SUMO1_RAT - dbPTM
SUMO1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUMO1_RAT
UniProt AC Q5I0H3
Protein Name Small ubiquitin-related modifier 1
Gene Name Sumo1
Organism Rattus norvegicus (Rat).
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..
Protein Sequence MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSDQEAKPS
------CCCCCCCCC
48.26-
2Phosphorylation------MSDQEAKPS
------CCCCCCCCC
48.2630411139
7Acetylation-MSDQEAKPSTEDLG
-CCCCCCCCCCCCCC
38.4522902405
9PhosphorylationSDQEAKPSTEDLGDK
CCCCCCCCCCCCCCC
43.6623298284
10PhosphorylationDQEAKPSTEDLGDKK
CCCCCCCCCCCCCCC
41.8823298284
16AcetylationSTEDLGDKKEGEYIK
CCCCCCCCCCCCEEE
51.4222902405
23AcetylationKKEGEYIKLKVIGQD
CCCCCEEEEEEECCC
41.1622902405
31PhosphorylationLKVIGQDSSEIHFKV
EEEECCCCCEEEEEE
23.2223984901
32PhosphorylationKVIGQDSSEIHFKVK
EEECCCCCEEEEEEE
49.1923984901

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUMO1_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SUMO1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUMO1_RAT

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Related Literatures of Post-Translational Modification

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