dbPTM

UBE2C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE2C_HUMAN
UniProt AC	O00762
Protein Name	Ubiquitin-conjugating enzyme E2 C
Gene Name	UBE2C
Organism	Homo sapiens (Human).
Sequence Length	179
Subcellular Localization
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit..
Protein Sequence	MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASQNRDPA ------CCCCCCCHH	21.59	21406692
3	Phosphorylation	-----MASQNRDPAA -----CCCCCCCHHH	27.04	25159151
11	Phosphorylation	QNRDPAATSVAAARK CCCCHHHHHHHHHHC	26.32	25850435
12	Phosphorylation	NRDPAATSVAAARKG CCCHHHHHHHHHHCC	12.67	27251275
18	Methylation	TSVAAARKGAEPSGG HHHHHHHCCCCCCCC	58.72	98666219
28	Dimethylation	EPSGGAARGPVGKRL CCCCCCCCCHHHHHH	49.79	-
28	Methylation	EPSGGAARGPVGKRL CCCCCCCCCHHHHHH	49.79	115919337
34	Methylation	ARGPVGKRLQQELMT CCCHHHHHHHHHHHH	31.62	24379737
34	Dimethylation	ARGPVGKRLQQELMT CCCHHHHHHHHHHHH	31.62	-
45 (in isoform 3)	Phosphorylation	-	29.85	27067055
51	Phosphorylation	MSGDKGISAFPESDN HHCCCCCCCCCCCCC	32.31	21712546
51	Ubiquitination	MSGDKGISAFPESDN HHCCCCCCCCCCCCC	32.31	21890473
80	Ubiquitination	VYEDLRYKLSLEFPS HHHHHCHHEEEECCC	25.76	21890473
82	Phosphorylation	EDLRYKLSLEFPSGY HHHCHHEEEECCCCC	23.00	20068231
87	Phosphorylation	KLSLEFPSGYPYNAP HEEEECCCCCCCCCC	57.17	28152594
87 (in isoform 4)	Phosphorylation	-	57.17	20068231
89	Phosphorylation	SLEFPSGYPYNAPTV EEECCCCCCCCCCEE	13.59	28152594
91	Phosphorylation	EFPSGYPYNAPTVKF ECCCCCCCCCCEEEE	18.57	28152594
92	Ubiquitination	FPSGYPYNAPTVKFL CCCCCCCCCCEEEEC	34.63	21890473
95	Phosphorylation	GYPYNAPTVKFLTPC CCCCCCCEEEECCCC	33.64	28152594
97	Ubiquitination	PYNAPTVKFLTPCYH CCCCCEEEECCCCCC	36.81	-
119	Acetylation	NICLDILKEKWSALY CCHHHHHHHHHHHHH	58.54	26051181
119	Ubiquitination	NICLDILKEKWSALY CCHHHHHHHHHHHHH	58.54	21906983
121	Ubiquitination	CLDILKEKWSALYDV HHHHHHHHHHHHHHH	44.88	21906983
160	Phosphorylation	AELWKNPTAFKKYLQ HHHHCCHHHHHHHHH	54.87	-
164	Ubiquitination	KNPTAFKKYLQETYS CCHHHHHHHHHHHHH	44.75	-
165	Phosphorylation	NPTAFKKYLQETYSK CHHHHHHHHHHHHHH	17.76	28851738
169	Phosphorylation	FKKYLQETYSKQVTS HHHHHHHHHHHHCCC	21.82	28851738
170	Phosphorylation	KKYLQETYSKQVTSQ HHHHHHHHHHHCCCC	17.08	28851738
171	Phosphorylation	KYLQETYSKQVTSQE HHHHHHHHHHCCCCC	24.83	29496907
172	Ubiquitination	YLQETYSKQVTSQEP HHHHHHHHHCCCCCC	38.07	21906983

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 UBE2C_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBE2C_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 UBE2C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPOLM_HUMAN	POLM	physical	17588522
UBS3B_HUMAN	UBASH3B	physical	17588522
ANC2_HUMAN	ANAPC2	physical	17443186
CDC20_HUMAN	CDC20	physical	17443186
MD2L1_HUMAN	MAD2L1	physical	17443186
BUB1B_HUMAN	BUB1B	physical	17443186
DTX1_HUMAN	DTX1	physical	19690564
PSB5_HUMAN	PSMB5	physical	20007692
CKAP2_HUMAN	CKAP2	physical	17339342
TF65_HUMAN	RELA	physical	14690596
UBE2C_HUMAN	UBE2C	physical	18485873
UBP34_HUMAN	USP34	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
UBXN7_HUMAN	UBXN7	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
UBQL1_HUMAN	UBQLN1	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZRAB2_HUMAN	ZRANB2	physical	22939629
UBQL4_HUMAN	UBQLN4	physical	22939629
UNK_HUMAN	UNK	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
UBXN1_HUMAN	UBXN1	physical	22939629
UBE2C_HUMAN	UBE2C	physical	20061386
PCGF3_HUMAN	PCGF3	physical	19549727
UBE2C_HUMAN	UBE2C	physical	19475398
KLHL2_HUMAN	KLHL2	physical	25416956
ANC2_HUMAN	ANAPC2	physical	11739784
PRS7_HUMAN	PSMC2	physical	20007692
NNRD_HUMAN	CARKD	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
RBX2_HUMAN	RNF7	physical	27910872
UBE2S_HUMAN	UBE2S	physical	27910872

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 UBE2C_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]