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Protein

HLA class II histocompatibility antigen, DRB1-1 beta chain

Gene

HLA-DRB1

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
  • peptide antigen binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.
REACT_25078. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
HLA class II histocompatibility antigen, DRB1-1 beta chain
Alternative name(s):
MHC class II antigen DRB1*1
Short name:
DR-1
Short name:
DR1
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4948. HLA-DRB1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 227198ExtracellularSequence AnalysisAdd
BLAST
Transmembranei228 – 25023HelicalSequence AnalysisAdd
BLAST
Topological domaini251 – 26616CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Sarcoidosis 1 (SS1)

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionAn idiopathic, systemic, inflammatory disease characterized by the formation of immune granulomas in involved organs. Granulomas predominantly invade the lungs and the lymphatic system, but also skin, liver, spleen, eyes and other organs may be involved.

See also OMIM:181000

Organism-specific databases

MIMi181000. phenotype.
Orphaneti703. Bullous pemphigoid.
555. Celiac disease.
243377. Diabetes mellitus type 1.
220393. Diffuse cutaneous systemic sclerosis.
545. Follicular lymphoma.
220402. Limited cutaneous systemic sclerosis.
220407. Limited systemic sclerosis.
802. Multiple sclerosis.
83465. Narcolepsy without cataplexy.
2073. Narcolepsy-cataplexy.
284130. Rheumatoid arthritis.
797. Sarcoidosis.
536. Systemic lupus erythematosus.

Chemistry

DrugBankiDB05259. Glatiramer Acetate.

Polymorphism and mutation databases

DMDMi34395916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 266237HLA class II histocompatibility antigen, DRB1-1 beta chainPRO_0000018949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 108PROSITE-ProRule annotation
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi146 ↔ 202PROSITE-ProRule annotation
Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP04229.
PRIDEiP04229.

PTM databases

PhosphoSiteiP04229.

Expressioni

Gene expression databases

BgeeiP04229.
CleanExiHS_HLA-DRB1.
ExpressionAtlasiP04229. baseline and differential.
GenevestigatoriP04229.

Organism-specific databases

HPAiCAB015400.
CAB034021.
HPA043151.

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.

Protein-protein interaction databases

DIPiDIP-6143N.
IntActiP04229. 6 interactions.
MINTiMINT-203282.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 4712Combined sources
Turni48 – 514Combined sources
Beta strandi52 – 6312Combined sources
Beta strandi65 – 706Combined sources
Turni71 – 733Combined sources
Beta strandi75 – 806Combined sources
Helixi81 – 833Combined sources
Helixi84 – 918Combined sources
Helixi94 – 10613Combined sources
Helixi108 – 1158Combined sources
Helixi116 – 1183Combined sources
Turni119 – 1213Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 15413Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1929Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi213 – 2186Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQDX-ray2.45B/E/H/K30-227[»]
1DLHX-ray2.80B/E32-219[»]
1FYTX-ray2.60B30-221[»]
1HXYX-ray2.60B30-219[»]
1JWMX-ray2.70B30-219[»]
1JWSX-ray2.60B30-219[»]
1JWUX-ray2.30B30-219[»]
1KG0X-ray2.65B32-219[»]
1KLGX-ray2.40B30-219[»]
1KLUX-ray1.93B30-219[»]
1LO5X-ray3.20B30-219[»]
1PYWX-ray2.10B30-219[»]
1R5IX-ray2.60B/F30-219[»]
1SEBX-ray2.70B/F30-221[»]
1SJEX-ray2.45B30-219[»]
1SJHX-ray2.25B30-219[»]
1T5WX-ray2.40B/E30-219[»]
1T5XX-ray2.50B30-219[»]
2FSEX-ray3.10B/D33-219[»]
2G9HX-ray2.00B30-219[»]
2IAMX-ray2.80B30-219[»]
2IANX-ray2.80B/G/L/Q30-219[»]
2ICWX-ray2.41B/E30-219[»]
2IPKX-ray2.30B30-219[»]
2OJEX-ray3.00B/F30-219[»]
2XN9X-ray2.30E30-219[»]
3L6FX-ray2.10B30-221[»]
3PDOX-ray1.95B30-227[»]
3PGCX-ray2.66B/E30-227[»]
3PGDX-ray2.72B/E30-227[»]
3QXAX-ray2.71B/E30-219[»]
3QXDX-ray2.30B/E30-219[»]
3S4SX-ray2.40B/E30-221[»]
3S5LX-ray2.10B/E30-221[»]
4AENX-ray2.20B30-227[»]
4AH2X-ray2.36B30-227[»]
4C56X-ray2.90E/K30-219[»]
4E41X-ray2.60B/G30-219[»]
4FQXX-ray2.60B30-221[»]
4GBXX-ray3.00B30-220[»]
4I5BX-ray2.12B/E31-222[»]
4OV5X-ray2.20B/E/H/K/N/Q30-219[»]
ProteinModelPortaliP04229.
SMRiP04229. Positions 30-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04229.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 21489Ig-like C1-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 12495Beta-1Add
BLAST
Regioni125 – 227103Beta-2Add
BLAST

