dbPTM

SUMO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUMO1_HUMAN
UniProt AC	P63165
Protein Name	Small ubiquitin-related modifier 1
Gene Name	SUMO1
Organism	Homo sapiens (Human).
Sequence Length	101
Subcellular Localization	Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Cell membrane . Nucleus . Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely
Protein Description	Ubiquitin-like protein that can be covalently attached to proteins as a monomer or 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 E3 ligases such as PIAS1-4, RANBP2 or CBX4. 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. [PubMed: 19223394 Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3]
Protein Sequence	MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDQEAKPS ------CCCCCCCCC	48.26	29255136
2	Acetylation	------MSDQEAKPS ------CCCCCCCCC	48.26	19691289
2 (in isoform 2)	Phosphorylation	-	48.26	-
6 (in isoform 2)	Phosphorylation	-	24.35	21949786
7	Acetylation	-MSDQEAKPSTEDLG -CCCCCCCCCCCCCC	38.45	25953088
7 (in isoform 2)	Phosphorylation	-	38.45	21949786
7	Sumoylation	-MSDQEAKPSTEDLG -CCCCCCCCCCCCCC	38.45	28112733
7	Sumoylation	-MSDQEAKPSTEDLG -CCCCCCCCCCCCCC	38.45	-
7	Ubiquitination	-MSDQEAKPSTEDLG -CCCCCCCCCCCCCC	38.45	-
9	Phosphorylation	SDQEAKPSTEDLGDK CCCCCCCCCCCCCCC	43.66	25159151
10	Phosphorylation	DQEAKPSTEDLGDKK CCCCCCCCCCCCCCC	41.88	25159151
16	Acetylation	STEDLGDKKEGEYIK CCCCCCCCCCCCEEE	51.42	25953088
16	Ubiquitination	STEDLGDKKEGEYIK CCCCCCCCCCCCEEE	51.42	-
16	Sumoylation	STEDLGDKKEGEYIK CCCCCCCCCCCCEEE	51.42	28112733
16	Sumoylation	STEDLGDKKEGEYIK CCCCCCCCCCCCEEE	51.42	-
17	Ubiquitination	TEDLGDKKEGEYIKL CCCCCCCCCCCEEEE	75.57	-
17	Sumoylation	TEDLGDKKEGEYIKL CCCCCCCCCCCEEEE	75.57	28112733
17	Sumoylation	TEDLGDKKEGEYIKL CCCCCCCCCCCEEEE	75.57	-
21	Phosphorylation	GDKKEGEYIKLKVIG CCCCCCCEEEEEEEC	17.76	26074081
23	Ubiquitination	KKEGEYIKLKVIGQD CCCCCEEEEEEECCC	41.16	21890473
23	Acetylation	KKEGEYIKLKVIGQD CCCCCEEEEEEECCC	41.16	19608861
23	Sumoylation	KKEGEYIKLKVIGQD CCCCCEEEEEEECCC	41.16	-
23	Ubiquitination	KKEGEYIKLKVIGQD CCCCCEEEEEEECCC	41.16	19608861
23	Sumoylation	KKEGEYIKLKVIGQD CCCCCEEEEEEECCC	41.16	28112733
25	Ubiquitination	EGEYIKLKVIGQDSS CCCEEEEEEECCCCC	27.14	21906983
25	Sumoylation	EGEYIKLKVIGQDSS CCCEEEEEEECCCCC	27.14	-
25	Sumoylation	EGEYIKLKVIGQDSS CCCEEEEEEECCCCC	27.14	28112733
31	Phosphorylation	LKVIGQDSSEIHFKV EEEECCCCCEEEEEE	23.22	25159151
32	Phosphorylation	KVIGQDSSEIHFKVK EEECCCCCEEEEEEE	49.19	25159151
37	Sumoylation	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	-
37	Acetylation	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	23749302
37	Methylation	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	83039913
37	Sumoylation	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	-
37	Ubiquitination	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	21906983
39	Sumoylation	SEIHFKVKMTTHLKK CEEEEEEEEHHHHHH	30.99	28112733
39	Methylation	SEIHFKVKMTTHLKK CEEEEEEEEHHHHHH	30.99	82992521
39	Acetylation	SEIHFKVKMTTHLKK CEEEEEEEEHHHHHH	30.99	20458745
