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P03989 (1B27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
HLA class I histocompatibility antigen, B-27 alpha chain
Alternative name(s):
MHC class I antigen B*27
Gene names
Name:HLA-B
Synonyms:HLAB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the presentation of foreign antigens to the immune system.

Subunit structure

Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Interacts with human herpesvirus 8 MIR1 protein By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system By similarity.

Polymorphism

The following alleles of B-27 are known: B*27:01=B*27:05, B*27:02 (B27.2; B-27k; B27e), B*27:03 (B27d), B*27:04, B*27:06, B*27:07, B*27:08 (B7Qui) and B*27:09 (B27-ci). The sequence shown is that of B*27:01.

Involvement in disease

Spondyloarthropathy 1 (SPDA1) [MIM:106300]: A chronic rheumatic disease with multifactorial inheritance. It includes a spectrum of related disorders comprising ankylosing spondylitis, a subset of psoriatic arthritis, reactive arthritis (e.g. Reiter syndrome), arthritis associated with inflammatory bowel disease and undifferentiated spondyloarthropathy. These disorders may occur simultaneously or sequentially in the same patient, probably representing various phenotypic expressions of the same disease. Ankylosing spondylitis is the form of rheumatoid arthritis affecting the spine and is considered the prototype of seronegative spondyloarthropathies. It produces pain and stiffness as a result of inflammation of the sacroiliac, intervertebral, and costovertebral joints.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A restricted number of HLA-B27 subtypes can be associated with ankylosing spondylitis and other B27-related diseases, and an elevated frequency of the B*2702 allele in ankylosing spondylitis patients is identified. The allele B*2707 seems to have a protective role some populations because it was found only in the healthy controls. Ref.19

Sequence similarities

Belongs to the MHC class I family.

Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Immunity
   Cellular componentMembrane
MHC I
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent

Inferred from direct assay PubMed 22031944. Source: UniProt

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent

Traceable author statement. Source: Reactome

detection of bacterium

Inferred from mutant phenotype PubMed 22321387. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

positive regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: InterPro

regulation of immune response

Traceable author statement. Source: Reactome

type I interferon signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Traceable author statement. Source: Reactome

MHC class I protein complex

Inferred from direct assay PubMed 22031944. Source: UniProt

cell surface

Inferred from direct assay PubMed 22031944PubMed 9754572. Source: UniProt

early endosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

phagocytic vesicle membrane

Traceable author statement. Source: Reactome

   Molecular_functionpeptide antigen binding

Inferred from direct assay PubMed 22031944. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.3
Chain25 – 362338HLA class I histocompatibility antigen, B-27 alpha chain
PRO_0000018839

Regions

Topological domain25 – 308284Extracellular Potential
Transmembrane309 – 33224Helical; Potential
Topological domain333 – 36230Cytoplasmic Potential
Domain209 – 29587Ig-like C1-type
Region25 – 11490Alpha-1
Region115 – 20692Alpha-2
Region207 – 29892Alpha-3
Region299 – 30810Connecting peptide

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Ref.14
Disulfide bond125 ↔ 188
Disulfide bond227 ↔ 283

Natural variations

Natural variant651A → T. Ref.20
Corresponds to variant rs1050529 [ dbSNP | Ensembl ].
VAR_056341
Natural variant831Y → H in allele B*27:03.
VAR_016379
Natural variant1011D → N in allele B*27:02.
VAR_016380
Natural variant1011D → S in allele B*27:04, allele B*27:06 and allele B*27:08; requires 2 nucleotide substitutions.
VAR_016381
Natural variant104 – 1052TL → IA in allele B*27:02.
VAR_016382
Natural variant1041T → N in allele B*27:08.
VAR_016383
Natural variant106 – 1072LR → RG in allele B*27:08.
VAR_016384
Natural variant1211N → S in allele B*27:07.
VAR_016385
Natural variant137 – 1382YH → HN in allele B*27:07.
VAR_016386
Natural variant1381H → D in allele B*27:06.
VAR_016387
Natural variant1401D → H in allele B*27:09.
VAR_016388
Natural variant1401D → Y in allele B*27:06 and allele B*27:07.
VAR_016389
Natural variant1551S → R in allele B*27:07.
VAR_016390
Natural variant1761V → E in allele B*27:04 and allele B*27:06.
VAR_016391
Natural variant2351A → G in allele B*27:04 and allele B*27:06.
VAR_016392
Natural variant3061V → I.
Corresponds to variant rs1131500 [ dbSNP | Ensembl ].
VAR_056342
Natural variant3291A → T.
Corresponds to variant rs1051488 [ dbSNP | Ensembl ].
VAR_056343
Natural variant3491C → S.
Corresponds to variant rs2308655 [ dbSNP | Ensembl ].
VAR_061402
Natural variant3491C → Y.
Corresponds to variant rs2308655 [ dbSNP | Ensembl ].
VAR_061403

Experimental info

Sequence conflict2061A → V Ref.2
Sequence conflict2661Q → E AA sequence Ref.3

Secondary structure

................................................... 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03989 [UniParc].

Last modified August 13, 1987. Version 2.
Checksum: C8D2F154E3292031

FASTA36240,428
        10         20         30         40         50         60 
MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF 

        70         80         90        100        110        120 
DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE DLRTLLRYYN QSEAGSHTLQ 

       130        140        150        160        170        180 
NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL 

       190        200        210        220        230        240 
RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT 

       250        260        270        280        290        300 
WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP 

       310        320        330        340        350        360 
SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL 


TA 

« Hide

References

« Hide 'large scale' references
[1]"Organization, sequence and expression of the HLA-B27 gene: a molecular approach to analyze HLA and disease associations."
Weiss E.H., Kuon W., Doerner C., Lang M., Riethmueller G.
Immunobiology 170:367-380(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*27:01).
[2]"Complete sequence of HLA-B27 cDNA identified through the characterization of structural markers unique to the HLA-A, -B, and -C allelic series."
Szoets H., Riethmueller G., Weiss E., Meo T.
Proc. Natl. Acad. Sci. U.S.A. 83:1428-1432(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-361 (ALLELE B*27:01).
[3]"Primary structure of papain-solubilized human histocompatibility antigen HLA-B27."
Ezquerra A., Bragado R., Vega M.A., Strominger J.L., Woody J., Lopez de Castro J.A.
Biochemistry 24:1733-1741(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-295 (B*27:01).
[4]"Gene conversion-like mechanisms may generate polymorphism in human class I genes."
Seemann G.H.A., Rein R.S., Brown C.S., Ploegh H.L.
EMBO J. 5:547-552(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*27:01 AND B*27:02).
[5]"On the nucleotide sequences of B*2702 and B*2705."
Moses J.H., Marsh S.G.E., Arnett K.L., Adams E.J., Bodmer J.G., Parham P.
Tissue Antigens 46:50-53(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:02).
[6]"Structural analysis of an HLA-B27 functional variant: identification of residues that contribute to the specificity of recognition by cytolytic T lymphocytes."
Vega M.A., Ezquerra A., Rojo S., Aparicio P., Bragado R., Lopez de Castro J.A.
Proc. Natl. Acad. Sci. U.S.A. 82:7394-7398(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 86-107 AND 171-181 (B*27:02).
[7]"Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) identifies a unique single amino acid substitution."
Choo S.Y., St John T., Orr H.T., Hansen J.A.
Hum. Immunol. 21:209-219(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*27:03).
[8]"The nucleotide sequence of HLA-B*2704 reveals a new amino acid substitution in exon 4 which is also present in HLA-B*2706."
Rudwaleit M., Bowness P., Wordsworth P.
Immunogenetics 43:160-162(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*27:04 AND B*27:06).
[9]"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients."
Coppin H.L., McDevitt H.O.
J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
[10]"Nucleotide sequence of HLA-B*2706."
Vilches C., de Pablo R., Kreisler M.
Immunogenetics 39:219-219(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:06).
[11]"A novel HLA-B27 allele maps B27 allospecificity to the region around position 70 in the alpha 1 domain."
Choo Y.S., Fan L.A., Hansen J.A.
J. Immunol. 147:174-180(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:07).
[12]"The HLA-B7Qui antigen is encoded by a new subtype of HLA-B27 (B*2708)."
Hildebrand W.H., Domena J.D., Shen S.Y., Marsh S.G.E., Bunce M., Guttridge M.G., Darke C., Parham P.
Tissue Antigens 44:47-51(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:08).
[13]"Identification of a novel HLA-B27 subtype by restriction analysis of a cytotoxic gamma/delta T cell clone."
Del Porto P., D'Amato M., Fiorillo M.T., Tuosto L., Piccolella E., Sorrentino R.
J. Immunol. 153:3093-3100(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:09).
Tissue: Blood.
[14]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
Tissue: Liver.
