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P01909 (DQA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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 II histocompatibility antigen, DQ alpha 1 chain
Alternative name(s):
DC-1 alpha chain
DC-alpha
HLA-DCA
MHC class II DQA1
Gene names
Name:HLA-DQA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.

Subunit structure

Heterodimer of an alpha and a beta subunit; also referred as MHC class II molecule. In the endoplasmic reticulum (ER) it forms a heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system; CD74 undergoes sequential degradation by various proteases; leaving a small fragment termed CLIP on each MHC class II molecule. MHC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP and facilitate the binding of antigenic peptides. Ref.40 Ref.41 Ref.42 Ref.43

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note: The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation.

Polymorphism

The following alleles of DQA1 are known: DQA1*01:01, DQA1*01:02, DQA1*01:03, DQA1*01:04, DQA1*01:05, DQA1*01:06, DQA1*01:07, DQA1*02:01, DQA1*03:01, DQA1*03:02, DQA1*03:03, DQA1*04:01, DQA1*04:02, DQA1*04:03, DQA1*04:04, DQA1*05:01, DQA1*05:02, DQA1*05:03, DQA1*05:04, DQA1*05:05, DQA1*05:06, DQA1*05:07, DQA1*05:08, DQA1*05:09, DQA1*06:01, DQA1*06:02. The sequence shown is that of DQA1*05:01.

DQ2 (heterodimer of DQA1*05:01/DQB1*02:01) is associated with more than 90% of celiac disease patients. A minority displays DQ8 (heterodimer of DQA1*03/DQB1*03:02). DQ0602 (heterodimer of DQA1*01:02/DQB1*06:02) confers dominant protection against type 1 diabetes (T1D) and strong susceptibility to narcolepsy.

Sequence similarities

Belongs to the MHC class II family.

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

Sequence caution

The sequence AAD56720.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Membrane
MHC II
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

immune response

Non-traceable author statement Ref.4Ref.1. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Traceable author statement. Source: Reactome

MHC class II protein complex

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of plasma membrane

Non-traceable author statement Ref.4Ref.1. Source: UniProtKB

lysosomal membrane

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

trans-Golgi network membrane

Traceable author statement. Source: Reactome

transport vesicle membrane

Traceable author statement. Source: Reactome

   Molecular_functionMHC class II receptor activity

Non-traceable author statement Ref.4Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.20
Chain24 – 254231HLA class II histocompatibility antigen, DQ alpha 1 chain
PRO_0000018970

Regions

Topological domain24 – 216193Extracellular Potential
Transmembrane217 – 23923Helical; Potential
Topological domain240 – 25415Cytoplasmic
Domain112 – 20493Ig-like C1-type
Region24 – 11996Alpha-1
Region120 – 20384Alpha-2
Region204 – 21613Connecting peptide

Amino acid modifications

Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Disulfide bond132 ↔ 188 Ref.40 Ref.41 Ref.43

