HLA class II histocompatibility antigen, DR alpha chain precursor

Names and origin

Protein names

Recommended name:
HLA class II histocompatibility antigen, DR alpha chain
Alternative name(s):
MHC class II antigen DRA

Gene names

Name:	HLA-DRA
Synonyms:	HLA-DRA1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Subunit structure	Heterodimer of an alpha chain and a beta chain. Ref.26 Ref.27 Ref.28 Ref.29 Ref.30
Subcellular location	Membrane; Single-pass type I membrane protein.
Polymorphism	The following alleles of DRA are known: DRA0101 and DRA0102. The sequence shown is that of DRA*0101.
Involvement in disease	Genetic variations in HLA-DRA are associated with susceptibility to hepatitis B virus infection (HBV infection) [MIM:610424]. Approximately one third of all cases of cirrhosis and half of all cases of hepatocellular carcinoma can be attributed to chronic HBV infection. HBV infection may result in subclinical or asymptomatic infection, acute self-limited hepatitis, or fulminant hepatitis requiring liver transplantation.
Sequence similarities	Belongs to the MHC class II family. Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

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Ontologies

Keywords
Biological process	Immune response
Cellular component	MHC II Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	antigen processing and presentation of peptide or polysaccharide antigen via MHC class II Inferred from electronic annotation. Source: UniProtKB-KW immune response Ref.4 Ref.13 Non-traceable author statement. Source: UniProtKB
Cellular component	MHC class II protein complex Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Ref.4 Ref.13 Non-traceable author statement. Source: UniProtKB lysosome Inferred from direct assay. Source: MGI
Molecular function	MHC class II receptor activity Ref.4 Ref.13 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.11 Ref.12 Ref.13

Chain

26 – 254

229

HLA class II histocompatibility antigen, DR alpha chain

PRO_0000018947

Regions

Topological domain

26 – 216

191

Extracellular Potential

Transmembrane

217 – 239

23

Potential

Topological domain

240 – 254

15

Cytoplasmic Potential

Domain

112 – 204

93

Ig-like C1-type

Region

26 – 109

84

Alpha-1

Region

110 – 203

94

Alpha-2

Region

204 – 216

13

Connecting peptide

Amino acid modifications

Glycosylation

103

1

N-linked (GlcNAc...) Ref.19

Glycosylation

143

1

N-linked (GlcNAc...) Ref.19

Disulfide bond

132 ↔ 188

Ref.27 Ref.28 Ref.29 Ref.30

Natural variations

Natural variant

16

1

V → L: dbSNP rs16822586.

VAR_035241

Natural variant

242

1

V → L in allele DRA*0102. dbSNP rs7192. Ref.8 Ref.10

VAR_004399

Experimental info

Sequence conflict

28 – 29

2

EE → AD AA sequence Ref.13

Sequence conflict

33

1

I → T AA sequence Ref.13

Sequence conflict

34 – 35

2

QA → YP AA sequence Ref.13

Sequence conflict

48

1

M → Q AA sequence Ref.13

Sequence conflict

54

1

D → T AA sequence Ref.13

Sequence conflict

59

1

V → Y AA sequence Ref.12

Sequence conflict

64

1

K → L AA sequence Ref.12

Sequence conflict

67

1

V → A AA sequence Ref.11

Sequence conflict

69

1

R → L AA sequence Ref.12

Sequence conflict

75

1

R → P AA sequence Ref.12

Sequence conflict

78

1

S → D AA sequence Ref.12

Sequence conflict

149

1

N → E AA sequence Ref.11

Secondary structure

1

.

254

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P01903-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3CD1CDBA952B2350
Show »

FASTA

254

28,607

        10         20         30         40         50         60 
MAISGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD FDGDEIFHVD 

        70         80         90        100        110        120 
MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK RSNYTPITNV PPEVTVLTNS 

       130        140        150        160        170        180 
PVELREPNVL ICFIDKFTPP VVNVTWLRNG KPVTTGVSET VFLPREDHLF RKFHYLPFLP 

       190        200        210        220        230        240 
STEDVYDCRV EHWGLDEPLL KHWEFDAPSP LPETTENVVC ALGLTVGLVG IIIGTIFIIK 

