dbPTM

UB2D4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2D4_HUMAN
UniProt AC	Q9Y2X8
Protein Name	Ubiquitin-conjugating enzyme E2 D4
Gene Name	UBE2D4
Organism	Homo sapiens (Human).
Sequence Length	147
Subcellular Localization
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11' and 'Lys-48'-linked polyubiquitination..
Protein Sequence	MALKRIQKELTDLQRDPPAQCSAGPVGDDLFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPEIAHTYKADREKYNRLAREWTQKYAM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
74	Phosphorylation	VAFTTKIYHPNINSN EEEEEEEECCCCCCC	16.87	28152594
80	Phosphorylation	IYHPNINSNGSICLD EECCCCCCCCEEHHH	38.48	24076635
83	Phosphorylation	PNINSNGSICLDILR CCCCCCCEEHHHHHH	17.87	25849741
144	Acetylation	LAREWTQKYAM---- HHHHHHHHHCC----	27.83	23894911
144	Ubiquitination	LAREWTQKYAM---- HHHHHHHHHCC----	27.83	21906983
145	Phosphorylation	AREWTQKYAM----- HHHHHHHHCC-----	9.70	-

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 UB2D4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2D4_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 UB2D4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI39_HUMAN	TRIM39	physical	16189514
DTX2_HUMAN	DTX2	physical	16189514
RN126_HUMAN	RNF126	physical	16189514
UFM1_HUMAN	UFM1	physical	19690564
AMFR_HUMAN	AMFR	physical	19690564
MUL1_HUMAN	MUL1	physical	19690564
CAPS2_HUMAN	CADPS2	physical	19690564
CNOT4_HUMAN	CNOT4	physical	19690564
DTX1_HUMAN	DTX1	physical	19690564
UBE4A_HUMAN	UBE4A	physical	19690564
RN103_HUMAN	RNF103	physical	19690564
RN181_HUMAN	RNF181	physical	19690564
M3K1_HUMAN	MAP3K1	physical	19690564
MIB1_HUMAN	MIB1	physical	19690564
TRIM1_HUMAN	MID2	physical	19690564
PJA2_HUMAN	PJA2	physical	19690564
RFWD3_HUMAN	RFWD3	physical	19690564
RMD5B_HUMAN	RMND5B	physical	19690564
RNF11_HUMAN	RNF11	physical	19690564
RN111_HUMAN	RNF111	physical	19690564
RNF13_HUMAN	RNF13	physical	19690564
GOLI_HUMAN	RNF130	physical	19690564
RN150_HUMAN	RNF150	physical	19690564
RN165_HUMAN	RNF165	physical	19690564
RN167_HUMAN	RNF167	physical	19690564
RNF25_HUMAN	RNF25	physical	19690564
RNF43_HUMAN	RNF43	physical	19690564
SIAH1_HUMAN	SIAH1	physical	19690564
RNF4_HUMAN	RNF4	physical	19690564
TOPRS_HUMAN	TOPORS	physical	19690564
UHRF2_HUMAN	UHRF2	physical	19690564
RN115_HUMAN	RNF115	physical	19690564
ZNRF1_HUMAN	ZNRF1	physical	19690564
ZNRF2_HUMAN	ZNRF2	physical	19690564
ZNRF4_HUMAN	ZNRF4	physical	19690564
XIAP_HUMAN	XIAP	physical	19549727
RN125_HUMAN	RNF125	physical	19549727
RN138_HUMAN	RNF138	physical	19549727
RN126_HUMAN	RNF126	physical	19549727
RNF37_HUMAN	UBOX5	physical	19549727
RNF5_HUMAN	RNF5	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
RNF14_HUMAN	RNF14	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
RN114_HUMAN	RNF114	physical	19549727
RNF11_HUMAN	RNF11	physical	19549727
TRIM8_HUMAN	TRIM8	physical	19549727
DTX3L_HUMAN	DTX3L	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
RNF10_HUMAN	RNF10	physical	19549727
RN111_HUMAN	RNF111	physical	19549727
RN166_HUMAN	RNF166	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
RNF25_HUMAN	RNF25	physical	19549727
TRI43_HUMAN	TRIM43	physical	19549727
TRAF6_HUMAN	TRAF6	physical	19549727
BIRC8_HUMAN	BIRC8	physical	19549727
BFAR_HUMAN	BFAR	physical	19549727
ZN363_HUMAN	RCHY1	physical	19549727
RNF4_HUMAN	RNF4	physical	19549727
TRAF7_HUMAN	TRAF7	physical	19549727
RING1_HUMAN	RING1	physical	19549727
MARH3_HUMAN	MARCH3	physical	19549727
RNF12_HUMAN	RLIM	physical	19549727
LRSM1_HUMAN	LRSAM1	physical	19549727
AMFR_HUMAN	AMFR	physical	19549727
CHFR_HUMAN	CHFR	physical	19549727
ARI2_HUMAN	ARIH2	physical	19549727
MGRN1_HUMAN	MGRN1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
TRI27_HUMAN	TRIM27	physical	19549727
RFWD3_HUMAN	RFWD3	physical	19549727
RNF38_HUMAN	RNF38	physical	19549727
RBX2_HUMAN	RNF7	physical	19549727
TRI17_HUMAN	TRIM17	physical	19549727
TRIM2_HUMAN	TRIM2	physical	19549727
TRI25_HUMAN	TRIM25	physical	19549727
TRI31_HUMAN	TRIM31	physical	19549727
TRI35_HUMAN	TRIM35	physical	19549727
TRIM5_HUMAN	TRIM5	physical	19549727
HOIL1_HUMAN	RBCK1	physical	19549727
TRIM1_HUMAN	MID2	physical	21143188
TRI18_HUMAN	MID1	physical	21143188
TRI27_HUMAN	TRIM27	physical	21143188
UB2D4_HUMAN	UBE2D4	physical	20061386
DTX2_HUMAN	DTX2	physical	19549727
RNF26_HUMAN	RNF26	physical	19549727
OTUB1_HUMAN	OTUB1	physical	25416956
TRI39_HUMAN	TRIM39	physical	25416956
DTX2_HUMAN	DTX2	physical	25416956
INCA1_HUMAN	INCA1	physical	25416956
TF_HUMAN	F3	physical	27599717

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 UB2D4_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-144, AND MASS SPECTROMETRY.	19608861 [Abstract]