O94898 · LRIG2_HUMAN
- ProteinLeucine-rich repeats and immunoglobulin-like domains protein 2
- GeneLRIG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1065 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 | cytoplasm | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | growth cone | |
Cellular Component | intracellular vesicle | |
Cellular Component | plasma membrane | |
Molecular Function | signaling receptor binding | |
Biological Process | innervation | |
Biological Process | membrane protein ectodomain proteolysis | |
Biological Process | negative regulation of axon regeneration | |
Biological Process | negative regulation of membrane protein ectodomain proteolysis | |
Biological Process | positive regulation of protein localization to cell surface | |
Biological Process | protein localization to cell surface | |
Biological Process | regulation of neuron migration | |
Biological Process | regulation of platelet-derived growth factor receptor signaling pathway | |
Biological Process | sensory perception of sound |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeucine-rich repeats and immunoglobulin-like domains protein 2
- Short namesLIG-2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94898
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 41-807 | Extracellular | ||||
Sequence: GLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPPDTAILDFSHNRLSNWNISLESQTLQEVKMNYNELTEIPYFGEPTSNITLLSLVHNIIPEINAQALQFYPALESLDLSSNIISEIKTSSFPRMQLKYLNLSNNRITTLEAGCFDNLSSSLLVVKLNRNRMSMIPPKIFKLPHLQFLELKRNRIKIVEGLTFQGLDSLRSLKMQRNGISKLKDGAFFGLNNMEELELEHNNLTRVNKGWLYGLRMLQQLYVSQNAIERISPDAWEFCQRLSELDLSYNQLTRLDESAFVGLSLLERLNLGDNRVTHIADGVFRFLSNLQTLDLRNNEISWAIEDASEAFAGLTSLTKLILQGNQIKSITKKAFIGLESLEHLDLNNNAIMSIQENAFSQTHLKELILNTSSLLCDCHLKWLLQWLVDNNFQHSVNVSCAHPEWLAGQSILNVDLKDFVCDDFLKPQIRTHPETIIALRGMNVTLTCTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQCIVTNHFGSNYSQKAKLTVNEMPSFLKTPMDLTIRTGAMARLECAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSCMAQNTAGGLSANASLTVLETPSFIRPLEDKTVTRGETAVLQCIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTCIMSNTLGTERGHIYLNVISSPNCDSSQSSIGHEDDGWTTVG | ||||||
Transmembrane | 808-828 | Helical | ||||
Sequence: IVIIVVVCCVVGTSLIWVIVI | ||||||
Topological domain | 829-1065 | Cytoplasmic | ||||
Sequence: YHMRRKNEDYSITNTEELNLPADIPSYLSSQGTLSEPQEGYSNSEAGSHQQLMPPANGYIHKGTDGGTGTRVICSDCYDNANIYSRTREYCPYTYIAEEDVLDQTLSSLMVQMPKETYLVHPPQDTTALESLIPSANREPSAFPTNHERISEKKLPSTQMSGETLQRPVWNINRELGLPHPPFSQQPVHESPQLHQNEGLAGREPDCSASSMSCHRLQDHAFDFSRTRNIQDGSEGT |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Urofacial syndrome 2 (UFS2)
- Note
- DescriptionA rare autosomal recessive disorder characterized by facial grimacing when attempting to smile and failure of the urinary bladder to void completely despite a lack of anatomical bladder outflow obstruction or overt neurological damage. Affected individuals often have reflux of infected urine from the bladder to the upper renal tract, with a risk of kidney damage and renal failure.
- See alsoMIM:615112
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,162 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 signal, chain, glycosylation, disulfide bond, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-40 | UniProt | |||||
Sequence: MAPAPLGVPEEQLLGCRSRVLSRLLFIAQTALLLLPAAGA | |||||||
Chain | PRO_0000014829 | 41-1065 | UniProt | Leucine-rich repeats and immunoglobulin-like domains protein 2 | |||
Sequence: GLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPPDTAILDFSHNRLSNWNISLESQTLQEVKMNYNELTEIPYFGEPTSNITLLSLVHNIIPEINAQALQFYPALESLDLSSNIISEIKTSSFPRMQLKYLNLSNNRITTLEAGCFDNLSSSLLVVKLNRNRMSMIPPKIFKLPHLQFLELKRNRIKIVEGLTFQGLDSLRSLKMQRNGISKLKDGAFFGLNNMEELELEHNNLTRVNKGWLYGLRMLQQLYVSQNAIERISPDAWEFCQRLSELDLSYNQLTRLDESAFVGLSLLERLNLGDNRVTHIADGVFRFLSNLQTLDLRNNEISWAIEDASEAFAGLTSLTKLILQGNQIKSITKKAFIGLESLEHLDLNNNAIMSIQENAFSQTHLKELILNTSSLLCDCHLKWLLQWLVDNNFQHSVNVSCAHPEWLAGQSILNVDLKDFVCDDFLKPQIRTHPETIIALRGMNVTLTCTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQCIVTNHFGSNYSQKAKLTVNEMPSFLKTPMDLTIRTGAMARLECAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSCMAQNTAGGLSANASLTVLETPSFIRPLEDKTVTRGETAVLQCIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTCIMSNTLGTERGHIYLNVISSPNCDSSQSSIGHEDDGWTTVGIVIIVVVCCVVGTSLIWVIVIYHMRRKNEDYSITNTEELNLPADIPSYLSSQGTLSEPQEGYSNSEAGSHQQLMPPANGYIHKGTDGGTGTRVICSDCYDNANIYSRTREYCPYTYIAEEDVLDQTLSSLMVQMPKETYLVHPPQDTTALESLIPSANREPSAFPTNHERISEKKLPSTQMSGETLQRPVWNINRELGLPHPPFSQQPVHESPQLHQNEGLAGREPDCSASSMSCHRLQDHAFDFSRTRNIQDGSEGT | |||||||
Glycosylation | 91 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 121 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 173 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 189 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 274 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 441 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 468 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 514 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 519↔580 | UniProt | |||||
Sequence: CTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQC | |||||||
Glycosylation | 571 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 589 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 623↔675 | UniProt | |||||
Sequence: CAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSC | |||||||
Glycosylation | 687 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 717↔766 | UniProt | |||||
Sequence: CIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTC | |||||||
Glycosylation | 728 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 906 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 912 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94898 | EGFR P00533 | 4 | EBI-2830372, EBI-297353 | |
BINARY | O94898 | PDGFRB P09619 | 3 | EBI-2830372, EBI-641237 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-75 | LRRNT | ||||
Sequence: GLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPP | ||||||
Repeat | 76-97 | LRR 1 | ||||
Sequence: DTAILDFSHNRLSNWNISLESQ | ||||||
Repeat | 98-119 | LRR 2 | ||||
Sequence: TLQEVKMNYNELTEIPYFGEPT | ||||||
Repeat | 121-142 | LRR 3 | ||||
Sequence: NITLLSLVHNIIPEINAQALQF | ||||||
Repeat | 145-166 | LRR 4 | ||||
Sequence: ALESLDLSSNIISEIKTSSFPR | ||||||
Repeat | 168-189 | LRR 5 | ||||
Sequence: QLKYLNLSNNRITTLEAGCFDN | ||||||
Repeat | 193-214 | LRR 6 | ||||
Sequence: SLLVVKLNRNRMSMIPPKIFKL | ||||||
Repeat | 216-237 | LRR 7 | ||||
Sequence: HLQFLELKRNRIKIVEGLTFQG | ||||||
Repeat | 240-261 | LRR 8 | ||||
Sequence: SLRSLKMQRNGISKLKDGAFFG | ||||||
Repeat | 264-285 | LRR 9 | ||||
Sequence: NMEELELEHNNLTRVNKGWLYG | ||||||
Repeat | 288-309 | LRR 10 | ||||
Sequence: MLQQLYVSQNAIERISPDAWEF | ||||||
Repeat | 312-333 | LRR 11 | ||||
Sequence: RLSELDLSYNQLTRLDESAFVG | ||||||
Repeat | 336-357 | LRR 12 | ||||
Sequence: LLERLNLGDNRVTHIADGVFRF | ||||||
Repeat | 360-382 | LRR 13 | ||||
Sequence: NLQTLDLRNNEISWAIEDASEAF | ||||||
Repeat | 387-408 | LRR 14 | ||||
Sequence: SLTKLILQGNQIKSITKKAFIG | ||||||
Repeat | 411-432 | LRR 15 | ||||
Sequence: SLEHLDLNNNAIMSIQENAFSQ | ||||||
Domain | 443-494 | LRRCT | ||||
Sequence: SSLLCDCHLKWLLQWLVDNNFQHSVNVSCAHPEWLAGQSILNVDLKDFVCDD | ||||||
Domain | 498-597 | Ig-like C2-type 1 | ||||
Sequence: PQIRTHPETIIALRGMNVTLTCTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQCIVTNHFGSNYSQKAKLT | ||||||
Domain | 602-691 | Ig-like C2-type 2 | ||||
Sequence: PSFLKTPMDLTIRTGAMARLECAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSCMAQNTAGGLSANASLT | ||||||
Domain | 696-785 | Ig-like C2-type 3 | ||||
Sequence: PSFIRPLEDKTVTRGETAVLQCIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTCIMSNTLGTERGHIYLNVIS | ||||||
Region | 962-990 | Disordered | ||||
Sequence: PSANREPSAFPTNHERISEKKLPSTQMSG | ||||||
Region | 1003-1040 | Disordered | ||||
Sequence: ELGLPHPPFSQQPVHESPQLHQNEGLAGREPDCSASSM |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,065
- Mass (Da)118,965
- Last updated2004-10-11 v3
- ChecksumCD2903A861DC4887
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018349 EMBL· GenBank· DDBJ | BAA34526.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL161998 EMBL· GenBank· DDBJ | CAB82328.2 EMBL· GenBank· DDBJ | mRNA |