39	Sumoylation	SEIHFKVKMTTHLKK CEEEEEEEEHHHHHH	30.99	-
39	Ubiquitination	SEIHFKVKMTTHLKK CEEEEEEEEHHHHHH	30.99	-
41	Phosphorylation	IHFKVKMTTHLKKLK EEEEEEEHHHHHHHH	12.83	26074081
42	Phosphorylation	HFKVKMTTHLKKLKE EEEEEEHHHHHHHHH	23.01	26074081
45	2-Hydroxyisobutyrylation	VKMTTHLKKLKESYC EEEHHHHHHHHHHHH	48.75	-
45	Acetylation	VKMTTHLKKLKESYC EEEHHHHHHHHHHHH	48.75	20458745
45	Sumoylation	VKMTTHLKKLKESYC EEEHHHHHHHHHHHH	48.75	28112733
45	Ubiquitination	VKMTTHLKKLKESYC EEEHHHHHHHHHHHH	48.75	-
45	Sumoylation	VKMTTHLKKLKESYC EEEHHHHHHHHHHHH	48.75	-
46	Acetylation	KMTTHLKKLKESYCQ EEHHHHHHHHHHHHH	71.76	20458745
46	Ubiquitination	KMTTHLKKLKESYCQ EEHHHHHHHHHHHHH	71.76	-
46	Sumoylation	KMTTHLKKLKESYCQ EEHHHHHHHHHHHHH	71.76	28112733
46	Sumoylation	KMTTHLKKLKESYCQ EEHHHHHHHHHHHHH	71.76	-
48	Sumoylation	TTHLKKLKESYCQRQ HHHHHHHHHHHHHHC	54.19	-
48	Sumoylation	TTHLKKLKESYCQRQ HHHHHHHHHHHHHHC	54.19	-
48	Acetylation	TTHLKKLKESYCQRQ HHHHHHHHHHHHHHC	54.19	26051181
48	Ubiquitination	TTHLKKLKESYCQRQ HHHHHHHHHHHHHHC	54.19	21906983
59	Sulfoxidation	CQRQGVPMNSLRFLF HHHCCCCHHHHHHHH	5.03	21406390
61	Phosphorylation	RQGVPMNSLRFLFEG HCCCCHHHHHHHHCC	18.05	30108239
63	Methylation	GVPMNSLRFLFEGQR CCCHHHHHHHHCCCC	26.49	115918017
70	Methylation	RFLFEGQRIADNHTP HHHHCCCCCCCCCCC	36.60	115918021
76	Phosphorylation	QRIADNHTPKELGME CCCCCCCCCHHHCCC	42.16	27251275
78	Sumoylation	IADNHTPKELGMEEE CCCCCCCHHHCCCHH	67.72	-
78	Ubiquitination	IADNHTPKELGMEEE CCCCCCCHHHCCCHH	67.72	-

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 SUMO1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SUMO1_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 SUMO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TNR6_HUMAN	FAS	physical	8906799
CK065_HUMAN	C11orf65	physical	16189514
PIAS1_HUMAN	PIAS1	physical	14609633
PIAS2_HUMAN	PIAS2	physical	14609633
HIPK2_HUMAN	HIPK2	physical	14609633
TYDP2_HUMAN	TDP2	physical	14609633
RAGP1_HUMAN	RANGAP1	physical	12924945
UBC9_HUMAN	UBE2I	physical	12924945
SAE1_HUMAN	SAE1	physical	12924945
SAE2_HUMAN	UBA2	physical	12924945
SLX5_YEAST	SLX5	physical	17848550
P53_HUMAN	TP53	physical	10961991
P73_HUMAN	TP73	physical	10961991
SUMO1_HUMAN	SUMO1	physical	10961991
DNM3B_HUMAN	DNMT3B	physical	11735126
TNR1A_HUMAN	TNFRSF1A	physical	8906799
DAXX_HUMAN	DAXX	physical	11112409
UBC9_HUMAN	UBE2I	physical	8921390
TOP2B_HUMAN	TOP2B	physical	10862613
SAE2_HUMAN	UBA2	physical	10217437
CAF1A_HUMAN	CHAF1A	physical	19919826
MITF_HUMAN	MITF	physical	16029420
PML_HUMAN	PML	physical	21779164
RS3_HUMAN	RPS3	physical	21968017
TRIM5_HUMAN	TRIM5	physical	21490953
STAT_DROME	Stat92E	physical	20616536
TDG_HUMAN	TDG	physical	17060459
DYN1_RAT	Dnm1	physical	15123615
DAXX_HUMAN	DAXX	physical	20927612
UBP25_HUMAN	USP25	physical	18538659
RNF4_HUMAN	RNF4	physical	15707587
UBC9_HUMAN	UBE2I	physical	21949651
P63_HUMAN	TP63	physical	15539951
USPL1_HUMAN	USPL1	physical	22878415
PIAS1_HUMAN	PIAS1	physical	19217413
PIAS2_HUMAN	PIAS2	physical	19217413
PML_HUMAN	PML	physical	19217413
PIAS3_HUMAN	PIAS3	physical	19217413
PML_HUMAN	PML	physical	17081985
GAG_HV1H2	gag	physical	15613319
