dbPTM

UBC12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBC12_HUMAN
UniProt AC	P61081
Protein Name	NEDD8-conjugating enzyme Ubc12
Gene Name	UBE2M
Organism	Homo sapiens (Human).
Sequence Length	183
Subcellular Localization
Protein Description	Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation..
Protein Sequence	MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNFKLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWKPVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFERCLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MIKLFSLK -------CCCCCCCC	5.71	21940857
3	Acetylation	-----MIKLFSLKQQ -----CCCCCCCCHH	42.03	19608861
3	Ubiquitination	-----MIKLFSLKQQ -----CCCCCCCCHH	42.03	21906983
6	Phosphorylation	--MIKLFSLKQQKKE --CCCCCCCCHHHHH	45.13	27422710
8	Ubiquitination	MIKLFSLKQQKKEEE CCCCCCCCHHHHHHH	49.86	21890473
8	Acetylation	MIKLFSLKQQKKEEE CCCCCCCCHHHHHHH	49.86	25953088
11	Ubiquitination	LFSLKQQKKEEESAG CCCCCHHHHHHHCCC	60.71	-
20	Phosphorylation	EEESAGGTKGSSKKA HHHCCCCCCCCCHHH	31.17	22817900
23	Phosphorylation	SAGGTKGSSKKASAA CCCCCCCCCHHHHHH	40.31	-
26	Ubiquitination	GTKGSSKKASAAQLR CCCCCCHHHHHHHHH	49.90	-
28	Phosphorylation	KGSSKKASAAQLRIQ CCCCHHHHHHHHHHH	32.77	23911959
33	Methylation	KASAAQLRIQKDINE HHHHHHHHHHHCHHH	19.74	115919357
36	Acetylation	AAQLRIQKDINELNL HHHHHHHHCHHHCCC	59.20	26051181
36	Ubiquitination	AAQLRIQKDINELNL HHHHHHHHCHHHCCC	59.20	21890473
36	Malonylation	AAQLRIQKDINELNL HHHHHHHHCHHHCCC	59.20	26320211
45	Acetylation	INELNLPKTCDISFS HHHCCCCCCCCCCCC	66.02	26051181
45	Ubiquitination	INELNLPKTCDISFS HHHCCCCCCCCCCCC	66.02	-
46	Phosphorylation	NELNLPKTCDISFSD HHCCCCCCCCCCCCC	17.30	22199227
47	S-nitrosocysteine	ELNLPKTCDISFSDP HCCCCCCCCCCCCCH	5.66	-
47	S-nitrosylation	ELNLPKTCDISFSDP HCCCCCCCCCCCCCH	5.66	19483679
47	Glutathionylation	ELNLPKTCDISFSDP HCCCCCCCCCCCCCH	5.66	22555962
50	Phosphorylation	LPKTCDISFSDPDDL CCCCCCCCCCCHHHH	12.87	25159151
52	Phosphorylation	KTCDISFSDPDDLLN CCCCCCCCCHHHHCC	41.25	22199227
61	Ubiquitination	PDDLLNFKLVICPDE HHHHCCCEEEECCCC	40.55	-
61	"N6,N6-dimethyllysine"	PDDLLNFKLVICPDE HHHHCCCEEEECCCC	40.55	-
61	Methylation	PDDLLNFKLVICPDE HHHHCCCEEEECCCC	40.55	-
65	Glutathionylation	LNFKLVICPDEGFYK CCCEEEECCCCCCCC	2.44	22555962
65	S-nitrosylation	LNFKLVICPDEGFYK CCCEEEECCCCCCCC	2.44	19483679
65	S-nitrosocysteine	LNFKLVICPDEGFYK CCCEEEECCCCCCCC	2.44	-
72	Acetylation	CPDEGFYKSGKFVFS CCCCCCCCCCEEEEE	50.93	26822725
72	Malonylation	CPDEGFYKSGKFVFS CCCCCCCCCCEEEEE	50.93	26320211
72	Ubiquitination	CPDEGFYKSGKFVFS CCCCCCCCCCEEEEE	50.93	21890473
72	2-Hydroxyisobutyrylation	CPDEGFYKSGKFVFS CCCCCCCCCCEEEEE	50.93	-
75	Acetylation	EGFYKSGKFVFSFKV CCCCCCCEEEEEEEE	45.50	25953088
75	Ubiquitination	EGFYKSGKFVFSFKV CCCCCCCEEEEEEEE	45.50	21890473
79	Phosphorylation	KSGKFVFSFKVGQGY CCCEEEEEEEECCCC	20.89	24719451
81	Ubiquitination	GKFVFSFKVGQGYPH CEEEEEEEECCCCCC	44.23	21890473
86	Phosphorylation	SFKVGQGYPHDPPKV EEEECCCCCCCCCCC	6.90	28152594
92	Ubiquitination	GYPHDPPKVKCETMV CCCCCCCCCEEEEEE	60.77	21890473
94	Ubiquitination	PHDPPKVKCETMVYH CCCCCCCEEEEEEEC	32.26	-
157	Methylation	AEVLQNNRRLFEQNV HHHHHHHHHHHHHHH	44.20	115919345
166	Methylation	LFEQNVQRSMRGGYI HHHHHHHHHHCCCCC	28.30	115919349
169	Methylation	QNVQRSMRGGYIGST HHHHHHHCCCCCCHH	36.31	24129315
169	Asymmetric dimethylarginine	QNVQRSMRGGYIGST HHHHHHHCCCCCCHH	36.31	-
172	Phosphorylation	QRSMRGGYIGSTYFE HHHHCCCCCCHHHHH	12.63	28152594
175	Phosphorylation	MRGGYIGSTYFERCL HCCCCCCHHHHHHHC	15.46	28857561
176	Phosphorylation	RGGYIGSTYFERCLK CCCCCCHHHHHHHCC	27.32	23312004
177	Phosphorylation	GGYIGSTYFERCLK- CCCCCHHHHHHHCC-	12.73	29978859
180	Methylation	IGSTYFERCLK---- CCHHHHHHHCC----	22.59	115919353
183	Acetylation	TYFERCLK------- HHHHHHCC-------	63.02	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
Oops, there are no upstream regulatory protein records of UBC12_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1	M	Acetylation		15361859
The acetylation of Met-1 increases affinity for DCUN1D1 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins.