[15]"The three-dimensional structure of HLA-B27 at 2.1-A resolution suggests a general mechanism for tight peptide binding to MHC."
Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.
Cell 70:1035-1048(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300.
[16]"The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation."
Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.
Nature 353:321-325(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-300.
[17]"HLA-B27 subtypes differentially associated with disease exhibit subtle structural alterations."
Hulsmeyer M., Hillig R.C., Volz A., Ruhl M., Schroder W., Saenger W., Ziegler A., Uchanska-Ziegler B.
J. Biol. Chem. 277:47844-47853(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300.
[18]"Rational design of nonnatural peptides as high-affinity ligands for the HLA-B*2705 human leukocyte antigen."
Rognan D., Scapozza L., Folkers G., Daser A.
Proc. Natl. Acad. Sci. U.S.A. 92:753-757(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 115-206.
[19]"HLA-B27 in the Greek Cypriot population: distribution of subtypes in patients with ankylosing spondylitis and other HLA-B27-related diseases. The possible protective role of B*2707."
Varnavidou-Nicolaidou A., Karpasitou K., Georgiou D., Stylianou G., Kokkofitou A., Michalis C., Constantina C., Gregoriadou C., Kyriakides G.
Hum. Immunol. 65:1451-1454(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, POSSIBLE PROTECTIVE ROLE OF ALLELE B*27:07.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03945 Genomic DNA. Translation: CAA27578.1. Sequence problems.
X03664, X03667 Genomic DNA. Translation: CAA27301.1.
L38504 mRNA. Translation: AAA69724.1.
M54883 Genomic DNA. Translation: AAA59616.1.
X03665, X03666 Genomic DNA. Translation: CAA27302.1.
M12967 Genomic DNA. Translation: AAA36221.1.
U27608 mRNA. Translation: AAC50444.1.
U35734 mRNA. Translation: AAC50447.1.
M14013 Genomic DNA. Translation: AAA59643.1.
X73578 mRNA. Translation: CAA51980.1.
M62852 mRNA. Translation: AAA59647.1.
L19923 mRNA. Translation: AAA59658.1.
Z33453 mRNA. Translation: CAA83876.1.
PIRI37515.
I56116.
HLHUB2. S07441.
UniGeneHs.654404.
Hs.77961.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HSAX-ray2.10A/D25-300[»]
1JGDX-ray1.90A25-300[»]
1JGEX-ray2.10A25-300[»]
1K5NX-ray1.09A25-300[»]
1OF2X-ray2.20A25-300[»]
1OGTX-ray1.47A25-300[»]
1ROGmodel-A25-206[»]
1ROHmodel-A25-206[»]
1ROImodel-A25-206[»]
1ROJmodel-A25-206[»]
1ROKmodel-A25-206[»]
1ROLmodel-A25-206[»]
1UXSX-ray1.55A25-300[»]
1UXWX-ray1.71A25-300[»]
1W0VX-ray2.27A25-300[»]
1W0WX-ray2.10A25-300[»]
2A83X-ray1.40A25-300[»]
2BSRX-ray2.30A25-300[»]
2BSSX-ray2.00A25-300[»]
2BSTX-ray2.10A25-300[»]
3B3IX-ray1.86A25-300[»]
3B6SX-ray1.80A25-300[»]
3BP4X-ray1.85A25-300[»]
3BP7X-ray1.80A25-300[»]
3CZFX-ray1.20A25-300[»]
3D18X-ray1.74A25-300[»]
3DTXX-ray2.10A25-300[»]
3HCVX-ray1.95A25-300[»]
3LV3X-ray1.94A25-300[»]
4G8GX-ray2.40A25-300[»]
4G8IX-ray1.60A25-300[»]
4G9DX-ray1.60A25-300[»]
4G9FX-ray1.90A25-300[»]
ProteinModelPortalP03989.
SMRP03989. Positions 25-300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6188N.
IntActP03989. 1 interaction.
MINTMINT-247525.

Polymorphism databases

DMDM34305677.

Proteomic databases

PaxDbP03989.
PRIDEP03989.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000435618; ENSP00000405178; ENSG00000224608.

Organism-specific databases

GeneCardsGC06M031321.
GC06Ml31364.
HGNCHGNC:4932. HLA-B.
MIM106300. phenotype.
142830. gene.
neXtProtNX_P03989.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42056.
HOVERGENHBG016709.
InParanoidP03989.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

CleanExHS_HLA-B.
GenevestigatorP03989.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
IPR010579. MHC_I_a_C.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]
PRINTSPR01638. MHCCLASSI.
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHLA-B. human.
EvolutionaryTraceP03989.
SOURCESearch...

Entry information

Entry name1B27_HUMAN
AccessionPrimary (citable) accession number: P03989
Secondary accession number(s): O19692 expand/collapse secondary AC list , P10317, P10318, P19373, P30467, Q08136, Q29693, Q29846, Q29961
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: August 13, 1987
Last modified: March 19, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM