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Entry version 185 (08 May 2019)
Sequence version 2 (27 Jul 2011)
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Protein

Ran GTPase-activating protein 1

Gene

Rangap1

Organism
Mus musculus (Mouse)
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. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:18305100). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity). Required for postimplantation embryonic development (PubMed:8314081).By similarity2 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>Sitei564Hydrophobic interaction with UBE2IBy similarity1
Sitei567Hydrophobic 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

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

More...
Reactomei
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

<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:Fug11 Publication
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:103071 Rangap1

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic development is arrested around 6 dpc.1 Publication

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>Mutagenesisi411T → D: Greatly reduced phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-444. 1 Publication1
Mutagenesisi444S → D: Little change in phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-411. 1 Publication1
Mutagenesisi512N → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi516T → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi517R → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi520I → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi521H → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi522M → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi524L → A: No sumoylation. 1 Publication1
Mutagenesisi525L → A: Disrupted binding to UBE2I, and no sumoylation. 1 Publication1
Mutagenesisi526K → A: No UBE2I binding nor sumoylation. 4 Publications1
Mutagenesisi526K → R: Absence of sumoylation. Not targeted to the nuclear envelope rim nor to nuclear pore complexes. Disrupted sumoylation. No interaction with SUMO1; when associated with A-564 and with or without SUMO1 A-97. 4 Publications1
Mutagenesisi528E → A: No UBE2I binding nor sumoylation. 1 Publication1
Mutagenesisi529D → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi531I → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi537L → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi541 – 589Missing : Abolishes accumulation in the nucleus. 1 PublicationAdd BLAST49
Mutagenesisi560L → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi563A → L: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi564F → A: No UBE2I binding nor sumoylation. Not targeted to nuclear pore complexes; when associated with R-526. 2 Publications1
Mutagenesisi567 – 589Missing : No effect on accumulation in the nucleus. 1 PublicationAdd BLAST23
Mutagenesisi567K → A: No UBE2I binding nor sumoylation. 1 Publication1
Mutagenesisi569N → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1

<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 methionineiRemovedBy similarity
<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_00000567382 – 589Ran GTPase-activating protein 1Add BLAST588

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-acetylalanineBy similarity1
<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 SUMO); alternateBy similarity
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei24PhosphoserineBy similarity1
Cross-linki279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei301PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei411Phosphothreonine; by CDK2By similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei437PhosphoserineBy similarity1
Modified residuei438PhosphothreonineBy similarity1
Modified residuei441PhosphoserineCombined sources1
Modified residuei444PhosphoserineCombined sources1 Publication1
Cross-linki454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei526N6-acetyllysine; alternateBy similarity1
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

<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:26506250, PubMed:11853669). Sumoylation is necessary for targeting to the nuclear envelope (NE) (PubMed:16469311). Sumoylation is necessary for association with mitotic spindles and kinetochores during mitosis (By similarity). Also required for interaction with RANBP2 and is mediated by UBE2I (PubMed:9456312, PubMed:11853669).By similarity4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P46061

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P46061

MaxQB - The MaxQuant DataBase

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MaxQBi
P46061

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

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PaxDbi
P46061

PeptideAtlas

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PeptideAtlasi
P46061

PRoteomics IDEntifications database

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PRIDEi
P46061

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P46061

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

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PhosphoSitePlusi
P46061

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P46061

<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

Detected in adult brain, liver, kidney, intestine, uterus and ovary.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Detected in embryos at 7.5 dpc, but not at 6 dpc.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000022391 Expressed in 299 organ(s), highest expression level in neocortex

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P46061 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P46061 MM

<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:7891706). Interacts with RAN (PubMed:7891706). Forms a complex with RANBP2/NUP358, NXF1 and NXT1 (By similarity). Forms a tight complex in association with RANBP2 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2 (PubMed:11853669). Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2 (PubMed:9456312, PubMed:18305100, PubMed:11853669). The complex composed of RANBP2, SUMO1, RANGAP1 and UBE2I associates with nuclear pore complexes (By similarity). Identified in a complex composed of RAN, RANBP2, sumoylated RANGAP1, UBE2I and XPO1 (By similarity). Interacts with TRAF6 (By similarity). Interacts with SUMO1 and SENP1 (By similarity). Interacts (when sumoylated) with MYCBP2; interaction inhibits MYCBP2 E3 ubiquitin-protein ligase activity and promotes MYCBP2 translocation to the nucleus (PubMed:26304119).By similarity1 Publication4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202583, 11 interactors

Database of interacting proteins

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DIPi
DIP-17024N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P46061

Protein interaction database and analysis system

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IntActi
P46061, 7 interactors

Molecular INTeraction database

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MINTi
P46061

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000126849

<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

1589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P46061

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
P46061

<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 – 315LRR 5Add BLAST24
Repeati320 – 343LRR 6Add BLAST24

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni541 – 566Important for accumulation in the nucleus1 PublicationAdd BLAST26

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>Motifi525 – 528SUMO conjugationBy similarity4

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

<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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P46061

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

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
IPR036720 RanGAP1_C_sf

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

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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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 2 potential isoforms that are computationally mapped.Show allAlign All

