UniProtKB - P61006 (RAB8A_HUMAN)
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- BLAST>sp|P61006|RAB8A_HUMAN Ras-related protein Rab-8A OS=Homo sapiens OX=9606 GN=RAB8A PE=1 SV=1 MAKTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQ IWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILG NKCDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFFTLARDIKAKMDKKLEGN SPQGSNQGVKITPDQQKRSSFFRCVLL
- Align
Ras-related protein Rab-8A
RAB8A
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 which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
4 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.18"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.23"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.31"Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death."
Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A., Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S., Kabashi E., Charlet-Berguerand N.
EMBO J. 35:1276-1297(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
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 | 17 – 22 | GTPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 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
| 6 | |
| <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 | 34 – 40 | GTPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 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
| 7 | |
| <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 | 63 – 67 | GTPCombined 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 By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi 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
| 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 | 121 – 124 | GTPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 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
| 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 | 152 – 154 | GTPCombined 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 By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi 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
| 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
- GDP 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
- 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 <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
- protein kinase binding Source: Ensembl
- Rab GTPase binding Source: UniProtKB
<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
- autophagy Source: UniProtKB-KW
- axonogenesis Source: UniProtKB
- cellular response to insulin stimulus Source: UniProtKB
- cilium assembly Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Golgi vesicle fusion to target membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neurotransmitter receptor transport to postsynaptic membrane Source: Ensembl
- post-translational protein modification Source: Reactome
- protein localization to plasma membrane Source: UniProtKB
- protein secretion Source: GO_Central
- regulation of autophagy 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 exocytosis Source: GO_Central
- regulation of long-term neuronal synaptic plasticity Source: Ensembl
- regulation of protein transport Source: Ensembl
- vesicle docking involved in exocytosis Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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 | Autophagy, Cilium biogenesis/degradation, 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-2565942 Regulation of PLK1 Activity at G2/M Transition 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 R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs |
SIGNOR Signaling Network Open Resource More...SIGNORi | P61006 |
<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-8AAlternative name(s): Oncogene c-mel |
| <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:RAB8A Synonyms:MEL, RAB8 |
| <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:ENSG00000167461.11 |
Human Gene Nomenclature Database More...HGNCi | HGNC:7007 RAB8A |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 165040 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P61006 |
<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
Cytoskeleton
- centriole By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- cilium basal body By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- centriole By similarity
Endosome
- Recycling endosome 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.19"MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EHD1 AND MICALL1, MUTAGENESIS OF THR-22 AND GLN-67.
- Recycling endosome membrane 1 Publication
Plasma membrane
- Cell membrane 1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.11"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
Hattula K., Furuhjelm J., Arffman A., Peranen J.
Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB3IP, 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.11"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
Hattula K., Furuhjelm J., Arffman A., Peranen J.
Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB3IP, 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.11"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
Hattula K., Furuhjelm J., Arffman A., Peranen J.
Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB3IP, SUBCELLULAR LOCATION.
- Cell membrane 1 Publication
Golgi apparatus
- Golgi apparatus 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.12"Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN.
- Golgi apparatus 1 Publication
Other locations
- cilium 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
- 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.25"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.
- phagosome membrane By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
; Lipid-anchor By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
; Cytoplasmic side By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Midbody 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.22"Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody during cytokinesis by the doublecortin domain-containing 5 protein."
Kaplan A., Reiner O.
J. Cell Sci. 124:3989-4000(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DCDC5, SUBCELLULAR LOCATION.
Note: Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (PubMed:15837803). In the GDP-bound form, present in the perinuclear region (PubMed:12221131). Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form (PubMed:12221131). Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis (PubMed:20890297). Localizes to tubular recycling endosome (PubMed:19864458). Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211).5 Publications- cilium 1 Publication
- Ref.11"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
Hattula K., Furuhjelm J., Arffman A., Peranen J.
Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB3IP, SUBCELLULAR LOCATION. - Ref.12"Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN. - Ref.18"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.19"MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EHD1 AND MICALL1, MUTAGENESIS OF THR-22 AND GLN-67. - Ref.25"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
- centriole Source: UniProtKB-SubCell
- centrosome 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
- ciliary basal body Source: Ensembl
Cytosol
- cytosol Source: Reactome
Endosome
- recycling endosome 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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi membrane Source: Reactome
- trans-Golgi network membrane Source: Reactome
Plasma Membrane
- plasma membrane Source: GO_Central
Other locations
- ciliary base Source: Ensembl
- cilium 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
- dendritic spine Source: Ensembl
- midbody 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
- neuronal cell body Source: Ensembl
- non-motile cilium Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- 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
- phagocytic vesicle membrane Source: UniProtKB-SubCell
- postsynaptic density Source: Ensembl
- secretory granule membrane Source: GO_Central
- synaptic vesicle Source: GO_Central
- trans-Golgi network transport vesicle Source: Ensembl
<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, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Golgi apparatus, 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 | 22 | T → N: Loss of interaction with MICALL1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 67 | Q → L: Probable constitutively active mutant locked in the active GTP-bound form. Stimulates interaction with MICALL1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>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 - Diseasei
Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 4218 |
Open Targets More...OpenTargetsi | ENSG00000167461 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30743 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RAB8A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 46810392 |
<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 ‘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_0000121130 | 1 – 204 | Ras-related protein Rab-8AAdd BLAST | 204 | |
| <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_0000370793 | 205 – 207 | 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 | 181 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 185 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 204 | 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 | 204 | 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
Lipoprotein, Methylation, Phosphoprotein, PrenylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P61006 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P61006 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P61006 |
PeptideAtlas More...PeptideAtlasi | P61006 |
PRoteomics IDEntifications database More...PRIDEi | P61006 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57245 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P61006 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P61006 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P61006 |
<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 | ENSG00000167461 |
CleanEx database of gene expression profiles More...CleanExi | HS_RAB8A |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P61006 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P61006 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA041945 |
<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 which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
10 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
Hattula K., Furuhjelm J., Arffman A., Peranen J.
Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAB3IP, SUBCELLULAR LOCATION. - Ref.12"Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN. - Ref.14"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.17"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIFO. - Ref.19"MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EHD1 AND MICALL1, MUTAGENESIS OF THR-22 AND GLN-67. - Ref.22"Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody during cytokinesis by the doublecortin domain-containing 5 protein."
Kaplan A., Reiner O.
J. Cell Sci. 124:3989-4000(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DCDC5, SUBCELLULAR LOCATION. - Ref.23"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.27"OCRL localizes to the primary cilium: a new role for cilia in Lowe syndrome."
Luo N., West C.C., Murga-Zamalloa C.A., Sun L., Anderson R.M., Wells C.D., Weinreb R.N., Travers J.B., Khanna H., Sun Y.
Hum. Mol. Genet. 21:3333-3344(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH OCRL. - Ref.32"A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1."
Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S., Erdmann K.S., Itzen A.
EMBO J. 30:1659-1670(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-176 IN COMPLEX WITH OCRL. - Ref.33"bMERB domains are bivalent Rab8 family effectors evolved by gene duplication."
Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S., Gazdag E.M., Muller M.P.
Elife 5:E18675-E18675(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-207 IN COMPLEX WITH MICALCL, INTERACTION WITH MICAL3; MICAL1; EHBP1 AND EHBP1L1.
