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P04229 (2B11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
HLA class II histocompatibility antigen, DRB1-1 beta chain
Alternative name(s):
MHC class II antigen DRB1*1
Short name=DR-1
Short name=DR1
Gene names
Name:HLA-DRB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. 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. Ref.23

Post-translational modification

Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II Probable. Ref.23

Polymorphism

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.

Involvement in disease

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. Ref.17

Sequence similarities

Belongs to the MHC class II family.

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

Ontologies

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

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

T-helper 1 type immune response

Inferred from sequence or structural similarity. Source: UniProtKB

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

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

detection of bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

humoral immune response mediated by circulating immunoglobulin

Inferred from sequence or structural similarity. Source: UniProtKB

immune response

Inferred from sequence or structural similarity. Source: UniProtKB

immunoglobulin production involved in immunoglobulin mediated immune response

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response to antigenic stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

protein tetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of interleukin-10 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of interleukin-4 production

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Traceable author statement. Source: Reactome

MHC class II protein complex

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

late endosome membrane

Inferred from direct assay Ref.23. Source: UniProtKB

lysosomal membrane

Inferred from direct assay Ref.23. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

trans-Golgi network membrane

Traceable author statement. Source: Reactome

transport vesicle membrane

Traceable author statement. Source: Reactome

   Molecular_functionMHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

peptide antigen binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.9
Chain30 – 266237HLA class II histocompatibility antigen, DRB1-1 beta chain
PRO_0000018949

Regions

Topological domain30 – 227198Extracellular Potential
Transmembrane228 – 25023Helical; Potential
Topological domain251 – 26616Cytoplasmic Potential
Domain126 – 21489Ig-like C1-type
Region30 – 12495Beta-1
Region125 – 227103Beta-2

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 108 By similarity
Disulfide bond146 ↔ 202 By similarity
Cross-link254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant51K → R.
Corresponds to variant rs9270305 [ dbSNP | Ensembl ].
VAR_056527
Natural variant131T → A.
Corresponds to variant rs1059553 [ dbSNP | Ensembl ].
VAR_033377
Natural variant291A → S.
Corresponds to variant rs9270299 [ dbSNP | Ensembl ].
VAR_033378
Natural variant331R → K.
Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
VAR_033379
Natural variant331R → Q.
Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
VAR_033380
Natural variant391Q → E in allele DRB1*01:07.
VAR_016740
Natural variant661S → Y.
Corresponds to variant rs16822820 [ dbSNP | Ensembl ].
VAR_033381
Natural variant741G → R in allele DRB1*01:05.
VAR_016741
Natural variant761Y → F.
Corresponds to variant rs1060346 [ dbSNP | Ensembl ].
VAR_033382
Natural variant891Y → S.
Corresponds to variant rs36074728 [ dbSNP | Ensembl ].
VAR_033383
Natural variant961L → I in allele DRB1*01:03.
VAR_016710
Natural variant991Q → D in allele DRB1*01:03; requires 2 nucleotide substitutions.
VAR_016711
Natural variant991Q → E.
Corresponds to variant rs17881965 [ dbSNP | Ensembl ].
VAR_033384
Natural variant991Q → H.
Corresponds to variant rs17879599 [ dbSNP | Ensembl ].
VAR_033385
Natural variant1001R → A in allele DRB1*01:06; requires 2 nucleotide substitutions.
VAR_016742
Natural variant1001R → E in allele DRB1*01:03; requires 2 nucleotide substitutions.
VAR_016712
Natural variant1021A → G.
Corresponds to variant rs17878857 [ dbSNP | Ensembl ].
VAR_033386
Natural variant1031A → E.
Corresponds to variant rs16822805 [ dbSNP | Ensembl ].
VAR_033387
Natural variant1061T → N in allele DRB1*01:04.
Corresponds to variant rs16822752 [ dbSNP | Ensembl ].
VAR_016713
Natural variant1071Y → H.
Corresponds to variant rs16822512 [ dbSNP | Ensembl ].
VAR_033388
Natural variant1141V → A in allele DRB1*01:02.
Corresponds to variant rs17424145 [ dbSNP | Ensembl ].
VAR_016714
Natural variant1151G → V in allele DRB1*01:02, allele DRB1*01:04 and allele DRB1*01:06.
Corresponds to variant rs2230810 [ dbSNP | Ensembl ].
VAR_016715
Natural variant1641G → D.
Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
VAR_033389
Natural variant1691A → T.
Corresponds to variant rs2308768 [ dbSNP | Ensembl ].
VAR_033390
Natural variant1711V → M.
Corresponds to variant rs701829 [ dbSNP | Ensembl ].
VAR_033391
Natural variant1781Q → H.
Corresponds to variant rs701830 [ dbSNP | Ensembl ].
VAR_033392
Natural variant1951R → Q.
Corresponds to variant rs3205588 [ dbSNP | Ensembl ].
VAR_033393
Natural variant2101T → I.
Corresponds to variant rs17423930 [ dbSNP | Ensembl ].
VAR_033394
Natural variant2361V → M.
Corresponds to variant rs2230816 [ dbSNP | Ensembl ].
VAR_033395
Natural variant2531Q → E in allele DRB1*01:02.
VAR_016716
Natural variant2621T → R. Ref.5
Corresponds to variant rs9269744 [ dbSNP | Ensembl ].
VAR_056528

