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Protein Page:
SUMO1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
SUMO1 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. Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25. Belongs to the ubiquitin family. SUMO subfamily. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Ubiquitin-like modifier
Cellular Component: nucleoplasm; PML body; cytoplasm; dendrite; synapse; nuclear pore; nuclear speck; nucleus
Molecular Function: protein binding; ubiquitin protein ligase binding; transcription factor binding; SUMO ligase activity
Biological Process: cytokine and chemokine mediated signaling pathway; negative regulation of transcription factor activity; PML body organization and biogenesis; palate development; DNA repair; post-translational protein modification; negative regulation of DNA binding; regulation of protein localization; cellular protein metabolic process; protein sumoylation; positive regulation of protein complex assembly; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of transcription, DNA-dependent
Reference #:  P63165 (UniProtKB)
Alt. Names/Synonyms: DAP1; GAP modifying protein 1; GAP-modifying protein 1; GMP1; OFC10; PIC1; SENP2; Sentrin; Small ubiquitin-related modifier 1; SMT3; SMT3 homolog 3; SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae); SMT3C; SMT3H3; SUMO-1; SUMO1; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein SMT3C; Ubiquitin-like protein UBL1; UBL1
Gene Symbols: SUMO1
Molecular weight: 11,557 Da
Basal Isoelectric point: 5.34  Predict pI for various phosphorylation states
CST Pathways:  IL6 Signaling  |  NF-kB Signaling  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SUMO1

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: K39‑s

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 21 S2-p ______MsDQEAkPs
0 2 K7-s _MsDQEAkPstEDLG
0 3 S9-p sDQEAkPstEDLGDk
0 1 T10-p DQEAkPstEDLGDkk
1 0 K16-s stEDLGDkkEGEYIk
1 0 K17-s tEDLGDkkEGEYIkL
0 1 K23-a kkEGEYIkLkVIGQD
0 6 K25-u EGEYIkLkVIGQDSs
0 1 K25-s EGEYIkLkVIGQDSs
0 1 S32-p kVIGQDSsEIHFkVk
0 8 K37-u DSsEIHFkVkMTTHL
1 0 K37-s DSsEIHFkVkMTTHL
2 0 K39-s sEIHFkVkMTTHLKk
1 0 K46-s kMTTHLKkLkESYCQ
0 4 K48-u TTHLKkLkESYCQRQ
0 1 T76 QRIADNHTPkELGME
0 7 K78-u IADNHTPkELGMEEE
  SUMO1 iso2  
S2-p ______MsDQDSSEI
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K12 DSSEIHFKVKMTTHL
K12 DSSEIHFKVKMTTHL
K14 SEIHFKVKMTTHLKK
K21 KMTTHLKKLKESYCQ
K23 TTHLKKLKESYCQRQ
T51 QRIADNHTPKELGME
K53 IADNHTPKELGMEEE
  mouse

 
S2-p ______MsDQEAKPs
K7 _MsDQEAKPsTEDLG
S9-p sDQEAKPsTEDLGDK
T10 DQEAKPsTEDLGDKK
K16 sTEDLGDKKEGEYIK
K17 TEDLGDKKEGEYIKL
K23 KKEGEYIKLKVIGQD
K25 EGEYIKLKVIGQDSS
K25 EGEYIKLKVIGQDSS
S32 KVIGQDSSEIHFkVK
K37-u DSSEIHFkVKMTTHL
K37 DSSEIHFKVKMTTHL
K39 SEIHFkVKMTTHLKK
K46 KMTTHLKKLKESYCQ
K48 TTHLKKLKESYCQRQ
T76-p QRIADNHtPkELGME
K78-u IADNHtPkELGMEEE
  rat

 
S2 ______MSDQEAKPS
K7 _MSDQEAKPSTEDLG
S9 SDQEAKPSTEDLGDK
T10 DQEAKPSTEDLGDKK
K16 STEDLGDKKEGEYIK
K17 TEDLGDKKEGEYIKL
K23 KKEGEYIKLKVIGQD
K25 EGEYIKLKVIGQDSS
K25 EGEYIKLKVIGQDSS
S32 KVIGQDSSEIHFKVK
K37 DSSEIHFKVKMTTHL
K37 DSSEIHFKVKMTTHL
K39 SEIHFKVKMTTHLKK
K46 KMTTHLKKLKESYCQ
K48 TTHLKKLKESYCQRQ
T76 QRIADNHTPKELGME
K78 IADNHTPKELGMEEE
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