<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 |
|---|---|---|---|---|
| lpg0940 | Q5ZWZ3 | 3 | EBI-722293,EBI-6417967 | From Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513). |
| LRRK2 | Q5S007 | 6 | EBI-722293,EBI-5323863 | |
| OCRL | Q01968 | 13 | EBI-722293,EBI-6148898 | |
| OPTN | Q96CV9 | 4 | EBI-722293,EBI-748974 | |
| RAB3IP | Q96QF0 | 6 | EBI-722293,EBI-747844 | |
| RAB3IP | Q96QF0-2 | 2 | EBI-722293,EBI-747865 | |
| RABIF | P47224 | 4 | EBI-722293,EBI-713992 |
<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
- 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
- protein kinase binding Source: Ensembl
- Rab GTPase binding Source: UniProtKB
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110382, 92 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P61006 |
Database of interacting proteins More...DIPi | DIP-43703N |
Protein interaction database and analysis system More...IntActi | P61006, 83 interactors |
Molecular INTeraction database More...MINTi | P61006 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000300935 |
<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 | 7 – 14 | 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 | 8 | |
| <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 | 21 – 30 | 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 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 | 38 – 41 | 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 | 42 – 52 | 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 | 55 – 64 | 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 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 | 69 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 73 – 78 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 82 – 89 | 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 | 8 | |
| <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 | 93 – 97 | 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 | 99 – 109 | 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 | 115 – 121 | 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 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 | 122 – 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 | 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 | 126 – 128 | 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 | 133 – 142 | 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 | 146 – 149 | 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 | 152 – 155 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 158 – 174 | 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 | 17 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P61006 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P61006 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<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 | 37 – 45 | 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 | KOG0078 Eukaryota ENOG410XPUI LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00890000139330 |
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 | P61006 |
KEGG Orthology (KO) More...KOi | K07901 |
Identification of Orthologs from Complete Genome Data More...OMAi | NPQGSNQ |
Database of Orthologous Groups More...OrthoDBi | EOG091G0LA6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P61006 |
TreeFam database of animal gene trees More...TreeFami | TF314097 |
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
MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI
60 70 80 90 100
ELDGKRIKLQ IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR
110 120 130 140 150
NWIRNIEEHA SADVEKMILG NKCDVNDKRQ VSKERGEKLA LDYGIKFMET
160 170 180 190 200
SAKANINVEN AFFTLARDIK AKMDKKLEGN SPQGSNQGVK ITPDQQKRSS
FFRCVLL
The sequence of this isoform differs from the canonical sequence as follows:
161-205: AFFTLARDIK...QKRSSFFRCV → RYQSKNGQKI...PMCSSVRNTA
10 20 30 40 50
MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI
60 70 80 90 100
ELDGKRIKLQ IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR
110 120 130 140 150
NWIRNIEEHA SADVEKMILG NKCDVNDKRQ VSKERGEKLA LDYGIKFMET
160 170 180 190 200
SAKANINVEN RYQSKNGQKI GRQQPPGEQP GSQNHTGPAE EEQLFPMCSS
VRNTALL
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 177 – 183 | LEGNSPQ → WKATAP in AAB19681 (PubMed:1886711).Curated | 7 |
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 | X56741 mRNA Translation: CAA40065.1 S53268 mRNA Translation: AAB19681.1 AF498943 mRNA Translation: AAM21091.1 BT007184 mRNA Translation: AAP35848.1 AK293676 mRNA Translation: BAG57118.1 CR536583 mRNA Translation: CAG38820.1 AC008894 Genomic DNA No translation available. CR542274 mRNA Translation: CAG47070.1 CH471106 Genomic DNA Translation: EAW84526.1 BC002977 mRNA Translation: AAH02977.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12339.1 [P61006-1] |
Protein sequence database of the Protein Information Resource More...PIRi | B49647 |
NCBI Reference Sequences More...RefSeqi | NP_005361.2, NM_005370.4 [P61006-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.642874 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000300935; ENSP00000300935; ENSG00000167461 [P61006-1] ENST00000586682; ENSP00000467501; ENSG00000167461 [P61006-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4218 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4218 |
UCSC genome browser More...UCSCi | uc002ndn.5 human [P61006-1] |
<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 | |
|---|---|---|---|---|---|
| P61006 | Ras-related protein Rab-8A | 207 | |||
| Ras-related protein Rab-8A | 207 | ||||
| RAB8A, member RAS oncogene family, isoform CRA_a | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| Oncogene c-mel | 207 | ||||
| +18 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61006 | Ras-related protein Rab-8A | 207 | |||
| Ras-related protein Rab-8A | 207 | ||||
