P01909 (DQA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	254 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	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 miroenvironment 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 apparatus › trans-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 process	Immunity
Cellular component	Cell membrane Endoplasmic reticulum Endosome Golgi apparatus Lysosome MHC II Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T 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 interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	ER 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 endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to plasma membrane Non-traceable author statement Ref.4Ref.1. Source: UniProtKB lysosomal membrane Traceable author statement. Source: Reactome trans-Golgi network membrane Traceable author statement. Source: Reactome
Molecular_function	MHC class II receptor activity Non-traceable author statement Ref.4Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.20

Chain

24 – 254

231

HLA class II histocompatibility antigen, DQ alpha 1 chain

PRO_0000018970

Regions

Topological domain

24 – 216

193

Extracellular Potential

Transmembrane

217 – 239

23

Helical; Potential

Topological domain

240 – 254

15

Cytoplasmic

Domain

112 – 204

93

Ig-like C1-type

Region

24 – 119

96

Alpha-1

Region

120 – 203

84

Alpha-2

Region

204 – 216

13

Connecting peptide

Amino acid modifications

Glycosylation

103

1

N-linked (GlcNAc...) Potential

Glycosylation

143

1

N-linked (GlcNAc...) Potential

Disulfide bond

132 ↔ 188

Ref.40 Ref.41 Ref.43

Natural variations

Natural variant

8

1

M → 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 variant

11

1

A → T in allele DQA1*05:05, allele DQA1*05:08 and allele DQA1*05:09.
Corresponds to variant rs1047992 [ dbSNP | Ensembl ].

VAR_033400

Natural variant

17

1

V → M in allele DQA1*01:04 and allele DQA1*01:05.
Corresponds to variant rs12722039 [ dbSNP | Ensembl ].

VAR_050380

Natural variant

18

1

M → T in allele DQA1*03:03.
Corresponds to variant rs12722040 [ dbSNP | Ensembl ].

VAR_050381

Natural variant

24

1

E → K in allele DQA1*05:09.
Corresponds to variant rs41545012 [ dbSNP | Ensembl ].

VAR_060493

Natural variant

25

1

D → G in allele DQA1*01:04 and allele DQA1*01:05.
Corresponds to variant rs12722042 [ dbSNP | Ensembl ].

VAR_050382

Natural variant

34

1

Y → 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 variant

41

1

S → 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 variant

44

1

P → L in allele DQA1*05:04.
Corresponds to variant rs41549715 [ dbSNP | Ensembl ].

VAR_060495

Natural variant

48

1

Y → 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 variant

49

1

T → S in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs3188011 [ dbSNP | Ensembl ].

VAR_033403

Natural variant

57

1

Q → 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 variant

63

1

G → 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 variant

64

1

R → K in allele DQA1*01:03.
Corresponds to variant rs36219699 [ dbSNP | Ensembl ].

VAR_050383

Natural variant

67

1

T → A in allele DQA1*01:06.
Corresponds to variant rs41543221 [ dbSNP | Ensembl ].

VAR_060497

Natural variant

68

1

V → 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 variant

70

1

C → K in allele DQA1*02:01; requires 2 nucleotide substitutions.

VAR_060499

Natural variant

70

1

C → Q in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; requires 2 nucleotide substitutions.

VAR_060500

Natural variant

70

1

C → 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 variant

70

1

C → Y.
Corresponds to variant rs3207983 [ dbSNP | Ensembl ].

VAR_033404

Natural variant

71

1

L → 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 variant

73

1

V → D.

VAR_033406

Natural variant

73

1

V → 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 variant

73

1

V → L in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.

VAR_033405

Natural variant

74

1

L → 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 variant

75

1

R → H in allele DQA1*02:01.

VAR_060505

Natural variant

75

1

R → 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 variant

76

1

Q → 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 variant

76

1

Q → R in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.

VAR_060508

Natural variant

77

1

F → L in allele DQA1*02:01.
Corresponds to variant rs3188043 [ dbSNP | Ensembl ].

VAR_060509

Natural variant

78

1

R → 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 variant

78

1

R → RR in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.

VAR_060511

Natural variant

78

1

R → S.
Corresponds to variant rs36219345 [ dbSNP | Ensembl ].

VAR_033407

Natural variant

81

1

P → R in allele DQA1*05:02.
Corresponds to variant rs41541412 [ dbSNP | Ensembl ].

VAR_060512

Natural variant

83

1

F → 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 variant

86

1

T → 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 variant

88

1

I → 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 variant

91

1

L → 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 variant

91

1

L → 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 variant

91

1

L → V.
Corresponds to variant rs1048085 [ dbSNP | Ensembl ].

VAR_033410

Natural variant

97

1

S → 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 variant

98

1

L → 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 variant

98

1

L → V in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.

VAR_060518

Natural variant

101

1

R → C in allele DQA1*01:07.

VAR_060519

Natural variant

102

1

S → 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 variant

124

1

L → V in allele DQA1*05:06.

VAR_060520

Natural variant

129

1

I → 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 variant

151

1

H → 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 variant

152

1

S → A in allele DQA1*01:03.

VAR_060521

Natural variant

160

1

T → I in allele DQA1*04:02.

VAR_060522

Natural variant

161

1

S → I in allele DQA1*05:08.

VAR_060524

Natural variant

161

1

S → R in allele DQA1*06:02.

VAR_060523

Natural variant

175

1

Y → H in allele DQA1*04:04.

VAR_060525

Natural variant

178

1

L → 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 variant

182

1

A → D in allele DQA1*03:02 and allele DQA1*03:03.

VAR_060527

Natural variant

182

1

A → S in allele DQA1*05:03, allele DQA1*05:06 and allele DQA1*05:07.

VAR_060528

Natural variant

183

1

E → 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 variant

185

1

S → 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 variant

197

1

K → 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 variant

197

1

K → 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 variant

209

1

A → T in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.
Corresponds to variant rs9272785 [ dbSNP | Ensembl ].

VAR_050387

Natural variant

221

1

A → T in allele DQA1*01:04.
Corresponds to variant rs35087390 [ dbSNP | Ensembl ].

VAR_050388

Natural variant

229

1

V → M in allele DQA1*01:02.
Corresponds to variant rs9260 [ dbSNP | Ensembl ].

VAR_033411

Natural variant

230

1

G → C in allele DQA1*05:07.

VAR_060533

Natural variant

237

1

F → 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 variant

240

1

R → 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 conflict

11

1

A → S in AAA59760. Ref.4

Sequence conflict

23 – 27

5

Missing in AAA59754. Ref.16

Sequence conflict

91

1

L → H in AAA59760. Ref.4

Sequence conflict

107

1

A → P in AAA59754. Ref.16

Sequence conflict

156

1

G → D in CAA25141. Ref.3

Sequence conflict

213

1

E → D in AAA59754. Ref.16

Secondary structure

1

.

.

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.

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.

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.

254

Helix Strand Turn

Details...

Beta strand

29 – 40

12

Turn

41 – 44

4

Beta strand

45 – 52

8

Beta strand

55 – 61

7

Turn

62 – 65

4

Beta strand

66 – 71

6

Helix

72 – 77

6

Helix

81 – 101

21

Turn

102 – 104

3

Beta strand

113 – 120

8

Beta strand

128 – 137

10

Beta strand

143 – 148

6

Beta strand

151 – 153

3

Beta strand

157 – 159

3

Beta strand

170 – 178

9

Beta strand

186 – 191

6

Beta strand

195 – 197

3

Beta strand

199 – 203

5

Sequences

	Sequence		Length	Mass (Da)
	P01909 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 84E12B5A80E2A028	FASTA	254	27,805
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

GeneReviews

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 , DQ178400, DQ178401, DQ178402 Genomic DNA. Translation: ABA86855.1.
DQ178407 , DQ178404, DQ178405, DQ178406 Genomic DNA. Translation: ABA86856.1.
DQ178411 , DQ178408, DQ178409, DQ178410 Genomic DNA. Translation: ABA86857.1.
DQ178415 , DQ178412, DQ178413, DQ178414 Genomic DNA. Translation: ABA86858.1.
M29616, M29613 Genomic DNA. Translation: AAA59759.1.
AF322870 , AF322867, AF322868, AF322869 Genomic DNA. Translation: AAK11577.1.
AF395700 , 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.

IPI

IPI00976055.

PIR

HLHUD1. A02211.
HLHUDQ. A02213.
HLHUD7. A02214.
HLHU3C. A02215.
HLHUDC. A93326.
B27628.
D34512.

RefSeq

NP_002113.2. NM_002122.3.
XP_003120317.1. XM_003120269.1.
XP_003846794.1. XM_003846746.1.

UniGene

Hs.387679.
Hs.591798.
Hs.706240.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JK8	X-ray	2.40	A	27-206	[»]
1NBN	model	-	A	27-206	[»]
1S9V	X-ray	2.22	A/D	24-216	[»]
1UVQ	X-ray	1.80	A	24-219	[»]
2NNA	X-ray	2.10	A	24-206	[»]
4GG6	X-ray	3.20	A/C	24-206	[»]

ProteinModelPortal

P01909.

ModBase

Search...

Protein-protein interaction databases

IntAct

P01909. 10 interactions.

Polymorphism databases

DMDM

122188.

Proteomic databases

PaxDb

P01909.

PRIDE

P01909.

Protocols and materials databases

DNASU

3117.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343139; ENSP00000339398; ENSG00000196735.
ENST00000374949; ENSP00000364087; ENSG00000196735.
ENST00000383251; ENSP00000372738; ENSG00000206305.
ENST00000395363; ENSP00000378767; ENSG00000196735.
ENST00000395364; ENSP00000378768; ENSG00000196735.
ENST00000399675; ENSP00000382583; ENSG00000206305.
ENST00000399678; ENSP00000382586; ENSG00000206305.
ENST00000418023; ENSP00000387892; ENSG00000232062.
ENST00000444296; ENSP00000413237; ENSG00000232062.

GeneID

100509457.
3117.

KEGG

hsa:100509457.
hsa:3117.

UCSC

uc011fnq.1. human.

Organism-specific databases

CTD

3117.

GeneCards

GC06P032595.
GC06Pn32538.
GC06Po32698.

HGNC

HGNC:4942. HLA-DQA1.

HPA

HPA012315.

MIM

146880. gene.

neXtProt

NX_P01909.

PharmGKB

PA35066.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG26577.

HOVERGEN

HBG006862.

InParanoid

P04226.

KO

K06752.

OrthoDB

EOG4KWJTP.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P01909.

Bgee

P01909.

CleanEx

HS_HLA-DQA1.

Genevestigator

P01909.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
3.10.320.10. 1 hit.

InterPro

IPR007110. 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]

Pfam

PF07654. C1-set. 1 hit.
PF00993. MHC_II_alpha. 1 hit.
[Graphical view]

SMART

SM00407. IGc1. 1 hit.
SM00920. MHC_II_alpha. 1 hit.
[Graphical view]

SUPFAM

SSF54452. MHC_I/II-like_Ag-recog. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HLA-DQA1. human.

EvolutionaryTrace

P01909.

NextBio

12366.

SOURCE

Search...

Entry information

Entry name

DQA1_HUMAN

Accession

Primary (citable) accession number: P01909
Secondary accession number(s): O19630 , 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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.