dbPTM

UBE2K_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE2K_HUMAN
UniProt AC	P61086
Protein Name	Ubiquitin-conjugating enzyme E2 K
Gene Name	UBE2K
Organism	Homo sapiens (Human).
Sequence Length	200
Subcellular Localization	Cytoplasm .
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1..
Protein Sequence	MANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MANIAVQRI ------CCCHHHHHH	19.01	22223895
14	Acetylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	19608861
14	Sumoylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	-
14	Succinylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	23954790
14	Malonylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	26320211
14	Ubiquitination	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	19608861
14	Sumoylation	QRIKREFKEVLKSEE HHHHHHHHHHHHCCC	42.00	19608861
18	Ubiquitination	REFKEVLKSEETSKN HHHHHHHHCCCCCCC	62.08	21906983
18 (in isoform 1)	Ubiquitination	-	62.08	21890473
18	Acetylation	REFKEVLKSEETSKN HHHHHHHHCCCCCCC	62.08	25953088
18	Malonylation	REFKEVLKSEETSKN HHHHHHHHCCCCCCC	62.08	26320211
24	Ubiquitination	LKSEETSKNQIKVDL HHCCCCCCCCEEEEE	61.36	21906983
24 (in isoform 1)	Ubiquitination	-	61.36	21890473
28	Ubiquitination	ETSKNQIKVDLVDEN CCCCCCEEEEEECCC	21.67	-
40	Methylation	DENFTELRGEIAGPP CCCHHHHCCEECCCC	34.17	115919341
49	Phosphorylation	EIAGPPDTPYEGGRY EECCCCCCCCCCCEE	33.28	25022875
61 (in isoform 1)	Ubiquitination	-	42.72	21890473
61	Ubiquitination	GRYQLEIKIPETYPF CEEEEEEECCCCCCC	42.72	21906983
72 (in isoform 1)	Ubiquitination	-	47.50	21890473
72	Ubiquitination	TYPFNPPKVRFITKI CCCCCCCCEEEEEEE	47.50	21890473
72	Ubiquitination	TYPFNPPKVRFITKI CCCCCCCCEEEEEEE	47.50	21890473
91 (in isoform 2)	Ubiquitination	-	2.25	21890473
97	Ubiquitination	AICLDILKDQWAAAM CHHHHHHHHHHHHHH	48.48	-
113 (in isoform 2)	Ubiquitination	-	3.31	21890473
114 (in isoform 2)	Ubiquitination	-	26.96	21890473
142	Ubiquitination	KQNPEMFKQTARLWA HHCHHHHHHHHHHHH	45.49	21906983
142 (in isoform 1)	Ubiquitination	-	45.49	21890473
158	Phosphorylation	VYAGAPVSSPEYTKK HHCCCCCCCHHHHHH	38.83	28450419
159	Phosphorylation	YAGAPVSSPEYTKKI HCCCCCCCHHHHHHH	23.22	25159151
162	Phosphorylation	APVSSPEYTKKIENL CCCCCHHHHHHHHHH	27.52	28450419
163	Phosphorylation	PVSSPEYTKKIENLC CCCCHHHHHHHHHHH	24.97	28450419
164	Acetylation	VSSPEYTKKIENLCA CCCHHHHHHHHHHHH	51.34	26051181
164	Ubiquitination	VSSPEYTKKIENLCA CCCHHHHHHHHHHHH	51.34	21890473
164 (in isoform 1)	Ubiquitination	-	51.34	21890473
165 (in isoform 1)	Ubiquitination	-	47.67	21890473
165	Ubiquitination	SSPEYTKKIENLCAM CCHHHHHHHHHHHHC	47.67	21890473
172	Sulfoxidation	KIENLCAMGFDRNAV HHHHHHHCCCCCCEE	5.54	21406390
185	Phosphorylation	AVIVALSSKSWDVET EEEEEECCCCCCHHH	31.40	21712546

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	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
14	K	Sumoylation		19608861
Sumoylation at Lys-14 impairs catalytic activity.

