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P03989

- 1B27_HUMAN

UniProt

P03989 - 1B27_HUMAN

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Protein

HLA class I histocompatibility antigen, B-27 alpha chain

Gene

HLA-B

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

Functioni

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

GO - Molecular functioni

  1. peptide antigen binding Source: UniProt

GO - Biological processi

  1. antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent Source: UniProt
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
  5. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  6. cytokine-mediated signaling pathway Source: Reactome
  7. defense response Source: UniProtKB
  8. detection of bacterium Source: UniProtKB
  9. immune response Source: UniProtKB
  10. interferon-gamma-mediated signaling pathway Source: Reactome
  11. positive regulation of T cell mediated cytotoxicity Source: InterPro
  12. regulation of immune response Source: Reactome
  13. type I interferon signaling pathway Source: Reactome
  14. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Immunity

Enzyme and pathway databases

ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
REACT_111178. ER-Phagosome pathway.
REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
HLA class I histocompatibility antigen, B-27 alpha chain
Alternative name(s):
MHC class I antigen B*27
Gene namesi
Name:HLA-B
Synonyms:HLAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:4932. HLA-B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 308284ExtracellularSequence AnalysisAdd
BLAST
Transmembranei309 – 33224HelicalSequence AnalysisAdd
BLAST
Topological domaini333 – 36230CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProt
  2. early endosome membrane Source: Reactome
  3. endoplasmic reticulum Source: UniProt
  4. ER to Golgi transport vesicle membrane Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. Golgi apparatus Source: UniProt
  7. Golgi membrane Source: Reactome
  8. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  9. membrane Source: UniProtKB
  10. MHC class I protein complex Source: UniProt
  11. phagocytic vesicle membrane Source: Reactome
  12. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, MHC I

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

MIMi106300. phenotype.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 362338HLA class I histocompatibility antigen, B-27 alpha chainPRO_0000018839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
Disulfide bondi125 ↔ 188
Disulfide bondi227 ↔ 283

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiP03989.
PRIDEiP03989.

Expressioni

Gene expression databases

CleanExiHS_HLA-B.
GenevestigatoriP03989.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-6188N.
IntActiP03989. 1 interaction.
MINTiMINT-247525.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 3610Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 528Combined sources
Beta strandi55 – 617Combined sources
Beta strandi64 – 663Combined sources
Helixi74 – 763Combined sources
Helixi81 – 10828Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi157 – 1615Combined sources
Helixi162 – 17312Combined sources
Helixi176 – 18510Combined sources
Helixi187 – 19812Combined sources
Turni199 – 2046Combined sources
Beta strandi210 – 21910Combined sources
Beta strandi222 – 23514Combined sources
Beta strandi238 – 2436Combined sources
Helixi249 – 2513Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi265 – 27410Combined sources
Helixi278 – 2803Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi294 – 2963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP03989.
SMRiP03989. Positions 25-300.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03989.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini209 – 29587Ig-like C1-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 11490Alpha-1Add
BLAST
Regioni115 – 20692Alpha-2Add
BLAST
Regioni207 – 29892Alpha-3Add
BLAST
Regioni299 – 30810Connecting peptide

Sequence similaritiesi

Belongs to the MHC class I family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42056.
HOVERGENiHBG016709.
PhylomeDBiP03989.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiIPR007110. 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]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]
PRINTSiPR01638. MHCCLASSI.
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03989-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG
60 70 80 90 100
YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE
110 120 130 140 150
DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL
160 170 180 190 200
NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK
210 220 230 240 250
ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ
260 270 280 290 300
DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
310 320 330 340 350
SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS
360
DSAQGSDVSL TA
Length:362
Mass (Da):40,428
Last modified:August 13, 1987 - v2
Checksum:iC8D2F154E3292031
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061A → V(PubMed:3485286)Curated
Sequence conflicti266 – 2661Q → E AA sequence (PubMed:2408663)Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651A → T.1 Publication
Corresponds to variant rs1050529 [ dbSNP | Ensembl ].
VAR_056341
Natural varianti83 – 831Y → H in allele B*27:03.
VAR_016379
Natural varianti101 – 1011D → N in allele B*27:02.
VAR_016380
Natural varianti101 – 1011D → S in allele B*27:04, allele B*27:06 and allele B*27:08; requires 2 nucleotide substitutions.
VAR_016381
Natural varianti104 – 1052TL → IA in allele B*27:02.
VAR_016382
Natural varianti104 – 1041T → N in allele B*27:08.
VAR_016383
Natural varianti106 – 1072LR → RG in allele B*27:08.
VAR_016384
Natural varianti121 – 1211N → S in allele B*27:07.
VAR_016385
Natural varianti137 – 1382YH → HN in allele B*27:07.
VAR_016386
Natural varianti138 – 1381H → D in allele B*27:06.
VAR_016387
Natural varianti140 – 1401D → H in allele B*27:09.
VAR_016388
Natural varianti140 – 1401D → Y in allele B*27:06 and allele B*27:07.
VAR_016389
Natural varianti155 – 1551S → R in allele B*27:07.
VAR_016390
Natural varianti176 – 1761V → E in allele B*27:04 and allele B*27:06.
VAR_016391
Natural varianti235 – 2351A → G in allele B*27:04 and allele B*27:06.
VAR_016392
Natural varianti306 – 3061V → I.
Corresponds to variant rs1131500 [ dbSNP | Ensembl ].
VAR_056342
Natural varianti329 – 3291A → T.
Corresponds to variant rs1051488 [ dbSNP | Ensembl ].
VAR_056343
Natural varianti349 – 3491C → S.
Corresponds to variant rs2308655 [ dbSNP | Ensembl ].
VAR_061402
Natural varianti349 – 3491C → Y.
Corresponds to variant rs2308655 [ dbSNP | Ensembl ].
VAR_061403

