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Protein

HLA class II histocompatibility antigen, DR alpha chain

Gene

HLA-DRA

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

Functioni

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.

GO - Molecular functioni

  • MHC class II protein complex binding Source: UniProtKB
  • MHC class II receptor activity Source: UniProtKB
  • peptide antigen binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Immunity

Enzyme and pathway databases

BioCyciZFISH:G66-33430-MONOMER.
ReactomeiR-HSA-202424. Downstream TCR signaling.
R-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-202430. Translocation of ZAP-70 to Immunological synapse.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-389948. PD-1 signaling.
R-HSA-877300. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
HLA class II histocompatibility antigen, DR alpha chain
Alternative name(s):
MHC class II antigen DRA
Gene namesi
Name:HLA-DRA
Synonyms:HLA-DRA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4947. HLA-DRA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 216ExtracellularSequence analysisAdd BLAST191
Transmembranei217 – 239HelicalSequence analysisAdd BLAST23
Topological domaini240 – 254CytoplasmicSequence analysisAdd BLAST15

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • clathrin-coated endocytic vesicle membrane Source: Reactome
  • endocytic vesicle membrane Source: Reactome
  • ER to Golgi transport vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: Reactome
  • integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  • integral component of plasma membrane Source: UniProtKB
  • late endosome membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: MGI
  • MHC class II protein complex Source: UniProtKB
  • plasma membrane Source: MGI
  • trans-Golgi network membrane Source: Reactome
  • transport vesicle membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, MHC II

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi244K → R: Almost no change in down-regulation of MHC class II. No ubiquitination and complete loss of down-regulation of MHC class II; when associated with 'R-254' of HLA-DRB. 1 Publication1

Organism-specific databases

DisGeNETi3122.
MalaCardsiHLA-DRA.
MIMi610424. phenotype.
OpenTargetsiENSG00000206308.
ENSG00000226260.
ENSG00000228987.
ENSG00000230726.
ENSG00000234794.
Orphaneti505. Graham Little-Piccardi-Lassueur syndrome.
PharmGKBiPA35071.

Protein family/group databases

Allergomei8362. Hom s HLA-DR-alpha.

Polymorphism and mutation databases

BioMutaiHLA-DRA.
DMDMi122206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 253 PublicationsAdd BLAST25
ChainiPRO_000001894726 – 254HLA class II histocompatibility antigen, DR alpha chainAdd BLAST229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi103N-linked (GlcNAc...)2 Publications1
Disulfide bondi132 ↔ 188PROSITE-ProRule annotation5 Publications
Glycosylationi143N-linked (GlcNAc...)2 Publications1
Cross-linki244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated by MARCH1 or MARCH8 at Lys-244 leading to down-regulation of MHC class II. When associated with ubiquitination of the beta subunit of HLA-DR: HLA-DRB4 'Lys-254', the down-regulation of MHC class II may be highly effective.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP01903.
MaxQBiP01903.
PaxDbiP01903.
PeptideAtlasiP01903.
PRIDEiP01903.

PTM databases

iPTMnetiP01903.
PhosphoSitePlusiP01903.

Expressioni

Gene expression databases

BgeeiENSG00000204287.
CleanExiHS_HLA-DRA.
ExpressionAtlasiP01903. baseline and differential.
GenevisibleiP01903. HS.

Organism-specific databases

HPAiCAB002798.
CAB015402.
HPA050162.
HPA053176.

Interactioni

Subunit structurei

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. Interacts with Epstein-Barr virus BZLF2/gp42.8 Publications