       250 
GVRKSNAAER RGPL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of an HLA-DR alpha-chain cDNA clone and intron-exon organization of the corresponding gene." Lee J.S., Trowsdale J., Travers P.J., Carey J., Grosveld F., Jenkins J., Bodmer W.F. Nature 299:750-752(1982) [PubMed: 6811954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRA*0101).
[2]	"Cloning the heavy chain of human HLA-DR antigen using synthetic oligodeoxyribonucleotides as hybridization probes." Kajimura Y., Toyoda H., Sato M., Miyakoshi S., Kaplan S.A., Ike Y., Goyert S.M., Silver J., Hawke D., Shively J.E., Suggs S.V., Wallace R.B., Itakura K. DNA 2:175-182(1983) [PubMed: 6416803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRA*0101).
[3]	"Organization of the transcriptional unit of a human class II histocompatibility antigen: HLA-DR heavy chain." Schamboeck A., Korman A.J., Kamb A., Strominger J.L. Nucleic Acids Res. 11:8663-8675(1983) [PubMed: 6324094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRA*0102).
[4]	"Structure and nucleotide sequence of the heavy chain gene of HLA-DR." Das H.K., Lawrance S.K., Weissman S.M. Proc. Natl. Acad. Sci. U.S.A. 80:3543-3547(1983) [PubMed: 6304715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRA*0101).
[5]	Erratum Das H.K., Lawrance S.K., Weissman S.M. Proc. Natl. Acad. Sci. U.S.A. 80:7024-7024(1983) Cited for: SEQUENCE REVISION.
[6]	"Rapid nonlysosomal degradation of assembled HLA class II glycoproteins incorporating a mutant DR alpha-chain." Koppelman B., Cresswell P. J. Immunol. 145:2730-2736(1990) [PubMed: 2212658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRA*0102).
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRA*0101).
[8]	"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. Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DRA0101 AND DRA0102).
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRA*0101).
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRA0101 AND DRA0102). Tissue: Blood and Colon.
[11]	"Primary structure of class II human histocompatibility antigens. 2nd Communication. Amino acid sequence of the N-terminal 179 residues of the alpha-chain of an HLA-Dw2/DR2 alloantigen." Yang C.-Y., Kratzin H., Gotz H., Thinnes F.P., Kruse T., Egert G., Pauly E., Kolbel S., Wernet P., Hilschmann N. Hoppe-Seyler's Z. Physiol. Chem. 363:671-676(1982) [PubMed: 6955253] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-204.
[12]	"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: 6600932] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-94. Tissue: B-cell.
[13]	"Alpha chain of HLA-DR transplantation antigens is a member of the same protein superfamily as the immunoglobulins." Larhammar D., Gustafsson K., Claesson L., Bill P., Wiman K., Schenning L., Sundelin J., Widmark E., Peterson P.A., Rask L. Cell 30:153-161(1982) [PubMed: 6812963] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-60, NUCLEOTIDE SEQUENCE [MRNA] OF 32-202 AND 204-254.
[14]	"The amino acid sequence and gene organization of the heavy chain of the HLA-DR antigen: homology to immunoglobulins." Korman A.J., Auffray C., Schamboeck A., Strominger J.L. Proc. Natl. Acad. Sci. U.S.A. 79:6013-6017(1982) [PubMed: 6821129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-254 (ALLELE DRA*0102).
[15]	*"The HLA-DRA0102 allele: correct nucleotide sequence and associated HLA haplotypes."** Kralovicova J., Marsh S.G., Waller M.J., Hammarstrom L., Vorechovsky I. Tissue Antigens 60:266-267(2002) [PubMed: 12445311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-254 (ALLELE DRA*0102). Tissue: Blood.
[16]	"Heterozygote advantage for HLA class-II type in hepatitis B virus infection." Thursz M.R., Thomas H.C., Greenwood B.M., Hill A.V.S. Nat. Genet. 17:11-12(1997) [PubMed: 9288086] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION.
[17]	Erratum Thursz M.R., Thomas H.C., Greenwood B.M., Hill A.V.S. Nat. Genet. 18:88-88(1998)
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-143, MASS SPECTROMETRY. Tissue: Liver.
