Q9BXF6 · RFIP5_HUMAN
- ProteinRab11 family-interacting protein 5
- GeneRAB11FIP5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids653 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis.
Miscellaneous
Antibodies against RIP11 are found in sera from patients with autoimmune diseases such as systemic lupus erythematosus (SLE) or Sjoegren syndrome (SS). It is also found in the sera from mothers of children with neonatal lupus erythematosus (NLE).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centriolar satellite | |
Cellular Component | early endosome | |
Cellular Component | early endosome membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Cellular Component | phagocytic vesicle | |
Cellular Component | recycling endosome | |
Cellular Component | recycling endosome membrane | |
Cellular Component | secretory granule | |
Cellular Component | transport vesicle membrane | |
Molecular Function | gamma-tubulin binding | |
Molecular Function | small GTPase binding | |
Biological Process | cellular response to acidic pH | |
Biological Process | insulin secretion involved in cellular response to glucose stimulus | |
Biological Process | negative regulation of adiponectin secretion | |
Biological Process | regulated exocytosis | |
Biological Process | regulation of protein localization to cell surface |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRab11 family-interacting protein 5
- Short namesRab11-FIP5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BXF6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Recycling endosome membrane ; Peripheral membrane protein
Early endosome membrane ; Peripheral membrane protein
Golgi apparatus membrane ; Peripheral membrane protein
Cytoplasmic vesicle, secretory vesicle membrane ; Peripheral membrane protein
Mitochondrion membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 780 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000097307 | 1-653 | UniProt | Rab11 family-interacting protein 5 | |||
Sequence: MALVRGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWYKLHSKPGKKEKERGEIEVTIQFTRNNLSASMFDLSMKDKPRSPFSKIRDKMKGKKKYDLESASAILPSSAIEDPDLGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSASGSLAYQGPGAELLTRSPSRSSWLSTEGGRDSAQSPKLFTHKRTYSDEANQMRVAPPRALLDLQGHLDAASRSSLCVNGSHIYNEEPQGPVRHRSSISGSLPSSGSLQAVSSRFSEEGPRSTDDTWPRGSRSNSSSEAVLGQEELSAQAKVLAPGASHPGEEEGARLPEGKPVQVATPIVASSEAVAEKEGARKEERKPRMGLFHHHHQGLSRSELGRRSSLGEKGGPILGASPHHSSSGEEKAKSSWFGLREAKDPTQKPSPHPVKPLSAAPVEGSPDRKQSRSSLSIALSSGLEKLKTVTSGSIQPVTQAPQAGQMVDTKRLKDSAVLDQSAKYYHLTHDELISLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIPPGPPK | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 176 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 276 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 282 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 283 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 286 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 307 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 357 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 359 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 367 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 391 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 395 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 494 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 498 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 523 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 538 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 538 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 547 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 553 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected at low levels in heart, brain, placenta, lung, liver, adipocytes, kidney, spleen, skeletal muscle and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with RAB11FIP4 (PubMed:11278501, PubMed:12470645).
Interacts with NAPG (PubMed:11278501).
Interacts with RO60 (PubMed:10545525).
Interacts with RAB11A that has been activated by GTP binding (PubMed:11163216).
Interacts with NAPG (PubMed:11278501).
Interacts with RO60 (PubMed:10545525).
Interacts with RAB11A that has been activated by GTP binding (PubMed:11163216).
(Microbial infection) Interacts with Kaposi's sarcoma-associated herpesvirus/HHV-8 protein ORF45; this interaction results in the lysosomal degradation of ORF45 and the inhibition of viral particle release.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BXF6 | KIF3A Q9Y496 | 2 | EBI-1387068, EBI-1104844 | |
BINARY | Q9BXF6 | RAB11A P62491 | 7 | EBI-1387068, EBI-745098 | |
BINARY | Q9BXF6 | SNX18 Q96RF0 | 3 | EBI-1387068, EBI-298169 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-146 | C2 | ||||
Sequence: RGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWY | ||||||
Region | 269-300 | Disordered | ||||
Sequence: GPGAELLTRSPSRSSWLSTEGGRDSAQSPKLF | ||||||
Compositional bias | 275-294 | Polar residues | ||||
Sequence: LTRSPSRSSWLSTEGGRDSA | ||||||
Region | 342-402 | Disordered | ||||
Sequence: HIYNEEPQGPVRHRSSISGSLPSSGSLQAVSSRFSEEGPRSTDDTWPRGSRSNSSSEAVLG | ||||||
Compositional bias | 352-377 | Polar residues | ||||
Sequence: VRHRSSISGSLPSSGSLQAVSSRFSE | ||||||
Compositional bias | 386-402 | Polar residues | ||||
Sequence: TWPRGSRSNSSSEAVLG | ||||||
Region | 415-548 | Disordered | ||||
Sequence: PGASHPGEEEGARLPEGKPVQVATPIVASSEAVAEKEGARKEERKPRMGLFHHHHQGLSRSELGRRSSLGEKGGPILGASPHHSSSGEEKAKSSWFGLREAKDPTQKPSPHPVKPLSAAPVEGSPDRKQSRSSL | ||||||
Domain | 586-648 | FIP-RBD | ||||
Sequence: KDSAVLDQSAKYYHLTHDELISLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIP |
Domain
Binds to vesicles enriched in neutral phospholipids via its C2 domain. The interaction is favored by Mg2+ rather than Ca2+.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length653
- Mass (Da)70,415
- Last updated2001-06-01 v1
- Checksum716725537AA9D86E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1B0GTL5 | A0A1B0GTL5_HUMAN | RAB11FIP5 | 1324 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 176 | in Ref. 3; AAH35013 | ||||
Sequence: Missing | ||||||
Compositional bias | 275-294 | Polar residues | ||||
Sequence: LTRSPSRSSWLSTEGGRDSA | ||||||
Compositional bias | 352-377 | Polar residues | ||||
Sequence: VRHRSSISGSLPSSGSLQAVSSRFSE | ||||||
Compositional bias | 386-402 | Polar residues | ||||
Sequence: TWPRGSRSNSSSEAVLG | ||||||
Sequence conflict | 503 | in Ref. 3; AAH35013 | ||||
Sequence: E → G | ||||||
Sequence conflict | 599 | in Ref. 3; AAH35013 | ||||
Sequence: H → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF334812 EMBL· GenBank· DDBJ | AAK20892.1 EMBL· GenBank· DDBJ | mRNA | ||
AB020664 EMBL· GenBank· DDBJ | BAA74880.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC035013 EMBL· GenBank· DDBJ | AAH35013.1 EMBL· GenBank· DDBJ | mRNA | ||
AF153085 EMBL· GenBank· DDBJ | AAF34356.1 EMBL· GenBank· DDBJ | mRNA |