UniProt ID | RAGP2_ARATH | |
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UniProt AC | Q9M651 | |
Protein Name | RAN GTPase-activating protein 2 | |
Gene Name | RANGAP2 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 545 | |
Subcellular Localization |
Cytoplasm. Nucleus membrane Peripheral membrane protein Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Localized in patchy areas at the nuclear envelope of interphase cells. During mitosis, associates wit |
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Protein Description | GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.. | |
Protein Sequence | MADILDSRPHAFSIKLWPPSLPTRKALIERITNNFSSKTIFTEKYGSLTKDQATENAKRIEDIAFSTANQQFEREPDGDGGSAVQLYAKECSKLILEVLKKGPVAKVAARELISEDSVSPRETFFDISKGKRAFIEAEEAEELLKPLKEPGNAYTKICFSNRSFGLGAARVAEPILASLKDQLKEVDLSDFVAGRPELEALEVMNIFSDALQGSILSSLNLSDNALGEKGVRAFGALLKSLSSLEELYLMNDGISKEAAQAVSELIPSTENLRVLHFHNNMTGDEGALAIAEVVKRSPLLENFRCSSTRVGSKGGIALSEALEHCTHMEKLDLRDNMFGTEAGVSLSKTLSSFKHMTELYLSYLNLEDEGAIAIVNALKESASPIEVLEMAGNDITVEAASAIAACVAAKQDLNKLNLSENELKDEGCVQIANCIEEGHSKLQYIDMSTNYIRRAGARALAHVVVKKEAFKLLNIDGNIISEEGIEELKEIFKKSPELLGALDENDPDGEEDDDDEEDEEDEENEGNGNGELESKLKNLEVNQED | |
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 |
---|---|---|---|---|---|
114 | Phosphorylation | VAARELISEDSVSPR HHHHHHHCCCCCCCC | 48.23 | 23776212 | |
117 | Phosphorylation | RELISEDSVSPRETF HHHHCCCCCCCCHHE | 22.05 | 23776212 | |
119 | Phosphorylation | LISEDSVSPRETFFD HHCCCCCCCCHHEEE | 23.38 | 23776212 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of RAGP2_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of RAGP2_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of RAGP2_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Oops, there are no PPI records of RAGP2_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, SUBCELLULARLOCATION, AND MASS SPECTROMETRY. |