P46061-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASEDIAKLA ETLAKTQVAG GQLSFKGKGL KLNTAEDAKD VIKEIEEFDG
60 70 80 90 100
LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRSEIPPAL
110 120 130 140 150
ISLGEGLITA GAQLVELDLS DNAFGPDGVR GFEALLKSPA CFTLQELKLN
160 170 180 190 200
NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL
210 220 230 240 250
AEAFGIIGTL EEVHMPQNGI NHPGVTALAQ AFAINPLLRV INLNDNTFTE
260 270 280 290 300
KGGVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAVRG GLPKLKELNL
310 320 330 340 350
SFCEIKRDAA LVVAEAVADK AELEKLDLNG NALGEEGCEQ LQEVMDSFNM
360 370 380 390 400
AKVLASLSDD EGEDEDEEEE GEEDDEEEED EEDEEDDDEE EEEQEEEEEP
410 420 430 440 450
PQRGSGEEPA TPSRKILDPN SGEPAPVLSS PTPTDLSTFL SFPSPEKLLR
460 470 480 490 500
LGPKVSVLIV QQTDTSDPEK VVSAFLKVAS VFRDDASVKT AVLDAIDALM
510 520 530 540 550
KKAFSCSSFN SNTFLTRLLI HMGLLKSEDK IKAIPSLHGP LMVLNHVVRQ
560 570 580
DYFPKALAPL LLAFVTKPNG ALETCSFARH NLLQTLYNI
Length:589
Mass (Da):63,531
Last modified:July 27, 2011 - v2
<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:i775ADE3A53EFD558
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8VHK9A0A2R8VHK9_MOUSE
Ran GTPase-activating protein 1
Rangap1
257Annotation 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>
A0A2R8W753A0A2R8W753_MOUSE
Ran GTPase-activating protein 1
Rangap1
144Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti181A → R in AAA17681 (PubMed:8314081).Curated1
Sequence conflicti413S → L in AAB60517 (PubMed:7891706).Curated1

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
U08110 mRNA Translation: AAA17681.1
U20857 Genomic RNA Translation: AAB60517.1
AK146670 mRNA Translation: BAE27347.1
AK159009 mRNA Translation: BAE34767.1
AK159525 mRNA Translation: BAE35154.1
BC066213 mRNA Translation: AAH66213.1
BC071200 mRNA Translation: AAH71200.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS27670.1

Protein sequence database of the Protein Information Resource

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PIRi
A36983
T52070

NCBI Reference Sequences

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RefSeqi
NP_001139646.1, NM_001146174.1
NP_035371.4, NM_011241.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000052374; ENSMUSP00000057771; ENSMUSG00000022391
ENSMUST00000170134; ENSMUSP00000126849; ENSMUSG00000022391
ENSMUST00000171115; ENSMUSP00000130046; ENSMUSG00000022391

Database of genes from NCBI RefSeq genomes

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GeneIDi
19387

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19387

UCSC genome browser

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UCSCi
uc007wxa.2 mouse

<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
U08110 mRNA Translation: AAA17681.1
U20857 Genomic RNA Translation: AAB60517.1
AK146670 mRNA Translation: BAE27347.1
AK159009 mRNA Translation: BAE34767.1
AK159525 mRNA Translation: BAE35154.1
BC066213 mRNA Translation: AAH66213.1
BC071200 mRNA Translation: AAH71200.1
CCDSiCCDS27670.1
PIRiA36983
T52070
RefSeqiNP_001139646.1, NM_001146174.1
NP_035371.4, NM_011241.4

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
1KPSX-ray2.50B/D420-589[»]
SMRiP46061
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202583, 11 interactors
DIPiDIP-17024N
ELMiP46061
IntActiP46061, 7 interactors
MINTiP46061
STRINGi10090.ENSMUSP00000126849

PTM databases

iPTMnetiP46061
PhosphoSitePlusiP46061
SwissPalmiP46061

Proteomic databases

EPDiP46061
jPOSTiP46061
MaxQBiP46061
PaxDbiP46061
PeptideAtlasiP46061
PRIDEiP46061

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052374; ENSMUSP00000057771; ENSMUSG00000022391
ENSMUST00000170134; ENSMUSP00000126849; ENSMUSG00000022391
ENSMUST00000171115; ENSMUSP00000130046; ENSMUSG00000022391
GeneIDi19387
KEGGimmu:19387
UCSCiuc007wxa.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5905
MGIiMGI:103071 Rangap1

Phylogenomic databases

eggNOGiKOG1909 Eukaryota
COG5238 LUCA
GeneTreeiENSGT00440000039203
InParanoidiP46061
KOiK14319
OMAiWGVDELD
OrthoDBi1357476at2759
TreeFamiTF318283

Enzyme and pathway databases

ReactomeiR-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

Miscellaneous databases

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

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ChiTaRSi
Rangap1 mouse
EvolutionaryTraceiP46061

Protein Ontology

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PROi
PR:P46061

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000022391 Expressed in 299 organ(s), highest expression level in neocortex
ExpressionAtlasiP46061 baseline and differential
GenevisibleiP46061 MM

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
IPR036720 RanGAP1_C_sf
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_MOUSE
<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: P46061
Secondary accession number(s): Q60801, Q6NZB5
<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: July 27, 2011
Last modified: May 8, 2019
This is version 185 of the entry and version 2 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

<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, 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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