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P06734

- FCER2_HUMAN

UniProt

P06734 - FCER2_HUMAN

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Protein

Low affinity immunoglobulin epsilon Fc receptor

Gene

FCER2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei149 – 1502Cleavage
Metal bindingi249 – 2491Calcium1 Publication
Metal bindingi251 – 2511Calcium1 Publication
Metal bindingi269 – 2691Calcium1 Publication
Metal bindingi270 – 2701Calcium1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. integrin binding Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. Notch signaling pathway Source: Reactome
  2. positive regulation of humoral immune response mediated by circulating immunoglobulin Source: Ensembl
  3. positive regulation of killing of cells of other organism Source: BHF-UCL
  4. positive regulation of nitric-oxide synthase activity Source: BHF-UCL
  5. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Calcium, IgE-binding protein, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163910. NOTCH2 intracellular domain regulates transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Low affinity immunoglobulin epsilon Fc receptor
Alternative name(s):
BLAST-2
C-type lectin domain family 4 member J
Fc-epsilon-RII
Immunoglobulin E-binding factor
Lymphocyte IgE receptor
CD_antigen: CD23
Cleaved into the following 2 chains:
Gene namesi
Name:FCER2
Synonyms:CD23A, CLEC4J, FCE2, IGEBF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3612. FCER2.

Subcellular locationi

Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor. Secreted
Note: Also exists as a soluble excreted form, sCD23.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei22 – 4726Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini48 – 321274ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Low affinity immunoglobulin epsilon Fc receptor membrane-bound formPRO_0000017391Add
BLAST
Chaini150 – 321172Low affinity immunoglobulin epsilon Fc receptor soluble formPRO_0000017392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi17 – 171S-palmitoyl cysteine1 Publication
Lipidationi18 – 181S-palmitoyl cysteine1 Publication
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi160 ↔ 288
Disulfide bondi163 ↔ 174
Disulfide bondi191 ↔ 282
Disulfide bondi259 ↔ 273

Post-translational modificationi

N- and O-glycosylated.
The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding.

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP06734.
PaxDbiP06734.
PRIDEiP06734.

PTM databases

PhosphoSiteiP06734.

Miscellaneous databases

PMAP-CutDBP06734.

Expressioni

Gene expression databases

BgeeiP06734.
CleanExiHS_FCER2.
ExpressionAtlasiP06734. baseline and differential.
GenevestigatoriP06734.

Organism-specific databases

HPAiCAB002624.
HPA008928.

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

BioGridi108502. 3 interactions.
STRINGi9606.ENSP00000264072.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi159 – 1624Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi173 – 18210Combined sources
Helixi184 – 19310Combined sources
Beta strandi196 – 1983Combined sources
Helixi204 – 2118Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi219 – 2268Combined sources
Turni227 – 2304Combined sources
Beta strandi231 – 2344Combined sources
Turni247 – 2526Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi259 – 2624Combined sources
Turni264 – 2663Combined sources
Beta strandi268 – 2714Combined sources
Beta strandi277 – 2859Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi291 – 2944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLImodel-A173-285[»]
1KJEmodel-A173-285[»]
1T8CNMR-A156-298[»]
1T8DNMR-A156-298[»]
2H2RX-ray1.50A/B150-321[»]
2H2TX-ray1.30B150-321[»]
4EZMX-ray3.10G/H/I/J/K/L156-298[»]
4G96X-ray2.25A/B/C/D156-298[»]
4G9AX-ray2.00A/B/C/D156-298[»]
4GI0X-ray2.27A/B/C156-298[»]
4GJ0X-ray1.95A/B/C/D156-298[»]
4GJXX-ray2.80A/B/C/D/E/F/G/H156-298[»]
4GK1X-ray2.24A/B/C/D/E/F/G156-298[»]
4GKOX-ray3.30G/H/I/J/K/L156-298[»]
4J6JX-ray1.90A/B/C/D156-298[»]
4J6KX-ray2.30A/B/C/D/E/F/G/H156-298[»]
4J6LX-ray3.15A/B/C/D/E/F/G/H156-298[»]
4J6MX-ray2.48A/B/C/D/E/F/G/H156-298[»]
4J6NX-ray2.85A/B156-298[»]
4J6PX-ray1.90A/B/C/D156-298[»]
4J6QX-ray2.54A156-298[»]
4KI1X-ray3.20E/F/G/H156-298[»]
ProteinModelPortaliP06734.
SMRiP06734. Positions 134-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06734.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati69 – 8921Add
BLAST
Repeati90 – 11021Add
BLAST
Repeati111 – 13121Add
BLAST
Domaini162 – 284123C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG235454.
GeneTreeiENSGT00760000118924.
HOGENOMiHOG000089951.
HOVERGENiHBG051599.
InParanoidiP06734.
KOiK06468.
OMAiKCYYFGE.
OrthoDBiEOG7FV3QQ.
PhylomeDBiP06734.
TreeFamiTF333341.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06734-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT
60 70 80 90 100
QSLKQLEERA ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ
110 120 130 140 150
RLKSQDLELS WNLNGLQADL SSFKSQELNE RNEASDLLER LREEVTKLRM
160 170 180 190 200
ELQVSSGFVC NTCPEKWINF QRKCYYFGKG TKQWVHARYA CDDMEGQLVS
210 220 230 240 250
IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV DYSNWAPGEP
260 270 280 290 300
TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM
310 320
GPDSRPDPDG RLPTPSAPLH S
Length:321
Mass (Da):36,469
Last modified:January 1, 1988 - v1
Checksum:iF86708C0E6515B87
GO

