dbPTM

UBE2S_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE2S_HUMAN
UniProt AC	Q16763
Protein Name	Ubiquitin-conjugating enzyme E2 S
Gene Name	UBE2S
Organism	Homo sapiens (Human).
Sequence Length	222
Subcellular Localization
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. [PubMed: 22496338 Catalyzes 'Lys-11'-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 specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit]
Protein Sequence	MNSNVENLPPHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGANGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIHGGAGGPSGRAEAGRALASGTEASSTDPGAPGGPGGAEGPMAKKHAGERDKKLAAKKKTDKKRALRRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNSNVENL -------CCCCHHHC	12.84	19413330
18	Ubiquitination	HIIRLVYKEVTTLTA HHHHHHEEEEEECCC	37.92	21963094
32	Ubiquitination	ADPPDGIKVFPNEED CCCCCCEEECCCHHH	43.27	33845483
63	Acetylation	AGGLFRMKLLLGKDF CCCEEHEEHHHCCCC	31.55	25953088
63	Ubiquitination	AGGLFRMKLLLGKDF CCCEEHEEHHHCCCC	31.55	23000965
68	Acetylation	RMKLLLGKDFPASPP HEEHHHCCCCCCCCC	57.05	90475
68	2-Hydroxyisobutyrylation	RMKLLLGKDFPASPP HEEHHHCCCCCCCCC	57.05	-
68	Ubiquitination	RMKLLLGKDFPASPP HEEHHHCCCCCCCCC	57.05	23000965
73	Phosphorylation	LGKDFPASPPKGYFL HCCCCCCCCCCCEEE	41.81	30266825
76	Ubiquitination	DFPASPPKGYFLTKI CCCCCCCCCEEEEEE	70.40	27667366
78	Phosphorylation	PASPPKGYFLTKIFH CCCCCCCEEEEEECC	11.09	26074081
81	Phosphorylation	PPKGYFLTKIFHPNV CCCCEEEEEECCCCC	16.52	-
82	Ubiquitination	PKGYFLTKIFHPNVG CCCEEEEEECCCCCC	45.59	21963094
82	Acetylation	PKGYFLTKIFHPNVG CCCEEEEEECCCCCC	45.59	26051181
100	Ubiquitination	EICVNVLKRDWTAEL EEEEEECCCCCHHHH	43.99	23000965
100	Acetylation	EICVNVLKRDWTAEL EEEEEECCCCCHHHH	43.99	25953088
117	Ubiquitination	RHVLLTIKCLLIHPN HHHHHEEEEEECCCC	17.37	21906983
152	Phosphorylation	AARARLLTEIHGGAG HHHHHHHHHHHCCCC	37.17	-
162	Phosphorylation	HGGAGGPSGRAEAGR HCCCCCCCHHHHHHH	44.16	28555341
173	Phosphorylation	EAGRALASGTEASST HHHHHHHCCCCCCCC	47.28	26074081
175	Phosphorylation	GRALASGTEASSTDP HHHHHCCCCCCCCCC	26.36	18669648
178	Phosphorylation	LASGTEASSTDPGAP HHCCCCCCCCCCCCC	27.78	28555341
179	Phosphorylation	ASGTEASSTDPGAPG HCCCCCCCCCCCCCC	43.83	28985074
180	Phosphorylation	SGTEASSTDPGAPGG CCCCCCCCCCCCCCC	43.66	21712546
195	Sulfoxidation	PGGAEGPMAKKHAGE CCCCCCCHHHHCCCH	14.53	21406390
197	Acetylation	GAEGPMAKKHAGERD CCCCCHHHHCCCHHH	38.55	25953088
197	Ubiquitination	GAEGPMAKKHAGERD CCCCCHHHHCCCHHH	38.55	21963094
198	Ubiquitination	AEGPMAKKHAGERDK CCCCHHHHCCCHHHH	29.20	22817900

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
152	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBE2S_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 UBE2S_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HOIL1_HUMAN	RBCK1	physical	19549727
FZR1_HUMAN	FZR1	physical	19822757
CDC20_HUMAN	CDC20	physical	19822757
CDC27_HUMAN	CDC27	physical	19822757
UBE2S_HUMAN	UBE2S	physical	20622874
UBC_HUMAN	UBC	physical	20622874
UBC_HUMAN	UBC	physical	21376237
UBE2S_HUMAN	UBE2S	physical	8576261
A4_HUMAN	APP	physical	21832049
ZCH18_HUMAN	ZC3H18	physical	22939629
UBFD1_HUMAN	UBFD1	physical	22939629
UBP10_HUMAN	USP10	physical	22939629
ZC3HE_HUMAN	ZC3H14	physical	22939629
ZN598_HUMAN	ZNF598	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
ANC2_HUMAN	ANAPC2	physical	23708001
CDC23_HUMAN	CDC23	physical	23708001
FZR1_HUMAN	FZR1	physical	23708001
FBX5_HUMAN	FBXO5	physical	23708001
UBE2S_HUMAN	UBE2S	physical	20061386
UBE2S_HUMAN	UBE2S	physical	25306923
APC1_HUMAN	ANAPC1	physical	25306923
ANC2_HUMAN	ANAPC2	physical	25306923
APC4_HUMAN	ANAPC4	physical	25306923
CDC27_HUMAN	CDC27	physical	25306923
APC5_HUMAN	ANAPC5	physical	25306923
CDC16_HUMAN	CDC16	physical	25306923
APC7_HUMAN	ANAPC7	physical	25306923
CDC23_HUMAN	CDC23	physical	25306923
APC11_HUMAN	ANAPC11	physical	25306923
FZR1_HUMAN	FZR1	physical	25306923
CDC20_HUMAN	CDC20	physical	25306923
KC1E_HUMAN	CSNK1E	physical	26186194
CBP_HUMAN	CREBBP	physical	26344197
SYNC_HUMAN	NARS	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
US6NL_HUMAN	USP6NL	physical	26496610
BRE1B_HUMAN	RNF40	physical	26496610
RUSC1_HUMAN	RUSC1	physical	26496610
ELMO3_HUMAN	ELMO3	physical	26496610
UBB_HUMAN	UBB	physical	26828794
ANC2_HUMAN	ANAPC2	physical	25306918
APC11_HUMAN	ANAPC11	physical	25306918
CDC20_HUMAN	CDC20	physical	25306918
UBC_HUMAN	UBC	physical	25306918
CDC23_HUMAN	CDC23	physical	25306918
FZR1_HUMAN	FZR1	physical	25306918
UBE2S_HUMAN	UBE2S	physical	27685940
VHL_HUMAN	VHL	physical	27685940
RBX2_HUMAN	RNF7	physical	27910872
UBE2C_HUMAN	UBE2C	physical	27910872
UB2D3_HUMAN	UBE2D3	physical	27910872
AKT1_HUMAN	AKT1	physical	27593939
SVOPL_HUMAN	SVOPL	physical	27593939
PMF1_HUMAN	PMF1	physical	27593939
DPM3_HUMAN	DPM3	physical	27593939
XRCC6_HUMAN	XRCC6	physical	27593939
HSP7C_HUMAN	HSPA8	physical	27593939
XRCC5_HUMAN	XRCC5	physical	27593939
NUCL_HUMAN	NCL	physical	27593939
SRP68_HUMAN	SRP68	physical	27593939
HS71L_HUMAN	HSPA1L	physical	27593939
IF2B1_HUMAN	IGF2BP1	physical	27593939
HNRPR_HUMAN	HNRNPR	physical	27593939
GRP78_HUMAN	HSPA5	physical	27593939

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 UBE2S_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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]