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 UBE2K_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RING2_HUMAN	RNF2	physical	11513855
HD_HUMAN	HTT	physical	8702625
DDX58_HUMAN	DDX58	physical	17719635
RN125_HUMAN	RNF125	physical	19549727
RN138_HUMAN	RNF138	physical	19549727
BFAR_HUMAN	BFAR	physical	19549727
RNF37_HUMAN	UBOX5	physical	19549727
RNF5_HUMAN	RNF5	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
MARH7_HUMAN	MARCH7	physical	19549727
SIAH1_HUMAN	SIAH1	physical	19549727
TRI27_HUMAN	TRIM27	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
TRI35_HUMAN	TRIM35	physical	19549727
BIRC7_HUMAN	BIRC7	physical	19549727
BIRC8_HUMAN	BIRC8	physical	19549727
RNF4_HUMAN	RNF4	physical	19549727
TRI34_HUMAN	TRIM34	physical	19549727
RN167_HUMAN	RNF167	physical	19549727
UHRF2_HUMAN	UHRF2	physical	19549727
TRAF7_HUMAN	TRAF7	physical	19549727
MKRN2_HUMAN	MKRN2	physical	19549727
TRAIP_HUMAN	TRAIP	physical	19549727
RING1_HUMAN	RING1	physical	19549727
RNF41_HUMAN	RNF41	physical	19549727
MARH3_HUMAN	MARCH3	physical	19549727
RNF32_HUMAN	RNF32	physical	19549727
RN114_HUMAN	RNF114	physical	19549727
LRSM1_HUMAN	LRSAM1	physical	19549727
CBLC_HUMAN	CBLC	physical	19549727
DTX3L_HUMAN	DTX3L	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
RN111_HUMAN	RNF111	physical	19549727
R144A_HUMAN	RNF144A	physical	19549727
TRIM2_HUMAN	TRIM2	physical	19549727
TRI31_HUMAN	TRIM31	physical	19549727
TRI43_HUMAN	TRIM43	physical	19549727
TRIM5_HUMAN	TRIM5	physical	19549727
HOIL1_HUMAN	RBCK1	physical	19549727
ITSN1_HUMAN	ITSN1	physical	21900206
PR40A_HUMAN	PRPF40A	physical	21900206
CCNB1_HUMAN	CCNB1	physical	20965177
DBLOH_HUMAN	DIABLO	physical	20537984
UBC_HUMAN	UBC	physical	16868077
UBC_HUMAN	UBC	physical	20826778
UBC_HUMAN	UBC	physical	21281599
CASPC_HUMAN	CASP12	physical	18710920
PIAS4_HUMAN	PIAS4	physical	15383276
UBC_HUMAN	UBC	physical	22496338
UBC_HUMAN	UBC	physical	16007098
WDR1_HUMAN	WDR1	physical	22939629
WDR61_HUMAN	WDR61	physical	22939629
P53_HUMAN	TP53	physical	23933584
MDM2_HUMAN	MDM2	physical	23933584
UBC_HUMAN	UBC	physical	24882218
UBC_HUMAN	UBC	physical	24912152
REL_HUMAN	REL	physical	25416956
RNF5_HUMAN	RNF5	physical	25416956
SIAH1_HUMAN	SIAH1	physical	25416956
RN138_HUMAN	RNF138	physical	25416956
TRI39_HUMAN	TRIM39	physical	25416956
MIPO1_HUMAN	MIPOL1	physical	25416956
DTX3_HUMAN	DTX3	physical	25416956
DDI1_HUMAN	DDI1	physical	25416956
MDM2_HUMAN	MDM2	physical	15280377
UBC_HUMAN	UBC	physical	9857030
UBC_HUMAN	UBC	physical	23105008
ROA1_HUMAN	HNRNPA1	physical	26344197
UB2D2_HUMAN	UBE2D2	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197
UBC_HUMAN	UBC	physical	25799589
CYHR1_HUMAN	CYHR1	physical	28514442
RN138_HUMAN	RNF138	physical	28514442
ARL15_HUMAN	ARL15	physical	28514442
CYHR1_HUMAN	CYHR1	physical	27173435

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 UBE2K_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [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 LYS-14, AND MASS SPECTROMETRY.	19608861 [Abstract]

show