dbPTM

SUMO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUMO2_HUMAN
UniProt AC	P61956
Protein Name	Small ubiquitin-related modifier 2 {ECO:0000305}
Gene Name	SUMO2 {ECO:0000312\|HGNC:HGNC:11125}
Organism	Homo sapiens (Human).
Sequence Length	95
Subcellular Localization	Nucleus. Nucleus, PML body.
Protein Description	Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451. [PubMed: 26524494 This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins]
Protein Sequence	MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Sumoylation	---MADEKPKEGVKT ---CCCCCCCCCCCC	63.03	-
5	Ubiquitination	---MADEKPKEGVKT ---CCCCCCCCCCCC	63.03	21890473
5	Acetylation	---MADEKPKEGVKT ---CCCCCCCCCCCC	63.03	3755499
5	Sumoylation	---MADEKPKEGVKT ---CCCCCCCCCCCC	63.03	28112733
7	Sumoylation	-MADEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	-
7	Ubiquitination	-MADEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	21890473
7	Acetylation	-MADEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	21339330
7	Sumoylation	-MADEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	28112733
11	Acetylation	EKPKEGVKTENNDHI CCCCCCCCCCCCCCE	62.06	19608861
11	Sumoylation	EKPKEGVKTENNDHI CCCCCCCCCCCCCCE	62.06	-
11	Ubiquitination	EKPKEGVKTENNDHI CCCCCCCCCCCCCCE	62.06	21906983
11	Sumoylation	EKPKEGVKTENNDHI CCCCCCCCCCCCCCE	62.06	19608861
12	Phosphorylation	KPKEGVKTENNDHIN CCCCCCCCCCCCCEE	41.35	25159151
21	Acetylation	NNDHINLKVAGQDGS CCCCEEEEECCCCCC	26.08	25953088
21	Ubiquitination	NNDHINLKVAGQDGS CCCCEEEEECCCCCC	26.08	21890473
21	Sumoylation	NNDHINLKVAGQDGS CCCCEEEEECCCCCC	26.08	28112733
21	Sumoylation	NNDHINLKVAGQDGS CCCCEEEEECCCCCC	26.08	-
21	Ubiquitination	NNDHINLKVAGQDGS CCCCEEEEECCCCCC	26.08	21906983
28	Phosphorylation	KVAGQDGSVVQFKIK EECCCCCCEEEEEEE	27.66	30266825
33	Sumoylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	-
33	Ubiquitination	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	21890473
33	Methylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	72586761
33	Acetylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	72586761
33	Sumoylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	-
33	Ubiquitination	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	21890473
35	Ubiquitination	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	21890473
35	Sumoylation	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	-
35	Ubiquitination	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	21890473
38	Phosphorylation	QFKIKRHTPLSKLMK EEEEEECCHHHHHHH	29.92	28152594
41	Phosphorylation	IKRHTPLSKLMKAYC EEECCHHHHHHHHHH	25.58	28152594
42	Sumoylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	19608861
42	Ubiquitination	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	21890473
42	Sumoylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	-
42	Acetylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	19608861
42	Ubiquitination	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	21890473
45	Sumoylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	-
45	Acetylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	19608861
45	Methylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	19608861
45	Ubiquitination	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	21906983
45	Sumoylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	19608861
45	Ubiquitination	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	21890473
50	Methylation	LMKAYCERQGLSMRQ HHHHHHHHCCCCCEE	32.10	-
54	Phosphorylation	YCERQGLSMRQIRFR HHHHCCCCCEEEEEE	20.81	30377224
83	Phosphorylation	LEMEDEDTIDVFQQQ ECCCCCCCEEHHHHH	19.61	24732914
91	Phosphorylation	IDVFQQQTGGVY--- EEHHHHHCCCCC---	31.40	24732914
95	Phosphorylation	QQQTGGVY------- HHHCCCCC-------	18.99	24043423

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	RNF4	P78317	PMID:18408734
-	K	Ubiquitination	E3 ubiquitin ligase	RNF111	Q6ZNA4	PMID:23530056

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
6	K	ubiquitylation	18408734
Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.
11	K	ubiquitylation	11451954
Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.
48	K	ubiquitylation	18408734
Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.

