UniProtKB - P46060 (RAGP1_HUMAN)
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- BLAST>sp|P46060|RAGP1_HUMAN Ran GTPase-activating protein 1 OS=Homo sapiens OX=9606 GN=RANGAP1 PE=1 SV=1 MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNT VGVEAARVIAKALEKKSELKRCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLS DNAFGPDGVQGFEALLKSSACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPL ALKVFVAGRNRLENDGATALAEAFRVIGTLEEVHMPQNGINHPGITALAQAFAVNPLLRV INLNDNTFTEKGAVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAIRGGLPKLKELNL SFCEIKRDAALAVAEAMADKAELEKLDLNGNTLGEEGCEQLQEVLEGFNMAKVLASLSDD EDEEEEEEGEEEEEEAEEEEEEDEEEEEEEEEEEEEEPQQRGQGEKSATPSRKILDPNTG EPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVSSVF KDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYGPLM ALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV
- Align
Ran GTPase-activating protein 1
RANGAP1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"RanGAP1 induces GTPase activity of nuclear Ras-related Ran."
Bischoff F.R., Klebe C., Kretschmer J., Wittinghofer A., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 91:2587-2591(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.10"Identification of different roles for RanGDP and RanGTP in nuclear protein import."
Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.
EMBO J. 15:5584-5594(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAN, FUNCTION. - Ref.14"Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1."
Takeda E., Hieda M., Katahira J., Yoneda Y.
Cell Struct. Funct. 30:69-80(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RAN AND RANBP1, PHOSPHORYLATION AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, MUTAGENESIS OF ARG-91; SER-356 AND SER-358. - Ref.31"The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes."
Ritterhoff T., Das H., Hofhaus G., Schroeder R.R., Flotho A., Melchior F.
Nat. Commun. 7:11482-11482(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH XPO1; RAN; RANBP2; SUMO1 AND UBE2I, SUMOYLATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 562 | Hydrophobic interaction with UBE2IBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 565 | Hydrophobic interaction with UBE2IBy similarity | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- GTPase activator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Ran GTPase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- RNA binding Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase binding Source: Ensembl
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- activation of GTPase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to vasopressin Source: Ensembl
- negative regulation of protein export from nucleus Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to axon injury Source: Ensembl
- signal transduction Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | GTPase activation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal R-HSA-165054 Rev-mediated nuclear export of HIV RNA R-HSA-2467813 Separation of Sister Chromatids R-HSA-2500257 Resolution of Sister Chromatid Cohesion R-HSA-4615885 SUMOylation of DNA replication proteins R-HSA-5663220 RHO GTPases Activate Formins R-HSA-68877 Mitotic Prometaphase |
SIGNOR Signaling Network Open Resource More...SIGNORi | P46060 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Ran GTPase-activating protein 1Short name: RanGAP1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:RANGAP1 Synonyms:KIAA1835, SD |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000100401.19 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9854 RANGAP1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602362 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P46060 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- nucleoplasm 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"RanGAP1 induces GTPase activity of nuclear Ras-related Ran."
Bischoff F.R., Klebe C., Kretschmer J., Wittinghofer A., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 91:2587-2591(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
- Nucleus envelope 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524. - Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
- nucleoplasm 1 Publication
Cytoskeleton
- spindle 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524. - Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
- spindle 2 Publications
Other locations
- Cytoplasm 1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.7"RanGAP1 induces GTPase activity of nuclear Ras-related Ran."
Bischoff F.R., Klebe C., Kretschmer J., Wittinghofer A., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 91:2587-2591(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
- kinetochore 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524.
Note: Cytoplasmic during interphase. Detected at the nuclear envelope during interphase (PubMed:11854305, PubMed:15037602). Targeted to the nuclear pores after sumoylation (PubMed:11854305). During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles (PubMed:11854305, PubMed:15037602). Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase (PubMed:11854305). Mitotic location also requires sumoylation (PubMed:11854305).2 Publications- Cytoplasm 1 Publication
- Ref.11"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524. - Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytoskeleton
- mitotic spindle Source: Ensembl
Cytosol
- cytosol Source: HPA
Nucleus
- nuclear envelope Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear membrane Source: HPA
- nuclear pore Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- nuclear pore cytoplasmic filaments Source: Ensembl
- nucleoplasm Source: UniProtKB-SubCell
Other locations
- aggresome Source: HPA
- axon cytoplasm Source: Ensembl
- condensed chromosome kinetochore Source: UniProtKB-SubCell
- cytoplasm Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- cytoplasmic periphery of the nuclear pore complex Source: Ensembl
- dendrite Source: Ensembl
- intracellular membrane-bounded organelle Source: HPA
- perinuclear region of cytoplasm Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 91 | R → A: Abolishes RAN GTPase activation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 356 | S → A: No effect on phosphorylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 358 | S → A: Strongly decreased phosphorylation. No effect on sumoylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 524 | K → R: Loss of cross-link to SUMO1. Abolishes association with nuclear pores during interphase, and with mitotic spindles during mitosis. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 5905 |
Open Targets More...OpenTargetsi | ENSG00000100401 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34216 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RANGAP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1172922 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000056737 | 2 – 587 | Ran GTPase-activating protein 1Add BLAST | 586 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 8 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 8 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 15 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 24 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 279 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 301 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 358 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 409 | Phosphothreonine; by CDK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 428 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 435 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 436 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 442 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 452 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 524 | N6-acetyllysine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 524 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 524 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 586 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.31"The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes."