Natural variations

Natural variant81M → L in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*04:01 and allele DQA1*06:01.
Corresponds to variant rs1047989 [ dbSNP | Ensembl ].
VAR_033399
Natural variant111A → T in allele DQA1*05:05, allele DQA1*05:08 and allele DQA1*05:09.
Corresponds to variant rs1047992 [ dbSNP | Ensembl ].
VAR_033400
Natural variant171V → M in allele DQA1*01:04 and allele DQA1*01:05.
Corresponds to variant rs12722039 [ dbSNP | Ensembl ].
VAR_050380
Natural variant181M → T in allele DQA1*03:03.
Corresponds to variant rs12722040 [ dbSNP | Ensembl ].
VAR_050381
Natural variant241E → K in allele DQA1*05:09.
Corresponds to variant rs41545012 [ dbSNP | Ensembl ].
VAR_060493
Natural variant251D → G in allele DQA1*01:04 and allele DQA1*01:05.
Corresponds to variant rs12722042 [ dbSNP | Ensembl ].
VAR_050382
Natural variant341Y → C in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1129740 [ dbSNP | Ensembl ].
VAR_060494
Natural variant411S → F in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1071630 [ dbSNP | Ensembl ].
VAR_033401
Natural variant441P → L in allele DQA1*05:04.
Corresponds to variant rs41549715 [ dbSNP | Ensembl ].
VAR_060495
Natural variant481Y → F in allele DQA1*02:01, allele DQA1*01:03, allele DQA1*06:01 and allele DQA1*06:02.
Corresponds to variant rs12722051 [ dbSNP | Ensembl ].
VAR_033402
Natural variant491T → S in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs3188011 [ dbSNP | Ensembl ].
VAR_033403
Natural variant571Q → E in allele DQA1*01:01, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs10093 [ dbSNP | Ensembl ].
VAR_014604
Natural variant631G → E in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs1142323 [ dbSNP | Ensembl ].
VAR_060496
Natural variant641R → K in allele DQA1*01:03.
Corresponds to variant rs36219699 [ dbSNP | Ensembl ].
VAR_050383
Natural variant671T → A in allele DQA1*01:06.
Corresponds to variant rs41543221 [ dbSNP | Ensembl ].
VAR_060497
Natural variant681V → A in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1142324 [ dbSNP | Ensembl ].
VAR_060498
Natural variant701C → K in allele DQA1*02:01; requires 2 nucleotide substitutions.
VAR_060499
Natural variant701C → Q in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; requires 2 nucleotide substitutions.
VAR_060500
Natural variant701C → R in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
VAR_060501
Natural variant701C → Y.
Corresponds to variant rs3207983 [ dbSNP | Ensembl ].
VAR_033404
Natural variant711L → W in allele DQA1*01:01, allele DQA1*01:02,allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1142328 [ dbSNP | Ensembl ].
VAR_060502
Natural variant731V → D.
VAR_033406
Natural variant731V → E in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs3208105 [ dbSNP | Ensembl ].
VAR_060503
Natural variant731V → L in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
VAR_033405
Natural variant741L → F in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs9272698 [ dbSNP | Ensembl ].
VAR_060504
Natural variant751R → H in allele DQA1*02:01.
VAR_060505
Natural variant751R → S in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs9272699 [ dbSNP | Ensembl ].
VAR_060506
Natural variant761Q → K in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1048052 [ dbSNP | Ensembl ].
VAR_060507
Natural variant761Q → R in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
VAR_060508
Natural variant771F → L in allele DQA1*02:01.
Corresponds to variant rs3188043 [ dbSNP | Ensembl ].
VAR_060509
Natural variant781R → GG in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05,allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs4193 [ dbSNP | Ensembl ].
VAR_060510
Natural variant781R → RR in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
VAR_060511
Natural variant781R → S.
Corresponds to variant rs36219345 [ dbSNP | Ensembl ].
VAR_033407
Natural variant811P → R in allele DQA1*05:02.
Corresponds to variant rs41541412 [ dbSNP | Ensembl ].
VAR_060512
Natural variant831F → G in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07; requires 2 nucleotide substitutions.
VAR_060513
Natural variant861T → R in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1048073 [ dbSNP | Ensembl ].
VAR_033408
Natural variant881I → M in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1048080 [ dbSNP | Ensembl ].
VAR_033409
Natural variant911L → A in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07; requires 2 nucleotide substitutions.
VAR_060514
Natural variant911L → T in allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02; requires 2 nucleotide substitutions.
VAR_060515
Natural variant911L → V.
Corresponds to variant rs1048085 [ dbSNP | Ensembl ].
VAR_033410
Natural variant971S → I in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.
VAR_060516
Natural variant981L → M in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
VAR_060517
Natural variant981L → V in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
VAR_060518
Natural variant1011R → C in allele DQA1*01:07.
VAR_060519
Natural variant1021S → Y in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.
Corresponds to variant rs1129808 [ dbSNP | Ensembl ].
VAR_050384
Natural variant1241L → V in allele DQA1*05:06.
VAR_060520
Natural variant1291I → T in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.
Corresponds to variant rs707952 [ dbSNP | Ensembl ].
VAR_050385
Natural variant1511H → Q in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07.
Corresponds to variant rs707950 [ dbSNP | Ensembl ].
VAR_050386
Natural variant1521S → A in allele DQA1*01:03.
VAR_060521
Natural variant1601T → I in allele DQA1*04:02.
VAR_060522
Natural variant1611S → I in allele DQA1*05:08.
VAR_060524
Natural variant1611S → R in allele DQA1*06:02.
VAR_060523
Natural variant1751Y → H in allele DQA1*04:04.
VAR_060525
Natural variant1781L → F in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.
Corresponds to variant rs707949 [ dbSNP | Ensembl ].
VAR_060526
Natural variant1821A → D in allele DQA1*03:02 and allele DQA1*03:03.
VAR_060527
Natural variant1821A → S in allele DQA1*05:03, allele DQA1*05:06 and allele DQA1*05:07.
VAR_060528
Natural variant1831E → D in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.
Corresponds to variant rs707963 [ dbSNP | Ensembl ].
VAR_060529
Natural variant1851S → I in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.
VAR_060530
Natural variant1971K → E in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.
VAR_060531
Natural variant1971K → Q in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07.
VAR_060532
Natural variant2091A → T in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs9272785 [ dbSNP | Ensembl ].
VAR_050387
Natural variant2211A → T in allele DQA1*01:04.
Corresponds to variant rs35087390 [ dbSNP | Ensembl ].
VAR_050388
Natural variant2291V → M in allele DQA1*01:02.
Corresponds to variant rs9260 [ dbSNP | Ensembl ].
VAR_033411
Natural variant2301G → C in allele DQA1*05:07.
VAR_060533
Natural variant2371F → L in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs1048430 [ dbSNP | Ensembl ].
VAR_033412
Natural variant2401R → Q in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04 and allele DQA1*01:05.
Corresponds to variant rs9272793 [ dbSNP | Ensembl ].
VAR_033413