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 SUMO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAF1_HUMAN	MAF1	physical	16169070
VIME_HUMAN	VIM	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
SENP3_HUMAN	SENP3	physical	11029585
ZMYM2_HUMAN	ZMYM2	physical	18806873
PIAS1_HUMAN	PIAS1	physical	18806873
SAE1_HUMAN	SAE1	physical	16620772
SAE2_HUMAN	UBA2	physical	16620772
UBC9_HUMAN	UBE2I	physical	16620772
CAF1A_HUMAN	CHAF1A	physical	19919826
RCOR1_HUMAN	RCOR1	physical	19394292
KDM1A_HUMAN	KDM1A	physical	19394292
ULP1_YEAST	ULP1	physical	22034919
VIME_HUMAN	VIM	physical	21900206
CHD3_HUMAN	CHD3	physical	21900206
SETB1_HUMAN	SETDB1	physical	21900206
HEM1_HUMAN	ALAS1	physical	21900206
PML_HUMAN	PML	physical	21779164
UIMC1_HUMAN	UIMC1	physical	22689573
BRCA1_HUMAN	BRCA1	physical	22689573
BABA2_HUMAN	BRE	physical	22689573
ABRX1_HUMAN	FAM175A	physical	22689573
BRCC3_HUMAN	BRCC3	physical	22689573
UBC9_HUMAN	UBE2I	physical	21949651
EBNA4_EBVB9	EBNA3B	physical	22398289
CVC1_EBVB9	BGLF1	physical	22398289
CEP2_EBVB9	BGLF2	physical	22398289
CEP2_EBVG	BGLF2	physical	22398289
KR2_EBVG	BGLF4	physical	22398289
KR2_EBVB9	BGLF4	physical	22398289
AN_EBVB9	BGLF5	physical	22398289
LF1_EBVB9	LF1	physical	22398289
GN_EBVB9	BLRF1	physical	22398289
GN_EBVG	BLRF1	physical	22398289
GP42_EBVB9	BZLF2	physical	22398289
GP42_EBVG	BZLF2	physical	22398289
SENP6_HUMAN	SENP6	physical	17000875
PIAS4_HUMAN	PIAS4	physical	15383276
SETB1_HUMAN	SETDB1	physical	15383276
PIAS1_HUMAN	PIAS1	physical	19217413
PIAS2_HUMAN	PIAS2	physical	19217413
USPL1_HUMAN	USPL1	physical	22878415
PIAS3_HUMAN	PIAS3	physical	19217413
UIMC1_HUMAN	UIMC1	physical	23211528
ABRX1_HUMAN	FAM175A	physical	23211528
BRCC3_HUMAN	BRCC3	physical	23211528
BABA2_HUMAN	BRE	physical	23211528
PIAS1_HUMAN	PIAS1	physical	22578841
MYB_HUMAN	MYB	physical	20802522
TEAD3_HUMAN	TEAD3	physical	21988832
USPL1_HUMAN	USPL1	physical	21988832
TNIP1_HUMAN	TNIP1	physical	21988832
UBC9_HUMAN	UBE2I	physical	16524884
TDG_HUMAN	TDG	physical	16524884
TOPRS_HUMAN	TOPORS	physical	16524884
RBP2_HUMAN	RANBP2	physical	16524884
ZCHC7_HUMAN	ZCCHC7	physical	16524884
ZCH12_HUMAN	ZCCHC12	physical	16524884
ZMYM5_HUMAN	ZMYM5	physical	16524884
ZMYM2_HUMAN	ZMYM2	physical	16524884
ZHX1_HUMAN	ZHX1	physical	16524884
SETX_HUMAN	SETX	physical	16524884
BLM_HUMAN	BLM	physical	16524884
WRN_HUMAN	WRN	physical	16524884
PIAS1_HUMAN	PIAS1	physical	16524884
PIAS2_HUMAN	PIAS2	physical	16524884
PIAS3_HUMAN	PIAS3	physical	16524884
PIAS4_HUMAN	PIAS4	physical	16524884
TYDP2_HUMAN	TDP2	physical	16524884
SP100_HUMAN	SP100	physical	16524884
CR025_HUMAN	C18orf25	physical	16524884
ORF50_HHV8P	ORF50	physical	23990779
SUMO2_HUMAN	SUMO2	physical	24844634
IRF7_HUMAN	IRF7	physical	24267727
UBP25_HUMAN	USP25	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
SENP2_HUMAN	SENP2	physical	25416956
UBC9_HUMAN	UBE2I	physical	23871147
ORF73_HHV8P	HHV8GK18_gp81	physical	24278015