Sequence cautioni

The sequence AAA52433.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691N → T in CAA28465. (PubMed:3034567)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621R → W.
Corresponds to variant rs2228137 [ dbSNP | Ensembl ].
VAR_035387
Natural varianti284 – 2841R → Q.
Corresponds to variant rs8102872 [ dbSNP | Ensembl ].
VAR_035388
Natural varianti316 – 3161S → F.1 Publication
VAR_069800

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15059 mRNA. Translation: AAA52434.1.
M14766 mRNA. Translation: AAA52435.1.
X04772 mRNA. Translation: CAA28465.1.
AC008763 Genomic DNA. No translation available.
BC014108 mRNA. Translation: AAH14108.1.
BC062591 mRNA. Translation: AAH62591.1.
M23562 Genomic DNA. Translation: AAA52433.1. Sequence problems.
CCDSiCCDS12184.1.
PIRiA26067. LNHUER.
RefSeqiNP_001193948.2. NM_001207019.2.
NP_001207429.1. NM_001220500.1.
NP_001993.2. NM_002002.4.
XP_005272519.1. XM_005272462.2.
XP_006722750.1. XM_006722687.1.
UniGeneiHs.465778.

Genome annotation databases

EnsembliENST00000346664; ENSP00000264072; ENSG00000104921.
ENST00000597921; ENSP00000471974; ENSG00000104921.
GeneIDi2208.
KEGGihsa:2208.
UCSCiuc002mhm.2. human.

Polymorphism databases

DMDMi119862.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

CD23

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15059 mRNA. Translation: AAA52434.1 .
M14766 mRNA. Translation: AAA52435.1 .
X04772 mRNA. Translation: CAA28465.1 .
AC008763 Genomic DNA. No translation available.
BC014108 mRNA. Translation: AAH14108.1 .
BC062591 mRNA. Translation: AAH62591.1 .
M23562 Genomic DNA. Translation: AAA52433.1 . Sequence problems.
CCDSi CCDS12184.1.
PIRi A26067. LNHUER.
RefSeqi NP_001193948.2. NM_001207019.2.
NP_001207429.1. NM_001220500.1.
NP_001993.2. NM_002002.4.
XP_005272519.1. XM_005272462.2.
XP_006722750.1. XM_006722687.1.
UniGenei Hs.465778.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HLI model - A 173-285 [» ]
1KJE model - A 173-285 [» ]
1T8C NMR - A 156-298 [» ]
1T8D NMR - A 156-298 [» ]
2H2R X-ray 1.50 A/B 150-321 [» ]
2H2T X-ray 1.30 B 150-321 [» ]
4EZM X-ray 3.10 G/H/I/J/K/L 156-298 [» ]
4G96 X-ray 2.25 A/B/C/D 156-298 [» ]
4G9A X-ray 2.00 A/B/C/D 156-298 [» ]
4GI0 X-ray 2.27 A/B/C 156-298 [» ]
4GJ0 X-ray 1.95 A/B/C/D 156-298 [» ]
4GJX X-ray 2.80 A/B/C/D/E/F/G/H 156-298 [» ]
4GK1 X-ray 2.24 A/B/C/D/E/F/G 156-298 [» ]
4GKO X-ray 3.30 G/H/I/J/K/L 156-298 [» ]
4J6J X-ray 1.90 A/B/C/D 156-298 [» ]
4J6K X-ray 2.30 A/B/C/D/E/F/G/H 156-298 [» ]
4J6L X-ray 3.15 A/B/C/D/E/F/G/H 156-298 [» ]
4J6M X-ray 2.48 A/B/C/D/E/F/G/H 156-298 [» ]
4J6N X-ray 2.85 A/B 156-298 [» ]
4J6P X-ray 1.90 A/B/C/D 156-298 [» ]
4J6Q X-ray 2.54 A 156-298 [» ]
4KI1 X-ray 3.20 E/F/G/H 156-298 [» ]
ProteinModelPortali P06734.
SMRi P06734. Positions 134-291.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108502. 3 interactions.
STRINGi 9606.ENSP00000264072.

Chemistry

BindingDBi P06734.
ChEMBLi CHEMBL2940.

PTM databases

PhosphoSitei P06734.

Polymorphism databases

DMDMi 119862.

Proteomic databases

MaxQBi P06734.
PaxDbi P06734.
PRIDEi P06734.

Protocols and materials databases

DNASUi 2208.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346664 ; ENSP00000264072 ; ENSG00000104921 .
ENST00000597921 ; ENSP00000471974 ; ENSG00000104921 .
GeneIDi 2208.
KEGGi hsa:2208.
UCSCi uc002mhm.2. human.

Organism-specific databases

CTDi 2208.
GeneCardsi GC19M007754.
HGNCi HGNC:3612. FCER2.
HPAi CAB002624.
HPA008928.
MIMi 151445. gene.
neXtProti NX_P06734.
PharmGKBi PA28058.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235454.
GeneTreei ENSGT00760000118924.
HOGENOMi HOG000089951.
HOVERGENi HBG051599.
InParanoidi P06734.
KOi K06468.
OMAi KCYYFGE.
OrthoDBi EOG7FV3QQ.
PhylomeDBi P06734.
TreeFami TF333341.

Enzyme and pathway databases

Reactomei REACT_163910. NOTCH2 intracellular domain regulates transcription.

Miscellaneous databases

EvolutionaryTracei P06734.
GeneWikii CD23.
GenomeRNAii 2208.
NextBioi 8943.
PMAP-CutDB P06734.
PROi P06734.
SOURCEi Search...

Gene expression databases

Bgeei P06734.
CleanExi HS_FCER2.
ExpressionAtlasi P06734. baseline and differential.
Genevestigatori P06734.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins."
    Ikuta K., Takami M., Kim C.W., Honjo T., Miyoshi T., Tagaya Y., Kawabe T., Yodoi J.
    Proc. Natl. Acad. Sci. U.S.A. 84:819-823(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor."
    Luedin C., Hofstetter H., Sarfati M., Levy C.A., Suter U., Alaimo D., Kilchherr E., Frost H., Delespesse G.
    EMBO J. 6:109-114(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: B-cell and Blood.
  6. "Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue-specific and IL-4-specific regulation of gene expression."
    Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E.L., Suemura M., Kishimoto T.
    Cell 55:611-618(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Partial characterization of natural and recombinant human soluble CD23."
    Rose K., Turcatti G., Graber P., Pochon S., Regamey P.-O., Jansen K.U., Magnenat E., Aubonney N., Bonnefoy J.-Y.
    Biochem. J. 286:819-824(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
  8. "The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase ADAM10."
    Lemieux G.A., Blumenkron F., Yeung N., Zhou P., Williams J., Grammer A.C., Petrovich R., Lipsky P.E., Moss M.L., Werb Z.
    J. Biol. Chem. 282:14836-14844(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE BY ADAM10.
  9. "Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23."
    Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T., Garin J., Journet A.
    PLoS ONE 7:E37187-E37187(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-17 AND CYS-18, SUBCELLULAR LOCATION.
    Tissue: B-cell.
  10. "Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23)."
    Padlan E.A., Helm B.A.
    Receptor 3:325-341(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF LECTIN DOMAIN.
  11. "Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models."
    Bajorath J., Aruffo A.
    Protein Sci. 5:240-247(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 173-285.
  12. Cited for: STRUCTURE BY NMR OF 156-298, DISULFIDE BONDS, SUBUNIT.
  13. "Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding."
    Wurzburg B.A., Tarchevskaya S.S., Jardetzky T.S.
    Structure 14:1049-1058(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-321 ALONE AND IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
  14. Cited for: VARIANT PHE-316.

Entry informationi

Entry nameiFCER2_HUMAN
AccessioniPrimary (citable) accession number: P06734
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 26, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

There are two kinds of Fc receptors for IgE, which differ in both structure and function: high affinity receptors on basophils and mast cells and low affinity receptors on lymphocytes and monocytes.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3