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HLA class II histocompatibility antigen, DRB1-4 beta chain (MHC class II antigen DRB1*4) (DR-4) (DR4)

 2B14_HUMAN              Reviewed;         266 AA.
P13760; O19717; O19739; P13759; Q29875; Q30145; Q9GIX9; Q9GIY4;
Q9MY13; Q9XRY5;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
18-JUL-2018, entry version 175.
RecName: Full=HLA class II histocompatibility antigen, DRB1-4 beta chain;
AltName: Full=MHC class II antigen DRB1*4;
Short=DR-4;
Short=DR4;
Flags: Precursor;
Name=HLA-DRB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*04:01).
PubMed=3036826;
Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A.,
Rask L.;
"Class II genes of the human major histocompatibility complex.
Organization and evolutionary relationship of the DR beta genes.";
J. Biol. Chem. 262:8748-8758(1987).
[2]
ERRATUM, AND SEQUENCE REVISION.
Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A.,
Rask L.;
J. Biol. Chem. 263:8551-8551(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*04:01).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*04:01).
PubMed=3476943; DOI=10.1073/pnas.84.17.6234;
Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A.,
McDevitt H.O.;
"Allelic variation in the DR subregion of the human major
histocompatibility complex.";
Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01).
PubMed=3860851; DOI=10.1073/pnas.82.15.5165;
Spies T., Sorrentino R., Boss J.M., Okada K., Strominger J.L.;
"Structural organization of the DR subregion of the human major
histocompatibility complex.";
Proc. Natl. Acad. Sci. U.S.A. 82:5165-5169(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01).
PubMed=9098937; DOI=10.1111/j.1399-0039.1997.tb02751.x;
Thonnard J., Gervais T., Heusterpreute M., Mersch G., De Canck I.,
De Greef C., Demanet C., Van Waeyenberge C.;
"A new silent mutation at codon 35 in exon 2 yielding a DRB1*04012
allele.";
Tissue Antigens 49:274-276(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:02).
PubMed=12358860; DOI=10.1046/j.1365-2370.2002.00354.x;
Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A.,
Marsh S.G.E.;
"Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041
alleles.";
Eur. J. Immunogenet. 29:453-455(2002).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELE DRB1*04:03).
TISSUE=Blood;
Arnaiz-Villena A.;
"HLA class II polymorphism.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (ALLELE DRB1*04:03).
Greville W.D., van Eijck A., Dunckley H.;
"New HLA class II (DRB1) alleles detected by sequencing-based
typing.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:03).
Guttridge M.G., Hammond L.;
"Confirmatory sequence of HLA-DRB1*04032.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:04).
PubMed=3875800; DOI=10.1038/317166a0;
Cairns J.S., Curtsinger J.M., Dahl C.A., Freeman S., Alter B.J.,
Bach F.H.;
"Sequence polymorphism of HLA DR beta 1 alleles relating to T-cell-
recognized determinants.";
Nature 317:166-168(1985).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-123 (ALLELE DRB1*04:04).
PubMed=3458223; DOI=10.1073/pnas.83.8.2642;
Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T.,
Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y.,
Winchester R.J., Nepom G.T., Silver J.;
"Molecular diversity of HLA-DR4 haplotypes.";
Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986).
[13]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:11).
Zhao W., Fernandez-Vina M.A., Stastny P.;
"Full cDNA sequence of HLA-DRB1*0411.";
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[14]
REVIEW.
PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9;
Cresswell P.;
"Invariant chain structure and MHC class II function.";
Cell 84:505-507(1996).
[15]
REVIEW.
PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4;
Villadangos J.A.;
"Presentation of antigens by MHC class II molecules: getting the most
out of them.";
Mol. Immunol. 38:329-346(2001).
[16]
REVIEW.
PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005;
Menendez-Benito V., Neefjes J.;
"Autophagy in MHC class II presentation: sampling from within.";
Immunity 26:1-3(2007).
[17]
REVIEW.
PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
Rocha N., Neefjes J.;
"MHC class II molecules on the move for successful antigen
presentation.";
EMBO J. 27:1-5(2008).
[18]
UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION.