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI37515.
I56116.
S07441. HLHUB2.
UniGeneiHs.654404.
Hs.77961.

Genome annotation databases

EnsembliENST00000435618; ENSP00000405178; ENSG00000224608.

Polymorphism databases

DMDMi34305677.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi I37515.
I56116.
S07441. HLHUB2.
UniGenei Hs.654404.
Hs.77961.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HSA X-ray 2.10 A/D 25-300 [» ]
1JGD X-ray 1.90 A 25-300 [» ]
1JGE X-ray 2.10 A 25-300 [» ]
1K5N X-ray 1.09 A 25-300 [» ]
1OF2 X-ray 2.20 A 25-300 [» ]
1OGT X-ray 1.47 A 25-300 [» ]
1ROG model - A 25-206 [» ]
1ROH model - A 25-206 [» ]
1ROI model - A 25-206 [» ]
1ROJ model - A 25-206 [» ]
1ROK model - A 25-206 [» ]
1ROL model - A 25-206 [» ]
1UXS X-ray 1.55 A 25-300 [» ]
1UXW X-ray 1.71 A 25-300 [» ]
1W0V X-ray 2.27 A 25-300 [» ]
1W0W X-ray 2.10 A 25-300 [» ]
2A83 X-ray 1.40 A 25-300 [» ]
2BSR X-ray 2.30 A 25-300 [» ]
2BSS X-ray 2.00 A 25-300 [» ]
2BST X-ray 2.10 A 25-300 [» ]
3B3I X-ray 1.86 A 25-300 [» ]
3B6S X-ray 1.80 A 25-300 [» ]
3BP4 X-ray 1.85 A 25-300 [» ]
3BP7 X-ray 1.80 A 25-300 [» ]
3CZF X-ray 1.20 A 25-300 [» ]
3D18 X-ray 1.74 A 25-300 [» ]
3DTX X-ray 2.10 A 25-300 [» ]
3HCV X-ray 1.95 A 25-300 [» ]
3LV3 X-ray 1.94 A 25-300 [» ]
4G8G X-ray 2.40 A 25-300 [» ]
4G8I X-ray 1.60 A 25-300 [» ]
4G9D X-ray 1.60 A 25-300 [» ]
4G9F X-ray 1.90 A 25-300 [» ]
ProteinModelPortali P03989.
SMRi P03989. Positions 25-300.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6188N.
IntActi P03989. 1 interaction.
MINTi MINT-247525.

Polymorphism databases

DMDMi 34305677.

Proteomic databases

PaxDbi P03989.
PRIDEi P03989.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000435618 ; ENSP00000405178 ; ENSG00000224608 .

Organism-specific databases

GeneCardsi GC06M031321.
GC06Ml31364.
HGNCi HGNC:4932. HLA-B.
MIMi 106300. phenotype.
142830. gene.
neXtProti NX_P03989.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42056.
HOVERGENi HBG016709.
PhylomeDBi P03989.

Enzyme and pathway databases

Reactomei REACT_111168. Endosomal/Vacuolar pathway.
REACT_111178. ER-Phagosome pathway.
REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSi HLA-B. human.
EvolutionaryTracei P03989.
SOURCEi Search...

Gene expression databases

CleanExi HS_HLA-B.
Genevestigatori P03989.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProi IPR007110. 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 ]
Pfami PF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view ]
PRINTSi PR01638. MHCCLASSI.
SMARTi SM00407. IGc1. 1 hit.
[Graphical view ]
SUPFAMi SSF54452. SSF54452. 1 hit.
PROSITEi PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry namei1B27_HUMAN
AccessioniPrimary (citable) accession number: P03989
Secondary accession number(s): O19692
, P10317, P10318, P19373, P30467, Q08136, Q29693, Q29846, Q29961
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: August 13, 1987
Last modified: November 26, 2014
This is version 155 of the entry and version 2 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

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3