Q99J45 · NRBP_MOUSE
- ProteinNuclear receptor-binding protein
- GeneNrbp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids535 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for embryonic development (PubMed:22510880).
Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (PubMed:22510880).
May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (By similarity).
Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (PubMed:22510880).
May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (By similarity).
Miscellaneous
May act as a tumor suppressor to decrease tumor incidence and improve survival.
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 | cell cortex | |
Cellular Component | cytoplasm | |
Cellular Component | endomembrane system | |
Cellular Component | lamellipodium | |
Cellular Component | membrane | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | identical protein binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | epithelial cell differentiation | |
Biological Process | epithelial cell proliferation | |
Biological Process | in utero embryonic development | |
Biological Process | intracellular signal transduction |
Names & Taxonomy
Protein names
- Recommended nameNuclear receptor-binding protein
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99J45
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with activated RAC3 to endomembranes and at the cell periphery in lamellipodia.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic lethality by 7.5 dpc.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000086451 | 2-535 | Nuclear receptor-binding protein | |||
Sequence: SEGESQTVVSSGSDPKVESSSLAPGLTSVSPPVTSTTSAASPEEEEESEDESEILEESPCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADVKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDSLQREFIQKCLQSEPARRPTARELLFHPALFEVPSLKLLAAHCIVGHQHMIPENALEEITKNMDTSAVLAEIPAGPGREPVQTLYSQSPALELDKFLEDVRNGIYPLTAFGLPRPQQPQQEEVTSPVVPPSVKTPTPEPAEVETRKVVLMQCNIESVEEGVKHHLTLLLKLEDKLNRHLSCDLMPNESIPDLAAELVQLGFISEADQSRLTSLLEETLNKFNFTRNSTLNTATVTVSS | ||||||
Modified residue | 431 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 433 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in Paneth, enteroendocrine and precursor goblet cell lineages in the intestine.
Gene expression databases
Interaction
Subunit
Homodimer (PubMed:12176995).
Binds to MLF1, recruiting a serine kinase which phosphorylates both itself and MLF1 (PubMed:12176995).
Phosphorylated MLF1 binds to YWHAZ and is retained in the cytoplasm (PubMed:12176995).
Interacts with ELOC/TCEB1, ELOB/TCEB2, TSC22D2 and TSC22D4 (By similarity).
Interacts with the Elongin BC E3 ubiquitin ligase complex via its interaction with ELOB/TCEB2 and ELOC/TCEB1 (By similarity).
Interacts with SALL4 (PubMed:22510880).
Binds to MLF1, recruiting a serine kinase which phosphorylates both itself and MLF1 (PubMed:12176995).
Phosphorylated MLF1 binds to YWHAZ and is retained in the cytoplasm (PubMed:12176995).
Interacts with ELOC/TCEB1, ELOB/TCEB2, TSC22D2 and TSC22D4 (By similarity).
Interacts with the Elongin BC E3 ubiquitin ligase complex via its interaction with ELOB/TCEB2 and ELOC/TCEB1 (By similarity).
Interacts with SALL4 (PubMed:22510880).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q99J45 | Mlf1 Q9QWV4 | 5 | EBI-767484, EBI-354765 | |
BINARY | Q99J45 | Nrbp1 Q99J45 | 2 | EBI-767484, EBI-767484 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-42 | Polar residues | ||||
Sequence: MSEGESQTVVSSGSDPKVESSSLAPGLTSVSPPVTSTTSAAS | ||||||
Region | 1-70 | Disordered | ||||
Sequence: MSEGESQTVVSSGSDPKVESSSLAPGLTSVSPPVTSTTSAASPEEEEESEDESEILEESPCGRWQKRREE | ||||||
Compositional bias | 56-70 | Basic and acidic residues | ||||
Sequence: LEESPCGRWQKRREE | ||||||
Domain | 68-327 | Protein kinase | ||||
Sequence: REEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADVKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDSLQREFIQKCLQSEPARRPTARELLFHPAL | ||||||
Region | 409-437 | Disordered | ||||
Sequence: LPRPQQPQQEEVTSPVVPPSVKTPTPEPA | ||||||
Compositional bias | 410-426 | Polar residues | ||||
Sequence: PRPQQPQQEEVTSPVVP |
Domain
The protein kinase domain is predicted to be catalytically inactive.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length535
- Mass (Da)59,866
- Last updated2001-06-01 v1
- Checksum85DD5F6FC25C5AB7
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YUQ4 | A0A0J9YUQ4_MOUSE | Nrbp1 | 188 | ||
A0A0J9YUZ6 | A0A0J9YUZ6_MOUSE | Nrbp1 | 62 | ||
A0A0J9YTX8 | A0A0J9YTX8_MOUSE | Nrbp1 | 88 | ||
D3YUV1 | D3YUV1_MOUSE | Nrbp1 | 543 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-42 | Polar residues | ||||
Sequence: MSEGESQTVVSSGSDPKVESSSLAPGLTSVSPPVTSTTSAAS | ||||||
Compositional bias | 56-70 | Basic and acidic residues | ||||
Sequence: LEESPCGRWQKRREE | ||||||
Sequence conflict | 220 | in Ref. 2; BAC32612 | ||||
Sequence: S → SVFHRIFAN | ||||||
Compositional bias | 410-426 | Polar residues | ||||
Sequence: PRPQQPQQEEVTSPVVP | ||||||
Sequence conflict | 494 | in Ref. 2; BAC32612 | ||||
Sequence: V → G | ||||||
Sequence conflict | 508-510 | in Ref. 2; BAC32612 | ||||
Sequence: TSL → SSV | ||||||
Sequence conflict | 521 | in Ref. 2; BAC32612 | ||||
Sequence: T → S | ||||||
Sequence conflict | 535 | in Ref. 2; BAC32612 | ||||
Sequence: S → VVELT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF302138 EMBL· GenBank· DDBJ | AAK97260.1 EMBL· GenBank· DDBJ | mRNA | ||
AF302139 EMBL· GenBank· DDBJ | AAK97261.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK046142 EMBL· GenBank· DDBJ | BAC32612.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004756 EMBL· GenBank· DDBJ | AAH04756.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018463 EMBL· GenBank· DDBJ | AAH18463.1 EMBL· GenBank· DDBJ | mRNA |