Q92622 · RUBIC_HUMAN
- ProteinRun domain Beclin-1-interacting and cysteine-rich domain-containing protein
- GeneRUBCN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids972 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Following fungal or viral infection (implicating CLEC7A (dectin-1)-mediated myeloid cell activation or RIGI-dependent sensing of RNA viruses) negatively regulates pro-inflammatory cytokine production by association with CARD9 and sequestering it from signaling complexes (PubMed:22423967).
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 | cytosol | |
Cellular Component | early endosome | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | late endosome | |
Cellular Component | lysosome | |
Cellular Component | nucleoplasm | |
Molecular Function | phosphatidylinositol 3-kinase inhibitor activity | |
Molecular Function | phosphatidylinositol phosphate binding | |
Biological Process | autophagy | |
Biological Process | immune system process | |
Biological Process | multivesicular body sorting pathway | |
Biological Process | negative regulation of autophagosome maturation | |
Biological Process | negative regulation of autophagy | |
Biological Process | negative regulation of endocytosis | |
Biological Process | negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | |
Biological Process | phagocytosis |
Keywords
- Biological process
Enzyme and pathway databases
Interacts with GTP-bound RAB7. Involved in negative regulation of autophagy.
Names & Taxonomy
Protein names
- Recommended nameRun domain Beclin-1-interacting and cysteine-rich domain-containing protein
- Short namesRubicon
- Alternative names
Gene names
- Community suggested namesRubicon; RUBCN.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92622
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spinocerebellar ataxia, autosomal recessive, 15 (SCAR15)
- Note
- DescriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR15 patients manifest cerebellar ataxia in early childhood and delayed motor development with delayed walking. Additional features include dysarthria, upper limb involvement, abnormal eye movements, and hyporeflexia.
- See alsoMIM:615705
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 248 | Disrupts interaction with YWHAB. | ||||
Sequence: S → A | ||||||
Mutagenesis | 912 | Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-915, L-920 and G-923. | ||||
Sequence: C → G | ||||||
Mutagenesis | 915 | Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-912, L-920 and G-923. | ||||
Sequence: C → G | ||||||
Mutagenesis | 920 | Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-912,G-915 and G-923. | ||||
Sequence: H → L | ||||||
Mutagenesis | 923 | Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-912, G-915 and L-920. | ||||
Sequence: C → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,030 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
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_0000050736 | 1-972 | UniProt | Run domain Beclin-1-interacting and cysteine-rich domain-containing protein | |||
Sequence: MRPEGAGMELGGGEERLPEESRREHWQLLGNLKTTVEGLVSTNSPNVWSKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDASMFARKHESPLLVTKSQSLTALPSSTYTPPNSYAQHSYFGSFSSLHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVSVSALARDSPLTPNEMSSSTLTSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPSSLYMEYEGGRYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQEAEHGSFRVTSSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIRRNTASSSKSFVSSQSFSHCFLHSTSAEAVAMGLLKQFEGMQLPAASELEWLVPEHDAPQKLLPIPDSLPISPDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPSRVLRKWDFSKYYVSNFSKDLLIKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLCHMKNMFKTCRLAKELLDSFDTVPGHLTEDLHLYSLNDLTATRKGELGPRLAELTRAGATHVERCMLCQAKGFICEFCQNEDDIIFPFELHKCRTCEECKACYHKACFKSGSCPRCERLQARREALARQSLESYLSDYEEEPAEALALEAAVLEAT | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 197 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 246 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 248 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 266 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 388 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 399 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 410 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 413 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 416 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 469 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 528 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 562 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 562 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 671 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 671 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with Rab7 (RAB7A or RAB7B) (GTP-bound form); Rab7 and UVRAG compete for RUBCN binding; can interact simultaneously with Rab7 and the PI3K complex (PubMed:20943950, PubMed:20974968, PubMed:21062745).
Interacts with CYBA and CYBB; indicative for the association with the CYBA:CYBB NADPH oxidase heterodimer. Interacts with NOX4 and probably associates with the CYBA:NOX4 complex (PubMed:22423966).
