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P04229

- 2B11_HUMAN

UniProt

P04229 - 2B11_HUMAN

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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: 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

  1. MHC class II protein complex binding Source: UniProt
  2. peptide antigen binding Source: UniProtKB

GO - Biological processi

  1. T cell costimulation Source: Reactome
  2. T cell receptor signaling pathway Source: Reactome
  3. T-helper 1 type immune response Source: UniProtKB
  4. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  5. cytokine-mediated signaling pathway Source: Reactome
  6. detection of bacterium Source: UniProtKB
  7. humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
  8. immune response Source: UniProtKB
  9. immunoglobulin production involved in immunoglobulin mediated immune response Source: UniProtKB
  10. inflammatory response to antigenic stimulus Source: UniProtKB
  11. interferon-gamma-mediated signaling pathway Source: Reactome
  12. negative regulation of T cell proliferation Source: UniProtKB
  13. negative regulation of interferon-gamma production Source: UniProtKB
  14. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  15. protein tetramerization Source: UniProtKB
  16. regulation of interleukin-10 secretion Source: UniProtKB
  17. regulation of interleukin-4 production Source: UniProtKB
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:4948. HLA-DRB1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Late endosome 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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 227198Extracellular Reviewed prediction
Add
BLAST
Transmembranei228 – 25023Helical; Reviewed prediction
Add
BLAST
Topological domaini251 – 26616Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. ER to Golgi transport vesicle membrane Source: Reactome
  2. Golgi membrane Source: Reactome
  3. MHC class II protein complex Source: UniProt
  4. clathrin-coated endocytic vesicle membrane Source: Reactome
  5. endocytic vesicle membrane Source: Reactome
  6. external side of plasma membrane Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProt
  8. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  9. late endosome membrane Source: UniProtKB
  10. lysosomal membrane Source: UniProtKB
  11. plasma membrane Source: Reactome
  12. trans-Golgi network membrane Source: Reactome
  13. transport vesicle membrane Source: Reactome
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) [MIM:181000]: An 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 Publication
Add
BLAST
Chaini30 – 266237HLA class II histocompatibility antigen, DRB1-1 beta chain
PRO_0000018949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 108 By similarity
Glycosylationi48 – 481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi146 ↔ 202 By similarity
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 Inferred.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP04229.
PRIDEiP04229.

PTM databases

PhosphoSiteiP04229.

Expressioni

Gene expression databases

ArrayExpressiP04229.
BgeeiP04229.
CleanExiHS_HLA-DRB1.
GenevestigatoriP04229.

Organism-specific databases

HPAiCAB015400.
CAB034021.

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
4E41X-ray2.60B/G30-219[»]
4FQXX-ray2.60B30-221[»]
4GBXX-ray3.00B30-220[»]
4I5BX-ray2.12B/E31-222[»]
ProteinModelPortaliP04229.
SMRiP04229. Positions 30-219.

Miscellaneous databases

EvolutionaryTraceiP04229.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the MHC class II family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG68200.
HOVERGENiHBG012730.
InParanoidiP04229.
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

MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT    50
ERVRLLERCI YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR 100
RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG 150
FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY 200
TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF 250
RNQKGHSGLQ PTGFLS 266
Length:266
Mass (Da):29,914
Last modified:August 29, 2003 - v2
Checksum:iCC9CC7E2D0DD036C
GO