Sequence similaritiesi

Belongs to the MHC class II family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG68200.
HOVERGENiHBG012730.
OrthoDBiEOG7PS1GV.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProiIPR007110. 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.
IPR000353. MHC_II_b_N.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]
ProDomiPD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT
60 70 80 90 100
ERVRLLERCI YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR
110 120 130 140 150
RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG
160 170 180 190 200
FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY
210 220 230 240 250
TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF
260
RNQKGHSGLQ PTGFLS
Length:266
Mass (Da):29,914
Last modified:August 29, 2003 - v2
Checksum:iCC9CC7E2D0DD036C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251P → R in AAA59781 (PubMed:3858829).Curated
Sequence conflicti36 – 361F → S AA sequence (PubMed:6600932).Curated
Sequence conflicti58 – 592RC → LF AA sequence (PubMed:6600932).Curated
Sequence conflicti80 – 801T → E in AAA59781 (PubMed:3858829).Curated
Sequence conflicti100 – 1034RRAA → KRGQ in AAA59781 (PubMed:3858829).Curated
Sequence conflicti192 – 1921T → I in AAA59781 (PubMed:3858829).Curated

Polymorphismi

The following alleles of DRB1-1 are known: DRB1*01:01; DRB1*01:02; DRB1*01:03; DRB1*01:04; DRB1*01:05; DRB1*01:06; DRB1*01:07; DRB1*01:08; DRB1*01:09; DRB1*01:10; DRB1*01:11; DRB1*01:12; DRB1*01:13; DRB1*01:14; DRB1*01:15; DRB1*01:16; DRB1*01:17; DRB1*01:18; DRB1*01:19; DRB1*01:20 and DRB1*01:21. The sequence shown is that of DRB1*01:01.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51K → R.
Corresponds to variant rs9270305 [ dbSNP | Ensembl ].
VAR_056527
Natural varianti13 – 131T → A.
Corresponds to variant rs1059553 [ dbSNP | Ensembl ].
VAR_033377
Natural varianti29 – 291A → S.
Corresponds to variant rs9270299 [ dbSNP | Ensembl ].
VAR_033378
Natural varianti33 – 331R → K.
Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
VAR_033379
Natural varianti33 – 331R → Q.
Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
VAR_033380
Natural varianti39 – 391Q → E in allele DRB1*01:07.
VAR_016740
Natural varianti66 – 661S → Y.
Corresponds to variant rs16822820 [ dbSNP | Ensembl ].
VAR_033381
Natural varianti74 – 741G → R in allele DRB1*01:05.
VAR_016741
Natural varianti76 – 761Y → F.
Corresponds to variant rs1060346 [ dbSNP | Ensembl ].
VAR_033382
Natural varianti89 – 891Y → S.
Corresponds to variant rs36074728 [ dbSNP | Ensembl ].
VAR_033383
Natural varianti96 – 961L → I in allele DRB1*01:03.
VAR_016710
Natural varianti99 – 991Q → D in allele DRB1*01:03; requires 2 nucleotide substitutions.
VAR_016711
Natural varianti99 – 991Q → E.
Corresponds to variant rs17881965 [ dbSNP | Ensembl ].
VAR_033384
Natural varianti99 – 991Q → H.
Corresponds to variant rs17879599 [ dbSNP | Ensembl ].
VAR_033385
Natural varianti100 – 1001R → A in allele DRB1*01:06; requires 2 nucleotide substitutions. 1 Publication
VAR_016742
Natural varianti100 – 1001R → E in allele DRB1*01:03; requires 2 nucleotide substitutions.
VAR_016712
Natural varianti102 – 1021A → G.
Corresponds to variant rs17878857 [ dbSNP | Ensembl ].
VAR_033386
Natural varianti103 – 1031A → E.
Corresponds to variant rs16822805 [ dbSNP | Ensembl ].
VAR_033387
Natural varianti106 – 1061T → N in allele DRB1*01:04.
Corresponds to variant rs16822752 [ dbSNP | Ensembl ].
VAR_016713
Natural varianti107 – 1071Y → H.
Corresponds to variant rs16822512 [ dbSNP | Ensembl ].
VAR_033388
Natural varianti114 – 1141V → A in allele DRB1*01:02.
Corresponds to variant rs17424145 [ dbSNP | Ensembl ].
VAR_016714
Natural varianti115 – 1151G → V in allele DRB1*01:02, allele DRB1*01:04 and allele DRB1*01:06.
Corresponds to variant rs2230810 [ dbSNP | Ensembl ].
VAR_016715
Natural varianti164 – 1641G → D.
Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
VAR_033389
Natural varianti169 – 1691A → T.
Corresponds to variant rs2308768 [ dbSNP | Ensembl ].
VAR_033390
Natural varianti171 – 1711V → M.
Corresponds to variant rs701829 [ dbSNP | Ensembl ].
VAR_033391
Natural varianti178 – 1781Q → H.
Corresponds to variant rs701830 [ dbSNP | Ensembl ].
VAR_033392
Natural varianti195 – 1951R → Q.
Corresponds to variant rs3205588 [ dbSNP | Ensembl ].
VAR_033393
Natural varianti210 – 2101T → I.
Corresponds to variant rs17423930 [ dbSNP | Ensembl ].
VAR_033394
Natural varianti236 – 2361V → M.
Corresponds to variant rs2230816 [ dbSNP | Ensembl ].
VAR_033395
Natural varianti253 – 2531Q → E in allele DRB1*01:02.
VAR_016716
Natural varianti262 – 2621T → R.1 Publication
Corresponds to variant rs9269744 [ dbSNP | Ensembl ].
VAR_056528