Interacts with YWHAB and CARD9 in a competitive and stimulation-dependent manner; RUBCN exchanges interaction from YWHAB to CARD9 upon stimulation with beta-1,3-glucan (PubMed:22423967).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q92622 | ANKRD11 X5D778 | 3 | EBI-2952709, EBI-17183751 | |
BINARY | Q92622 | BECN1 Q14457 | 16 | EBI-2952709, EBI-949378 | |
BINARY | Q92622 | BRD1 O95696 | 3 | EBI-2952709, EBI-714754 | |
BINARY | Q92622 | BYSL Q13895 | 3 | EBI-2952709, EBI-358049 | |
BINARY | Q92622 | DPF2 Q92785 | 3 | EBI-2952709, EBI-359932 | |
BINARY | Q92622 | EGFR P00533 | 3 | EBI-2952709, EBI-297353 | |
BINARY | Q92622 | ENKD1 Q9H0I2 | 3 | EBI-2952709, EBI-744099 | |
BINARY | Q92622 | FAM161A Q3B820 | 3 | EBI-2952709, EBI-719941 | |
BINARY | Q92622 | FAM9B Q8IZU0 | 3 | EBI-2952709, EBI-10175124 | |
BINARY | Q92622 | GAS8 O95995 | 3 | EBI-2952709, EBI-1052570 | |
BINARY | Q92622 | NME7 Q9Y5B8 | 3 | EBI-2952709, EBI-744782 | |
BINARY | Q92622 | PIK3C3 Q8NEB9 | 9 | EBI-2952709, EBI-1056470 | |
BINARY | Q92622 | TCEANC Q8N8B7-2 | 3 | EBI-2952709, EBI-11955057 | |
BINARY | Q92622 | UVRAG Q9P2Y5 | 11 | EBI-2952709, EBI-2952704 | |
BINARY | Q92622 | VEZF1 Q14119 | 3 | EBI-2952709, EBI-11980193 | |
BINARY | Q92622 | ZNF250 P15622-3 | 3 | EBI-2952709, EBI-10177272 | |
BINARY | Q92622 | ZNF648 Q5T619 | 3 | EBI-2952709, EBI-11985915 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-22 | Disordered | ||||
Sequence: MRPEGAGMELGGGEERLPEESR | ||||||
Domain | 48-189 | RUN | ||||
Sequence: WSKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDAS | ||||||
Region | 49-180 | Interaction with PIK3C3 | ||||
Sequence: SKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNP | ||||||
Region | 204-447 | Interaction with YWHAB | ||||
Sequence: SQSLTALPSSTYTPPNSYAQHSYFGSFSSLHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVSVSALARDSPLTPNEMSSSTLTSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPSS | ||||||
Compositional bias | 233-254 | Polar residues | ||||
Sequence: LHQSVPNNGSERRSTSFPLSGP | ||||||
Region | 233-279 | Disordered | ||||
Sequence: LHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVS | ||||||
Region | 300-600 | Interaction with UVRAG | ||||
Sequence: TSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPSSLYMEYEGGRYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQEAEHGSFRVTSSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIR | ||||||
Region | 307-446 | Disordered | ||||
Sequence: WVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPS | ||||||
Compositional bias | 334-403 | Polar residues | ||||
Sequence: GRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKK | ||||||
Region | 505-557 | Interaction with BECN1 | ||||
Sequence: AIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQE | ||||||
Compositional bias | 562-584 | Polar residues | ||||
Sequence: SFRVTSSSSQFSSRDSAQLSDSG | ||||||
Region | 562-589 | Disordered | ||||
Sequence: SFRVTSSSSQFSSRDSAQLSDSGSADEV | ||||||
Region | 567-625 | Interaction with CYBA | ||||
Sequence: SSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIRRNTASSSKSFVSSQSFSHCFLHSTS | ||||||
Region | 672-760 | Interaction with CARD9 | ||||
Sequence: PDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPS | ||||||
Region | 721-972 | Interaction with Rab7 | ||||
Sequence: CAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPSRVLRKWDFSKYYVSNFSKDLLIKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLCHMKNMFKTCRLAKELLDSFDTVPGHLTEDLHLYSLNDLTATRKGELGPRLAELTRAGATHVERCMLCQAKGFICEFCQNEDDIIFPFELHKCRTCEECKACYHKACFKSGSCPRCERLQARREALARQSLESYLSDYEEEPAEALALEAAVLEAT |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q92622-1
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.
- Name1
- Length972
- Mass (Da)108,622
- Last updated2010-05-18 v4
- Checksum4B76166F29F5AF97
Q92622-2
- Name2
Q92622-3
- Name3
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A096LNI3 | A0A096LNI3_HUMAN | RUBCN | 24 | ||
H0Y6E6 | H0Y6E6_HUMAN | RUBCN | 934 | ||
A0A9L9PY84 | A0A9L9PY84_HUMAN | RUBCN | 1011 | ||
H7C3H3 | H7C3H3_HUMAN | RUBCN | 147 | ||
H7C357 | H7C357_HUMAN | RUBCN | 680 | ||
E9PEM3 | E9PEM3_HUMAN | RUBCN | 435 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039160 | 1-60 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 233-254 | Polar residues | ||||
Sequence: LHQSVPNNGSERRSTSFPLSGP | ||||||
Compositional bias | 334-403 | Polar residues | ||||
Sequence: GRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKK | ||||||
Alternative sequence | VSP_039161 | 420 | in isoform 2 | |||
Sequence: P → PGGPRNITIIVEDPIA | ||||||
Compositional bias | 562-584 | Polar residues | ||||
Sequence: SFRVTSSSSQFSSRDSAQLSDSG | ||||||
Alternative sequence | VSP_039471 | 596 | in isoform 3 | |||
Sequence: D → DGSEGSNLTHISKNGLSVSLASMFSD | ||||||
Alternative sequence | VSP_039472 | 883-896 | in isoform 3 | |||
Sequence: LCQAKGFICEFCQN → VRKSHCSMQLSPCF | ||||||
Alternative sequence | VSP_039473 | 897-972 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D86979 EMBL· GenBank· DDBJ | BAA13215.3 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC024560 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX437131 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC014173 EMBL· GenBank· DDBJ | AAH14173.2 EMBL· GenBank· DDBJ | mRNA |