Experimental info

Sequence conflict111A → S in AAA59760. Ref.4
Sequence conflict23 – 275Missing in AAA59754. Ref.16
Sequence conflict911L → H in AAA59760. Ref.4
Sequence conflict1071A → P in AAA59754. Ref.16
Sequence conflict1561G → D in CAA25141. Ref.3
Sequence conflict2131E → D in AAA59754. Ref.16

Secondary structure

.................................. 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01909 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 84E12B5A80E2A028

FASTA25427,805
        10         20         30         40         50         60 
MILNKALMLG ALALTTVMSP CGGEDIVADH VASYGVNLYQ SYGPSGQYTH EFDGDEQFYV 

        70         80         90        100        110        120 
DLGRKETVWC LPVLRQFRFD PQFALTNIAV LKHNLNSLIK RSNSTAATNE VPEVTVFSKS 

       130        140        150        160        170        180 
PVTLGQPNIL ICLVDNIFPP VVNITWLSNG HSVTEGVSET SFLSKSDHSF FKISYLTLLP 

       190        200        210        220        230        240 
SAEESYDCKV EHWGLDKPLL KHWEPEIPAP MSELTETVVC ALGLSVGLVG IVVGTVFIIR 

       250 
GLRSVGASRH QGPL 

« Hide

References

« Hide 'large scale' references
[1]"The heavy chain of human B-cell alloantigen HLA-DS has a variable N-terminal region and a constant immunoglobulin-like region."
Chang H.-C., Moriuchi T., Silver J.
Nature 305:813-815(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*02:01).
[2]"Both alpha and beta chains of HLA-DC class II histocompatibility antigens display extensive polymorphism in their amino-terminal domains."
Schenning L., Larhammar D., Bill P., Wiman K., Jonsson A.-K., Rask L., Peterson P.A.
EMBO J. 3:447-452(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*05:01).
[3]"Isotypic and allotypic variation of human class II histocompatibility antigen alpha-chain genes."
Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D., Strominger J.L.
Nature 308:327-333(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DQA1*01:02 AND ALLELE DQA1*03:01).
[4]"Complete sequence of the HLA DQ alpha and DQ beta cDNA from a DR5/DQw3 cell line."
Schiffenbauer J., Didier D.K., Klearman M., Rice K., Shuman S., Tieber V.L., Kittlesen D.J., Schwartz B.D.
J. Immunol. 139:228-233(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*05:01).
[5]"HLA class II haplotype and sequence analysis support a role for DQ in narcolepsy."
Ellis M.C., Hetisimer A.H., Ruddy D.A., Hansen S.L., Kronmal G.S., McClelland E., Quintana L., Drayna D.T., Aldrich M.S., Mignot E.
Immunogenetics 46:410-417(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*05:01).
[6]"Ancient haplotypes of the HLA Class II region."
Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.
Genome Res. 15:1250-1257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:01; DQA1*01:02 AND DQA1*03:01).
[7]"Four novel human leukocyte antigen-DQA1 alleles identified in the Korean population."
Lee K.W., Jung Y.A., Oh D.H.
Tissue Antigens 68:167-172(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:02; DQA1*05:06; DQA1*05:07 AND DQA1*05:08).
[8]"Class II genes of the human major histocompatibility complex. Comparisons of the DQ and DX alpha and beta genes."
Jonsson A.-K., Hyldig-Nielsen J.-J., Servenius B., Larhammar D., Andersson G., Joergensen F., Peterson P.A., Rask L.
J. Biol. Chem. 262:8767-8777(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*03:01).
[9]"Identification of a novel DQA1 allele, DQA1*01012, and confirmatory sequence of DQA1*01011."
Ashdown M.L., Leas L., Gavrilidis A., Wood J.M., Simons M.J.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*01:01).
[10]"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQA1*02:01).
[11]"New and confirmatory HLA sequences by SBT."
Voorter C.E., van den Berg-Loonen E.M.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:02 AND DQA1*05:09).
[12]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQA1*01:01).
