P13760 (2B14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
HLA class II histocompatibility antigen, DRB1-4 beta chain

Alternative name(s):
MHC class II antigen DRB1*4
Short name=DR-4
Short name=DR4

Gene names

Name:

HLA-DRB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 miroenvironment 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 apparatus › trans-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.18
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.18
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.
Sequence similarities	Belongs to the MHC class II family. Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Immunity
Cellular component	Cell membrane Endoplasmic reticulum Endosome Golgi apparatus Lysosome MHC II Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T 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 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 immunoglobulin production involved in immunoglobulin mediated immune response Inferred from sequence or structural similarity. Source: UniProtKB inflammatory response to antigenic stimulus Inferred from direct assay PubMed 15795121. 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 inflammatory response to antigenic stimulus Inferred from direct assay PubMed 18039812. 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_component	ER 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 external side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to plasma membrane Traceable author statement PubMed 10425186. Source: UniProtKB late endosome membrane Inferred from direct assay Ref.18. Source: UniProtKB lysosomal membrane Inferred from direct assay Ref.18. Source: UniProtKB trans-Golgi network membrane Traceable author statement. Source: Reactome
Molecular_function	MHC class II receptor activity Traceable author statement PubMed 10425186. Source: UniProtKB peptide antigen binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Chain

30 – 266

237

HLA class II histocompatibility antigen, DRB1-4 beta chain

PRO_0000018950

Regions

Topological domain

30 – 227

198

Extracellular Potential

Transmembrane

228 – 250

23

Helical; Potential

Topological domain

251 – 266

16

Cytoplasmic Potential

Domain

126 – 214

89

Ig-like C1-type

Region

30 – 124

95

Beta-1

Region

125 – 227

103

Beta-2

Amino acid modifications

Glycosylation

48

1

N-linked (GlcNAc...) Potential

Disulfide bond

44 ↔ 108

By similarity

Disulfide bond

146 ↔ 202

By similarity

Cross-link

254

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant

5

1

K → R.
Corresponds to variant rs9270305 [ dbSNP | Ensembl ].

VAR_056529

Natural variant

86

1

D → S in allele DRB1*04:11; requires 2 nucleotide substitutions.

VAR_016673

Natural variant

96

1

L → I in allele DRB1*04:02.

VAR_016674

Natural variant

99

1

Q → D in allele DRB1*04:02; requires 2 nucleotide substitutions.

VAR_016675

Natural variant

100

1

K → E in allele DRB1*04:02.

VAR_016676

Natural variant

100

1

K → R in allele DRB1*04:03, allele DRB1*04:04 and allele DRB1*04:11.

VAR_016677

Natural variant

103

1

A → E in allele DRB1*04:03 and allele DRB1*04:11.

VAR_016678

Natural variant

115

1

G → V in allele DRB1*04:02, allele DRB1*04:03, allele DRB1*04:04 and allele DRB1*04:11.

VAR_016679

Natural variant

236

1

V → M.
Corresponds to variant rs2230816 [ dbSNP | Ensembl ].

VAR_056530

Natural variant

262

1

T → R.
Corresponds to variant rs9269744 [ dbSNP | Ensembl ].

VAR_056531

Experimental info

Sequence conflict

154

1

G → A in AAA59805. Ref.4

Secondary structure

1

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266

Helix Strand Turn

Details...

