UniProtKB - P51151 (RAB9A_HUMAN)
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- BLAST>sp|P51151|RAB9A_HUMAN Ras-related protein Rab-9A OS=Homo sapiens OX=9606 GN=RAB9A PE=1 SV=1 MAGKSSLFKVILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGVEFLNKDLEVDGHFVTMQI WDTAGQERFRSLRTPFYRGSDCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPESFPFV ILGNKIDISERQVSTEEAQAWCRDNGDYPYFETSAKDATNVAAAFEEAVRRVLATEDRSD HLIQTDTVNLHRKPKPSSSCC
- Align
Ras-related protein Rab-9A
RAB9A
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
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 155 | GTP; via amide nitrogenCombined 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 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
| 1 |
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 | 14 – 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 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
| 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 | 62 – 66 | GTPBy similarity | 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 | 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 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
| 4 |
<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
- identical protein binding Source: Ensembl
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- negative regulation by host of symbiont molecular function Source: AgBase <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 exocytosis 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
- protein transport Source: UniProtKB-KW
- regulation of protein localization Source: AgBase <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
- retrograde transport, endosome to Golgi Source: GO_Central
<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 | Protein transport, Transport |
| Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6811440 Retrograde transport at the Trans-Golgi-Network R-HSA-8873719 RAB geranylgeranylation R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs |
SIGNOR Signaling Network Open Resource More...SIGNORi | P51151 |
<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-9A |
| <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:RAB9A Synonyms:RAB9 |
| <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:ENSG00000123595.6 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9792 RAB9A |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 300284 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P51151 |
<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 Curated; Lipid-anchor Curated; Cytoplasmic side Curated
Endosome
- Late endosome 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments."
Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.
Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Late endosome 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum membrane Curated
Golgi apparatus
- Golgi apparatus membrane Curated
Other locations
- phagosome membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated
- 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.16"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.
- Cytoplasmic vesicle 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
- Melanosome 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
Note: Colocalizes with OSBPL1A at the late endosome (PubMed:16176980). Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211).2 Publications- Ref.7"The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments."
Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.
Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.16"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
Cytosol
- cytosol Source: Reactome
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Endosome
- late endosome 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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- trans-Golgi network membrane Source: Reactome
Lysosome
- lysosome 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
- plasma membrane Source: UniProtKB-SubCell
Other locations
- melanosome Source: UniProtKB
- 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
- transport vesicle Source: Reactome
<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, Endoplasmic reticulum, 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 | 40 | I → L: Loss of interaction with HPS4; when associated with L-66. 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 | 44 | F → L: Loss of interaction with HPS4; when associated with L-66. 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 | 61 | W → L: Loss of interaction with HPS4; when associated with L-66. 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 | 66 | Q → L: Loss of interaction with HPS4; when associated with L-40 or L-44 or L-61. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 9367 |
Open Targets More...OpenTargetsi | ENSG00000123595 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34152 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1293294 |
Drug and drug target database More...DrugBanki | DB03793 Benzoic Acid DB04315 Guanosine-5'-Diphosphate |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RAB9A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1710003 |
<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 | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000121139 | 2 – 201 | Ras-related protein Rab-9AAdd BLAST | 200 |
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-acetylalanineCombined 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 | 179 | 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 | 187 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <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 | 200 | S-geranylgeranyl cysteineBy similarity | 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 | 201 | S-geranylgeranyl cysteineBy similarity | 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, Phosphoprotein, PrenylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P51151 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P51151 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P51151 |
PeptideAtlas More...PeptideAtlasi | P51151 |
PRoteomics IDEntifications database More...PRIDEi | P51151 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56285 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P51151 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P51151 |
<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 | ENSG00000123595 |
CleanEx database of gene expression profiles More...CleanExi | HS_RAB9A |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P51151 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P51151 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB016411 HPA003094 |
<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.9"A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling."
Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M., Pfeffer S.R.
