UniProtKB - P62491 (RB11A_HUMAN)
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- BLAST>sp|P62491|RB11A_HUMAN Ras-related protein Rab-11A OS=Homo sapiens OX=9606 GN=RAB11A PE=1 SV=3 MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTI KAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIM LVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQ MSDRRENDMSPSNNVVPIHVPPTTENKPKVQCCQNI
- Align
Ras-related protein Rab-11A
RAB11A
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.21"The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25. - Ref.22"Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin."
Lock J.G., Stow J.L.
Mol. Biol. Cell 16:1744-1755(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF SER-25 AND GLN-70. - Ref.24"Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MYO5B, IDENTIFICATION IN A COMPLEX WITH MYO5B AND CFTR. - Ref.27"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NPC1L1, MUTAGENESIS OF SER-25. - Ref.28"A molecular network for de novo generation of the apical surface and lumen."
Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.32"Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MYO5B.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 18 – 26 | GTP3 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
| 9 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 66 – 70 | GTP3 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
| 5 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 124 – 127 | GTP3 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
| 4 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 154 – 156 | GTP3 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
| 3 |
<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
- 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
- GTP binding Source: UniProtKB-KW
- microtubule binding 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
- myosin V 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
- syntaxin binding Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
<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
- astral microtubule organization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- ciliary basal body-plasma membrane docking Source: Reactome
- establishment of protein localization to membrane Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- establishment of protein localization to organelle Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- establishment of vesicle localization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- exosomal secretion Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- melanosome transport Source: UniProtKB
- mitotic metaphase plate congression Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- mitotic spindle assembly Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- multivesicular body assembly Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- neuron projection development Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- neurotransmitter receptor transport, endosome to postsynaptic membrane Source: Ensembl
- plasma membrane to endosome transport Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- positive regulation of axon extension Source: Ensembl
- positive regulation of epithelial cell migration Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of G2/M transition of mitotic cell cycle Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein localization to plasma membrane Source: Ensembl
- post-translational protein modification Source: Reactome
- protein localization to plasma membrane 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
- regulation of cytokinesis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of long-term neuronal synaptic plasticity Source: Ensembl
- regulation of multivesicular body size Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of protein transport Source: Ensembl
- regulation of vesicle-mediated transport Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- renal water homeostasis Source: Reactome
- vesicle-mediated transport 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
<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
| Biological process | Cell cycle, Protein transport, Transport |
| Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1445148 Translocation of GLUT4 to the plasma membrane R-HSA-432040 Vasopressin regulates renal water homeostasis via Aquaporins R-HSA-5620912 Anchoring of the basal body to the plasma membrane R-HSA-5620916 VxPx cargo-targeting to cilium R-HSA-8854214 TBC/RABGAPs R-HSA-8873719 RAB geranylgeranylation |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P62491 |
<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: Ras-related protein Rab-11AShort name: Rab-11 Alternative name(s): YL8 |
| <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:RAB11A Synonyms:RAB11 |
| <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:ENSG00000103769.9 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9760 RAB11A |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605570 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P62491 |
<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
Plasma membrane
- Cell membrane 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.18"The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane."
Lindsay A.J., McCaffrey M.W.
J. Cell Sci. 117:4365-4375(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
<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.36"Large-scale top down proteomics of the human proteome: membrane proteins, mitochondria, and senescence."
Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T., Tran J.C., Thomas P.M., Kelleher N.L.
Mol. Cell. Proteomics 12:3465-3473(2013) [PubMed] [Europe PMC] [Abstract]Cited for: ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
- Cell membrane 1 Publication
Endosome
- Recycling endosome membrane 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.15"Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain."
Lindsay A.J., McCaffrey M.W.
J. Biol. Chem. 277:27193-27199(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.19"The RCP-Rab11 complex regulates endocytic protein sorting."
Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H., Prekeris R.
Mol. Biol. Cell 15:3530-3541(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP1, SUBCELLULAR LOCATION.