PubMed=18305173; DOI=10.1073/pnas.0708874105;
De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N.,
Pierre P., Gatti E.;
"MHC class II stabilization at the surface of human dendritic cells is
the result of maturation-dependent MARCH I down-regulation.";
Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
[19]
REVIEW.
PubMed=19092054; DOI=10.1242/jcs.035089;
Berger A.C., Roche P.A.;
"MHC class II transport at a glance.";
J. Cell Sci. 122:1-4(2009).
[20]
REVIEW.
PubMed=19533806; DOI=10.3748/wjg.15.2855;
Beswick E.J., Reyes V.E.;
"CD74 in antigen presentation, inflammation, and cancers of the
gastrointestinal tract.";
World J. Gastroenterol. 15:2855-2861(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH A COLLAGEN
PEPTIDE.
PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6;
Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.;
"X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed
with a peptide from human collagen II.";
Immunity 7:473-481(1997).
-!- 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: 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.
-!- INTERACTION:
P0A6Y8:dnaK (xeno); NbExp=5; IntAct=EBI-1033104, EBI-542092;
P0DMV8:HSPA1A; NbExp=10; IntAct=EBI-1033104, EBI-11052499;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}.
Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Lysosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Late endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. 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.
-!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to
sorting into the endosome system and down-regulation of MHC class
II. {ECO:0000305|PubMed:18305173}.
-!- POLYMORPHISM: The following alleles of DRB1-4 are known:
DRB1*04:01, DRB1*04:02, DRB1*04:03, DRB1*04:04, DRB1*04:05,
DRB1*04:06, DRB1*04:07, DRB1*04:08, DRB1*04:09, DRB1*04:10,
DRB1*04:11, DRB1*04:12, DRB1*04:13, DRB1*04:14, DRB1*04:15,
DRB1*04:16, DRB1*04:17, DRB1*04:18, DRB1*04:19, DRB1*04:20,
DRB1*04:21, DRB1*04:22, DRB1*04:23, DRB1*04:24, DRB1*04:25,
DRB1*04:26, DRB1*04:27, DRB1*04:28, DRB1*04:29, DRB1*04:30,
DRB1*04:31, DRB1*04:32, DRB1*04:33, DRB1*04:34, DRB1*04:35,
DRB1*04:36, DRB1*04:37, DRB1*04:38, DRB1*04:39, DRB1*04:40,
DRB1*04:41, DRB1*04:42, DRB1*04:43, DRB1*04:44, DRB1*04:45,
DRB1*04:46, DRB1*04:47, DRB1*04:48, DRB1*04:49, DRB1*04:50,
DRB1*04:51, DRB1*04:52, DRB1*04:53, DRB1*04:54, DRB1*04:55,
DRB1*04:56, DRB1*04:57, DRB1*04:58, DRB1*04:59, DRB1*04:60,
DRB1*04:61, DRB1*04:62, DRB1*04:63, DRB1*04:64, DRB1*04:65,
DRB1*04:66, DRB1*04:67, DRB1*04:68, DRB1*04:69, DRB1*04:70,
DRB1*04:71, DRB1*04:72, DRB1*04:73, DRB1*04:74, DRB1*04:75,
DRB1*04:76, DRB1*04:77 and DRB1*04:78. The sequence shown is that
of DRB1*04:01.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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EMBL; M20548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M20549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M20550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137064; CAC19360.1; -; Genomic_DNA.
EMBL; M17381; AAA59805.1; -; mRNA.
EMBL; K02776; AAA59808.1; -; Genomic_DNA.
EMBL; X96851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ297586; CAC08826.2; -; mRNA.
EMBL; AF029269; AAF65479.1; -; Genomic_DNA.
EMBL; AF112876; AAD29581.1; -; Genomic_DNA.
EMBL; AJ295845; CAC08181.1; -; Genomic_DNA.
EMBL; X02902; CAA26660.1; -; mRNA.
EMBL; M15069; AAA59809.1; -; mRNA.
EMBL; L42143; AAA67104.1; -; mRNA.
PIR; A94681; A29310.
PIR; I79419; I79419.
UniGene; Hs.534322; -.
UniGene; Hs.696211; -.
UniGene; Hs.736560; -.
PDB; 1D5M; X-ray; 2.00 A; B=30-221.
PDB; 1D5X; X-ray; 2.45 A; B=30-221.