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03069 mRNA. Translation: CAA26873.1.
M11161 mRNA. Translation: AAA59781.1.
M33600 mRNA. Translation: AAA59782.1.
AY663400 Genomic DNA. Translation: AAU87993.1.
AM419948 Genomic DNA. Translation: CAL99240.1.
AK289463 mRNA. Translation: BAF82152.1.
X64547 Genomic DNA. Translation: CAA45845.1.
X99896 mRNA. Translation: CAA68171.1.
AF089723 Genomic DNA. Translation: AAD51131.1.
AJ276206 Genomic DNA. Translation: CAC27123.1.
AB015184 Genomic DNA. Translation: BAA28761.1.
AJ303118 Genomic DNA. Translation: CAC19693.1.
Z50871 Genomic DNA. No translation available.
M21008 mRNA. Translation: AAA59780.1.
AF029288 Genomic DNA. Translation: AAF65497.1.
AF029293 Genomic DNA. Translation: AAF65502.1.
PIRiA19197.
D24669. HLHU1B.
I56072.
PH0147.
UniGeneiHs.534322.
Hs.696211.
Hs.736560.

Genome annotation databases

EnsembliENST00000360004; ENSP00000353099; ENSG00000196126.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03069 mRNA. Translation: CAA26873.1.
M11161 mRNA. Translation: AAA59781.1.
M33600 mRNA. Translation: AAA59782.1.
AY663400 Genomic DNA. Translation: AAU87993.1.
AM419948 Genomic DNA. Translation: CAL99240.1.
AK289463 mRNA. Translation: BAF82152.1.
X64547 Genomic DNA. Translation: CAA45845.1.
X99896 mRNA. Translation: CAA68171.1.
AF089723 Genomic DNA. Translation: AAD51131.1.
AJ276206 Genomic DNA. Translation: CAC27123.1.
AB015184 Genomic DNA. Translation: BAA28761.1.
AJ303118 Genomic DNA. Translation: CAC19693.1.
Z50871 Genomic DNA. No translation available.
M21008 mRNA. Translation: AAA59780.1.
AF029288 Genomic DNA. Translation: AAF65497.1.
AF029293 Genomic DNA. Translation: AAF65502.1.
PIRiA19197.
D24669. HLHU1B.
I56072.
PH0147.
UniGeneiHs.534322.
Hs.696211.
Hs.736560.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQDX-ray2.45B/E/H/K30-227[»]
1DLHX-ray2.80B/E32-219[»]
1FYTX-ray2.60B30-221[»]
1HXYX-ray2.60B30-219[»]
1JWMX-ray2.70B30-219[»]
1JWSX-ray2.60B30-219[»]
1JWUX-ray2.30B30-219[»]
1KG0X-ray2.65B32-219[»]
1KLGX-ray2.40B30-219[»]
1KLUX-ray1.93B30-219[»]
1LO5X-ray3.20B30-219[»]
1PYWX-ray2.10B30-219[»]