Ritterhoff T., Das H., Hofhaus G., Schroeder R.R., Flotho A., Melchior F.
Nat. Commun. 7:11482-11482(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH XPO1; RAN; RANBP2; SUMO1 AND UBE2I, SUMOYLATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524. - Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I. - Ref.14"Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1."
Takeda E., Hieda M., Katahira J., Yoneda Y.
Cell Struct. Funct. 30:69-80(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RAN AND RANBP1, PHOSPHORYLATION AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, MUTAGENESIS OF ARG-91; SER-356 AND SER-358. - Ref.21"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-8 AND LYS-524, ACETYLATION AT ALA-2. - Ref.29"MYCBP2 is a guanosine exchange factor for Ran protein and determines its localization in neurons of dorsal root ganglia."
Doerr A., Pierre S., Zhang D.D., Henke M., Holland S., Scholich K.
J. Biol. Chem. 290:25620-25635(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MYCBP2, SUMOYLATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P46060 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P46060 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P46060 |
PeptideAtlas More...PeptideAtlasi | P46060 |
PRoteomics IDEntifications database More...PRIDEi | P46060 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55712 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P46060 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P46060 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P46060 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1."
Krebber H., Ponstingl H.
Gene 180:7-11(1996) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100401 |
CleanEx database of gene expression profiles More...CleanExi | HS_RANGAP1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P46060 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P46060 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB004293 HPA050110 HPA062034 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"RanGAP1 induces GTPase activity of nuclear Ras-related Ran."
Bischoff F.R., Klebe C., Kretschmer J., Wittinghofer A., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 91:2587-2591(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.8"Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing."
Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M., Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.
Mol. Cell. Biol. 15:2117-2124(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAN. - Ref.10"Identification of different roles for RanGDP and RanGTP in nuclear protein import."
Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.
EMBO J. 15:5584-5594(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAN, FUNCTION. - Ref.12"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I. - Ref.13"RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the nuclear pore complex and functions in nuclear mRNA export."
Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R., Bork P., Ellenberg J., Izaurralde E.
Mol. Cell. Biol. 24:1155-1167(2004) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH RANBP2; NXF1 AND NXT1. - Ref.14"Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1."
Takeda E., Hieda M., Katahira J., Yoneda Y.
Cell Struct. Funct. 30:69-80(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RAN AND RANBP1, PHOSPHORYLATION AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY, SUMOYLATION, MUTAGENESIS OF ARG-91; SER-356 AND SER-358. - Ref.16"Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification."
Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.
J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TRAF6. - Ref.29"MYCBP2 is a guanosine exchange factor for Ran protein and determines its localization in neurons of dorsal root ganglia."
Doerr A., Pierre S., Zhang D.D., Henke M., Holland S., Scholich K.
J. Biol. Chem. 290:25620-25635(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MYCBP2, SUMOYLATION. - Ref.31"The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes."
Ritterhoff T., Das H., Hofhaus G., Schroeder R.R., Flotho A., Melchior F.
Nat. Commun. 7:11482-11482(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH XPO1; RAN; RANBP2; SUMO1 AND UBE2I, SUMOYLATION. - Ref.33"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
Reverter D., Lima C.D.
Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 418-587 IN COMPLEX WITH SUMO1; RANBP2 AND UBE2I. - Ref.34"SUMO protease SENP1 induces isomerization of the scissile peptide bond."
Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 432-587 IN COMPLEX WITH SUMO1 AND SENP1.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| SUMO1 | P63165 | 13 | EBI-396091,EBI-80140 | |
| UBE2I | P63279 | 9 | EBI-396091,EBI-80168 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- Ran GTPase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ubiquitin protein ligase binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111840, 138 interactors |
Database of interacting proteins More...DIPi | DIP-29079N |
Protein interaction database and analysis system More...IntActi | P46060, 58 interactors |
Molecular INTeraction database More...MINTi | P46060 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000348577 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 434 – 439 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 443 – 448 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 450 – 452 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 453 – 459 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 466 – 477 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 484 – 502 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 503 – 507 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 509 – 519 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 522 – 526 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 536 – 545 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 548 – 551 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 553 – 555 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 556 – 564 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 568 – 571 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 574 – 586 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P46060 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P46060 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P46060 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 48 – 71 | LRR 1Add BLAST | 24 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 111 – 134 | LRR 2Add BLAST | 24 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 207 – 230 | LRR 3Add BLAST | 24 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 235 – 258 | LRR 4Add BLAST | 24 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 292 – 319 | LRR 5Add BLAST | 28 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 320 – 343 | LRR 6Add BLAST | 24 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 523 – 526 | SUMO conjugation | 4 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 359 – 399 | Asp/Glu-rich (highly acidic)Add BLAST | 41 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 359 – 397 | Asp/Glu-rich (highly acidic)Add BLAST | 39 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Leucine-rich repeat, RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1909 Eukaryota COG5238 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00440000039203 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000195026 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG017720 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P46060 |
KEGG Orthology (KO) More...KOi | K14319 |
Identification of Orthologs from Complete Genome Data More...OMAi | DLETVIC |
Database of Orthologous Groups More...OrthoDBi | EOG091G02K4 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P46060 |
TreeFam database of animal gene trees More...TreeFami | TF318283 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.40.200, 1 hit 3.80.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001611 Leu-rich_rpt IPR032675 LRR_dom_sf IPR009109 Ran_GTPase_activating_1_C IPR027038 RanGap IPR036720 RanGAP1_C_sf |
The PANTHER Classification System More...PANTHERi | PTHR24113 PTHR24113, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF13516 LRR_6, 3 hits PF07834 RanGAP1_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF69099 SSF69099, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS
60 70 80 90 100
LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL
110 120 130 140 150
ISLGEGLITA GAQLVELDLS DNAFGPDGVQ GFEALLKSSA CFTLQELKLN
160 170 180 190 200
NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL
210 220 230 240 250
AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV INLNDNTFTE
260 270 280 290 300
KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL
310 320 330 340 350
SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM
360 370 380 390 400
AKVLASLSDD EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ
410 420 430 440 450
RGQGEKSATP SRKILDPNTG EPAPVLSSPP PADVSTFLAF PSPEKLLRLG
460 470 480 490 500
PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF KDEATVRMAV QDAVDALMQK
510 520 530 540 550
AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM ALNHMVQQDY
560 570 580
FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029240 | 133 | E → Q. Corresponds to variant dbSNP:rs2229752Ensembl. | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X82260 mRNA Translation: CAA57714.1 AB058738 mRNA Translation: BAB47464.1 Different initiation. CR456557 mRNA Translation: CAG30443.1 AL035681 Genomic DNA No translation available. BC014044 mRNA Translation: AAH14044.1 BC041396 mRNA Translation: AAH41396.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14012.1 |
Protein sequence database of the Protein Information Resource More...PIRi | JC5300 |
NCBI Reference Sequences More...RefSeqi | NP_001265580.1, NM_001278651.1 NP_001304859.1, NM_001317930.1 NP_002874.1, NM_002883.3 XP_006724352.1, XM_006724289.3 XP_011528596.1, XM_011530294.2 XP_011528597.1, XM_011530295.2 XP_016884382.1, XM_017028893.1 XP_016884383.1, XM_017028894.1 XP_016884384.1, XM_017028895.1 XP_016884385.1, XM_017028896.1 XP_016884386.1, XM_017028897.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.183800 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000356244; ENSP00000348577; ENSG00000100401 ENST00000405486; ENSP00000385866; ENSG00000100401 ENST00000455915; ENSP00000401470; ENSG00000100401 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5905 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5905 |
UCSC genome browser More...UCSCi | uc003azs.5 human |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P46060 | Ran GTPase activating protein 1, isoform CRA_d | 587 | |||
| RANGAP1 isoform 6 (Fragment) | 133 | ||||
| RANGAP1 isoform 6 (Fragment) | 133 | ||||
| UPI000387C60E | 642 | ||||
| UPI0000DBECAF | 156 | ||||
| +7 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P46060 | Ran GTPase activating protein 1, isoform CRA_d | 587 | |||
| RANGAP1 isoform 6 (Fragment) | 133 | ||||
| RANGAP1 isoform 6 (Fragment) | 133 | ||||
| Uncharacterized protein | 642 | ||||
| UPI000C29C51B | 642 | ||||
| +105 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P46060 | Ran GTPase-activating protein 1 | ) | 589 | ||
| UPI000A3188CC | 637 | ||||
| RAN GTPase-activating protein 1 | 586 | ||||
| Ran GTPase-activating protein 1 (Fragment) | 553 | ||||
| UPI00092F9A39 | 600 | ||||
| +422 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X82260 mRNA Translation: CAA57714.1 AB058738 mRNA Translation: BAB47464.1 Different initiation. CR456557 mRNA Translation: CAG30443.1 AL035681 Genomic DNA No translation available. BC014044 mRNA Translation: AAH14044.1 BC041396 mRNA Translation: AAH41396.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14012.1 |
Protein sequence database of the Protein Information Resource More...PIRi | JC5300 |
NCBI Reference Sequences More...RefSeqi | NP_001265580.1, NM_001278651.1 NP_001304859.1, NM_001317930.1 NP_002874.1, NM_002883.3 XP_006724352.1, XM_006724289.3 XP_011528596.1, XM_011530294.2 XP_011528597.1, XM_011530295.2 XP_016884382.1, XM_017028893.1 XP_016884383.1, XM_017028894.1 XP_016884384.1, XM_017028895.1 XP_016884385.1, XM_017028896.1 XP_016884386.1, XM_017028897.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.183800 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1Z5S | X-ray | 3.01 | C | 418-587 | [»] | |
| 2GRN | X-ray | 1.80 | B | 419-587 | [»] | |
| 2GRO | X-ray | 1.70 | B | 419-587 | [»] | |
| 2GRP | X-ray | 2.05 | B | 419-587 | [»] | |
| 2GRQ | X-ray | 1.70 | B | 419-587 | [»] | |
| 2GRR | X-ray | 1.30 | B | 419-587 | [»] | |
| 2IO2 | X-ray | 2.90 | C | 418-587 | [»] | |
| 2IO3 | X-ray | 3.20 | C | 418-587 | [»] | |
| 2IY0 | X-ray | 2.77 | C | 432-587 | [»] | |
| 3UIN | X-ray | 2.60 | C | 419-587 | [»] | |
| 3UIO | X-ray | 2.60 | C | 419-587 | [»] | |
| 3UIP | X-ray | 2.29 | C | 419-587 | [»] | |
| 5D2M | X-ray | 2.40 | C/F | 418-587 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P46060 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P46060 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111840, 138 interactors |
Database of interacting proteins More...DIPi | DIP-29079N |
Protein interaction database and analysis system More...IntActi | P46060, 58 interactors |
Molecular INTeraction database More...MINTi | P46060 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000348577 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P46060 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P46060 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P46060 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RANGAP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1172922 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P46060 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P46060 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P46060 |
PeptideAtlas More...PeptideAtlasi | P46060 |
PRoteomics IDEntifications database More...PRIDEi | P46060 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55712 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5905 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000356244; ENSP00000348577; ENSG00000100401 ENST00000405486; ENSP00000385866; ENSG00000100401 ENST00000455915; ENSP00000401470; ENSG00000100401 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5905 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5905 |
UCSC genome browser More...UCSCi | uc003azs.5 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5905 |
DisGeNET More...DisGeNETi | 5905 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000100401.19 |
GeneCards: human genes, protein and diseases More...GeneCardsi | RANGAP1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9854 RANGAP1 |
Human Protein Atlas More...HPAi | CAB004293 HPA050110 HPA062034 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602362 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P46060 |
Open Targets More...OpenTargetsi | ENSG00000100401 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34216 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1909 Eukaryota COG5238 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00440000039203 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000195026 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG017720 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P46060 |
KEGG Orthology (KO) More...KOi | K14319 |
Identification of Orthologs from Complete Genome Data More...OMAi | DLETVIC |
Database of Orthologous Groups More...OrthoDBi | EOG091G02K4 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P46060 |
TreeFam database of animal gene trees More...TreeFami | TF318283 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal R-HSA-165054 Rev-mediated nuclear export of HIV RNA R-HSA-2467813 Separation of Sister Chromatids R-HSA-2500257 Resolution of Sister Chromatid Cohesion R-HSA-4615885 SUMOylation of DNA replication proteins R-HSA-5663220 RHO GTPases Activate Formins R-HSA-68877 Mitotic Prometaphase |
SIGNOR Signaling Network Open Resource More...SIGNORi | P46060 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | RANGAP1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P46060 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | RANGAP1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5905 |
Protein Ontology More...PROi | PR:P46060 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100401 |
CleanEx database of gene expression profiles More...CleanExi | HS_RANGAP1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P46060 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P46060 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.40.200, 1 hit 3.80.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001611 Leu-rich_rpt IPR032675 LRR_dom_sf IPR009109 Ran_GTPase_activating_1_C IPR027038 RanGap IPR036720 RanGAP1_C_sf |
The PANTHER Classification System More...PANTHERi | PTHR24113 PTHR24113, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF13516 LRR_6, 3 hits PF07834 RanGAP1_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF69099 SSF69099, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | RAGP1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P46060Primary (citable) accession number: P46060 Secondary accession number(s): Q96JJ2 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
| Last sequence update: | November 1, 1995 | |
| Last modified: | July 18, 2018 | |
| This is version 202 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
