Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Small ubiquitin-related modifier 1  

UniProtKB / Swiss-Prot ID :  SUMO1_HUMAN

Gene Name (Synonyms) : 
SUMO1, SMT3C, SMT3H3, UBL1 OK/SW-cl.43  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus membrane. Nucleus speckle. Cytoplasm. Note=Recruited by BCL11A into the nuclear body (By similarity). 

Protein Function :  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. 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. 

Protein Sequence MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQR...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCEEEEEEEECCCCEEEEEECCCCCHHHHHHHHHHHHCCCHHHEEEEECCCE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine.---MSDQEA
---CCCCCC
48.26UniProtKB
Link
2Phosphoserine---MSDQEA
---CCCCCC
48.26HPRD
Link
2Phosphoserine---MSDQEA
---CCCCCC
48.26HPRD
Link
2Phosphoserine---MSDQEA
---CCCCCC
48.26PhosphoELM
Link
2Phosphoserine---MSDQEA
---CCCCCC
48.26Phosphositeplus
Link
2Phosphoserine---MSDQEA
---CCCCCC
48.26SysPTM
Link
2Phosphoserine.---MSDQEA
---CCCCCC
48.26UniProtKB
Link
7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)DQEAKPSTE
CCCCCCCCC
38.45Phosphositeplus
Link
7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (interchain with G-Cter in SUMO-DQEAKPSTE
CCCCCCCCC
38.45UniProtKB
Link
9PhosphoserineEAKPSTEDL
CCCCCCCCC
43.66HPRD
Link
9PhosphoserineEAKPSTEDL
CCCCCCCCC
43.66Phosphositeplus
Link
9PhosphoserineEAKPSTEDL
CCCCCCCCC
43.66SysPTM
Link
9Phosphoserine.EAKPSTEDL
CCCCCCCCC
43.66UniProtKB
Link
10PhosphothreonineAKPSTEDLG
CCCCCCCCC
41.88HPRD
Link
10PhosphothreonineAKPSTEDLG
CCCCCCCCC
41.88Phosphositeplus
Link
10PhosphothreonineAKPSTEDLG
CCCCCCCCC
41.88SysPTM
Link
16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)DLGDKKEGE
CCCCCCCCC
51.42Phosphositeplus
Link
17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)LGDKKEGEY
CCCCCCCCE
75.57Phosphositeplus
Link
23N6-acetyllysineGEYIKLKVI
CCEEEEEEE
41.16HPRD
Link
23N6-acetyllysineGEYIKLKVI
CCEEEEEEE
41.16Phosphositeplus
Link
25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)YIKLKVIGQ
EEEEEEEEC
27.14Phosphositeplus
Link
25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (interchain with G-Cter in SUMO-YIKLKVIGQ
EEEEEEEEC
27.14UniProtKB
Link
25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YIKLKVIGQ
EEEEEEEEC
27.14Phosphositeplus
Link
37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)EIHFKVKMT
EEEEEECCC
27.12Phosphositeplus
Link
37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIHFKVKMT
EEEEEECCC
27.12Phosphositeplus
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)HFKVKMTTH
EEEECCCCC
30.99Phosphositeplus
Link
46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)THLKKLKES
CCHHHHHHH
71.76Phosphositeplus
Link
48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LKKLKESYC
HHHHHHHHH
54.19Phosphositeplus
Link
97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) (interchain with K-? in acceptor proteinsEQTGGHSTV
HHCCCCCCC