TANK_HUMAN	TANK	physical	21212807
UBC9_HUMAN	UBE2I	physical	22578841
ZBTB1_HUMAN	ZBTB1	physical	20797634
ZBT21_HUMAN	ZBTB21	physical	20797634
K2C5_HUMAN	KRT5	physical	20797634
NOP58_HUMAN	NOP58	physical	20797634
HIPK2_HUMAN	HIPK2	physical	21145359
DAXX_HUMAN	DAXX	physical	22578841
PIAS2_HUMAN	PIAS2	physical	22578841
PIAS4_HUMAN	PIAS4	physical	22578841
AHNK_HUMAN	AHNAK	physical	19394292
ANXA1_HUMAN	ANXA1	physical	19394292
MCAF1_HUMAN	ATF7IP	physical	19394292
ATRX_HUMAN	ATRX	physical	19394292
BAZ1A_HUMAN	BAZ1A	physical	19394292
BAZ1B_HUMAN	BAZ1B	physical	19394292
SLX4_HUMAN	SLX4	physical	19394292
SLX4I_HUMAN	SLX4IP	physical	19394292
PYR1_HUMAN	CAD	physical	19394292
SYCC_HUMAN	CARS	physical	19394292
CAF1B_HUMAN	CHAF1B	physical	19394292
CHD4_HUMAN	CHD4	physical	19394292
CTND1_HUMAN	CTNND1	physical	19394292
CUX1_HUMAN	CUX1	physical	19394292
CASP_HUMAN	CUX1	physical	19394292
DAXX_HUMAN	DAXX	physical	19394292
DCD_HUMAN	DCD	physical	19394292
DDX17_HUMAN	DDX17	physical	19394292
DDX21_HUMAN	DDX21	physical	19394292
DDX3X_HUMAN	DDX3X	physical	19394292
PRKDC_HUMAN	PRKDC	physical	19394292
EF1A1_HUMAN	EEF1A1	physical	19394292
EF1G_HUMAN	EEF1G	physical	19394292
EME1_HUMAN	EME1	physical	19394292
ENOA_HUMAN	ENO1	physical	19394292
XPF_HUMAN	ERCC4	physical	19394292
EXOSX_HUMAN	EXOSC10	physical	19394292
EXOS9_HUMAN	EXOSC9	physical	19394292
P66B_HUMAN	GATAD2B	physical	19394292
HDAC1_HUMAN	HDAC1	physical	19394292
HDAC2_HUMAN	HDAC2	physical	19394292
HNRPF_HUMAN	HNRNPF	physical	19394292
HNRH1_HUMAN	HNRNPH1	physical	19394292
HNRPK_HUMAN	HNRNPK	physical	19394292
HP1B3_HUMAN	HP1BP3	physical	19394292
HS90B_HUMAN	HSP90AB1	physical	19394292
HSP7C_HUMAN	HSPA8	physical	19394292
GRP75_HUMAN	HSPA9	physical	19394292
IPO5_HUMAN	IPO5	physical	19394292
LAS1L_HUMAN	LAS1L	physical	19394292
MDC1_HUMAN	MDC1	physical	19394292
MDN1_HUMAN	MDN1	physical	19394292
KI67_HUMAN	MKI67	physical	19394292
MRE11_HUMAN	MRE11A	physical	19394292
MSH2_HUMAN	MSH2	physical	19394292
MTA1_HUMAN	MTA1	physical	19394292
MTA2_HUMAN	MTA2	physical	19394292
MUS81_HUMAN	MUS81	physical	19394292
NBN_HUMAN	NBN	physical	19394292
NOL9_HUMAN	NOL9	physical	19394292
NOP2_HUMAN	NOP2	physical	19394292
NUMA1_HUMAN	NUMA1	physical	19394292
PARN_HUMAN	PARN	physical	19394292
PELP1_HUMAN	PELP1	physical	19394292
PFKAM_HUMAN	PFKM	physical	19394292
PHF5A_HUMAN	PHF5A	physical	19394292
PHF8_HUMAN	PHF8	physical	19394292
PIAS1_HUMAN	PIAS1	physical	19394292
PIAS2_HUMAN	PIAS2	physical	19394292
PIAS4_HUMAN	PIAS4	physical	19394292
POGZ_HUMAN	POGZ	physical	19394292
RAD50_HUMAN	RAD50	physical	19394292
ARIP4_HUMAN	RAD54L2	physical	19394292
RBBP4_HUMAN	RBBP4	physical	19394292
RBBP7_HUMAN	RBBP7	physical	19394292
RCOR2_HUMAN	RCOR2	physical	19394292
RCOR3_HUMAN	RCOR3	physical	19394292
RL3_HUMAN	RPL3	physical	19394292
RL4_HUMAN	RPL4	physical	19394292
RUVB1_HUMAN	RUVBL1	physical	19394292
SENP2_HUMAN	SENP2	physical	19394292
SENP3_HUMAN	SENP3	physical	19394292