1R5IX-ray2.60B/F30-219[»]
1SEBX-ray2.70B/F30-221[»]
1SJEX-ray2.45B30-219[»]
1SJHX-ray2.25B30-219[»]
1T5WX-ray2.40B/E30-219[»]
1T5XX-ray2.50B30-219[»]
2FSEX-ray3.10B/D33-219[»]
2G9HX-ray2.00B30-219[»]
2IAMX-ray2.80B30-219[»]
2IANX-ray2.80B/G/L/Q30-219[»]
2ICWX-ray2.41B/E30-219[»]
2IPKX-ray2.30B30-219[»]
2OJEX-ray3.00B/F30-219[»]
2XN9X-ray2.30E30-219[»]
3L6FX-ray2.10B30-221[»]
3PDOX-ray1.95B30-227[»]
3PGCX-ray2.66B/E30-227[»]
3PGDX-ray2.72B/E30-227[»]
3QXAX-ray2.71B/E30-219[»]
3QXDX-ray2.30B/E30-219[»]
3S4SX-ray2.40B/E30-221[»]
3S5LX-ray2.10B/E30-221[»]
4AENX-ray2.20B30-227[»]
4AH2X-ray2.36B30-227[»]
4C56X-ray2.90E/K30-219[»]
4E41X-ray2.60B/G30-219[»]
4FQXX-ray2.60B30-221[»]
4GBXX-ray3.00B30-220[»]
4I5BX-ray2.12B/E31-222[»]
4OV5X-ray2.20B/E/H/K/N/Q30-219[»]
ProteinModelPortaliP04229.
SMRiP04229. Positions 30-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6143N.
IntActiP04229. 6 interactions.
MINTiMINT-203282.

Chemistry

BindingDBiP04229.
ChEMBLiCHEMBL1943.
DrugBankiDB05259. Glatiramer Acetate.

PTM databases

PhosphoSiteiP04229.

Polymorphism and mutation databases

DMDMi34395916.

Proteomic databases

PaxDbiP04229.
PRIDEiP04229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360004; ENSP00000353099; ENSG00000196126.

Organism-specific databases

GeneCardsiGC06M032546.
HGNCiHGNC:4948. HLA-DRB1.
HPAiCAB015400.
CAB034021.
HPA043151.
MIMi142857. gene.
181000. phenotype.
neXtProtiNX_P04229.
Orphaneti703. Bullous pemphigoid.
555. Celiac disease.
243377. Diabetes mellitus type 1.
220393. Diffuse cutaneous systemic sclerosis.
545. Follicular lymphoma.
220402. Limited cutaneous systemic sclerosis.
220407. Limited systemic sclerosis.
802. Multiple sclerosis.
83465. Narcolepsy without cataplexy.
2073. Narcolepsy-cataplexy.
284130. Rheumatoid arthritis.
797. Sarcoidosis.
536. Systemic lupus erythematosus.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG68200.
HOVERGENiHBG012730.
OrthoDBiEOG7PS1GV.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.
REACT_25078. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiHLA-DRB1. human.
EvolutionaryTraceiP04229.
SOURCEiSearch...

