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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MSDQEAKPS ------CCCCCCCCC | 48.26 | - | |
2 | Phosphorylation | ------MSDQEAKPS ------CCCCCCCCC | 48.26 | 30411139 | |
7 | Acetylation | -MSDQEAKPSTEDLG -CCCCCCCCCCCCCC | 38.45 | 22902405 | |
9 | Phosphorylation | SDQEAKPSTEDLGDK CCCCCCCCCCCCCCC | 43.66 | 23298284 | |
10 | Phosphorylation | DQEAKPSTEDLGDKK CCCCCCCCCCCCCCC | 41.88 | 23298284 | |
16 | Acetylation | STEDLGDKKEGEYIK CCCCCCCCCCCCEEE | 51.42 | 22902405 | |
23 | Acetylation | KKEGEYIKLKVIGQD CCCCCEEEEEEECCC | 41.16 | 22902405 | |
31 | Phosphorylation | LKVIGQDSSEIHFKV EEEECCCCCEEEEEE | 23.22 | 23984901 | |
32 | Phosphorylation | KVIGQDSSEIHFKVK EEECCCCCEEEEEEE | 49.19 | 23984901 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SUMO1_RAT !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SUMO1_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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