18.24UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ELK1_HUMANphysical interactionMINT-3380443MINT17036045
NF1_HUMANphysical interactionMINT-3380416MINT17036045
RAGP1_HUMANphysical interactionMINT-3380510MINT17036045
SOX10_HUMANsumoylation reactionMINT-1781773MINT16494873
UBC9_HUMANdirect interactionMINT-4958436MINT17491593
UBC9_HUMANdirect interactionMINT-4958452MINT17491593
UBC9_HUMANdirect interactionMINT-4958422MINT17491593
MEF2A_HUMANphysical interactionMINT-3380349MINT17036045
TDG_HUMANphysical interactionMINT-2789719MINT16763556
Q15959_HUMANphysical interactionMINT-3380460MINT17036045
SIN3A_HUMANphysical interactionMINT-3380493MINT17036045
HIPK2_HUMANcovalent bindingMINT-60084MINT15896780
SENP1_HUMANphysical interactionMINT-60089MINT15896780
MBD1_HUMANphysical interactionMINT-3382840MINT17066076
MBD1_HUMANphysical interactionMINT-3382797MINT17066076
P53_HUMANcovalent bindingDIP:57081EDIP16732283
CHD8_HUMANphysical interactionEBI-1210299
intact17000644
ZF106_HUMANphysical interactionEBI-1210299
intact17000644
STOM_HUMANphysical interactionEBI-1210299
intact17000644
PPB1_HUMANphysical interactionEBI-1210299
intact17000644
DHX30_HUMANphysical interactionEBI-1210299
intact17000644
H2B2E_HUMANphysical interactionEBI-1210299
intact17000644
K1553_HUMANphysical interactionEBI-1210299
intact17000644
ZNHI4_HUMANphysical interactionEBI-1210299
intact17000644
ARI5B_HUMANphysical interactionEBI-1210299
intact17000644
Q5BJG6_HUMANphysical interactionEBI-1210299
intact17000644
RED2_HUMANphysical interactionEBI-1210299
intact17000644
ZN768_HUMANphysical interactionEBI-1210299
intact17000644
RREB1_HUMANphysical interactionEBI-1210299
intact17000644
PAR12_HUMANphysical interactionEBI-1210299
intact17000644
ZN317_HUMANphysical interactionEBI-1210299
intact17000644
ZSC12_HUMANphysical interactionEBI-1210299
intact17000644
F120C_HUMANphysical interactionEBI-1210299
intact17000644
ZN362_HUMANphysical interactionEBI-1210299
intact17000644
SPTB2_HUMANphysical interactionEBI-1210299
intact17000644
CHD2_HUMANphysical interactionEBI-1210299
intact17000644
RBAK_HUMANphysical interactionEBI-1210299
intact17000644
Q9NYW8_HUMANphysical interactionEBI-1210299
intact17000644
PRR6_HUMANphysical interactionEBI-1210299
intact17000644
ZN592_HUMANphysical interactionEBI-1210299
intact17000644
Q96G95_HUMANphysical interactionEBI-1210299
intact17000644
ZN174_HUMANphysical interactionEBI-1210299
intact17000644
RSBN1_HUMANphysical interactionEBI-1210299
intact17000644
PP1RA_HUMANphysical interactionEBI-1210299
intact17000644
OGT1_HUMANphysical interactionEBI-1210299
intact17000644
WDR33_HUMANphysical interactionEBI-1210299
intact17000644
ZN687_HUMANphysical interactionEBI-1210299
intact17000644
Q08AJ7_HUMANdirect interaction
direct interaction
EBI-1549915
EBI-1549907
intact17956732
17956732
CK065_HUMANphysical interactionEBI-754177
intact16189514
PML_HUMANphysical interactionEBI-367073
intact11948183
SUMO1_HUMANphysical interactionEBI-1559403
intact11112409
PML_HUMANin vitro
in vivo
HPRD:03554HPRD8806687
