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Entry version 207 (13 Feb 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Ran GTPase-activating protein 1

Gene

RANGAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

GTPase activator for RAN (PubMed:8146159, PubMed:8896452, PubMed:16428860). Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:8896452, PubMed:27160050). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (PubMed:27160050).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei562Hydrophobic interaction with UBE2IBy similarity1
Sitei565Hydrophobic interaction with UBE2IBy similarity1

<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-UCL
  • GTPase activator activity Source: UniProtKB
  • Ran GTPase binding Source: UniProtKB
  • RNA binding Source: FlyBase
  • ubiquitin protein ligase binding Source: Ensembl

GO - Biological processi

<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 functionGTPase activation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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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

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SIGNORi
P46060

Protein family/group databases

Transport Classification Database

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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 1
Short 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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000100401.19

Human Gene Nomenclature Database

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HGNCi
HGNC:9854 RANGAP1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602362 gene

neXtProt; the human protein knowledge platform

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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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi91R → A: Abolishes RAN GTPase activation. 1 Publication1
Mutagenesisi356S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi358S → A: Strongly decreased phosphorylation. No effect on sumoylation. 1 Publication1
Mutagenesisi524K → R: Loss of cross-link to SUMO1. Abolishes association with nuclear pores during interphase, and with mitotic spindles during mitosis. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5905

Open Targets

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OpenTargetsi
ENSG00000100401

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34216

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RANGAP1

Domain mapping of disease mutations (DMDM)

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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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 methionineiRemoved1 Publication
<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_00000567372 – 587Ran GTPase-activating protein 1Add BLAST586

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylalanine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, 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-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei24PhosphoserineCombined sources1
Cross-linki279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei301PhosphoserineCombined sources1
Modified residuei358PhosphoserineCombined sources1 Publication1
Modified residuei409Phosphothreonine; by CDK21 Publication1
Modified residuei428PhosphoserineCombined sources1 Publication1
Modified residuei435PhosphoserineCombined sources1
Modified residuei436PhosphothreonineCombined sources1
Modified residuei442PhosphoserineCombined sources1 Publication1
Cross-linki452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei524N6-acetyllysine; alternateCombined sources1
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources1 Publication
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki586Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<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

Phosphorylation occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBE2I, on nuclear pore complex (NPC) diassembly and during mitosis.1 Publication
Sumoylated (PubMed:11854305, PubMed:15037602, PubMed:26304119, PubMed:27160050). Sumoylation is necessary for targeting to the nuclear envelope (NE), and for association with mitotic spindles and kinetochores during mitosis (PubMed:11854305). Also required for interaction with RANBP2 and is mediated by UBE2I (PubMed:27160050).1 Publication5 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P46060

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P46060

MaxQB - The MaxQuant DataBase

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MaxQBi
P46060

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P46060

PeptideAtlas

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PeptideAtlasi
P46060

PRoteomics IDEntifications database

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PRIDEi
P46060

ProteomicsDB human proteome resource

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ProteomicsDBi
55712

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P46060

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P46060

SwissPalm database of S-palmitoylation events

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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

Highly expressed in brain, thymus and testis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000100401 Expressed in 220 organ(s), highest expression level in right testis

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P46060 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P46060 HS

Organism-specific databases

Human Protein Atlas

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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

Homodimer (PubMed:8146159). Interacts with RAN (PubMed:7891706, PubMed:8896452, PubMed:16428860). Forms a complex with RANBP2/NUP358, NXF1 and NXT1 (PubMed:14729961). Forms a tight complex in association with RANBP2/NUP358 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2 (PubMed:15037602, PubMed:27160050, PubMed:15931224, PubMed:22194619). Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2/NUP358 (PubMed:15037602, PubMed:27160050, PubMed:15931224). The complex composed of RANBP2, SUMO1, RANGAP1 and UBE2I associates with nuclear pore complexes (PubMed:15037602, PubMed:15931224). Identified in a complex composed of RAN, RANBP2, sumoylated RANGAP1, UBE2I and XPO1 (PubMed:27160050). Identified in a complex composed of RAN, RANGAP1 and RANBP1 (PubMed:16428860). Interacts with TRAF6 (PubMed:18093978). Interacts with SUMO1 and SENP1 (PubMed:17099698). Interacts (when sumoylated) with MYCBP2; interaction inhibits MYCBP2 E3 ubiquitin-protein ligase activity and promotes MYCBP2 translocation to the nucleus (PubMed:26304119).11 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111840, 149 interactors

Database of interacting proteins

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DIPi
DIP-29079N

Protein interaction database and analysis system

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IntActi
P46060, 59 interactors

Molecular INTeraction database

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MINTi
P46060

STRING: functional protein association networks

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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

1587
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z5SX-ray3.01C418-587[»]
2GRNX-ray1.80B419-587[»]
2GROX-ray1.70B419-587[»]
2GRPX-ray2.05B419-587[»]
2GRQX-ray1.70B419-587[»]
2GRRX-ray1.30B419-587[»]
2IO2X-ray2.90C418-587[»]
2IO3X-ray3.20C418-587[»]
2IY0X-ray2.77C432-587[»]
3UINX-ray2.60C419-587[»]
3UIOX-ray2.60C419-587[»]
3UIPX-ray2.29C419-587[»]
5D2MX-ray2.40C/F418-587[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P46060

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P46060

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Repeati48 – 71LRR 1Add BLAST24
Repeati111 – 134LRR 2Add BLAST24
Repeati207 – 230LRR 3Add BLAST24
Repeati235 – 258LRR 4Add BLAST24
Repeati292 – 319LRR 5Add BLAST28
Repeati320 – 343LRR 6Add BLAST24