| RAB8A, member RAS oncogene family, isoform CRA_a | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| Oncogene c-mel | 207 | ||||
| +21 | |||||
| P61006-2 | UPI00032AEAD0 | 255 | |||
| RAB8A isoform 2 | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| RAB8A isoform 2 | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61006 | Ras-related protein Rab-8A | 207 | |||
| Ras-related protein Rab-8A | 207 | ||||
| RAB8A, member RAS oncogene family, isoform CRA_a | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| Oncogene c-mel | 207 | ||||
| +29 | |||||
| P61006-2 | UPI00032AEAD0 | 255 | |||
| RAB8A isoform 2 | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| RAB8A isoform 2 | 207 | ||||
| RAB8A, member RAS oncogene family | 207 | ||||
| +208 | |||||
<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 | X56741 mRNA Translation: CAA40065.1 S53268 mRNA Translation: AAB19681.1 AF498943 mRNA Translation: AAM21091.1 BT007184 mRNA Translation: AAP35848.1 AK293676 mRNA Translation: BAG57118.1 CR536583 mRNA Translation: CAG38820.1 AC008894 Genomic DNA No translation available. CR542274 mRNA Translation: CAG47070.1 CH471106 Genomic DNA Translation: EAW84526.1 BC002977 mRNA Translation: AAH02977.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12339.1 [P61006-1] |
Protein sequence database of the Protein Information Resource More...PIRi | B49647 |
NCBI Reference Sequences More...RefSeqi | NP_005361.2, NM_005370.4 [P61006-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.642874 |
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 |
| 3QBT | X-ray | 2.00 | A/C/E/G | 6-176 | [»] | |
| 3TNF | X-ray | 2.50 | A | 6-176 | [»] | |
| 4LHV | X-ray | 1.95 | A/B/C/D/E | 6-176 | [»] | |
| 4LHW | X-ray | 1.55 | A/B/C/D/E | 6-176 | [»] | |
| 4LHX | X-ray | 3.05 | A/B | 1-184 | [»] | |
| 4LHY | X-ray | 3.10 | A/B | 1-184 | [»] | |
| 4LHZ | X-ray | 3.20 | A/B | 1-184 | [»] | |
| 4LI0 | X-ray | 3.30 | A/B | 1-184 | [»] | |
| 5SZI | X-ray | 2.85 | A | 1-207 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P61006 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P61006 | |||||
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 | 110382, 92 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P61006 |
Database of interacting proteins More...DIPi | DIP-43703N |
Protein interaction database and analysis system More...IntActi | P61006, 83 interactors |
Molecular INTeraction database More...MINTi | P61006 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000300935 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P61006 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P61006 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P61006 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RAB8A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 46810392 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P61006 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P61006 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P61006 |
PeptideAtlas More...PeptideAtlasi | P61006 |
PRoteomics IDEntifications database More...PRIDEi | P61006 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57245 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4218 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000300935; ENSP00000300935; ENSG00000167461 [P61006-1] ENST00000586682; ENSP00000467501; ENSG00000167461 [P61006-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4218 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4218 |
UCSC genome browser More...UCSCi | uc002ndn.5 human [P61006-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4218 |
DisGeNET More...DisGeNETi | 4218 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000167461.11 |
GeneCards: human genes, protein and diseases More...GeneCardsi | RAB8A |
Human Gene Nomenclature Database More...HGNCi | HGNC:7007 RAB8A |
Human Protein Atlas More...HPAi | HPA041945 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 165040 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P61006 |
Open Targets More...OpenTargetsi | ENSG00000167461 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30743 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0078 Eukaryota ENOG410XPUI LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00890000139330 |
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 | P61006 |
KEGG Orthology (KO) More...KOi | K07901 |
Identification of Orthologs from Complete Genome Data More...OMAi | NPQGSNQ |
Database of Orthologous Groups More...OrthoDBi | EOG091G0LA6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P61006 |
TreeFam database of animal gene trees More...TreeFami | TF314097 |
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-2565942 Regulation of PLK1 Activity at G2/M Transition 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 R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs |
SIGNOR Signaling Network Open Resource More...SIGNORi | P61006 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | RAB8A human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | RAB8A |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4218 |
Protein Ontology More...PROi | PR:P61006 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000167461 |
CleanEx database of gene expression profiles More...CleanExi | HS_RAB8A |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P61006 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P61006 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 | RAB8A_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 | P61006Primary (citable) accession number: P61006 Secondary accession number(s): B4DEK7, P24407, Q6FHV5 | |
| <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: | April 26, 2004 |
| Last sequence update: | April 26, 2004 | |
| Last modified: | July 18, 2018 | |
| This is version 163 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: 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
