CD83_HUMAN
ID CD83_HUMAN Reviewed; 205 AA.
AC Q01151; Q5THX9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=CD83 antigen;
DE Short=hCD83;
DE AltName: Full=B-cell activation protein;
DE AltName: Full=Cell surface protein HB15;
DE AltName: CD_antigen=CD83;
DE Flags: Precursor;
GN Name=CD83;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tonsil;
RX PubMed=1378080;
RA Zhou L.-J., Schwarting R., Smith H.M., Tedder T.F.;
RT "A novel cell-surface molecule expressed by human interdigitating reticulum
RT cells, Langerhans cells, and activated lymphocytes is a new member of the
RT Ig superfamily.";
RL J. Immunol. 149:735-742(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell;
RX PubMed=8422464;
RA Kozlow E.J., Wilson G.L., Fox C.H., Kehrl J.H.;
RT "Subtractive cDNA cloning of a novel member of the Ig gene superfamily
RT expressed at high levels in activated B lymphocytes.";
RL Blood 81:454-461(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: May play a significant role in antigen presentation or the
CC cellular interactions that follow lymphocyte activation.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC Q01151; Q969F0: FATE1; NbExp=3; IntAct=EBI-2873723, EBI-743099;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed by activated lymphocytes, Langerhans
CC cells and interdigitating reticulum cells.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=CD83 antigen;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Other_00148";
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DR EMBL; Z11697; CAA77755.1; -; mRNA.
DR EMBL; S53354; AAB25085.1; -; mRNA.
DR EMBL; CR457019; CAG33300.1; -; mRNA.
DR EMBL; AL133259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL022396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030830; AAH30830.1; -; mRNA.
DR CCDS; CCDS4532.1; -.
DR PIR; A48929; A48929.
DR RefSeq; NP_001035370.1; NM_001040280.1.
DR RefSeq; NP_001238830.1; NM_001251901.1.
DR RefSeq; NP_004224.1; NM_004233.3.
DR PDB; 5MIX; X-ray; 1.70 A; A=20-131.
DR PDB; 5MJ0; X-ray; 3.20 A; A/B=20-131.
DR PDB; 5MJ1; X-ray; 1.80 A; A=20-131.
DR PDB; 5MJ2; X-ray; 1.98 A; A=20-131.
DR PDBsum; 5MIX; -.
DR PDBsum; 5MJ0; -.
DR PDBsum; 5MJ1; -.
DR PDBsum; 5MJ2; -.
DR AlphaFoldDB; Q01151; -.
DR SMR; Q01151; -.
DR BioGRID; 114721; 70.
DR IntAct; Q01151; 45.
DR STRING; 9606.ENSP00000368450; -.
DR GlyGen; Q01151; 3 sites.
DR iPTMnet; Q01151; -.
DR PhosphoSitePlus; Q01151; -.
DR SwissPalm; Q01151; -.
DR BioMuta; CD83; -.
DR DMDM; 232223; -.
DR jPOST; Q01151; -.
DR MassIVE; Q01151; -.
DR MaxQB; Q01151; -.
DR PaxDb; Q01151; -.
DR PeptideAtlas; Q01151; -.
DR PRIDE; Q01151; -.
DR ProteomicsDB; 57923; -.
DR ABCD; Q01151; 22 sequenced antibodies.
DR Antibodypedia; 3744; 973 antibodies from 41 providers.
DR DNASU; 9308; -.
DR Ensembl; ENST00000379153.4; ENSP00000368450.3; ENSG00000112149.10.
DR GeneID; 9308; -.
DR KEGG; hsa:9308; -.
DR MANE-Select; ENST00000379153.4; ENSP00000368450.3; NM_004233.4; NP_004224.1.
DR UCSC; uc003nbi.4; human.
DR CTD; 9308; -.
DR DisGeNET; 9308; -.
DR GeneCards; CD83; -.
DR HGNC; HGNC:1703; CD83.
DR HPA; ENSG00000112149; Tissue enhanced (bone).
DR MIM; 604534; gene.
DR neXtProt; NX_Q01151; -.
DR OpenTargets; ENSG00000112149; -.
DR PharmGKB; PA26241; -.
DR VEuPathDB; HostDB:ENSG00000112149; -.
DR eggNOG; ENOG502S7FP; Eukaryota.
DR GeneTree; ENSGT00390000007302; -.
DR HOGENOM; CLU_099481_0_0_1; -.
DR InParanoid; Q01151; -.
DR OMA; SKPGMER; -.
DR OrthoDB; 1491669at2759; -.
DR PhylomeDB; Q01151; -.
DR TreeFam; TF337861; -.
DR PathwayCommons; Q01151; -.
DR SignaLink; Q01151; -.
DR SIGNOR; Q01151; -.
DR BioGRID-ORCS; 9308; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; CD83; human.
DR GeneWiki; CD83; -.
DR GenomeRNAi; 9308; -.
DR Pharos; Q01151; Tbio.
DR PRO; PR:Q01151; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q01151; protein.
DR Bgee; ENSG00000112149; Expressed in adrenal tissue and 190 other tissues.
DR ExpressionAtlas; Q01151; baseline and differential.
DR Genevisible; Q01151; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0032713; P:negative regulation of interleukin-4 production; IEA:Ensembl.
DR GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..205
FT /note="CD83 antigen"
FT /id="PRO_0000014657"
FT TOPO_DOM 20..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..114
FT /note="Ig-like V-type"
FT REGION 60..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 182
FT /note="R -> Q (in dbSNP:rs2230193)"
FT /id="VAR_033609"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5MIX"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5MIX"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:5MIX"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5MIX"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5MIX"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5MIX"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:5MJ0"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:5MIX"
SQ SEQUENCE 205 AA; 23042 MW; 1D77133595F2B852 CRC64;
MSRGLQLLLL SCAYSLAPAT PEVKVACSED VDLPCTAPWD PQVPYTVSWV KLLEGGEERM
ETPQEDHLRG QHYHQKGQNG SFDAPNERPY SLKIRNTTSC NSGTYRCTLQ DPDGQRNLSG
KVILRVTGCP AQRKEETFKK YRAEIVLLLA LVIFYLTLII FTCKFARLQS IFPDFSKAGM
ERAFLPVTSP NKHLGLVTPH KTELV