<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.36"Large-scale top down proteomics of the human proteome: membrane proteins, mitochondria, and senescence."
Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T., Tran J.C., Thomas P.M., Kelleher N.L.
Mol. Cell. Proteomics 12:3465-3473(2013) [PubMed] [Europe PMC] [Abstract]Cited for: ISOPRENYLATION AT CYS-212 AND CYS-213, IDENTIFICATION BY MASS SPECTROMETRY.
- Recycling endosome membrane 2 Publications
Other locations
- Cleavage furrow 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.21"The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25.
- phagosome 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.33"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
Seto S., Tsujimura K., Koide Y.
Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane (PubMed:11994279). Localizes to the cleavage furrow (PubMed:15601896). Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis (PubMed:20890297). Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211).4 Publications- Cleavage furrow 1 Publication
- Ref.15"Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain."
Lindsay A.J., McCaffrey M.W.
J. Biol. Chem. 277:27193-27199(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.21"The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25. - Ref.28"A molecular network for de novo generation of the apical surface and lumen."
Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.33"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
Seto S., Tsujimura K., Koide Y.
Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]Cited for: 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
Cytoskeleton
- microtubule organizing center Source: HPA
- spindle pole 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
Cytosol
- cytosol Source: Reactome
Endosome
- multivesicular body 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
- postsynaptic recycling endosome Source: Ensembl
- recycling endosome 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
- recycling endosome membrane Source: Reactome
Extracellular region or secreted
- extracellular exosome 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
Golgi apparatus
- Golgi apparatus Source: UniProtKBInferred from high throughput direct assayi
- trans-Golgi network Source: MGI <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
Plasma Membrane
- cleavage furrow 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
Other locations
- axon Source: Ensembl
- cytoplasmic vesicle 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
- cytoplasmic vesicle membrane Source: Reactome
- intracellular membrane-bounded organelle Source: HPA
- perinuclear region of cytoplasm Source: Ensembl
- phagocytic vesicle 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
- protein-containing complex 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
- transport vesicle Source: Ensembl
- vesicle 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
<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
Cell membrane, Cytoplasmic vesicle, Endosome, Membrane<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 | 25 | S → N: Dominant-negative mutant. Induces increased number of binucleated cells, indicating defects in cytokinesis. Inhibits the transport of NPC1L1 to the plama membrane. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. 3 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
| 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 | 70 | Q → L: Constitutively active mutant. Decreases GTPase activity. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. 5 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
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 8766 |
MalaCards human disease database More...MalaCardsi | RAB11A |
Open Targets More...OpenTargetsi | ENSG00000103769 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34101 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB01864 5'-Guanosine-Diphosphate-Monothiophosphate DB04315 Guanosine-5'-Diphosphate |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RAB11A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 50402542 |
<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_0000121151 | 2 – 213 | Ras-related protein Rab-11AAdd BLAST | 212 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000370807 | 214 – 216 | Removed in mature formSequence analysis | 3 |
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-acetylglycine1 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 specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 212 | S-geranylgeranyl cysteine1 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 | 213 | Cysteine methyl esterSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 213 | S-geranylgeranyl cysteine1 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>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, Lipoprotein, Methylation, PrenylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P62491 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P62491 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P62491 |
PeptideAtlas More...PeptideAtlasi | P62491 |
PRoteomics IDEntifications database More...PRIDEi | P62491 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57402 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P62491-1 [P62491-1] |
2D gel databases
USC-OGP 2-DE database More...OGPi | P62491 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P62491 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P62491 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P62491 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000103769 |
CleanEx database of gene expression profiles More...CleanExi | HS_RAB11A |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P62491 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P62491 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB013097 HPA051697 HPA060686 |
<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.12"Identification and characterization of a family of Rab11-interacting proteins."
Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.
J. Biol. Chem. 276:39067-39075(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4. - Ref.13"Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells."
Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
Biochem. Biophys. Res. Commun. 299:770-779(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP4. - Ref.14"Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein."
Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B., Bucci C., McCaffrey M.W.
J. Biol. Chem. 277:12190-12199(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP4. - Ref.16"Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
Lindsay A.J., McCaffrey M.W.
FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP1. - Ref.17"Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins."
Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H., Prekeris R.
J. Biol. Chem. 279:33430-33437(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP2. - Ref.19"The RCP-Rab11 complex regulates endocytic protein sorting."
Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H., Prekeris R.
Mol. Biol. Cell 15:3530-3541(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP1, SUBCELLULAR LOCATION. - Ref.20"Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis."
Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.
EMBO J. 24:3389-3399(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP3 AND RAB11FIP4. - Ref.21"The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis."
Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.
Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF SER-25. - Ref.23"Protrudin induces neurite formation by directional membrane trafficking."
Shirane M., Nakayama K.I.
Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZFYVE27. - Ref.24"Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MYO5B, IDENTIFICATION IN A COMPLEX WITH MYO5B AND CFTR. - Ref.25"Identification of Rab11 as a small GTPase binding protein for the Evi5 oncogene."
Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R., Scheller R.H., Jackson P.K., Eldridge A.G.
Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB11FIP3 AND EVI5. - Ref.26"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
Pohl C., Jentsch S.
Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BIRC6/BRUCE. - Ref.27"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NPC1L1, MUTAGENESIS OF SER-25. - Ref.29"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization."
Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z. , Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.
Nat. Genet. 42:303-312(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VIPAS39. - Ref.31"Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation."
Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.
Mol. Biol. Cell 22:4602-4620(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZFYVE27 AND KIF5A. - Ref.32"Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MYO5B. - Ref.34"TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."
Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.
J. Cell Biol. 197:659-675(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TBC1D14. - Ref.35"UNC119a bridges the transmission of Fyn signals to Rab11, leading to the completion of cytokinesis."
Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.
Cell Cycle 12:1303-1315(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH UNC119. - Ref.37"REI-1 is a guanine nucleotide exchange factor regulating RAB-11 localization and function in C. elegans embryos."
Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T., Nakai J., Hara T., Sato K., Sato K.
Dev. Cell 35:211-221(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SH3BP5. - Ref.39"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP ANALOG. - Ref.40"Crystallographic evidence for substrate-assisted GTP hydrolysis by a small GTP binding protein."
Pasqualato S., Cherfils J.
Structure 13:533-540(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP ANALOG AND GDP, MUTAGENESIS OF GLN-70. - Ref.41"Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes."
Eathiraj S., Mishra A., Prekeris R., Lambright D.G.
J. Mol. Biol. 364:121-135(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 6-175 IN COMPLEX WITH GTP AND RAB11FIP3, MUTAGENESIS OF GLN-70. - Ref.42"Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1."
Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.
Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 7-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, MUTAGENESIS OF GLN-70. - Ref.43"Crystal structure of rab11 in complex with rab11 family interacting protein 2."
Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.
Structure 14:1273-1283(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP, INTERACTION WITH RAB11FIP2, MUTAGENESIS OF GLN-70.