GO - Molecular functioni

  • MHC class II protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109367. 43 interactors.
DIPiDIP-6063N.
IntActiP01903. 10 interactors.
MINTiMINT-203259.
STRINGi9606.ENSP00000378786.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 40Combined sources13
Turni41 – 43Combined sources3
Beta strandi44 – 51Combined sources8
Beta strandi54 – 60Combined sources7
Turni61 – 64Combined sources4
Beta strandi65 – 70Combined sources6
Helixi71 – 75Combined sources5
Helixi82 – 101Combined sources20
Turni102 – 104Combined sources3
Beta strandi113 – 120Combined sources8
Beta strandi124 – 126Combined sources3
Beta strandi128 – 140Combined sources13
Beta strandi143 – 148Combined sources6
Beta strandi151 – 153Combined sources3
Beta strandi155 – 159Combined sources5
Beta strandi170 – 178Combined sources9
Beta strandi186 – 191Combined sources6
Beta strandi195 – 197Combined sources3
Beta strandi199 – 203Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A6AX-ray2.75A30-205[»]
1AQDX-ray2.45A/D/G/J26-217[»]
1BX2X-ray2.60A/D27-206[»]
1D5MX-ray2.00A26-206[»]
1D5XX-ray2.45A26-206[»]
1D5ZX-ray2.00A26-206[»]
1D6EX-ray2.45A26-206[»]
1DLHX-ray2.80A/D28-207[»]
1FV1X-ray1.90A/D26-206[»]
1FYTX-ray2.60A26-206[»]
1H15X-ray3.10A/D26-207[»]
1HQRX-ray3.20A26-206[»]
1HXYX-ray2.60A26-207[»]
1J8HX-ray2.40A26-206[»]
1JWMX-ray2.70A26-207[»]
1JWSX-ray2.60A26-207[»]
1JWUX-ray2.30A26-207[»]
1KG0X-ray2.65A28-207[»]
1KLGX-ray2.40A29-205[»]
1KLUX-ray1.93A29-207[»]
1LO5X-ray3.20A26-207[»]
1PYWX-ray2.10A26-207[»]
1R5IX-ray2.60A/E26-206[»]
1SEBX-ray2.70A/E26-206[»]
1SJEX-ray2.45A28-207[»]
1SJHX-ray2.25A28-207[»]
1T5WX-ray2.40A/D27-206[»]
1T5XX-ray2.50A27-207[»]
1YMMX-ray3.50A26-216[»]
1ZGLX-ray2.80A/D/G/J26-206[»]
2FSEX-ray3.10A/C29-205[»]
2G9HX-ray2.00A26-207[»]
2IAMX-ray2.80A26-207[»]
2IANX-ray2.80A/F/K/P26-207[»]
2ICWX-ray2.41A/D28-206[»]
2IPKX-ray2.30A26-207[»]
2OJEX-ray3.00A/E27-206[»]
2Q6WX-ray2.25A/D26-207[»]
2SEBX-ray2.50A26-206[»]
2WBJX-ray3.00A/E26-218[»]
2XN9X-ray2.30D26-207[»]
3C5JX-ray1.80A26-206[»]
3L6FX-ray2.10A26-207[»]
3O6FX-ray2.80A/E26-207[»]
3PDOX-ray1.95A26-217[»]
3PGCX-ray2.66A/D26-217[»]
3PGDX-ray2.72A/D26-217[»]
3QXAX-ray2.71A/D26-207[»]
3QXDX-ray2.30A/D26-207[»]
3S4SX-ray2.40A/D26-207[»]
3S5LX-ray2.10A/D26-207[»]
3T0EX-ray4.00A26-207[»]
4AENX-ray2.20A26-217[»]
4AH2X-ray2.36A26-217[»]
4C56X-ray2.90D/J26-207[»]
4E41X-ray2.60A/F26-207[»]
4FQXX-ray2.60A26-216[»]
4GBXX-ray3.00A26-216[»]
4H1LX-ray3.30A/D28-205[»]
4H25X-ray2.20A/D28-207[»]
4H26X-ray2.50A/D28-206[»]
4I5BX-ray2.12A/D27-213[»]
4IS6X-ray2.50A26-207[»]
4MCYX-ray2.30A26-206[»]
4MCZX-ray2.41A26-206[»]
4MD0X-ray2.19A26-206[»]
4MD4X-ray1.95A26-206[»]
4MD5X-ray1.65A26-206[»]
4MDIX-ray2.00A26-206[»]
4MDJX-ray1.70A26-206[»]
4OV5X-ray2.20A/D/G/J/M/P26-207[»]
4X5WX-ray1.34A26-217[»]
4X5XX-ray3.20A/C26-217[»]
4Y19X-ray2.50A26-206[»]
4Y1AX-ray4.00A26-206[»]
ProteinModelPortaliP01903.
SMRiP01903.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01903.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini112 – 204Ig-like C1-typeAdd BLAST93

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 109Alpha-1Add BLAST84
Regioni110 – 203Alpha-2Add BLAST94
Regioni204 – 216Connecting peptideAdd BLAST13

Sequence similaritiesi

Belongs to the MHC class II family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IZMF. Eukaryota.
ENOG410YHX9. LUCA.
HOVERGENiHBG006862.
InParanoidiP01903.
KOiK06752.
OMAiMIKRSNH.
OrthoDBiEOG091G0IC9.
PhylomeDBiP01903.
TreeFamiTF333797.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProiIPR032431. C1-set_C.
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]
PfamiPF07654. C1-set. 1 hit.
PF16196. C1-set_C. 1 hit.
PF00993. MHC_II_alpha. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
SM00920. MHC_II_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. 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.

P01903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD
60 70 80 90 100
FDGDEIFHVD MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK
110 120 130 140 150
RSNYTPITNV PPEVTVLTNS PVELREPNVL ICFIDKFTPP VVNVTWLRNG
160 170 180 190 200
KPVTTGVSET VFLPREDHLF RKFHYLPFLP STEDVYDCRV EHWGLDEPLL
210 220 230 240 250
KHWEFDAPSP LPETTENVVC ALGLTVGLVG IIIGTIFIIK GVRKSNAAER

RGPL
Length:254
Mass (Da):28,607
Last modified:July 21, 1986 - v1
Checksum:i3CD1CDBA952B2350
GO

Sequence cautioni

The sequence CAA25076 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28 – 29EE → AD AA sequence (PubMed:6812963).Curated2
Sequence conflicti33I → T AA sequence (PubMed:6812963).Curated1
Sequence conflicti34 – 35QA → YP AA sequence (PubMed:6812963).Curated2
Sequence conflicti48M → Q AA sequence (PubMed:6812963).Curated1
Sequence conflicti54D → T AA sequence (PubMed:6812963).Curated1
Sequence conflicti59V → Y AA sequence (PubMed:6600932).Curated1
Sequence conflicti64K → L AA sequence (PubMed:6600932).Curated1
Sequence conflicti67V → A AA sequence (PubMed:6955253).Curated1
Sequence conflicti69R → L AA sequence (PubMed:6600932).Curated1
Sequence conflicti75R → P AA sequence (PubMed:6600932).Curated1
Sequence conflicti78S → D AA sequence (PubMed:6600932).Curated1
Sequence conflicti149N → E AA sequence (PubMed:6955253).Curated1

Polymorphismi

The following alleles of DRA are known: DRA*01:01 and DRA*01:02. The sequence shown is that of DRA*01:01.
Genetic variations in HLA-DRA influence susceptibility to hepatitis B virus (HBV) infection [MIMi:610424].

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03524116V → L.Corresponds to variant rs16822586dbSNPEnsembl.1
Natural variantiVAR_004399242V → L in allele DRA*01:02. Corresponds to variant rs7192dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00194 mRNA. Translation: AAA36275.1.
K01171 mRNA. Translation: AAA59785.1.
X00274 Genomic DNA. Translation: CAA25076.1. Different initiation.
J00204, J00203 Genomic DNA. Translation: AAA36302.1.
M60334 mRNA. Translation: AAA59783.1.
CR457013 mRNA. Translation: CAG33294.1.
AL662796 Genomic DNA. Translation: CAI18266.1.
AL670296 Genomic DNA. Translation: CAI17571.1.
AL935032 Genomic DNA. Translation: CAI18476.1.
BX120007 Genomic DNA. Translation: CAM26203.1.
Z84814 Genomic DNA. Translation: CAB06609.1.
CH471081 Genomic DNA. Translation: EAX03630.1.
BC032350 mRNA. Translation: AAH32350.1.
BC071659 mRNA. Translation: AAH71659.1.
V00523 mRNA. Translation: CAA23782.1.
J00201 Genomic DNA. Translation: AAA36301.1.
AF481359 Genomic DNA. Translation: AAO23887.1.
CCDSiCCDS4750.1.
PIRiA93952. HLHUDA.
RefSeqiNP_061984.2. NM_019111.4.
UniGeneiHs.520048.

Genome annotation databases

EnsembliENST00000383127; ENSP00000372608; ENSG00000227993.
ENST00000383259; ENSP00000372746; ENSG00000206308.
ENST00000395388; ENSP00000378786; ENSG00000204287.
ENST00000411524; ENSP00000405295; ENSG00000234794.
ENST00000414698; ENSP00000402951; ENSG00000230726.
ENST00000416883; ENSP00000410443; ENSG00000228987.
ENST00000442960; ENSP00000404533; ENSG00000226260.
GeneIDi3122.
KEGGihsa:3122.
UCSCiuc003obh.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00194 mRNA. Translation: AAA36275.1.
K01171 mRNA. Translation: AAA59785.1.
X00274 Genomic DNA. Translation: CAA25076.1. Different initiation.
J00204, J00203 Genomic DNA. Translation: AAA36302.1.
M60334 mRNA. Translation: AAA59783.1.
CR457013 mRNA. Translation: CAG33294.1.
AL662796 Genomic DNA. Translation: CAI18266.1.
AL670296 Genomic DNA. Translation: CAI17571.1.
AL935032 Genomic DNA. Translation: CAI18476.1.
BX120007 Genomic DNA. Translation: CAM26203.1.
Z84814 Genomic DNA. Translation: CAB06609.1.
CH471081 Genomic DNA. Translation: EAX03630.1.
BC032350 mRNA. Translation: AAH32350.1.
BC071659 mRNA. Translation: AAH71659.1.
V00523 mRNA. Translation: CAA23782.1.
J00201 Genomic DNA. Translation: AAA36301.1.
AF481359 Genomic DNA. Translation: AAO23887.1.
CCDSiCCDS4750.1.
PIRiA93952. HLHUDA.
RefSeqiNP_061984.2. NM_019111.4.
UniGeneiHs.520048.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A6AX-ray2.75A30-205[»]
1AQDX-ray2.45A/D/G/J26-217[»]
1BX2X-ray2.60A/D27-206[»]
1D5MX-ray2.00A26-206[»]
1D5XX-ray2.45A26-206[»]
1D5ZX-ray2.00A26-206[»]
1D6EX-ray2.45A26-206[»]
1DLHX-ray2.80A/D28-207[»]
1FV1X-ray1.90A/D26-206[»]
1FYTX-ray2.60A26-206[»]
1H15X-ray3.10A/D26-207[»]
1HQRX-ray3.20A26-206[»]
1HXYX-ray2.60A26-207[»]
1J8HX-ray2.40A26-206[»]
1JWMX-ray2.70A26-207[»]
1JWSX-ray2.60A26-207[»]
1JWUX-ray2.30A26-207[»]
1KG0X-ray2.65A28-207[»]
1KLGX-ray2.40A29-205[»]
1KLUX-ray1.93A29-207[»]
1LO5X-ray3.20A26-207[»]
1PYWX-ray2.10A26-207[»]
1R5IX-ray2.60A/E26-206[»]
1SEBX-ray2.70A/E26-206[»]
1SJEX-ray2.45A28-207[»]
1SJHX-ray2.25A28-207[»]
1T5WX-ray2.40A/D27-206[»]
1T5XX-ray2.50A27-207[»]
1YMMX-ray3.50A26-216[»]
1ZGLX-ray2.80A/D/G/J26-206[»]
2FSEX-ray3.10A/C29-205[»]
2G9HX-ray2.00A26-207[»]
2IAMX-ray2.80A26-207[»]
2IANX-ray2.80A/F/K/P26-207[»]
2ICWX-ray2.41A/D28-206[»]
2IPKX-ray2.30A26-207[»]
2OJEX-ray3.00A/E27-206[»]
2Q6WX-ray2.25A/D26-207[»]
2SEBX-ray2.50A26-206[»]
2WBJX-ray3.00A/E26-218[»]
2XN9X-ray2.30D26-207[»]
3C5JX-ray1.80A26-206[»]
3L6FX-ray2.10A26-207[»]
3O6FX-ray2.80A/E26-207[»]
3PDOX-ray1.95A26-217[»]
3PGCX-ray2.66A/D26-217[»]
3PGDX-ray2.72A/D26-217[»]
3QXAX-ray2.71A/D26-207[»]
3QXDX-ray2.30A/D26-207[»]
3S4SX-ray2.40A/D26-207[»]
3S5LX-ray2.10A/D26-207[»]
3T0EX-ray4.00A26-207[»]
4AENX-ray2.20A26-217[»]
4AH2X-ray2.36A26-217[»]
4C56X-ray2.90D/J26-207[»]
4E41X-ray2.60A/F26-207[»]
4FQXX-ray2.60A26-216[»]
4GBXX-ray3.00A26-216[»]
4H1LX-ray3.30A/D28-205[»]
4H25X-ray2.20A/D28-207[»]
4H26X-ray2.50A/D28-206[»]
4I5BX-ray2.12A/D27-213[»]
4IS6X-ray2.50A26-207[»]
4MCYX-ray2.30A26-206[»]
4MCZX-ray2.41A26-206[»]
4MD0X-ray2.19A26-206[»]
4MD4X-ray1.95A26-206[»]
4MD5X-ray1.65A26-206[»]
4MDIX-ray2.00A26-206[»]
4MDJX-ray1.70A26-206[»]
4OV5X-ray2.20A/D/G/J/M/P26-207[»]
4X5WX-ray1.34A26-217[»]
4X5XX-ray3.20A/C26-217[»]
4Y19X-ray2.50A26-206[»]
4Y1AX-ray4.00A26-206[»]
ProteinModelPortaliP01903.
SMRiP01903.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109367. 43 interactors.
DIPiDIP-6063N.
IntActiP01903. 10 interactors.
MINTiMINT-203259.
STRINGi9606.ENSP00000378786.

Protein family/group databases

Allergomei8362. Hom s HLA-DR-alpha.

PTM databases

iPTMnetiP01903.
PhosphoSitePlusiP01903.

Polymorphism and mutation databases

BioMutaiHLA-DRA.
DMDMi122206.

Proteomic databases

EPDiP01903.
MaxQBiP01903.
PaxDbiP01903.
PeptideAtlasiP01903.
PRIDEiP01903.

Protocols and materials databases

DNASUi3122.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000383127; ENSP00000372608; ENSG00000227993.
ENST00000383259; ENSP00000372746; ENSG00000206308.
ENST00000395388; ENSP00000378786; ENSG00000204287.
ENST00000411524; ENSP00000405295; ENSG00000234794.
ENST00000414698; ENSP00000402951; ENSG00000230726.
ENST00000416883; ENSP00000410443; ENSG00000228987.
ENST00000442960; ENSP00000404533; ENSG00000226260.
GeneIDi3122.
KEGGihsa:3122.
UCSCiuc003obh.5. human.

Organism-specific databases

CTDi3122.
DisGeNETi3122.
GeneCardsiHLA-DRA.
H-InvDBHIX0005752.
HIX0031098.
HIX0166957.
HIX0167205.
HIX0167443.
HGNCiHGNC:4947. HLA-DRA.
HPAiCAB002798.
CAB015402.
HPA050162.
HPA053176.
MalaCardsiHLA-DRA.
MIMi142860. gene.
610424. phenotype.
neXtProtiNX_P01903.
OpenTargetsiENSG00000206308.
ENSG00000226260.
ENSG00000228987.
ENSG00000230726.
ENSG00000234794.
Orphaneti505. Graham Little-Piccardi-Lassueur syndrome.
PharmGKBiPA35071.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZMF. Eukaryota.
ENOG410YHX9. LUCA.
HOVERGENiHBG006862.
InParanoidiP01903.
KOiK06752.
OMAiMIKRSNH.
OrthoDBiEOG091G0IC9.
PhylomeDBiP01903.
TreeFamiTF333797.

Enzyme and pathway databases

BioCyciZFISH:G66-33430-MONOMER.
ReactomeiR-HSA-202424. Downstream TCR signaling.
R-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-202430. Translocation of ZAP-70 to Immunological synapse.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-389948. PD-1 signaling.
R-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiHLA-DRA. human.
EvolutionaryTraceiP01903.
GeneWikiiHLA-DRA.
GenomeRNAii3122.
PROiP01903.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204287.
CleanExiHS_HLA-DRA.
ExpressionAtlasiP01903. baseline and differential.
GenevisibleiP01903. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProiIPR032431. C1-set_C.
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]
PfamiPF07654. C1-set. 1 hit.
PF16196. C1-set_C. 1 hit.
PF00993. MHC_II_alpha. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
SM00920. MHC_II_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDRA_HUMAN
AccessioniPrimary (citable) accession number: P01903
Secondary accession number(s): A2BET4
, Q30160, Q6IAZ1, Q861I2, Q9TP70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 179 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.