Beta strand

36 – 47

12

Turn

48 – 51

4

Beta strand

52 – 61

10

Beta strand

64 – 70

7

Turn

71 – 73

3

Beta strand

75 – 80

6

Helix

81 – 83

3

Helix

84 – 91

8

Helix

94 – 101

8

Helix

103 – 106

4

Helix

108 – 115

8

Helix

116 – 118

3

Turn

119 – 121

3

Beta strand

127 – 132

6

Beta strand

143 – 154

12

Beta strand

157 – 162

6

Beta strand

165 – 167

3

Beta strand

169 – 173

5

Beta strand

180 – 182

3

Beta strand

184 – 191

8

Beta strand

199 – 205

7

Beta strand

213 – 218

6

Sequences

	Sequence		Length	Mass (Da)
	P13760 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 8116E91DA38294E5	FASTA	266	30,112
	10 20 30 40 50 60 MVCLKFPGGS CMAALTVTLM VLSSPLALAG DTRPRFLEQV KHECHFFNGT ERVRFLDRYF 70 80 90 100 110 120 YHQEEYVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQK RAAVDTYCRH NYGVGESFTV 130 140 150 160 170 180 QRRVYPEVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNG 190 200 210 220 230 240 DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL 250 260 FLGAGLFIYF RNQKGHSGLQ PTGFLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Class II genes of the human major histocompatibility complex. Organization and evolutionary relationship of the DR beta genes." Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., Rask L. J. Biol. Chem. 262:8748-8758(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*04:01).
[2]	Erratum Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., Rask L. J. Biol. Chem. 263:8551-8551(1988) Cited for: SEQUENCE REVISION.
[3]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*04:01).
[4]	"Allelic variation in the DR subregion of the human major histocompatibility complex." Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., McDevitt H.O. Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*04:01).
[5]	"Structural organization of the DR subregion of the human major histocompatibility complex." Spies T., Sorrentino R., Boss J.M., Okada K., Strominger J.L. Proc. Natl. Acad. Sci. U.S.A. 82:5165-5169(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01).
[6]	"A new silent mutation at codon 35 in exon 2 yielding a DRB1*04012 allele." Thonnard J., Gervais T., Heusterpreute M., Mersch G., De Canck I., De Greef C., Demanet C., Van Waeyenberge C. Tissue Antigens 49:274-276(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01).
[7]	"Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 alleles." Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., Marsh S.G.E. Eur. J. Immunogenet. 29:453-455(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:02).
[8]	"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 (ALLELE DRB1*04:03). Tissue: Blood.
[9]	"New HLA class II (DRB1) alleles detected by sequencing-based typing." Greville W.D., van Eijck A., Dunckley H. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (ALLELE DRB1*04:03).
[10]	"Confirmatory sequence of HLA-DRB1*04032." Guttridge M.G., Hammond L. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:03).
[11]	"Sequence polymorphism of HLA DR beta 1 alleles relating to T-cell-recognized determinants." Cairns J.S., Curtsinger J.M., Dahl C.A., Freeman S., Alter B.J., Bach F.H. Nature 317:166-168(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:04).
[12]	"Molecular diversity of HLA-DR4 haplotypes." 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. Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-123 (ALLELE DRB1*04:04).
[13]	"Full cDNA sequence of HLA-DRB1*0411." Zhao W., Fernandez-Vina M.A., Stastny P. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:11).
[14]	"Invariant chain structure and MHC class II function." Cresswell P. Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II." Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C. Immunity 7:473-481(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH A COLLAGEN PEPTIDE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M20548 Genomic DNA. No translation available.
M20549 Genomic DNA. No translation available.
M20550 Genomic DNA. No translation available.
AL137064 Genomic DNA. Translation: CAC19360.1.
M17381 mRNA. Translation: AAA59805.1.
K02776 Genomic DNA. Translation: AAA59808.1.
X96851 Genomic DNA. No translation available.
AJ297586 mRNA. Translation: CAC08826.2.
AF029269 Genomic DNA. Translation: AAF65479.1.
AF112876 Genomic DNA. Translation: AAD29581.1.
AJ295845 Genomic DNA. Translation: CAC08181.1.
X02902 mRNA. Translation: CAA26660.1.
M15069 mRNA. Translation: AAA59809.1.
L42143 mRNA. Translation: AAA67104.1.

IPI

IPI00887633.

PIR

A29310. A94681.
I79419.

UniGene

Hs.534322.
Hs.696211.
Hs.716081.
Hs.723344.
Hs.736560.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D5M	X-ray	2.00	B	30-221	[»]
1D5X	X-ray	2.45	B	30-221	[»]
1D5Z	X-ray	2.00	B	30-221	[»]
1D6E	X-ray	2.45	B	30-221	[»]
1J8H	X-ray	2.40	B	30-221	[»]
2SEB	X-ray	2.50	B	30-221	[»]
3O6F	X-ray	2.80	B/F	30-221	[»]
3T0E	X-ray	4.00	B	30-221	[»]

ProteinModelPortal

P13760.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13760. 6 interactions.

PTM databases

PhosphoSite

P13760.

Polymorphism databases

DMDM

122253.

Proteomic databases

PaxDb

P13760.

PRIDE

P13760.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000419393; ENSP00000403458; ENSG00000228080.

Organism-specific databases

GeneCards

GC06M032546.

H-InvDB

HIX0207659.

HGNC

HGNC:4948. HLA-DRB1.

MIM

142857. gene.

neXtProt

NX_P13760.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG68200.

HOVERGEN

HBG012730.

InParanoid

P13760.

OrthoDB

EOG461454.

PhylomeDB

P13760.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P13760.

CleanEx

HS_HLA-DRB1.

Genevestigator

P13760.

GermOnline

ENSG00000196126. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
3.10.320.10. 1 hit.

InterPro

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]

Pfam

PF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]

ProDom

PD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]

SUPFAM

SSF54452. MHC_I/II-like_Ag-recog. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
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ProtoNet

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Other

ChiTaRS

HLA-DRB1. human.

EvolutionaryTrace

P13760.

SOURCE

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Entry information

Entry name

2B14_HUMAN

Accession

Primary (citable) accession number: P13760
Secondary accession number(s): O19717 , O19739, P13759, Q29875, Q30145, Q9GIX9, Q9GIY4, Q9MY13, Q9XRY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.