<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 |
|---|---|---|---|---|
| CHMP1B | Q7LBR1 | 3 | EBI-745098,EBI-2118090 | |
| EVI5 | O60447 | 6 | EBI-745098,EBI-852291 | |
| PI4KB | Q9UBF8-2 | 5 | EBI-745098,EBI-16107849 | |
| RAB11FIP1 | Q6WKZ4 | 5 | EBI-745098,EBI-1043591 | |
| RAB11FIP2 | Q7L804 | 8 | EBI-745098,EBI-1049676 | |
| RAB11FIP3 | O75154-1 | 16 | EBI-745098,EBI-15605207 | |
| RAB11FIP4 | Q86YS3-1 | 2 | EBI-745098,EBI-15605259 | |
| RAB11FIP5 | Q9BXF6 | 3 | EBI-745098,EBI-1387068 | |
| RAB3IP | Q96QF0-2 | 8 | EBI-745098,EBI-747865 | |
| YAP1 | P46937 | 2 | EBI-745098,EBI-1044059 | |
| ZFYVE27 | Q5T4F4 | 4 | EBI-745098,EBI-3892947 |
<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
- microtubule binding 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
- myosin V 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
- syntaxin binding Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114299, 94 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P62491 |
Database of interacting proteins More...DIPi | DIP-29138N |
Protein interaction database and analysis system More...IntActi | P62491, 143 interactors |
Molecular INTeraction database More...MINTi | P62491 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000261890 |
<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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 9 – 18 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 24 – 33 | 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 | 45 – 55 | 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 | 58 – 67 | 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 | 72 – 74 | 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 | 78 – 81 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 86 – 92 | 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 | 96 – 100 | 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 | 102 – 112 | 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 | 118 – 124 | 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 | 126 – 131 | 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 | 136 – 145 | 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 | 149 – 152 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 155 – 157 | 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 | 161 – 172 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P62491 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P62491 |
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 | P62491 |
<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
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 | 40 – 48 | Effector regionBy similarity | 9 |
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0087 Eukaryota COG1100 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118841 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233968 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG009351 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P62491 |
KEGG Orthology (KO) More...KOi | K07904 |
Identification of Orthologs from Complete Genome Data More...OMAi | DISKHAT |
Database of Orthologous Groups More...OrthoDBi | EOG091G0O1R |
Database for complete collections of gene phylogenies More...PhylomeDBi | P62491 |
TreeFam database of animal gene trees More...TreeFami | TF300099 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027417 P-loop_NTPase IPR005225 Small_GTP-bd_dom IPR001806 Small_GTPase |
Pfam protein domain database More...Pfami | View protein in Pfam PF00071 Ras, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00231 small_GTP, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51419 RAB, 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>Sequences (2)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT
60 70 80 90 100
RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE
110 120 130 140 150
NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF
160 170 180 190 200
IETSALDSTN VEAAFQTILT EIYRIVSQKQ MSDRRENDMS PSNNVVPIHV
210
PPTTENKPKV QCCQNI
The sequence of this isoform differs from the canonical sequence as follows:
147-216: GLSFIETSAL...KPKVQCCQNI → EANVRQTRK
10 20 30 40 50
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT
60 70 80 90 100
RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE
110 120 130 140 150
NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNEANV
RQTRK
Alternative sequence
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 | X53143 mRNA Translation: CAA37300.1 X56740 mRNA Translation: CAA40064.1 AF000231 mRNA Translation: AAC32887.1 AF498946 mRNA Translation: AAM21094.1 CR407669 mRNA Translation: CAG28597.1 CR536493 mRNA Translation: CAG38732.1 BT020151 mRNA Translation: AAV38953.1 BT020154 mRNA Translation: AAV38956.1 AK300008 mRNA Translation: BAG61825.1 AK311770 mRNA Translation: BAG34713.1 AC011939 Genomic DNA No translation available. AC084854 Genomic DNA No translation available. CH471082 Genomic DNA Translation: EAW77752.1 BC013348 mRNA Translation: AAH13348.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS10212.1 [P62491-1] CCDS58373.1 [P62491-2] |