UBC9_HUMAN	UBE2I	physical	9353268
ZCH12_HUMAN	ZCCHC12	physical	19416967
CASP2_HUMAN	CASP2	physical	15882978
UIMC1_HUMAN	UIMC1	physical	23211528
HNRPK_HUMAN	HNRNPK	physical	23092970
PIAS1_HUMAN	PIAS1	physical	22578841
MYB_HUMAN	MYB	physical	20802522
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
SP100_HUMAN	SP100	physical	16524884
CR025_HUMAN	C18orf25	physical	16524884
TYDP2_HUMAN	TDP2	physical	16524884
ORF50_HHV8P	ORF50	physical	23990779
UBC9_HUMAN	UBE2I	physical	18359863
PGH2_HUMAN	PTGS2	physical	21187340
ARC1B_HUMAN	ARPC1B	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
KAPCB_HUMAN	PRKACB	physical	22863883
RNF4_HUMAN	RNF4	physical	24907272
PIAS2_HUMAN	PIAS2	physical	25416956
HGS_HUMAN	HGS	physical	25416956
ZMYM5_HUMAN	ZMYM5	physical	25416956
TRAF4_HUMAN	TRAF4	physical	25416956
SAE2_HUMAN	UBA2	physical	25416956
ZBTB6_HUMAN	ZBTB6	physical	25416956
ARIP4_HUMAN	RAD54L2	physical	25416956
FSBP_HUMAN	RAD54B	physical	25416956
RA54B_HUMAN	RAD54B	physical	25416956
ZBT26_HUMAN	ZBTB26	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
F118B_HUMAN	FAM118B	physical	25416956
RHXF2_HUMAN	RHOXF2	physical	25416956
FBF1_HUMAN	FBF1	physical	25416956
MISSL_HUMAN	MAPK1IP1L	physical	25416956
DTX2_HUMAN	DTX2	physical	25416956
EDAD_HUMAN	EDARADD	physical	25416956
CR025_HUMAN	C18orf25	physical	25416956
DEUP1_HUMAN	CCDC67	physical	25416956
ZCH12_HUMAN	ZCCHC12	physical	25416956
DAXX_HUMAN	DAXX	physical	25409927
ZN451_HUMAN	ZNF451	physical	18656483
RBP2_HUMAN	RANBP2	physical	18359863
BUB1B_HUMAN	BUB1B	physical	22374677
PML_HUMAN	PML	physical	17344210
NR1H4_HUMAN	NR1H4	physical	23546875
PIAS1_HUMAN	PIAS1	physical	18806873
SENP2_HUMAN	SENP2	physical	14673145
RN111_HUMAN	RNF111	physical	23530056
DAXX_HUMAN	DAXX	physical	17081986
HIPK2_HUMAN	HIPK2	physical	21145359
RBP2_HUMAN	RANBP2	physical	22578841
DAXX_HUMAN	DAXX	physical	22578841
KR2_EBVG	BGLF4	physical	22398289
KR2_EBVB9	BGLF4	physical	22398289
PRKN_HUMAN	PARK2	physical	16955485
ZMYM3_HUMAN	ZMYM3	physical	25133527
PFD2_HUMAN	PFDN2	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
MX1_HUMAN	MX1	physical	25447205
KLF5_HUMAN	KLF5	physical	18500350
DAXX_MOUSE	Daxx	physical	25497731
PML_HUMAN	PML	physical	25497731
ATX3_HUMAN	ATXN3	physical	28275011
PSIP1_HUMAN	PSIP1	physical	22748127
HSF1_HUMAN	HSF1	physical	22748127
PIAS1_HUMAN	PIAS1	physical	27032383

Drug and Disease Associations

Kegg Disease
H00516	Isolated orofacial clefts, including: Cleft lip with or without cleft palate; Cleft palate
OMIM Disease
613705	Non-syndromic orofacial cleft 10 (OFC10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SUMO1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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-7 AND LYS-25, AND ACETYLATION AT SER-2.	20388717 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphorylation of SUMO-1 occurs in vivo and is conserved throughevolution."; Matic I., Macek B., Hilger M., Walther T.C., Mann M.; J. Proteome Res. 7:4050-4057(2008). Cited for: PHOSPHORYLATION AT SER-2.	18707152 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	17081983 [Abstract]