Reviewed, UniProtKB/Swiss-Prot Q01151 (CD83_HUMAN)

Names and origin

Protein names

Recommended name:
    CD83 antigen
      Short name=hCD83
Alternative name(s):
    Cell surface protein HB15
    B-cell activation protein
    CD_antigen=CD83

Gene names

Name:

CD83

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a significant role in antigen presentation or the cellular interactions that follow lymphocyte activation.
Subunit structure	Monomer.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed by activated lymphocytes, Langerhans cells and interdigitating reticulum cells.
Sequence similarities	Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Signal Transmembrane
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Ref.1 Traceable author statement. Source: ProtInc humoral immune response Ref.2 Traceable author statement. Source: ProtInc signal transduction Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.6
	Chain	20 – 205	186	CD83 antigen		PRO_0000014657
Regions
	Topological domain	20 – 144	125	Extracellular Potential
	Transmembrane	145 – 166	22	Potential
	Topological domain	167 – 205	39	Cytoplasmic Potential
	Domain	20 – 114	95	Ig-like V-type
Amino acid modifications
	Glycosylation	79	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	86	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	117	1	N-linked (GlcNAc...) Potential
	Disulfide bond	35 ↔ 107		Potential
Natural variations
	Natural variant	182	1	R → Q: dbSNP rs2230193.		VAR_033609

Sequences

	Sequence		Length	Mass (Da)
	Q01151-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 1D77133595F2B852	FASTA	205	23,042
	10 20 30 40 50 60 MSRGLQLLLL SCAYSLAPAT PEVKVACSED VDLPCTAPWD PQVPYTVSWV KLLEGGEERM 70 80 90 100 110 120 ETPQEDHLRG QHYHQKGQNG SFDAPNERPY SLKIRNTTSC NSGTYRCTLQ DPDGQRNLSG 130 140 150 160 170 180 KVILRVTGCP AQRKEETFKK YRAEIVLLLA LVIFYLTLII FTCKFARLQS IFPDFSKAGM 190 200 ERAFLPVTSP NKHLGLVTPH KTELV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel cell-surface molecule expressed by human interdigitating reticulum cells, Langerhans cells, and activated lymphocytes is a new member of the Ig superfamily." Zhou L.-J., Schwarting R., Smith H.M., Tedder T.F. J. Immunol. 149:735-742(1992) [PubMed: 1378080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Tonsil.
[2]	"Subtractive cDNA cloning of a novel member of the Ig gene superfamily expressed at high levels in activated B lymphocytes." Kozlow E.J., Wilson G.L., Fox C.H., Kehrl J.H. Blood 81:454-461(1993) [PubMed: 8422464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-34.
[7]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79 AND ASN-86, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

CD83 antigen

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11697 mRNA. Translation: CAA77755.1. S53354 mRNA. Translation: AAB25085.1. CR457019 mRNA. Translation: CAG33300.1. AL133259, AL022396 Genomic DNA. Translation: CAB96723.2. AL022396, AL133259 Genomic DNA. Translation: CAI20374.1. BC030830 mRNA. Translation: AAH30830.1.
IPI	IPI00006003.
PIR	A48929.
RefSeq	NP_001035370.1. NP_004224.1.
UniGene	Hs.595133 Hs.654558
3D structure databases
SMR	Q01151. Positions 19-131.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01151.
PTM databases
PhosphoSite	Q01151.
Proteomic databases
PRIDE	Q01151.
Genome annotation databases
Ensembl	ENST00000379153; ENSP00000368450; ENSG00000112149; Homo sapiens. [Genome view]
GeneID	9308.
KEGG	hsa:9308.
UCSC	uc003nbh.1. human. uc003nbi.1. human.
Organism-specific databases
CTD	9308.
GeneCards	GC06P014225.
H-InvDB	HIX0005593.
HGNC	HGNC:1703. CD83.
HPA	CAB002509.
MIM	604534. gene.
PharmGKB	PA26241.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11350.
HOGENOM	HBG125262.
HOVERGEN	Q01151.
InParanoid	Q01151.
OMA	EVKVACS.
OrthoDB	EOG9J9QK6.
PhylomeDB	Q01151.
Gene expression databases
ArrayExpress	Q01151.
Bgee	Q01151.
CleanEx	HS_CD83.
Genevestigator	Q01151.
GermOnline	ENSG00000112149. Homo sapiens.
Family and domain databases
InterPro	IPR007110. Ig-like. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR013106. Ig_V-set. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF07686. V-set. 1 hit. [Graphical view]
SMART	SM00409. IG. 1 hit. [Graphical view]
PROSITE	PS50835. IG_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34865.
SOURCE	Search...

Entry information

Entry name

CD83_HUMAN

Accession

Primary (citable) accession number: Q01151
Secondary accession number(s): Q5THX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	January 19, 2010
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.