUMAN	ARIH1	physical	10521492
CUL9_HUMAN	CUL9	physical	10521492
CBL_HUMAN	CBL	physical	10966114
CBL_HUMAN	CBL	physical	12234920
RN125_HUMAN	RNF125	physical	19549727
RNF37_HUMAN	UBOX5	physical	19549727
ARI2_HUMAN	ARIH2	physical	19549727
R144B_HUMAN	RNF144B	physical	19549727
R113B_HUMAN	RNF113B	physical	19549727
R144A_HUMAN	RNF144A	physical	19549727
HOIL1_HUMAN	RBCK1	physical	19549727
TRAF7_HUMAN	TRAF7	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
CBLC_HUMAN	CBLC	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
PRKN_HUMAN	PARK2	physical	20089136
ATX3_HUMAN	ATXN3	physical	22081612
IKBA_HUMAN	NFKBIA	physical	10329681
FOS_HUMAN	FOS	physical	8524278
P53_MOUSE	Trp53	physical	8144545
UBE3A_HUMAN	UBE3A	physical	19899154
NCOA1_HUMAN	NCOA1	physical	15367689
CBL_HUMAN	CBL	physical	15062086
PRKN_HUMAN	PARK2	physical	21694720
ARI2_HUMAN	ARIH2	physical	22037423
TF65_HUMAN	RELA	physical	14690596
SMAD7_HUMAN	SMAD7	physical	16061177
ARI2_HUMAN	ARIH2	physical	19340006
USP9X_HUMAN	USP9X	physical	22939629
UBP34_HUMAN	USP34	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
UBP26_HUMAN	USP26	physical	22939629
UBXN7_HUMAN	UBXN7	physical	22939629
UB2V2_HUMAN	UBE2V2	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
UCHL3_HUMAN	UCHL3	physical	22939629
VDAC2_HUMAN	VDAC2	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
UBXN1_HUMAN	UBXN1	physical	22939629
HSP74_HUMAN	HSPA4	physical	14702098
UB2L3_HUMAN	UBE2L3	physical	20061386
UBA1_HUMAN	UBA1	physical	25026213
ARI2_HUMAN	ARIH2	physical	25224329
ARI2_HUMAN	ARIH2	physical	16118314
UBE3A_HUMAN	UBE3A	physical	8576257
UBE3A_HUMAN	UBE3A	physical	22350887
CH10_HUMAN	HSPE1	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
SNX12_HUMAN	SNX12	physical	26344197
SNX3_HUMAN	SNX3	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197
ITCH_HUMAN	ITCH	physical	26245901

Drug and Disease Associations

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

Regulatory Network of UB2L3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-131 AND LYS-138, ANDMASS SPECTROMETRY.	19608861 [Abstract]