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.
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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251P → R in AAA59781. 1 Publication
Sequence conflicti36 – 361F → S AA sequence 1 Publication
Sequence conflicti58 – 592RC → LF AA sequence 1 Publication
Sequence conflicti80 – 801T → E in AAA59781. 1 Publication
Sequence conflicti100 – 1034RRAA → KRGQ in AAA59781. 1 Publication
Sequence conflicti192 – 1921T → I in AAA59781. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi34395916.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A19197.
D24669. HLHU1B.
I56072.
PH0147.
UniGenei Hs.534322.
Hs.696211.
Hs.736560.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AQD X-ray 2.45 B/E/H/K 30-227 [» ]
1DLH X-ray 2.80 B/E 32-219 [» ]
1FYT X-ray 2.60 B 30-221 [» ]
1HXY X-ray 2.60 B 30-219 [» ]
1JWM X-ray 2.70 B 30-219 [» ]
1JWS X-ray 2.60 B 30-219 [» ]
1JWU X-ray 2.30 B 30-219 [» ]
1KG0 X-ray 2.65 B 32-219 [» ]
1KLG X-ray 2.40 B 30-219 [» ]
1KLU X-ray 1.93 B 30-219 [» ]
1LO5 X-ray 3.20 B 30-219 [» ]
1PYW X-ray 2.10 B 30-219 [» ]
1R5I X-ray 2.60 B/F 30-219 [» ]
1SEB X-ray 2.70 B/F 30-221 [» ]
1SJE X-ray 2.45 B 30-219 [» ]
1SJH X-ray 2.25 B 30-219 [» ]
1T5W X-ray 2.40 B/E 30-219 [» ]
1T5X X-ray 2.50 B 30-219 [» ]
2FSE X-ray 3.10 B/D 33-219 [» ]
2G9H X-ray 2.00 B 30-219 [» ]
2IAM X-ray 2.80 B 30-219 [» ]
2IAN X-ray 2.80 B/G/L/Q 30-219 [» ]
2ICW X-ray 2.41 B/E 30-219 [» ]
2IPK X-ray 2.30 B 30-219 [» ]
2OJE X-ray 3.00 B/F 30-219 [» ]
2XN9 X-ray 2.30 E 30-219 [» ]
3L6F X-ray 2.10 B 30-221 [» ]
3PDO X-ray 1.95 B 30-227 [» ]
3PGC X-ray 2.66 B/E 30-227 [» ]
3PGD X-ray 2.72 B/E 30-227 [» ]
3QXA X-ray 2.71 B/E 30-219 [» ]
3QXD X-ray 2.30 B/E 30-219 [» ]
3S4S X-ray 2.40 B/E 30-221 [» ]
3S5L X-ray 2.10 B/E 30-221 [» ]
4AEN X-ray 2.20 B 30-227 [» ]
4AH2 X-ray 2.36 B 30-227 [» ]
4E41 X-ray 2.60 B/G 30-219 [» ]
4FQX X-ray 2.60 B 30-221 [» ]
4GBX X-ray 3.00 B 30-220 [» ]
4I5B X-ray 2.12 B/E 31-222 [» ]
ProteinModelPortali P04229.
SMRi P04229. Positions 30-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6143N.
IntActi P04229. 6 interactions.
MINTi MINT-203282.

Chemistry

BindingDBi P04229.
ChEMBLi CHEMBL1943.
DrugBanki DB05259. Glatiramer Acetate.

PTM databases

PhosphoSitei P04229.

Polymorphism databases

DMDMi 34395916.

Proteomic databases

PaxDbi P04229.
PRIDEi P04229.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360004 ; ENSP00000353099 ; ENSG00000196126 .

Organism-specific databases

GeneCardsi GC06M032546.
HGNCi HGNC:4948. HLA-DRB1.
HPAi CAB015400.
CAB034021.
MIMi 142857. gene.
181000. phenotype.
neXtProti NX_P04229.
Orphaneti 703. 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.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG68200.
HOVERGENi HBG012730.
InParanoidi P04229.
OrthoDBi EOG7PS1GV.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi HLA-DRB1. human.
EvolutionaryTracei P04229.
PROi P04229.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04229.
Bgeei P04229.
CleanExi HS_HLA-DRB1.
Genevestigatori P04229.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProi 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.
IPR000353. MHC_II_b_N.
[Graphical view ]
Pfami PF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view ]
ProDomi PD000328. MHC_II_b_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view ]
SUPFAMi SSF54452. SSF54452. 1 hit.
PROSITEi PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.

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: September 3, 2014
This is version 144 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

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