Tissue: Trachea.
[13]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DQA1*01:02; DQA1*03:01 AND DQA1*05:01).
[14]"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] (ALLELES DQA1*03:01 AND DQA1*05:01).
Tissue: Lymph.
[15]"Sequence polymorphisms in HLA-DQA1 exon1."
Yasunaga S., Kimura A., Sasazuki T.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-27 (ALLELES DQA1*01:01/DQA1*01:02/DQA1*01:03; DQA1*01:04; DQA1*01:05; DQA1*02:01/DQA1*03:01/DQA1*03:03; DQA1*04:01/DQA1*06:01 AND DQA1*05:01/DQA1*05:03/DQA1*05:05).
Tissue: B-cell.
[16]"Nucleotide sequence of an HLA-DQ alpha chain derived from a DRw9 cell line: genetic and evolutionary implications."
Moriuchi J., Moriuchi T., Silver J.
Proc. Natl. Acad. Sci. U.S.A. 82:3420-3424(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-254 (ALLELE DQA1*03:02).
[17]"MHC class II sequences of an HLA-DR2 narcoleptic."
Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.
Immunogenetics 27:449-455(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-254 (ALLELE DQA1*01:02).
[18]"Different contribution of HLA-DR and -DQ genes in susceptibility and resistance to insulin-dependent diabetes mellitus (IDDM)."
Yasunaga S., Kimura A., Hamaguchi K., Ronningen K.S., Sasazuki T.
Tissue Antigens 47:37-48(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-250 (ALLELE DQA1*03:02/DQA1*03:03) AND NUCLEOTIDE SEQUENCE [MRNA] OF 24-249 (ALLELES DQA1*01:01; DQA1*01:03; DQA1*01:04; DQA1*04:01; DQA1*05:03; DQA1*05:05 AND DQA1*06:01).
[19]Yasunaga S.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-249 (ALLELE DQA1*01:05).
[20]"Primary structure of human class II histocompatibility antigens 3rd communication. Amino acid sequence comparison between DR and DC subclass antigens derived from a lymphoblastoid B cell line homozygous at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1)."
Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E., Koelbel S., Egert G., Wernet P., Hilschmann N.
Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-89; 102-120 AND 164-212 (ALLELE DQA1*01:02).
[21]"Molecular analysis of the HLA class II genes in two DRw6-related haplotypes, DRw13 DQw1 and DRw14 DQw3."
Kao H.T., Gregersen P.K., Tang J.C., Takahashi T., Wang C.Y., Silver J.
J. Immunol. 142:1743-1747(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-209 (ALLELE DQA1*05:01).
[22]"High-resolution genotyping of HLA-DQA1 in the GoKinD study and identification of novel alleles HLA-DQA1*040102, HLA-DQA1*0402 and HLA-DQA1*0404."
Cordovado S.K., Hancock L.N., Simone A.E., Hendrix M., Mueller P.W.
Tissue Antigens 65:448-458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELES DQA1*04:02 AND DQA1*04:04).
[23]"Identification of a novel HLA-DQA1*06 allele detected by sequence-based typing."
Simone A.E., Cordovado S.K., Hendrix M.M., Mueller P.W.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELE DQA1*06:02).
[24]"Identification of a novel HLA-DQA1*01 allele detected by sequence-based typing."
Hancock L.N., Cordovado S.K., Mueller P.W.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELE DQA1*01:07).
[25]"Sequence analysis of HLA class II genes from insulin-dependent diabetic individuals."
Horn G.T., Bugawan T.L., Long C.M., Manos M.M., Erlich H.A.
Hum. Immunol. 21:249-263(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-110 (ALLELE DQA1*01:02), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-109 (ALLELE DQA1*05:01).
[26]"DQA1 subtyping in Australian Aborigines. Additional evidence for heterogeneity."
Trejaut J.A., Greville W.D., Dunckley H.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-109 (ALLELE DQA1*05:04).
[27]"Identification of a novel HLA-DQA1 allele (DQA1*0106) by sequence-based DQA1 typing."
Luo M., Blanchard J., Maclean I., Brunham R.
Tissue Antigens 53:595-596(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-109 (ALLELE DQA1*01:06).
[28]"HLA class II nucleotide sequences, 1992."
Marsh S.G., Bodomer J.G.
Tissue Antigens 40:229-243(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-74 (ALLELE DQA1*05:02).
[29]"Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype. Multiple genetic mechanisms in the generation of polymorphic HLA class II genes."
Liu C.P., Bach F.H., Wu S.K.
J. Immunol. 140:3631-3639(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-254 (ALLELE DQA1*05:01).
[30]Erratum
Liu C.P., Bach F.H., Wu S.K.
J. Immunol. 144:15441-15441(1990)
[31]"cDNA clone for the heavy chain of the human B cell alloantigen DC1: strong sequence homology to the HLA-DR heavy chain."
Auffray C., Korman A.J., Roux-Dosseto M., Bono R., Strominger J.L.
Proc. Natl. Acad. Sci. U.S.A. 79:6337-6341(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-254 (ALLELE DQA1*03:01).
[32]"Ancient roots for polymorphism at the HLA-DQ alpha locus in primates."
Gyllensten U.B., Erlich H.A.
Proc. Natl. Acad. Sci. U.S.A. 86:9986-9990(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-102 (ALLELE DQA1*05:01), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-103 (ALLELE DQA1*01:02).
[33]"Allelic forms of the alpha- and beta-chain genes encoding DQw1-positive heterodimers."
Turco E., Care A., Compagnone-Post P., Robinson C., Cascino I., Trucco M.
Immunogenetics 26:282-290(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-254 (ALLELE DQA1*01:02).
[34]"Invariant chain structure and MHC class II function."
Cresswell P.
Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[35]"Presentation of antigens by MHC class II molecules: getting the most out of them."
Villadangos J.A.
Mol. Immunol. 38:329-346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[36]"Autophagy in MHC class II presentation: sampling from within."
Menendez-Benito V., Neefjes J.
Immunity 26:1-3(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[37]"MHC class II molecules on the move for successful antigen presentation."
Rocha N., Neefjes J.
EMBO J. 27:1-5(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[38]"MHC class II transport at a glance."
Berger A.C., Roche P.A.
J. Cell Sci. 122:1-4(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[39]"CD74 in antigen presentation, inflammation, and cancers of the gastrointestinal tract."
Beswick E.J., Reyes V.E.
World J. Gastroenterol. 15:2855-2861(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[40]"Structure of a human insulin peptide-HLA-DQ8 complex and susceptibility to type 1 diabetes."
Lee K.H., Wucherpfennig K.W., Wiley D.C.
Nat. Immunol. 2:501-507(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 27-207 OF HLA-DQA1/HLA-DQB1 HETERODIMER IN COMPLEX WITH INS PEPTIDE, SUBUNIT, GLYCOSYLATION AT ASN-103, DISULFIDE BOND.
[41]"Crystal structure of HLA-DQ0602 that protects against type 1 diabetes and confers strong susceptibility to narcolepsy."
Siebold C., Hansen B.E., Wyer J.R., Harlos K., Esnouf R.E., Svejgaard A., Bell J.I., Strominger J.L., Jones E.Y., Fugger L.
Proc. Natl. Acad. Sci. U.S.A. 101:1999-2004(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-219 OF HLA-DQA1/HLA-DQB1 HETERODIMER (HLA-DQ0602) IN COMPLEX WITH HCRT PEPTIDE, POLYMORPHISM, SUBUNIT, DISULFIDE BOND.
[42]"Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease."
Kim C.Y., Quarsten H., Bergseng E., Khosla C., Sollid L.M.
Proc. Natl. Acad. Sci. U.S.A. 101:4175-4179(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 24-216 OF HLA-DQA1/HLA-DQB1 HETERODIMER (DQ2) IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN PEPTIDE, SUBUNIT, POLYMORPHISM.
[43]"A structural and immunological basis for the role of human leukocyte antigen DQ8 in celiac disease."
Henderson K.N., Tye-Din J.A., Reid H.H., Chen Z., Borg N.A., Beissbarth T., Tatham A., Mannering S.I., Purcell A.W., Dudek N.L., van Heel D.A., McCluskey J., Rossjohn J., Anderson R.P.