Protein sequence database of the Protein Information Resource More...PIRi | S47169 |
NCBI Reference Sequences More...RefSeqi | NP_001193765.1, NM_001206836.1 [P62491-2] NP_004654.1, NM_004663.4 [P62491-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.321541 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000261890; ENSP00000261890; ENSG00000103769 [P62491-1] ENST00000569896; ENSP00000456420; ENSG00000103769 [P62491-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 8766 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:8766 |
UCSC genome browser More...UCSCi | uc002apk.4 human [P62491-1] |
<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
Alternative splicing<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 | |
|---|---|---|---|---|---|
| P62491 | Ras-related protein Rab-11A | 216 | |||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| +40 | |||||
| P62491-2 | Ras-related protein Rab-11A | 153 | |||
| RAB11A isoform 2 | 155 | ||||
| RAB11A isoform 2 | 155 | ||||
| RAB11A, member RAS oncogene family | 155 | ||||
| RAB11A, member RAS oncogene family | 155 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P62491 | Ras-related protein Rab-11A | 216 | |||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| +41 | |||||
| P62491-2 | Ras-related protein Rab-11A | 153 | |||
| RAB11A isoform 2 | 155 | ||||
| RAB11A isoform 2 | 155 | ||||
| RAB11A, member RAS oncogene family | 155 | ||||
| RAB11A, member RAS oncogene family | 155 | ||||
| +8 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P62491 | Ras-related protein Rab-11A | 216 | |||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| Ras-related protein Rab-11A | 216 | ||||
| +178 | |||||
| P62491-2 | Ras-related protein Rab-11A | 153 | |||
| RAB11A isoform 2 | 155 | ||||
| RAB11A isoform 2 | 155 | ||||
| RAB11A, member RAS oncogene family | 155 | ||||
| RAB11A, member RAS oncogene family | 155 | ||||
| +13 | |||||
<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 | X53143 mRNA Translation: CAA37300.1 X56740 mRNA Translation: CAA40064.1 AF000231 mRNA Translation: AAC32887.1 AF498946 mRNA Translation: AAM21094.1 CR407669 mRNA Translation: CAG28597.1 CR536493 mRNA Translation: CAG38732.1 BT020151 mRNA Translation: AAV38953.1 BT020154 mRNA Translation: AAV38956.1 AK300008 mRNA Translation: BAG61825.1 AK311770 mRNA Translation: BAG34713.1 AC011939 Genomic DNA No translation available. AC084854 Genomic DNA No translation available. CH471082 Genomic DNA Translation: EAW77752.1 BC013348 mRNA Translation: AAH13348.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS10212.1 [P62491-1] CCDS58373.1 [P62491-2] |
Protein sequence database of the Protein Information Resource More...PIRi | S47169 |
NCBI Reference Sequences More...RefSeqi | NP_001193765.1, NM_001206836.1 [P62491-2] NP_004654.1, NM_004663.4 [P62491-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.321541 |
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 |
| 1OIV | X-ray | 1.98 | A/B | 1-173 | [»] | |
| 1OIW | X-ray | 2.05 | A | 1-173 | [»] | |
| 1OIX | X-ray | 1.70 | A | 1-173 | [»] | |
| 1YZK | X-ray | 2.00 | A | 8-175 | [»] | |
| 2D7C | X-ray | 1.75 | A/B | 7-173 | [»] | |
| 2GZD | X-ray | 2.44 | A/B | 2-173 | [»] | |
| 2GZH | X-ray | 2.47 | A | 2-173 | [»] | |
| 2HV8 | X-ray | 1.86 | A/B/C | 6-175 | [»] | |
| 4C4P | X-ray | 2.00 | A | 1-173 | [»] | |
| 4D0L | X-ray | 2.94 | B/D/F | 1-216 | [»] | |
| 4D0M | X-ray | 6.00 | B/D/H/J/N/P/R/T/X/Z/d/h | 1-216 | [»] | |
| 4LWZ | X-ray | 2.55 | A/C | 1-177 | [»] | |
| 4LX0 | X-ray | 2.19 | A/C | 1-177 | [»] | |
| 4UJ3 | X-ray | 3.00 | A/D/G/J/M/P/S/V | 4-186 | [»] | |
| 4UJ4 | X-ray | 4.20 | A/D/G/J | 4-186 | [»] | |
| 4UJ5 | X-ray | 2.60 | A/B | 6-186 | [»] | |
| 5C46 | X-ray | 2.65 | F | 1-216 | [»] | |
| 5C4G | X-ray | 3.20 | B | 1-216 | [»] | |
| 5EUQ | X-ray | 3.20 | B | 1-216 | [»] | |
| 5EZ5 | X-ray | 2.40 | A/B | 8-175 | [»] | |
| 5FBL | X-ray | 3.37 | B | 1-216 | [»] | |
| 5FBQ | X-ray | 3.79 | B | 1-216 | [»] | |
| 5FBR | X-ray | 3.28 | B | 1-216 | [»] | |
| 5FBV | X-ray | 3.29 | B | 1-216 | [»] | |
| 5FBW | X-ray | 3.49 | B | 1-216 | [»] | |
| 5JCZ | X-ray | 2.06 | A/D/I | 1-177 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P62491 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P62491 | |||||
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 | 114299, 94 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P62491 |
Database of interacting proteins More...DIPi | DIP-29138N |
Protein interaction database and analysis system More...IntActi | P62491, 143 interactors |
Molecular INTeraction database More...MINTi | P62491 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000261890 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB01864 5'-Guanosine-Diphosphate-Monothiophosphate DB04315 Guanosine-5'-Diphosphate |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P62491 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P62491 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P62491 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RAB11A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 50402542 |
2D gel databases
USC-OGP 2-DE database More...OGPi | P62491 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P62491 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P62491 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P62491 |
PeptideAtlas More...PeptideAtlasi | P62491 |
PRoteomics IDEntifications database More...PRIDEi | P62491 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57402 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P62491-1 [P62491-1] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 8766 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000261890; ENSP00000261890; ENSG00000103769 [P62491-1] ENST00000569896; ENSP00000456420; ENSG00000103769 [P62491-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 8766 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:8766 |
UCSC genome browser More...UCSCi | uc002apk.4 human [P62491-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 8766 |
DisGeNET More...DisGeNETi | 8766 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000103769.9 |
GeneCards: human genes, protein and diseases More...GeneCardsi | RAB11A |
Human Gene Nomenclature Database More...HGNCi | HGNC:9760 RAB11A |
Human Protein Atlas More...HPAi | CAB013097 HPA051697 HPA060686 |
MalaCards human disease database More...MalaCardsi | RAB11A |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605570 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P62491 |
Open Targets More...OpenTargetsi | ENSG00000103769 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34101 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0087 Eukaryota COG1100 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118841 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233968 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG009351 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P62491 |
KEGG Orthology (KO) More...KOi | K07904 |
Identification of Orthologs from Complete Genome Data More...OMAi | DISKHAT |
Database of Orthologous Groups More...OrthoDBi | EOG091G0O1R |
Database for complete collections of gene phylogenies More...PhylomeDBi | P62491 |
TreeFam database of animal gene trees More...TreeFami | TF300099 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1445148 Translocation of GLUT4 to the plasma membrane R-HSA-432040 Vasopressin regulates renal water homeostasis via Aquaporins R-HSA-5620912 Anchoring of the basal body to the plasma membrane R-HSA-5620916 VxPx cargo-targeting to cilium R-HSA-8854214 TBC/RABGAPs R-HSA-8873719 RAB geranylgeranylation |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P62491 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | RAB11A human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P62491 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | RAB11A |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 8766 |
Protein Ontology More...PROi | PR:P62491 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000103769 |
CleanEx database of gene expression profiles More...CleanExi | HS_RAB11A |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P62491 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P62491 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027417 P-loop_NTPase IPR005225 Small_GTP-bd_dom IPR001806 Small_GTPase |
Pfam protein domain database More...Pfami | View protein in Pfam PF00071 Ras, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00231 small_GTP, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51419 RAB, 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 | RB11A_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 | P62491Primary (citable) accession number: P62491 Secondary accession number(s): B2R4B6 , B4DT13, P24410, Q5TZN9, Q9JLX1 | |
| <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: | July 19, 2004 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 171 of the entry and version 3 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 15
Human chromosome 15: entries, gene names and cross-references to MIM - 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