PDB; 1D5Z; X-ray; 2.00 A; B=30-221.
PDB; 1D6E; X-ray; 2.45 A; B=30-221.
PDB; 1J8H; X-ray; 2.40 A; B=30-221.
PDB; 2SEB; X-ray; 2.50 A; B=30-221.
PDB; 3O6F; X-ray; 2.80 A; B/F=31-221.
PDB; 3T0E; X-ray; 4.00 A; B=30-221.
PDB; 4IS6; X-ray; 2.50 A; B=30-221.
PDB; 4MCY; X-ray; 2.30 A; B=30-219.
PDB; 4MCZ; X-ray; 2.41 A; B=30-219.
PDB; 4MD0; X-ray; 2.19 A; B=30-219.
PDB; 4MD4; X-ray; 1.95 A; B=30-219.
PDB; 4MD5; X-ray; 1.65 A; B=30-219.
PDB; 4MDI; X-ray; 2.00 A; B=30-219.
PDB; 4MDJ; X-ray; 1.70 A; B=30-219.
PDB; 4Y19; X-ray; 2.50 A; B=30-219.
PDB; 4Y1A; X-ray; 4.00 A; B=30-219.
PDB; 5JLZ; X-ray; 1.99 A; B/D=30-219.
PDB; 5LAX; X-ray; 2.60 A; B/D=30-219.
PDB; 6BIJ; X-ray; 2.10 A; B=31-219.
PDB; 6BIL; X-ray; 2.40 A; B=30-219.
PDB; 6BIN; X-ray; 2.50 A; B=30-219.
PDB; 6BIR; X-ray; 2.30 A; B=30-219.
PDB; 6BIV; X-ray; 2.90 A; A=30-219.
PDB; 6BIX; X-ray; 2.20 A; B=30-219.
PDB; 6BIY; X-ray; 2.05 A; B=30-219.
PDB; 6BIZ; X-ray; 2.10 A; B=30-219.
PDBsum; 1D5M; -.
PDBsum; 1D5X; -.
PDBsum; 1D5Z; -.
PDBsum; 1D6E; -.
PDBsum; 1J8H; -.
PDBsum; 2SEB; -.
PDBsum; 3O6F; -.
PDBsum; 3T0E; -.
PDBsum; 4IS6; -.
PDBsum; 4MCY; -.
PDBsum; 4MCZ; -.
PDBsum; 4MD0; -.
PDBsum; 4MD4; -.
PDBsum; 4MD5; -.
PDBsum; 4MDI; -.
PDBsum; 4MDJ; -.
PDBsum; 4Y19; -.
PDBsum; 4Y1A; -.
PDBsum; 5JLZ; -.
PDBsum; 5LAX; -.
PDBsum; 6BIJ; -.
PDBsum; 6BIL; -.
PDBsum; 6BIN; -.
PDBsum; 6BIR; -.
PDBsum; 6BIV; -.
PDBsum; 6BIX; -.
PDBsum; 6BIY; -.
PDBsum; 6BIZ; -.
ProteinModelPortal; P13760; -.
SMR; P13760; -.
IntAct; P13760; 11.
ChEMBL; CHEMBL3988561; -.
iPTMnet; P13760; -.
PhosphoSitePlus; P13760; -.
DMDM; 122253; -.
EPD; P13760; -.
MaxQB; P13760; -.
PeptideAtlas; P13760; -.
PRIDE; P13760; -.
Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080.
DisGeNET; 3123; -.
GeneCards; HLA-DRB1; -.
H-InvDB; HIX0207659; -.
HGNC; HGNC:4948; HLA-DRB1.
HPA; HPA043151; -.
MalaCards; HLA-DRB1; -.
MIM; 142857; gene.
neXtProt; NX_P13760; -.
HOVERGEN; HBG012730; -.
PhylomeDB; P13760; -.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
ChiTaRS; HLA-DRB1; human.
EvolutionaryTrace; P13760; -.
Proteomes; UP000005640; Chromosome 6.
CleanEx; HS_HLA-DRB1; -.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA.
GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB.
GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB.
GO; GO:0006955; P:immune response; ISS:UniProtKB.
GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:CAFA.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0033674; P:positive regulation of kinase activity; IDA:CAFA.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:CAFA.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:CAFA.
GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA.
GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB.
GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR014745; MHC_II_a/b_N.
InterPro; IPR000353; MHC_II_b_N.
Pfam; PF07654; C1-set; 1.
Pfam; PF00969; MHC_II_beta; 1.
ProDom; PD000328; MHC_II_b_N; 1.
SMART; SM00407; IGc1; 1.
SMART; SM00921; MHC_II_beta; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
Immunity; Lysosome; Membrane; MHC II; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1 29
CHAIN 30 266 HLA class II histocompatibility antigen,
DRB1-4 beta chain.
/FTId=PRO_0000018950.
TOPO_DOM 30 227 Extracellular. {ECO:0000255}.
TRANSMEM 228 250 Helical. {ECO:0000255}.
TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}.
DOMAIN 126 214 Ig-like C1-type.
REGION 30 124 Beta-1.
REGION 125 227 Beta-2.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 5 5 K -> R (in dbSNP:rs707953).
/FTId=VAR_056529.
VARIANT 86 86 D -> S (in allele DRB1*04:11; requires 2
nucleotide substitutions).
/FTId=VAR_016673.
VARIANT 96 96 L -> I (in allele DRB1*04:02).
/FTId=VAR_016674.
VARIANT 99 99 Q -> D (in allele DRB1*04:02; requires 2
nucleotide substitutions).
/FTId=VAR_016675.
VARIANT 100 100 K -> E (in allele DRB1*04:02).
/FTId=VAR_016676.
VARIANT 100 100 K -> R (in allele DRB1*04:03, allele
DRB1*04:04 and allele DRB1*04:11).
/FTId=VAR_016677.
VARIANT 103 103 A -> E (in allele DRB1*04:03 and allele
DRB1*04:11).
/FTId=VAR_016678.
VARIANT 115 115 G -> V (in allele DRB1*04:02, allele
DRB1*04:03, allele DRB1*04:04 and allele
DRB1*04:11).
/FTId=VAR_016679.
VARIANT 262 262 T -> R (in dbSNP:rs9269744).
/FTId=VAR_056531.
CONFLICT 154 154 G -> A (in Ref. 4; AAA59805).
{ECO:0000305}.
STRAND 36 47 {ECO:0000244|PDB:4MD5}.
TURN 48 51 {ECO:0000244|PDB:4MD5}.
STRAND 52 61 {ECO:0000244|PDB:4MD5}.
STRAND 64 70 {ECO:0000244|PDB:4MD5}.
TURN 71 73 {ECO:0000244|PDB:4MD5}.
STRAND 74 80 {ECO:0000244|PDB:4MD5}.
HELIX 81 83 {ECO:0000244|PDB:4MD5}.
HELIX 84 91 {ECO:0000244|PDB:4MD5}.
HELIX 94 106 {ECO:0000244|PDB:4MD5}.
HELIX 108 115 {ECO:0000244|PDB:4MD5}.
HELIX 116 118 {ECO:0000244|PDB:4MD5}.
TURN 119 121 {ECO:0000244|PDB:4MD5}.
STRAND 127 133 {ECO:0000244|PDB:4MD5}.
STRAND 135 137 {ECO:0000244|PDB:6BIY}.
STRAND 143 154 {ECO:0000244|PDB:4MD5}.
STRAND 157 162 {ECO:0000244|PDB:4MD5}.
STRAND 165 167 {ECO:0000244|PDB:4MD5}.
STRAND 171 173 {ECO:0000244|PDB:4MD5}.
STRAND 180 182 {ECO:0000244|PDB:4MD5}.
STRAND 184 191 {ECO:0000244|PDB:4MD5}.
STRAND 199 205 {ECO:0000244|PDB:4MD5}.
STRAND 213 218 {ECO:0000244|PDB:4MD5}.
SEQUENCE 266 AA; 30112 MW; 8116E91DA38294E5 CRC64;
MVCLKFPGGS CMAALTVTLM VLSSPLALAG DTRPRFLEQV KHECHFFNGT ERVRFLDRYF
YHQEEYVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQK RAAVDTYCRH NYGVGESFTV
QRRVYPEVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNG
DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL
FLGAGLFIYF RNQKGHSGLQ PTGFLS


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