Immunity 27:23-34(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-206 OF HLA-DQA1/HLA-DQB1 HETERODIMER IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN, SUBUNIT, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00033 mRNA. Translation: CAA24917.1.
X00370 mRNA. No translation available.
X00452 mRNA. Translation: CAA25141.1.
M16995 mRNA. Translation: AAA59760.1.
U92032 Genomic DNA. Translation: AAB91990.1.
AY663395 Genomic DNA. Translation: AAU87978.1.
AY663398 Genomic DNA. Translation: AAU87987.1.
AY663400 Genomic DNA. Translation: AAU87992.1.
AY663406 Genomic DNA. Translation: AAU88007.1.
AY663411 Genomic DNA. Translation: AAU88022.1.
AY663413 Genomic DNA. Translation: AAU88028.1.
DQ178403 expand/collapse EMBL AC list , DQ178400, DQ178401, DQ178402 Genomic DNA. Translation: ABA86855.1.
DQ178407 expand/collapse EMBL AC list , DQ178404, DQ178405, DQ178406 Genomic DNA. Translation: ABA86856.1.
DQ178411 expand/collapse EMBL AC list , DQ178408, DQ178409, DQ178410 Genomic DNA. Translation: ABA86857.1.
DQ178415 expand/collapse EMBL AC list , DQ178412, DQ178413, DQ178414 Genomic DNA. Translation: ABA86858.1.
M29616, M29613 Genomic DNA. Translation: AAA59759.1.
AF322870 expand/collapse EMBL AC list , AF322867, AF322868, AF322869 Genomic DNA. Translation: AAK11577.1.
AF395700 expand/collapse EMBL AC list , AF395697, AF395698, AF395699 Genomic DNA. Translation: AAM69677.1.
CR450297 mRNA. Translation: CAG29293.1.
AM042559 Genomic DNA. Translation: CAJ14960.1.
AM042560 Genomic DNA. Translation: CAJ14961.1.
AK313975 mRNA. Translation: BAG36689.1.
BX248406 Genomic DNA. Translation: CAM26191.1.
AL662789 Genomic DNA. Translation: CAI18230.1.
Z84489 Genomic DNA. Translation: CAB06491.1.
BC008585 mRNA. Translation: AAH08585.1.
BC157865 mRNA. Translation: AAI57866.1.
L46875 mRNA. No translation available.
L46876 mRNA. No translation available.
L46877 mRNA. No translation available.
L46878 mRNA. No translation available.
L46880 mRNA. No translation available.
L46881 mRNA. No translation available.
M11124 mRNA. Translation: AAA59754.1.
M20431 mRNA. Translation: AAA59758.1.
L34082 mRNA. Translation: AAC41950.1.
L34085 mRNA. Translation: AAC41953.1.
L34086 mRNA. Translation: AAC41954.1.
L34089 mRNA. Translation: AAC41957.1.
L34090 mRNA. Translation: AAC41958.1.
L34092 mRNA. Translation: AAC41960.1.
L34093 mRNA. Translation: AAC41961.1.
L34094 mRNA. Translation: AAC41962.1.
L42625 mRNA. Translation: AAA85334.1.
AY197775 Genomic DNA. Translation: AAO45622.1.
AY547314 Genomic DNA. Translation: AAS49496.1.
AY206406 Genomic DNA. Translation: AAO47362.1.
AY585236 Genomic DNA. Translation: AAT09985.1.
M34997 Genomic DNA. Translation: AAA35772.1.
M34999 Genomic DNA. Translation: AAA74633.1.
U85035 Genomic DNA. Translation: AAB41891.1.
AF109734 Genomic DNA. Translation: AAD56720.1. Sequence problems.
U03675 Genomic DNA. Translation: AAB60341.1.
M20506 mRNA. Translation: AAA59774.1.
J00199 mRNA. No translation available.
M17846 mRNA. Translation: AAA59707.1.
PIRHLHUD1. A02211.
HLHUDQ. A02213.
HLHUD7. A02214.
HLHU3C. A02215.
HLHUDC. A93326.
B27628.
D34512.
RefSeqNP_002113.2. NM_002122.3.
XP_003120317.1. XM_003120269.3.
XP_005275010.1. XM_005274953.2.
XP_005275165.1. XM_005275108.2.
XP_005275599.1. XM_005275542.2.
XP_005276137.1. XM_005276080.2.
XP_006725547.1. XM_006725484.1.
XP_006726062.1. XM_006725999.1.
UniGeneHs.387679.
Hs.591798.
Hs.706240.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JK8X-ray2.40A27-206[»]
1NBNmodel-A27-206[»]
1S9VX-ray2.22A/D24-216[»]
1UVQX-ray1.80A24-218[»]
2NNAX-ray2.10A24-206[»]
4GG6X-ray3.20A/C24-206[»]
4OZFX-ray2.70A24-206[»]
4OZGX-ray3.00A/C24-206[»]
4OZHX-ray2.80A/C24-206[»]
4OZIX-ray3.20A/C24-206[»]
ProteinModelPortalP01909.
SMRP01909. Positions 27-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109362. 8 interactions.
IntActP01909. 10 interactions.