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Motifi523 – 526SUMO conjugation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 biasi359 – 399Asp/Glu-rich (highly acidic)Add BLAST41
Compositional biasi359 – 397Asp/Glu-rich (highly acidic)Add BLAST39

<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

Belongs to the RNA1 family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1909 Eukaryota
COG5238 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00440000039203

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000195026

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG017720

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P46060

KEGG Orthology (KO)

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KOi
K14319

Identification of Orthologs from Complete Genome Data

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OMAi
WGVDELD

Database of Orthologous Groups

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OrthoDBi
1357476at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P46060

TreeFam database of animal gene trees

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TreeFami
TF318283

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.200, 1 hit
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR24113 PTHR24113, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF13516 LRR_6, 3 hits
PF07834 RanGAP1_C, 1 hit

Superfamily database of structural and functional annotation

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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>Sequence (1+)i

<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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P46060-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:587
Mass (Da):63,542
Last modified:November 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3C18068AAC06B98F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y4Q3H0Y4Q3_HUMAN
Ran GTPase-activating protein 1
RANGAP1
253Annotation score:

Annotation score:2 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>
B0QYT4B0QYT4_HUMAN
Ran GTPase-activating protein 1
RANGAP1
133Annotation score:

Annotation score:2 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>
B0QYT5B0QYT5_HUMAN
Ran GTPase-activating protein 1
RANGAP1
100Annotation score:

Annotation score:2 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>
B0QYT6B0QYT6_HUMAN
Ran GTPase-activating protein 1
RANGAP1
37Annotation score:

Annotation score:1 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>

<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

The sequence BAB47464 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_029240133E → Q. Corresponds to variant dbSNP:rs2229752Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links 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

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CCDSi
CCDS14012.1

Protein sequence database of the Protein Information Resource

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PIRi
JC5300

NCBI Reference Sequences

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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

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UniGenei
Hs.183800

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000356244; ENSP00000348577; ENSG00000100401
ENST00000405486; ENSP00000385866; ENSG00000100401
ENST00000455915; ENSP00000401470; ENSG00000100401

Database of genes from NCBI RefSeq genomes

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GeneIDi
5905

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5905

UCSC genome browser

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UCSCi
uc003azs.5 human

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

<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:
EMBLi
GenBanki
DDBJi
Links 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
CCDSiCCDS14012.1
PIRiJC5300
RefSeqiNP_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
UniGeneiHs.183800

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z5SX-ray3.01C418-587[»]
2GRNX-ray1.80B419-587[»]
2GROX-ray1.70B419-587[»]
2GRPX-ray2.05B419-587[»]
2GRQX-ray1.70B419-587[»]
2GRRX-ray1.30B419-587[»]
2IO2X-ray2.90C418-587[»]
2IO3X-ray3.20C418-587[»]
2IY0X-ray2.77C432-587[»]
3UINX-ray2.60C419-587[»]
3UIOX-ray2.60C419-587[»]
3UIPX-ray2.29C419-587[»]
5D2MX-ray2.40C/F418-587[»]
ProteinModelPortaliP46060
SMRiP46060
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111840, 149 interactors
DIPiDIP-29079N
IntActiP46060, 59 interactors
MINTiP46060
STRINGi9606.ENSP00000348577

Protein family/group databases

TCDBi1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family

PTM databases

iPTMnetiP46060
PhosphoSitePlusiP46060
SwissPalmiP46060

Polymorphism and mutation databases

BioMutaiRANGAP1
DMDMi1172922

Proteomic databases

EPDiP46060
jPOSTiP46060
MaxQBiP46060
PaxDbiP46060
PeptideAtlasiP46060
PRIDEiP46060
ProteomicsDBi55712

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5905
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356244; ENSP00000348577; ENSG00000100401
ENST00000405486; ENSP00000385866; ENSG00000100401
ENST00000455915; ENSP00000401470; ENSG00000100401
GeneIDi5905
KEGGihsa:5905
UCSCiuc003azs.5 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5905
DisGeNETi5905
EuPathDBiHostDB:ENSG00000100401.19

GeneCards: human genes, protein and diseases

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GeneCardsi
RANGAP1
HGNCiHGNC:9854 RANGAP1
HPAiCAB004293
HPA050110
HPA062034
MIMi602362 gene
neXtProtiNX_P46060
OpenTargetsiENSG00000100401
PharmGKBiPA34216

Human Unidentified Gene-Encoded large proteins database

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HUGEi
Search...

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1909 Eukaryota
COG5238 LUCA
GeneTreeiENSGT00440000039203
HOGENOMiHOG000195026
HOVERGENiHBG017720
InParanoidiP46060
KOiK14319
OMAiWGVDELD
OrthoDBi1357476at2759
PhylomeDBiP46060
TreeFamiTF318283

Enzyme and pathway databases

ReactomeiR-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
SIGNORiP46060

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
RANGAP1 human
EvolutionaryTraceiP46060

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
RANGAP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5905

Protein Ontology

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PROi
PR:P46060

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100401 Expressed in 220 organ(s), highest expression level in right testis
ExpressionAtlasiP46060 baseline and differential
GenevisibleiP46060 HS

Family and domain databases

Gene3Di1.25.40.200, 1 hit
3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR001611 Leu-rich_rpt
IPR032675 LRR_dom_sf
IPR009109 Ran_GTPase_activating_1_C
IPR027038 RanGap
IPR036720 RanGAP1_C_sf
PANTHERiPTHR24113 PTHR24113, 1 hit
PfamiView protein in Pfam
PF13516 LRR_6, 3 hits
PF07834 RanGAP1_C, 1 hit
SUPFAMiSSF69099 SSF69099, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiRAGP1_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 13, 2019
This is version 207 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
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