SETB1_HUMAN	SETDB1	physical	19394292
SMHD1_HUMAN	SMCHD1	physical	19394292
SSRP1_HUMAN	SSRP1	physical	19394292
SUMO2_HUMAN	SUMO2	physical	19394292
SP16H_HUMAN	SUPT16H	physical	19394292
TDG_HUMAN	TDG	physical	19394292
TEX10_HUMAN	TEX10	physical	19394292
LAP2A_HUMAN	TMPO	physical	19394292
LAP2B_HUMAN	TMPO	physical	19394292
TOP2A_HUMAN	TOP2A	physical	19394292
TOP2B_HUMAN	TOP2B	physical	19394292
TP53B_HUMAN	TP53BP1	physical	19394292
TPR_HUMAN	TPR	physical	19394292
TRAF1_HUMAN	TRAF1	physical	19394292
TRI26_HUMAN	TRIM26	physical	19394292
TIF1B_HUMAN	TRIM28	physical	19394292
TRIMM_HUMAN	TRIML2	physical	19394292
TBA1B_HUMAN	TUBA1B	physical	19394292
TBB5_HUMAN	TUBB	physical	19394292
TBB4B_HUMAN	TUBB4B	physical	19394292
TBB6_HUMAN	TUBB6	physical	19394292
XRCC5_HUMAN	XRCC5	physical	19394292
XRCC6_HUMAN	XRCC6	physical	19394292
ZBED1_HUMAN	ZBED1	physical	19394292
ZBTB2_HUMAN	ZBTB2	physical	19394292
ZBT25_HUMAN	ZBTB25	physical	19394292
KAISO_HUMAN	ZBTB33	physical	19394292
ZMAT3_HUMAN	ZMAT3	physical	19394292
ZMYM2_HUMAN	ZMYM2	physical	19394292
ZMYM4_HUMAN	ZMYM4	physical	19394292
ZN451_HUMAN	ZNF451	physical	19394292
ZN496_HUMAN	ZNF496	physical	19394292
CHAP1_HUMAN	CHAMP1	physical	19394292
ZMYM2_HUMAN	ZMYM2	physical	25133527
ZMYM3_HUMAN	ZMYM3	physical	25133527
ALDOA_HUMAN	ALDOA	physical	26344197
PEPL1_HUMAN	NPEPL1	physical	26344197
6PGD_HUMAN	PGD	physical	26344197
SC23A_HUMAN	SEC23A	physical	26344197
SC23B_HUMAN	SEC23B	physical	26344197
SLX4_HUMAN	SLX4	physical	25533185
MUS81_HUMAN	MUS81	physical	25533185
RNF4_HUMAN	RNF4	physical	25533185
XPF_HUMAN	ERCC4	physical	25533185
EME1_HUMAN	EME1	physical	25533185
SLX4I_HUMAN	SLX4IP	physical	25533185
MSH2_HUMAN	MSH2	physical	25533185
UBP25_HUMAN	USP25	physical	28538147
RNF8_HUMAN	RNF8	physical	28983621

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 SUMO2_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-11, AND MASS SPECTROMETRY.	19608861 [Abstract]
Sumoylation
Reference	PubMed
"In vivo identification of sumoylation sites by a signature tag andcysteine-targeted affinity purification."; Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,Eriksson J.E., Sistonen L.; J. Biol. Chem. 285:19324-19329(2010). Cited for: SUMOYLATION AT LYS-11.	20388717 [Abstract]
"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required forarsenic-induced PML degradation."; Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N.,Jaffray E.G., Palvimo J.J., Hay R.T.; Nat. Cell Biol. 10:538-546(2008). Cited for: FUNCTION, AND POLYUBIQUITINATION AT LYS-11 BY RNF4.	18408734 [Abstract]
"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to proteinsubstrates by SAE1/SAE2 and Ubc9."; Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H.,Naismith J.H., Hay R.T.; J. Biol. Chem. 276:35368-35374(2001). Cited for: SUMOYLATION AT LYS-11, AND MUTAGENESIS OF LYS-11.	11451954 [Abstract]

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