dbPTM

SUMO1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUMO1_MOUSE
UniProt AC	P63166
Protein Name	Small ubiquitin-related modifier 1
Gene Name	Sumo1
Organism	Mus musculus (Mouse).
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. 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 (By similarity)..
Protein Sequence	MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDQEAKPS ------CCCCCCCCC	48.26	-
2	Phosphorylation	------MSDQEAKPS ------CCCCCCCCC	48.26	26824392
7	Sumoylation	-MSDQEAKPSTEDLG -CCCCCCCCCCCCCC	38.45	28289178
9	Phosphorylation	SDQEAKPSTEDLGDK CCCCCCCCCCCCCCC	43.66	25168779
10	Phosphorylation	DQEAKPSTEDLGDKK CCCCCCCCCCCCCCC	41.88	25168779
21	Phosphorylation	GDKKEGEYIKLKVIG CCCCCCCEEEEEEEC	17.76	25367039
31	Phosphorylation	LKVIGQDSSEIHFKV EEEECCCCCEEEEEE	23.22	26824392
32	Phosphorylation	KVIGQDSSEIHFKVK EEECCCCCEEEEEEE	49.19	27841257
37	Ubiquitination	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	22790023
37	Sumoylation	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	28289178
37	Acetylation	DSSEIHFKVKMTTHL CCCEEEEEEEEHHHH	27.12	23236377
39	Sumoylation	SEIHFKVKMTTHLKK CEEEEEEEEHHHHHH	30.99	28289178
45	Sumoylation	VKMTTHLKKLKESYC EEEHHHHHHHHHHHH	48.75	28289178
76	Phosphorylation	QRIADNHTPKELGME CCCCCCCCCHHHCCC	42.16	18779572
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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SUMO1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRF1_MOUSE	Irf1	physical	18955028
PIAS3_MOUSE	Pias3	physical	12387893
VHL_MOUSE	Vhl	physical	17981124

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SUMO1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	19367708 [Abstract]