| UniProt ID | RCC1_MOUSE | |
|---|---|---|
| UniProt AC | Q8VE37 | |
| Protein Name | Regulator of chromosome condensation | |
| Gene Name | Rcc1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 421 | |
| Subcellular Localization | Nucleus . Chromosome . Cytoplasm . Predominantly nuclear in interphase cells. Binds to mitotic chromosomes. | |
| Protein Description | Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis. Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis. Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA.. | |
| Protein Sequence | MPPKRIAKRRSPPEDAIPKSKKVKVSHRSHNTEPGLVLTLGQGDVGQLGLGESVLERKKPALVPLLQDVVQAEAGGMHTVCLSQSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTEDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDAPVVKVASGNDHLVMLTNDGDLYTLGCGEQGQLGRVPELFANRGGRQGLGRLLVPRCVLLKSRGTRGRVRFQDAFCGAYFTFAISREGHVYGFGLSNYHQLGTPGTGSCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPVVSSVACGASVGYAVSKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMTGKQLENRVVLTVSSGGQHTVLLVKDQAQS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Methylation | ------MPPKRIAKR ------CCHHHHCCC | 43.02 | 20668449 | |
| 11 | Phosphorylation | KRIAKRRSPPEDAIP HHHCCCCCCCHHCCC | 49.17 | 26824392 | |
| 29 | Phosphorylation | KVKVSHRSHNTEPGL CEEEECCCCCCCCCE | 18.70 | 22705319 | |
| 32 | Phosphorylation | VSHRSHNTEPGLVLT EECCCCCCCCCEEEE | 37.83 | 22705319 | |
| 103 | Phosphorylation | EGALGRDTSVEGSEM CCCCCCCCCCCCCCC | 33.05 | 28066266 | |
| 104 | Phosphorylation | GALGRDTSVEGSEMV CCCCCCCCCCCCCCC | 23.59 | 28066266 | |
| 214 | Methylation | VPELFANRGGRQGLG CCHHHCCCCCCCCCH | 45.58 | 30989211 | |
| 403 | Phosphorylation | LENRVVLTVSSGGQH ECCEEEEEEECCCEE | 13.51 | 19854140 | |
| 411 | Phosphorylation | VSSGGQHTVLLVKDQ EECCCEEEEEEEECC | 12.64 | 19854140 |
| 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 RCC1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RCC1_MOUSE !! | ||||||
* 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 RCC1_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Methylation | |
| Reference | PubMed |
| "NRMT is an alpha-N-methyltransferase that methylates RCC1 andretinoblastoma protein."; Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; Nature 466:1125-1128(2010). Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2. | |
| Phosphorylation | |
| Reference | PubMed |
| "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-11, AND MASSSPECTROMETRY. | |