Mol. Biol. Cell 17:4353-4363(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GCC2. - Ref.10"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185."
Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.
Cell 132:286-298(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GCC2. - Ref.12"Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9."
Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N., Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.
J. Biol. Chem. 285:7794-7804(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HPS4 AND BLOC-3 COMPLEX, ABSENCE OF INTERACTION WITH HPS1, MUTAGENESIS OF ILE-40; PHE-44; TRP-61 AND GLN-66. - Ref.15"RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins."
Nottingham R.M., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.
J. Biol. Chem. 286:33213-33222(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SGSM2. - Ref.17"RUTBC2 protein, a Rab9A effector and GTPase-activating protein for Rab36."
Nottingham R.M., Pusapati G.V., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.
J. Biol. Chem. 287:22740-22748(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SGSM1.
<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 |
|---|---|---|---|---|
| NISCH | Q9Y2I1 | 8 | EBI-4401353,EBI-2688731 | |
| PLEKHM2 | Q8IWE5 | 4 | EBI-4401353,EBI-726484 |
<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
- identical protein binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114768, 34 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P51151 |
Database of interacting proteins More...DIPi | DIP-46409N |
Protein interaction database and analysis system More...IntActi | P51151, 148 interactors |
Molecular INTeraction database More...MINTi | P51151 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000420127 |
<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 | 5 – 13 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 20 – 29 | 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 | 41 – 51 | 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 | 54 – 62 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 67 – 69 | 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 | 70 – 73 | 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 | 74 – 77 | 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 | 81 – 88 | 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 | 92 – 96 | 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 | 98 – 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 | 12 | |
| <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 | 114 – 116 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 119 – 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 | 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 | 135 – 144 | 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 | 150 – 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 | 3 | |
| <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 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P51151 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P51151 |
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 | P51151 |
<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 | 36 – 44 | 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 | KOG0394 Eukaryota ENOG410XNZV LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119125 |
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 | P51151 |
KEGG Orthology (KO) More...KOi | K07899 |
Identification of Orthologs from Complete Genome Data More...OMAi | RSSCCMP |
Database of Orthologous Groups More...OrthoDBi | EOG091G0JIV |
Database for complete collections of gene phylogenies More...PhylomeDBi | P51151 |
TreeFam database of animal gene trees More...TreeFami | TF326442 |
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>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE
60 70 80 90 100
VDGHFVTMQI WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN
110 120 130 140 150
WKKEFIYYAD VKEPESFPFV ILGNKIDISE RQVSTEEAQA WCRDNGDYPY
160 170 180 190 200
FETSAKDATN VAAAFEEAVR RVLATEDRSD HLIQTDTVNL HRKPKPSSSC
C
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 | U44103 mRNA Translation: AAC51200.1 AF498944 mRNA Translation: AAM21092.1 CR450362 mRNA Translation: CAG29358.1 AK290505 mRNA Translation: BAF83194.1 CH471074 Genomic DNA Translation: EAW98826.1 BC017265 mRNA Translation: AAH17265.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14156.1 |
Protein sequence database of the Protein Information Resource More...PIRi | G02361 |
NCBI Reference Sequences More...RefSeqi | NP_001182257.1, NM_001195328.1 NP_004242.1, NM_004251.4 XP_016885453.1, XM_017029964.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.495704 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000464506; ENSP00000420127; ENSG00000123595 ENST00000618931; ENSP00000480777; ENSG00000123595 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9367 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9367 |
UCSC genome browser More...UCSCi | uc004cvm.5 human |
<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 | |
|---|---|---|---|---|---|
| P51151 | RAB9A, member RAS oncogene family, isoform CRA_a | 201 | |||
| ras-related protein Rab-9A | 201 | ||||
| RAB9A, member RAS oncogene family | 201 | ||||
| RAB9A, member RAS oncogene family | 201 | ||||
| RAB9A isoform 1 | 201 | ||||