Gene expression databases

BgeeiP04229.
CleanExiHS_HLA-DRB1.
ExpressionAtlasiP04229. baseline and differential.
GenevestigatoriP04229.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProiIPR007110. 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.
IPR000353. MHC_II_b_N.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]
ProDomiPD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DO beta: a new beta chain gene in HLA-D with a distinct regulation of expression."
    Tonnelle C., Demars R., Long E.O.
    EMBO J. 4:2839-2847(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
  2. "DNA sequence and characterization of human class II major histocompatibility complex beta chains from the DR1 haplotype."
    Bell J.I., Estess P., St John T., Saiki R., Watling D.L., Erlich H.A., McDevitt H.O.
    Proc. Natl. Acad. Sci. U.S.A. 82:3405-3409(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
  3. "Evolution of the HLA-DR1 gene family. Structural and functional analysis of the new allele 'DR-BON'."
    Coppin H.L., Avoustin P., Fabron J., Huchenq A., Garnier J.-M., Thomsen M., De Preval C.
    J. Immunol. 144:984-989(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:03).
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Full-length sequence analysis of the HLA-DRB1 locus suggests a recent origin of alleles."
    von Salome J., Gyllensten U., Bergstroem T.F.
    Immunogenetics 59:261-271(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*01:01), VARIANT ARG-262.
  6. "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].
    Tissue: Cerebellum.
  7. "Polymorphism in the regulatory region of HLA-DRB genes correlating with haplotype evolution."
    Louis P., Eliaou J.F., Kerlan-Candon S., Pinet V., Vincent R., Clot J.
    Immunogenetics 38:21-26(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    Tissue: B-cell.
  8. Middleton D., Versluis L.F., Tilanus M.G.J.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*01:04).
  9. "N-terminal amino acid sequences of the alpha and beta chains of HLA-DR1 and HLA-DR2 antigens."
    Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., Reisfeld R.A.
    Biochemistry 22:185-188(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-64.
    Tissue: B-cell.
  10. "Identification of a novel DRB1-allele (DRB1*0106) by sequence-based typing."
    Palou E., Mongay L., Arias M.T., Isart F., Suarez B., Masso M., Fabregat V., Martorell J., Gaya A.
    Tissue Antigens 53:308-310(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:06).
  11. "Identification of three new DRB1 alleles, DRB1*0107, *0425 and *13012 and confirmation of DRB4*01033."
    Voorter C.E.M., Hepkema B.G., Lems S.P.M., van den Berg-Loonen E.M.
    Tissue Antigens 61:398-402(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07).
  12. "HLA-DRB1 new alleles."
    Kashiwase K., Akaza T., Juji T.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:05).
  13. "A new HLA-DRB1*01 allele."
    Dormoy A., Froelich N., Leisenbach R., Tongio M.M.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07).
  14. "Identification and sequencing of a novel DRB1*01 allele."
    Hashemi S., Couture C., Cole R., Buyse I.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*01:02).
    Tissue: Blood.
  15. "Polymorphism of the HLA-DR1 haplotype in American blacks. Identification of a DR1 beta-chain determinant recognized in the mixed lymphocyte reaction."
    Hurley C.K., Ziff B.L., Silver J., Gregersen P.K., Hartzman R., Johnson A.H.
    J. Immunol. 140:4019-4023(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-266 (ALLELE DRB1*01:02).
  16. "HLA class II polymorphism."
    Arnaiz-Villena A.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELES DRB1*01:01 AND DRB1*01:02).
    Tissue: Blood.
  17. Cited for: DISEASE.
  18. "Invariant chain structure and MHC class II function."
    Cresswell P.
    Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  19. "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.
  20. "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.
  21. "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.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation."
    De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., Pierre P., Gatti E.
    Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MARCH1, SUBCELLULAR LOCATION.
  24. "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.
  25. "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.
  26. "Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1."
    Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L., Wiley D.C.
    Nature 364:33-39(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219.
  27. "Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide."
    Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., Strominger J.L., Wiley D.C.
    Nature 368:215-221(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219.
  28. "Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen."
    Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.
    Nature 368:711-718(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB.
  29. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry namei2B11_HUMAN
AccessioniPrimary (citable) accession number: P04229
Secondary accession number(s): A4F5N0
, A8K098, O62869, P13758, Q06662, Q30116, Q30117, Q5Y7E9, Q7M2H4, Q95461, Q9BCL7, Q9GIK5, Q9MXZ0, Q9MXZ5, Q9TQ91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: August 29, 2003
Last modified: May 27, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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 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.