Experimental info

Sequence conflict251P → R in AAA59781. Ref.2
Sequence conflict361F → S AA sequence Ref.9
Sequence conflict58 – 592RC → LF AA sequence Ref.9
Sequence conflict801T → E in AAA59781. Ref.2
Sequence conflict100 – 1034RRAA → KRGQ in AAA59781. Ref.2
Sequence conflict1921T → I in AAA59781. Ref.2

Secondary structure

...................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04229 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: CC9CC7E2D0DD036C

FASTA26629,914
        10         20         30         40         50         60 
MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT ERVRLLERCI 

        70         80         90        100        110        120 
YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR RAAVDTYCRH NYGVGESFTV 

       130        140        150        160        170        180 
QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG 

       190        200        210        220        230        240 
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL 

       250        260 
FLGAGLFIYF RNQKGHSGLQ PTGFLS 

« Hide

References

« Hide 'large scale' references
[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]"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].
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]"HLA-DRB1*1101: a significant risk factor for sarcoidosis in blacks and whites."
Rossman M.D., Thompson B., Frederick M., Maliarik M., Iannuzzi M.C., Rybicki B.A., Pandey J.P., Newman L.S., Magira E., Beznik-Cizman B., Monos D.
Am. J. Hum. Genet. 73:720-735(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA19197.
HLHU1B. D24669.
I56072.
PH0147.
UniGeneHs.534322.
Hs.696211.
Hs.736560.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D33-217[»]
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-ray3.00B30-221[»]
4I5BX-ray2.12B/E31-222[»]
ProteinModelPortalP04229.
SMRP04229. Positions 30-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6143N.
IntActP04229. 6 interactions.
MINTMINT-203282.

Chemistry

BindingDBP04229.
ChEMBLCHEMBL1943.
DrugBankDB05259. Glatiramer Acetate.

PTM databases

PhosphoSiteP04229.

Polymorphism databases

DMDM34395916.

Proteomic databases

PaxDbP04229.
PRIDEP04229.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360004; ENSP00000353099; ENSG00000196126.

Organism-specific databases

GeneCardsGC06M032546.
HGNCHGNC:4948. HLA-DRB1.
HPACAB015400.
CAB034021.
MIM142857. gene.
181000. phenotype.
neXtProtNX_P04229.
Orphanet703. 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.
93567. Pediatric systemic sclerosis.
284130. Rheumatoid arthritis.
797. Sarcoidosis.
536. Systemic lupus erythematosus.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68200.
HOVERGENHBG012730.
InParanoidP04229.
OrthoDBEOG7PS1GV.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP04229.
BgeeP04229.
CleanExHS_HLA-DRB1.
GenevestigatorP04229.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011162. MHC_I/II-like_Ag-recog.
IPR014745. MHC_II_a/b_N.
IPR000353. MHC_II_b_N.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]
ProDomPD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHLA-DRB1. human.
EvolutionaryTraceP04229.
PROP04229.
SOURCESearch...

Entry information

Entry name2B11_HUMAN
AccessionPrimary (citable) accession number: P04229
Secondary accession number(s): A4F5N0 expand/collapse secondary AC list , A8K098, O62869, P13758, Q06662, Q30116, Q30117, Q5Y7E9, Q7M2H4, Q95461, Q9BCL7, Q9GIK5, Q9MXZ0, Q9MXZ5, Q9TQ91
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: August 29, 2003
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM