FCRLB
Fc receptor-like B
Also known as: FCRL2, FCRLB_HUMAN, FCRLM2, FCRLY, FLJ31052, FREB-2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q6BAA4
- Gene
- FCRLB
- Ensembl
- ENSG00000162746
- Chromosome
- 1
- Canonical length
- 426 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Cytosol
- Secretome location
- Intracellular and membrane
OverviewNCBI Gene
FCRL2 belongs to the Fc receptor family. Fc receptors are involved in phagocytosis, antibody-dependent cell cytotoxicity, immediate hypersensitivity, and transcytosis of immunoglobulins via their ability to bind immunoglobulin (Ig) constant regions (Chikaev et al., 2005 [PubMed 15676285]).[supplied by OMIM, Mar 2008]
Canonical amino-acid sequenceUniProt
426 residues, UniProt reviewed canonical sequence.
>Q6BAA4|FCRLB
1 MWPLTALLLL VPSSGQAATL EKPILSLHPP WTTIFKGERV TLKCDGYHPL LLELQPISTL
61 WYLGHLLLPS HKKSIEVQTP GVYRCQTRGA PVSDPIHLSV SNDWLILQVP YAPVFEGEPL
121 VLRCRGWYDK VVYKLHYYHD GQAVRYFHSS ANYTVLQARA SDSGRYQCSG TMRIPVESAP
181 MFSAKVAVTV QELFRAPVLR VMGPREARGA ALGGVVLRCD TRLHPQKRDT PLQFAFYKYS
241 RAVRRFDWGA EYTVPEPEVE ELESYWCEAA TATRSVRKRS PWLQLPGPGS PLDPASTTAP
301 APWAAALAPG NRPLSFRKPP VSRSVPLVTS VRNTTSTGLQ FPASGAPTAG PPACAPPTPL
361 EQSAGALKPD VDLLLREMQL LKGLLSRVVL ELKEPQALRE LRGTPETPTS HFAVSPGTPE
421 TTPVESLocalizationUniProt · AlphaFold · HPA
Whether an antibody against FCRLB can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.45
- Highest tissue expression
- 1.6 nTPM
Expression across tissuesHPA
Tissue
- tonsil: 1.6 nTPM
- kidney: 0.8 nTPM
- lymph node: 0.8 nTPM
- seminal vesicle: 0.8 nTPM
- appendix: 0.6 nTPM
- cerebral cortex: 0.3 nTPM
Single-cell type
- thymic myoid cells: 11 nCPM
- urothelial cells: 8.2 nCPM
- extravillous trophoblasts: 7.3 nCPM
- granulosa cells: 7.3 nCPM
- hepatic stellate cells: 6.5 nCPM
- fallopian secretory cells: 6 nCPM
Immune cell
- basophil: 4 nTPM
- NK-cell: 3.6 nTPM
- memory B-cell: 3.3 nTPM
- naive B-cell: 2.9 nTPM
- eosinophil: 1.8 nTPM
- gdT-cell: 1.8 nTPM
Brain region
- cerebral cortex: 0.9 nTPM
- white matter: 0.9 nTPM
- pons: 0.8 nTPM
- hippocampal formation: 0.7 nTPM
- medulla oblongata: 0.7 nTPM
- basal ganglia: 0.6 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.5
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.52
- DepMap mean gene effect
- 0
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell surface receptor signaling pathway
- immunoglobulin mediated immune response
- negative regulation of immune response
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads FCRLB as an antibody target. Whether an autoantibody or antibody against FCRLB could matter depends on whether native FCRLB is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
FCRLB is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Source-annotated serology context
The source annotations explicitly mention antibody, autoantibody, autoantigen, or autoimmune context. This is biological context, not study-specific reactivity.
- Fc receptors are involved in phagocytosis, antibody-dependent cell cytotoxicity, immediate hypersensitivity, and transcytosis of immunoglobulins via their ability to bind immunoglobulin (Ig) constant regions (Chikaev et al., 2005 [PubMed 15676285]).[supplied by OMIM, Mar 2008]
Loading the interactive Seroatlas protein explorer...