Polymorphism databases

DMDM122188.

Proteomic databases

MaxQBP01909.
PaxDbP01909.
PRIDEP01909.

Protocols and materials databases

DNASU3117.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343139; ENSP00000339398; ENSG00000196735.
ENST00000374949; ENSP00000364087; ENSG00000196735.
ENST00000383251; ENSP00000372738; ENSG00000206305.
ENST00000395363; ENSP00000378767; ENSG00000196735.
ENST00000399675; ENSP00000382583; ENSG00000206305.
ENST00000399678; ENSP00000382586; ENSG00000206305.
ENST00000418023; ENSP00000387892; ENSG00000232062.
ENST00000444296; ENSP00000413237; ENSG00000232062.
GeneID100509457.
3117.
KEGGhsa:100509457.
hsa:3117.
UCSCuc011fnq.1. human.

Organism-specific databases

CTD3117.
GeneCardsGC06P032595.
GC06Pn32538.
GC06Po32698.
GeneReviewsHLA-DQA1.
HGNCHGNC:4942. HLA-DQA1.
HPAHPA012315.
MIM146880. gene.
neXtProtNX_P01909.
Orphanet555. Celiac disease.
243377. Diabetes mellitus type 1.
PharmGKBPA35066.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26577.
HOVERGENHBG006862.
InParanoidP04226.
KOK06752.
OMAHWEPEIS.
PhylomeDBP01909.
TreeFamTF333797.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP01909.
BgeeP01909.
CleanExHS_HLA-DQA1.
GenevestigatorP01909.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011162. MHC_I/II-like_Ag-recog.
IPR014745. MHC_II_a/b_N.
IPR001003. MHC_II_a_N.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00993. MHC_II_alpha. 1 hit.
[Graphical view]
SMARTSM00407. IGc1. 1 hit.
SM00920. MHC_II_alpha. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHLA-DQA1. human.
EvolutionaryTraceP01909.
NextBio12366.
PROP01909.
SOURCESearch...

Entry information

Entry nameDQA1_HUMAN
AccessionPrimary (citable) accession number: P01909
Secondary accession number(s): O19630 expand/collapse secondary AC list , O19706, P01907, P01908, P04225, P04226, P05536, P79553, Q06751, Q29876, Q29994, Q2Q6Y6, Q2Q6Y7, Q2Q6Y8, Q2WCM3, Q30064, Q30067, Q30068, Q30070, Q30071, Q30072, Q30073, Q30086, Q30101, Q5Y7D5, Q5Y7F5, Q6ICU6, Q6PR46, Q6QDB1, Q860W2, Q860W4, Q9BD37, Q9TPM3, Q9UM31
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 141 of the entry and version 1 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