[20]	"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: 8316295] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-207.
[21]	"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: 8145819] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-207.
[22]	"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: 8152483] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB.
[23]	"The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3." Ghosh P., Amaya M., Mellins E., Wiley D.C. Nature 378:457-462(1995) [PubMed: 7477400] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 30-205 OF HLA-DRA/HLA-DRB1 HETERODIMER IN COMPLEX WITH CD74 PEPTIDE (CLIP), SUBUNIT, GLYCOSYLATION AT ASN-103 AND ASN-143, DISULFIDE BOND.
[24]	*"X-ray crystal structure of HLA-DR4 (DRA0101, DRB10401) 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: 9354468] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH PEPTIDE FROM COLLAGEN.
[25]	*"Crystal structure of HLA-DR2 (DRA0101, DRB11501) complexed with a peptide from human myelin basic protein."* Smith K.J., Pyrdol J., Gauthier L., Wiley D.C., Wucherpfennig K.W. J. Exp. Med. 188:1511-1520(1998) [PubMed: 9782128] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH PEPTIDE FROM MYELIN BASIC PROTEIN.
[26]	"Structural basis for the binding of an immunodominant peptide from myelin basic protein in different registers by two HLA-DR2 proteins." Li Y., Li H., Martin R., Mariuzza R.A. J. Mol. Biol. 304:177-188(2000) [PubMed: 11080454] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX WITH MBP PEPTIDE, SUBUNIT.
[27]	"Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II." Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P., Schlievert P.M., Mariuzza R.A. Immunity 14:93-104(2001) [PubMed: 11163233] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND STREPTOCOCCUS PYOGENES SPEC PEPTIDE, SUBUNIT, DISULFIDE BONDS.
[28]	"A functional and structural basis for TCR cross-reactivity in multiple sclerosis." Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K., Madsen L., Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K., Stuart D.I., Bell J.I., Jones E.Y., Fugger L. Nat. Immunol. 3:940-943(2002) [PubMed: 12244309] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 26-207 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX EPSTEIN-BARR VIRUS BALF5 PEPTIDE, SUBUNIT, DISULFIDE BOND.
[29]	"Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule." Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A. EMBO J. 24:2968-2979(2005) [PubMed: 16079912] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND TRAC, SUBUNIT, DISULFIDE BONDS.
[30]	*"Crystallographic structure of the human leukocyte antigen DRA, DRB30101: models of a directional alloimmune response and autoimmunity."** Parry C.S., Gorski J., Stern L.J. J. Mol. Biol. 371:435-446(2007) [PubMed: 17583734] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 26-207 OF HLA-DRA/HLA-DRB3 HETERODIMER IN COMPLEX WITH ITGB3 PEPTIDE (ALLOANTIGEN HPA-1A), SUBUNIT, DISULFIDE BOND.
[31]	"The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles." Dai S., Crawford F., Marrack P., Kappler J.W. Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008) [PubMed: 18697946] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB3 HETERODIMER IN COMPLEX WITH EEF1A2 PEPTIDE.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00194 mRNA. Translation: AAA36275.1.
K01171 mRNA. Translation: AAA59785.1.
X00274 Genomic DNA. Translation: CAA25076.1. Different initiation.
J00204, J00203 Genomic DNA. Translation: AAA36302.1.
M60334 mRNA. Translation: AAA59783.1.
CR457013 mRNA. Translation: CAG33294.1.
AL662796 Genomic DNA. Translation: CAI18266.1.
AL670296 Genomic DNA. Translation: CAI17571.1.
AL935032 Genomic DNA. Translation: CAI18476.1.
BX120007 Genomic DNA. Translation: CAM26203.1.
Z84814 Genomic DNA. Translation: CAB06609.1.
CH471081 Genomic DNA. Translation: EAX03630.1.
BC032350 mRNA. Translation: AAH32350.1.
BC071659 mRNA. Translation: AAH71659.1.
V00523 mRNA. Translation: CAA23782.1.
J00201 Genomic DNA. Translation: AAA36301.1.
AF481359 Genomic DNA. Translation: AAO23887.1.

IPI

IPI00005171.

PIR

HLHUDA. A93952.

RefSeq

NP_061984.2.

UniGene

Hs.520048

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A6A	X-ray	2.75	A	30-205	[»]
1AQD	X-ray	2.45	A/D/G/J	26-217	[»]
1BX2	X-ray	2.60	A/D	27-206	[»]
1D5M	X-ray	2.00	A	26-206	[»]
1D5X	X-ray	2.45	A	26-206	[»]
1D5Z	X-ray	2.00	A	26-206	[»]
1D6E	X-ray	2.45	A	26-206	[»]
1DLH	X-ray	2.80	A/D	28-207	[»]
1FV1	X-ray	1.90	A/D	26-206	[»]
1FYT	X-ray	2.60	A	26-206	[»]
1H15	X-ray	3.10	A/D	26-207	[»]
1HQR	X-ray	3.20	A	26-206	[»]
1HXY	X-ray	2.60	A	26-207	[»]
1J8H	X-ray	2.40	A	26-206	[»]
1JWM	X-ray	2.70	A	26-207	[»]
1JWS	X-ray	2.60	A	26-207	[»]
1JWU	X-ray	2.30	A	26-207	[»]
1KG0	X-ray	2.65	A	28-207	[»]
1KLG	X-ray	2.40	A	29-205	[»]
1KLU	X-ray	1.93	A	29-207	[»]
1LO5	X-ray	3.20	A	26-207	[»]
1PYW	X-ray	2.10	A	26-207	[»]
1R5I	X-ray	2.60	A/E	26-206	[»]
1SEB	X-ray	2.70	A/E	26-206	[»]
1SJE	X-ray	2.45	A	28-207	[»]
1SJH	X-ray	2.25	A	28-207	[»]
1T5W	X-ray	2.40	A/D	27-206	[»]
1T5X	X-ray	2.50	A	27-207	[»]
1YMM	X-ray	3.50	A	26-216	[»]
1ZGL	X-ray	2.80	A/D/G/J	26-206	[»]
2FSE	X-ray	3.10	A/C	29-205	[»]
2G9H	X-ray	2.00	A	26-207	[»]
2IAM	X-ray	2.80	A	26-207	[»]
2IAN	X-ray	2.80	A/F/K/P	26-207	[»]
2ICW	X-ray	2.41	A/D	28-206	[»]
2IPK	X-ray	2.30	A	26-207	[»]
2OJE	X-ray	3.00	A/E	27-206	[»]
2Q6W	X-ray	2.25	A/D	26-207	[»]
2SEB	X-ray	2.50	A	26-206	[»]
2WBJ	X-ray	3.00	A/E	26-218	[»]
3C5J	X-ray	1.80	A	26-206	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6063N.

STRING

P01903.

PTM databases

PhosphoSite

P01903.

Proteomic databases

PRIDE

P01903.

Genome annotation databases

Ensembl

ENST00000383259; ENSP00000372746; ENSG00000206308; Homo sapiens. [Genome view]
ENST00000411524; ENSP00000405295; ENSG00000234794; Homo sapiens. [Genome view]
ENST00000414698; ENSP00000402951; ENSG00000230726; Homo sapiens. [Genome view]
ENST00000416883; ENSP00000410443; ENSG00000228987; Homo sapiens. [Genome view]
ENST00000442960; ENSP00000404533; ENSG00000226260; Homo sapiens. [Genome view]

GeneID

3122.

KEGG

hsa:3122.

Organism-specific databases

CTD

3122.

GeneCards

GC06P032434.
GC06Pf32507.

H-InvDB

HIX0005752.

HGNC

HGNC:4947. HLA-DRA.

HPA

CAB015402.

MIM

142860. gene.
610424. phenotype.

Orphanet

505. Lassueur-Graham-Little syndrome.

PharmGKB

PA35071.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13462.

HOVERGEN

P01903.

InParanoid

P01903.

OrthoDB

EOG96X1TH.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_stat4pathway. IL12 signaling mediated by STAT4.
il12_2pathway. IL12-mediated signaling events.
tcrpathway. TCR signaling in naive CD4+ T cells.

Reactome

REACT_6900. Signaling in Immune system.

Gene expression databases

CleanEx

HS_HLA-DRA.

Genevestigator

P01903.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011162. MHC_I/II-like_Ag-recog.
IPR001003. MHC_II_a_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF07654. C1-set. 1 hit.
PF00993. MHC_II_alpha. 1 hit.
[Graphical view]

SMART

SM00407. IGc1. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

12390.

SOURCE

Search...

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Entry information

Entry name

2DRA_HUMAN

Accession

Primary (citable) accession number: P01903
Secondary accession number(s): A2BET4

Q9TP70

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 19, 2010
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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