Primary Information |
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BoMiProt ID | Bomi2672 |
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Protein Name | GTP-binding nuclear protein Ran |
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Organism | Bos taurus |
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Uniprot ID | Q3T054 |
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Milk Fraction | Exosome |
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Ref Sequence ID | NP_001029877.1 |
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Aminoacid Length | 216 |
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Molecular Weight | 24423 |
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FASTA Sequence |
Download |
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Gene Name | RAN |
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Gene ID | 540457 |
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Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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Protein Function | Ran is a small GTP-binding protein of the Ras superfamily regulating fundamental cellular processes: nucleo-cytoplasmic transport, nuclear envelope formation and mitotic spindle assembly. |
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Biochemical Properties | As a member of the Ras superfamily, Ran is structurally composed of a fold known as the G-domain (GTP-binding domain), a central six-stranded β-sheet that is surrounded by α-helices. Ras-family members bind to GTP and GDP nucleotides with high picomolar affinity. However, only in the GTP-bound form and the switch I- and switch II-loops adopt a stable conformation. |
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PTMs | N6-Acetylation at Lys, Isopeptide bond formation, Phosphorylation at Thr, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | 33-44,123-144,170-216 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Acetylation at Lys residues interferes with essential aspects of Ran function: nucleotide exchange and hydrolysis, subcellular Ran localization, GTP hydrolysis, and the interaction with import and export receptors.Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding. |
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Bibliography | 1.de Boor S, Knyphausen P, Kuhlmann N, Wroblowski S, Brenig J, Scislowski L, Baldus L, Nolte H, Krüger M, Lammers M. Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation. Proc Natl Acad Sci U S A. 2015 Jul 14;112(28):E3679-88. doi: 10.1073/pnas.1505995112. Epub 2015 Jun 29. PMID: 26124124; PMCID: PMC4507232. |