11080164
11948183
9756909
TOP1_HUMANin vitro
in vivo
HPRD:03554HPRD11709553
12149243
12439742
TOP2A_HUMANin vitro
in vivo
HPRD:03554HPRD10862613
12832072
TOP2B_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03554HPRD10862613
TNR6_HUMANin vitro
yeast 2-hybrid
HPRD:03554HPRD9740801
8906799
TNFL6_HUMANyeast 2-hybridHPRD:03554HPRD8906799
GCR_HUMANin vivoHPRD:03554HPRD12193561
12144530
GTR1_HUMANin vivoHPRD:03554HPRD10655495
HSF1_HUMANin vitro
in vivo
HPRD:03554HPRD12665592
12646186
MDM2_HUMANin vitro
in vivo
HPRD:03554HPRD11384992
12393906
JUN_HUMANin vitro
in vivo
HPRD:03554HPRD11867732
MITF_HUMANin vitro
in vivo
HPRD:03554HPRD10694430
SRBP1_HUMANin vitroHPRD:03554HPRD12615929
CK065_HUMANyeast 2-hybridHPRD:03554HPRD16189514
RAD51_HUMANin vivo
yeast 2-hybrid
HPRD:03554HPRD8812453
9891849
ANDR_HUMANin vitro
in vivo
HPRD:03554HPRD12177000
SP3_HUMANin vivoHPRD:03554HPRD12419227
TDG_HUMANin vitro
yeast 2-hybrid
HPRD:03554HPRD11889051
NCOA1_HUMANin vitro
in vivo
HPRD:03554HPRD12529333
DAXX_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03554HPRD11112409
11948183
12150977
TIF1A_HUMANin vitro
in vivo
HPRD:03554HPRD11313457
HIPK2_HUMANin vivo
yeast 2-hybrid
HPRD:03554HPRD14609633
10535925
SP100_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03554HPRD11313457
10212234
16189514
PARK7_HUMANin vitro
in vivo
HPRD:03554HPRD12526767
12761214
IKBA_HUMANin vivoHPRD:03554HPRD9734360
SRBP2_HUMANin vitro
in vivo
HPRD:03554HPRD12615929
ETV6_HUMANin vivoHPRD:03554HPRD11078523
12626745
NCOA2_HUMANin vitro
in vivo
HPRD:03554HPRD12060666
TNR1A_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03554HPRD10187798
8906799
HIPK3_HUMANyeast 2-hybridHPRD:03554HPRD10961991
FOS_HUMANin vitroHPRD:03554HPRD16055710
TTRAP_HUMANyeast 2-hybridHPRD:03554HPRD14609633
MSX1_HUMANin vivoHPRD:03554HPRD16678795
16600910
SOX6_HUMANin vitro
in vivo
HPRD:03554HPRD16442531
TOE1_HUMANyeast 2-hybridHPRD:03554HPRD16169070
SENP1_HUMANENSP00000264281STRING
TNR1A_HUMANENSP00000264281STRING
IKBA_HUMANENSP00000264281STRING
PIAS1_HUMANENSP00000264281STRING
NEDD8_HUMANENSP00000264281STRING
MDM2_HUMANENSP00000264281STRING
HIPK2_HUMANENSP00000264281STRING
DAXX_HUMANENSP00000264281STRING
TDG_HUMANENSP00000264281STRING
RAD51_HUMANENSP00000264281STRING
PML_HUMANENSP00000264281STRING
P53_HUMANENSP00000264281STRING
RBP2_HUMANENSP00000264281STRING
CTBP1_HUMANENSP00000264281STRING
SENP2_HUMANENSP00000264281STRING
DNM3B_HUMANENSP00000264281STRING
CHD3_HUMANENSP00000264281STRING
UBA1_HUMANENSP00000264281STRING
PARK7_HUMANENSP00000264281STRING
TNR6_HUMANENSP00000264281STRING
UBC9_HUMANENSP00000264281STRING
RAGP1_HUMANENSP00000264281STRING
TOPRS_HUMANENSP00000264281STRING
TOP1_HUMANENSP00000264281STRING
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Disease Reference
Kegg disease
H00516 Isolated orofacial clefts, including: Cleft lip with or without cleft palate; Cleft palate
OMIM disease
613705Non-syndromic orofacial cleft 10 (OFC10)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures