UBE2F_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBE2F_HUMAN
• UniProt AC: Q969M7
• Protein Name: NEDD8-conjugating enzyme UBE2F
• Gene Name: UBE2F
• Organism: Homo sapiens (Human).
• Sequence Length: 185
• 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 RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5..
• Protein Sequence: MLTLASKLKRDDGLKGSRTAATASDSTRRVSVRDKLLVKEVAELEANLPCTCKVHFPDPNKLHCFQLTVTPDEGYYQGGKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRNKVDDYIKRYAR

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
1	Acetylation	-------MLTLASKL -------CCCHHHHC	6.10	23201271
7	Acetylation	-MLTLASKLKRDDGL -CCCHHHHCCCCCCC	53.04	19608861
7 (in isoform 3)	Ubiquitination	-	53.04	-
7	Ubiquitination	-MLTLASKLKRDDGL -CCCHHHHCCCCCCC	53.04	23000965
9 (in isoform 2)	Ubiquitination	-	58.48	-
9	Ubiquitination	LTLASKLKRDDGLKG CCHHHHCCCCCCCCC	58.48	23000965
15	Ubiquitination	LKRDDGLKGSRTAAT CCCCCCCCCCCEECC	61.44	33845483
26	Phosphorylation	TAATASDSTRRVSVR EECCCCCCCCCCCHH	22.71	27535140
27	Phosphorylation	AATASDSTRRVSVRD ECCCCCCCCCCCHHH	27.73	23882029
31	Phosphorylation	SDSTRRVSVRDKLLV CCCCCCCCHHHHHHH	15.04	23882029
53	Ubiquitination	ANLPCTCKVHFPDPN CCCCCEEEEECCCCC	22.16	33845483
65	Ubiquitination	DPNKLHCFQLTVTPD CCCCEEEEEEEECCC	4.67	33845483
71	Ubiquitination	CFQLTVTPDEGYYQG EEEEEECCCCCCCCC	33.06	33845483
73	Ubiquitination	QLTVTPDEGYYQGGK EEEECCCCCCCCCCE	50.74	33845483
79	Ubiquitination	DEGYYQGGKFQFETE CCCCCCCCEEEEEEE	16.45	33845483
85	Phosphorylation	GGKFQFETEVPDAYN CCEEEEEEECCCHHH	43.50	24719451
97	Ubiquitination	AYNMVPPKVKCLTKI HHHCCCCCCEEEECC	48.53	33845483
103	Ubiquitination	PKVKCLTKIWHPNIT CCCEEEECCCCCCCC	30.74	33845483
124	Phosphorylation	LSLLREHSIDGTGWA HHHHHHCCCCCCCCC	20.02	20873877
179	Phosphorylation	FRNKVDDYIKRYAR- HHHHHHHHHHHHCC-	12.13	21253578

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

Oops, there are no upstream regulatory protein records of UBE2F_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1	M	Acetylation	The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins.	23201271

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UBE2F_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RNF34_HUMAN	RNF34	physical	19549727
CUL5_HUMAN	CUL5	physical	22190037
VIF_HV1B1	vif	physical	22190037
VIF_HV1BR	vif	physical	22190037
VIF_HV1H2	vif	physical	22190037
CUL5_HUMAN	CUL5	physical	23300442
RBX2_HUMAN	RNF7	physical	23300442
DCNL1_HUMAN	DCUN1D1	physical	23201271
DCNL2_HUMAN	DCUN1D2	physical	23201271
DCNL3_HUMAN	DCUN1D3	physical	23201271
CUL1_HUMAN	CUL1	physical	19942853

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-7, AND MASSSPECTROMETRY.
PubMed: 19608861