| +8 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P51151 | RAB9A, member RAS oncogene family, isoform CRA_a | 201 | |||
| ras-related protein Rab-9A | 201 | ||||
| RAB9A, member RAS oncogene family | 201 | ||||
| RAB9A, member RAS oncogene family | 201 | ||||
| RAB9A isoform 1 | 201 | ||||
| +10 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P51151 | RAB9A, member RAS oncogene family, isoform CRA_a | 201 | |||
| ras-related protein Rab-9A | 201 | ||||
| RAB9A, member RAS oncogene family | 201 | ||||
| RAB9A, member RAS oncogene family | 201 | ||||
| RAB9A isoform 1 | 201 | ||||
| +54 | |||||
<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 | U44103 mRNA Translation: AAC51200.1 AF498944 mRNA Translation: AAM21092.1 CR450362 mRNA Translation: CAG29358.1 AK290505 mRNA Translation: BAF83194.1 CH471074 Genomic DNA Translation: EAW98826.1 BC017265 mRNA Translation: AAH17265.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14156.1 |
Protein sequence database of the Protein Information Resource More...PIRi | G02361 |
NCBI Reference Sequences More...RefSeqi | NP_001182257.1, NM_001195328.1 NP_004242.1, NM_004251.4 XP_016885453.1, XM_017029964.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.495704 |
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 |
| 1WMS | X-ray | 1.25 | A/B | 1-177 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P51151 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P51151 | |||||
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 | 114768, 34 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P51151 |
Database of interacting proteins More...DIPi | DIP-46409N |
Protein interaction database and analysis system More...IntActi | P51151, 148 interactors |
Molecular INTeraction database More...MINTi | P51151 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000420127 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1293294 |
Drug and drug target database More...DrugBanki | DB03793 Benzoic Acid DB04315 Guanosine-5'-Diphosphate |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P51151 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P51151 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RAB9A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1710003 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P51151 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P51151 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P51151 |
PeptideAtlas More...PeptideAtlasi | P51151 |
PRoteomics IDEntifications database More...PRIDEi | P51151 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56285 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 9367 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000464506; ENSP00000420127; ENSG00000123595 ENST00000618931; ENSP00000480777; ENSG00000123595 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9367 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9367 |
UCSC genome browser More...UCSCi | uc004cvm.5 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9367 |
DisGeNET More...DisGeNETi | 9367 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000123595.6 |
GeneCards: human genes, protein and diseases More...GeneCardsi | RAB9A |
Human Gene Nomenclature Database More...HGNCi | HGNC:9792 RAB9A |
Human Protein Atlas More...HPAi | CAB016411 HPA003094 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 300284 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P51151 |
Open Targets More...OpenTargetsi | ENSG00000123595 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34152 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0394 Eukaryota ENOG410XNZV LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119125 |
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 | P51151 |
KEGG Orthology (KO) More...KOi | K07899 |
Identification of Orthologs from Complete Genome Data More...OMAi | RSSCCMP |
Database of Orthologous Groups More...OrthoDBi | EOG091G0JIV |
Database for complete collections of gene phylogenies More...PhylomeDBi | P51151 |
TreeFam database of animal gene trees More...TreeFami | TF326442 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6811440 Retrograde transport at the Trans-Golgi-Network R-HSA-8873719 RAB geranylgeranylation R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs |
SIGNOR Signaling Network Open Resource More...SIGNORi | P51151 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | RAB9A human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P51151 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | RAB9A |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9367 |
Protein Ontology More...PROi | PR:P51151 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000123595 |
CleanEx database of gene expression profiles More...CleanExi | HS_RAB9A |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P51151 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P51151 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 | RAB9A_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 | P51151Primary (citable) accession number: P51151 Secondary accession number(s): A8K390, Q6ICN1 | |
| <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: | October 1, 1996 |
| Last sequence update: | October 1, 1996 | |
| Last modified: | June 20, 2018 | |
| This is version 187 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 X
Human chromosome X: 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