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 UBC12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ULA1_HUMAN	NAE1	physical	17353931
KAP0_HUMAN	PRKAR1A	physical	17353931
UBA3_HUMAN	UBA3	physical	17353931
PED1A_HUMAN	PCED1A	physical	17353931
RN111_HUMAN	RNF111	physical	19549727
CUL7_HUMAN	CUL7	physical	21946088
UBA3_HUMAN	UBA3	physical	15694336
P53_HUMAN	TP53	physical	15242646
A4_HUMAN	APP	physical	18096514
CUL1_HUMAN	CUL1	physical	21247897
CUL3_HUMAN	CUL3	physical	21247897
PRKN_HUMAN	PARK2	physical	22388932
PINK1_HUMAN	PINK1	physical	22388932
A4_HUMAN	APP	physical	21832049
UBE2T_HUMAN	UBE2T	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
DCNL3_HUMAN	DCUN1D3	physical	23201271
DCNL4_HUMAN	DCUN1D4	physical	23201271
DCNL5_HUMAN	DCUN1D5	physical	23201271
DCNL1_HUMAN	DCUN1D1	physical	23201271
DCNL2_HUMAN	DCUN1D2	physical	23201271
RBX1_HUMAN	RBX1	physical	21765416
SMUF1_HUMAN	SMURF1	physical	24821572
DCNL3_HUMAN	DCUN1D3	physical	19617556
DCNL1_HUMAN	DCUN1D1	physical	18826954
RBX1_HUMAN	RBX1	physical	18826954
CUL1_HUMAN	CUL1	physical	18826954
UBC12_HUMAN	UBE2M	physical	20061386
RBX1_HUMAN	RBX1	physical	19549727
DCNL1_HUMAN	DCUN1D1	physical	21940857
CUL1_HUMAN	CUL1	physical	21946088
CUL1_HUMAN	CUL1	physical	19245792
UBC12_HUMAN	UBE2M	physical	19245792
CUL5_HUMAN	CUL5	physical	18805092
MDM2_HUMAN	MDM2	physical	25624478
BLOM7_HUMAN	KIAA0907	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
SAE1_HUMAN	SAE1	physical	26344197
UB2V2_HUMAN	UBE2V2	physical	26344197
TERF1_HUMAN	TERF1	physical	27214791
DCNL1_HUMAN	DCUN1D1	physical	28514442
KCTD6_HUMAN	KCTD6	physical	28514442
KLH42_HUMAN	KLHL42	physical	28514442
ULA1_HUMAN	NAE1	physical	28514442
UBA3_HUMAN	UBA3	physical	28514442
KLH18_HUMAN	KLHL18	physical	28514442
RHBT1_HUMAN	RHOBTB1	physical	28514442
KBTB7_HUMAN	KBTBD7	physical	28514442
CSN7A_HUMAN	COPS7A	physical	28514442
CSN2_HUMAN	COPS2	physical	28514442
CSN6_HUMAN	COPS6	physical	28514442
BTBD1_HUMAN	BTBD1	physical	28514442
KBTB6_HUMAN	KBTBD6	physical	28514442
CSN5_HUMAN	COPS5	physical	28514442
KLH20_HUMAN	KLHL20	physical	28514442
CSN4_HUMAN	COPS4	physical	28514442
CSN7B_HUMAN	COPS7B	physical	28514442
KCTD3_HUMAN	KCTD3	physical	28514442
NISCH_HUMAN	NISCH	physical	28514442
KLH24_HUMAN	KLHL24	physical	28514442
NEDD8_HUMAN	NEDD8	physical	28514442
SHKB1_HUMAN	SHKBP1	physical	28514442
CSN1_HUMAN	GPS1	physical	28514442
ITCH_HUMAN	ITCH	physical	27245101
DCNL1_HUMAN	DCUN1D1	physical	29074978

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 UBC12_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"N-terminal acetylation acts as an avidity enhancer within aninterconnected multiprotein complex."; Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.; Science 334:674-678(2011). Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-15 IN COMPLEX WITH CUL1 ANDDCUN1D1, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-12 IN COMPLEX WITHCUL1 AND DCUN1D1, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.	21940857 [Abstract]
"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 MET-1 AND LYS-3, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.	18669648 [Abstract]

show