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Protein

HLA class II histocompatibility antigen, DR beta 5 chain

Gene

HLA-DRB5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • peptide antigen binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiR-HSA-202424. Downstream TCR signaling.
R-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-202430. Translocation of ZAP-70 to Immunological synapse.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-389948. PD-1 signaling.
R-HSA-877300. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
HLA class II histocompatibility antigen, DR beta 5 chain
Alternative name(s):
DR beta-5
DR2-beta-2
Dw2
MHC class II antigen DRB5
Gene namesi
Name:HLA-DRB5Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4953. HLA-DRB5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 227198ExtracellularSequence analysisAdd
BLAST
Transmembranei228 – 24821HelicalSequence analysisAdd
BLAST
Topological domaini249 – 26618CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, MHC II

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35076.

Polymorphism and mutation databases

BioMutaiHLA-DRB5.
DMDMi74754558.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 266237HLA class II histocompatibility antigen, DR beta 5 chainPRO_5000143106Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to down-regulation of MHC class II.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

EPDiQ30154.
PaxDbiQ30154.
PeptideAtlasiQ30154.
PRIDEiQ30154.

Expressioni

Gene expression databases

BgeeiQ30154.
GenevisibleiQ30154. HS.

Organism-specific databases

HPAiHPA043151.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit; also referred as MHC class II molecule. In the endoplasmic reticulum (ER) it forms a heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system; CD74 undergoes sequential degradation by various proteases; leaving a small fragment termed CLIP on each MHC class II molecule. MHC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP and facilitate the binding of antigenic peptides.4 Publications

Protein-protein interaction databases

BioGridi109372. 15 interactions.
IntActiQ30154. 6 interactions.
MINTiMINT-6630223.
STRINGi9606.ENSP00000364114.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 4712Combined sources
Turni48 – 514Combined sources
Beta strandi52 – 6110Combined sources
Beta strandi64 – 707Combined sources
Turni71 – 733Combined sources
Beta strandi75 – 806Combined sources
Helixi81 – 833Combined sources
Helixi84 – 918Combined sources
Helixi94 – 1018Combined sources
Helixi103 – 1064Combined sources
Helixi108 – 1158Combined sources
Helixi116 – 1183Combined sources
Turni119 – 1213Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi137 – 15418Combined sources
Beta strandi157 – 16610Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1929Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi213 – 2186Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FV1X-ray1.90B/E30-219[»]
1H15X-ray3.10B/E30-219[»]
1HQRX-ray3.20B30-219[»]
1ZGLX-ray2.80B/E/H/K30-221[»]
ProteinModelPortaliQ30154.
SMRiQ30154. Positions 30-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ30154.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the MHC class II family.Sequence analysis

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWG3. Eukaryota.
ENOG410YI0S. LUCA.
GeneTreeiENSGT00760000118970.
HOVERGENiHBG012730.
InParanoidiQ30154.
KOiK06752.
OMAiNIFECHF.
OrthoDBiEOG7PS1GV.
PhylomeDBiQ30154.
TreeFamiTF336626.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011162. MHC_I/II-like_Ag-recog.
IPR014745. MHC_II_a/b_N.
IPR000353. MHC_II_b_N.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]
ProDomiPD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q30154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVCLKLPGGS YMAKLTVTLM VLSSPLALAG DTRPRFLQQD KYECHFFNGT
60 70 80 90 100
ERVRFLHRDI YNQEEDLRFD SDVGEYRAVT ELGRPDAEYW NSQKDFLEDR
110 120 130 140 150
RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPARTQTLQH HNLLVCSVNG
160 170 180 190 200
FYPGSIEVRW FRNSQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY
210 220 230 240 250
TCQVEHPSVT SPLTVEWRAQ SESAQSKMLS GVGGFVLGLL FLGAGLFIYF
260
KNQKGHSGLH PTGLVS
Length:266
Mass (Da):30,056
Last modified:November 1, 1996 - v1
Checksum:i0D4335BAEEA6AF22
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391Q → E AA sequence (PubMed:6576979).Curated

Polymorphismi

The following alleles of DRB5 are known: DRB5*01:01, DRB5*01:02, DRB5*01:03, DRB5*01:04, DRB5*01:05, DRB5*01:06, DRB5*01:07, DRB5*01:09, DRB5*01:11, DRB5*01:12 DRB5*01:13, DRB5*01:14, DRB5*02:02, DRB5*02:03, DRB5*02:04, DRB5*02:05. The sequence shown is that of DRB5*01:01.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141K → M.
Corresponds to variant rs1064587 [ dbSNP | Ensembl ].
VAR_060951
Natural varianti14 – 141K → Q.
Corresponds to variant rs701884 [ dbSNP | Ensembl ].
VAR_060952
Natural varianti14 – 141K → V in allele DRB5*02:02; requires 2 nucleotide substitutions.
VAR_060953
Natural varianti20 – 201M → T.
Corresponds to variant rs17211043 [ dbSNP | Ensembl ].
VAR_050355
Natural varianti28 – 281L → S.3 Publications
VAR_039871
Natural varianti33 – 331R → Q.
Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
VAR_050356
Natural varianti35 – 351R → C in allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05.
Corresponds to variant rs1136744 [ dbSNP | Ensembl ].
VAR_060954
Natural varianti41 – 411K → T.
Corresponds to variant rs200581589 [ dbSNP | Ensembl ].
VAR_050357
Natural varianti57 – 571H → Q.
Corresponds to variant rs202185589 [ dbSNP | Ensembl ].
VAR_060955
Natural varianti59 – 591D → G in allele DRB5*01:02, allele DRB5*01:03, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05.
Corresponds to variant rs41546317 [ dbSNP | Ensembl ].
VAR_060956
Natural varianti59 – 591D → H.
Corresponds to variant rs707955 [ dbSNP | Ensembl ].
VAR_060957
Natural varianti62 – 621N → H.
Corresponds to variant rs1059576 [ dbSNP | Ensembl ].
VAR_050358
Natural varianti66 – 661D → N in allele DRB5*01:02, allele DRB5*01:03, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05.
Corresponds to variant rs77853982 [ dbSNP | Ensembl ].
VAR_060958
Natural varianti66 – 661D → Y in allele DRB5*01:14.
Corresponds to variant rs77853982 [ dbSNP | Ensembl ].
VAR_060959
Natural varianti67 – 671L → V in allele DRB5*01:02, allele DRB5*01:03, allele DRB5*01:05, allele DRB5*01:14, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05.
Corresponds to variant rs1059580 [ dbSNP | Ensembl ].
VAR_060960
Natural varianti87 – 871A → E in allele DRB5*01:13.
VAR_060961
Natural varianti89 – 891Y → S in allele DRB5*01:12.
Corresponds to variant rs41541218 [ dbSNP | Ensembl ].
VAR_060962
Natural varianti96 – 961F → I in allele DRB5*01:06, allele DRB5*01:07, allele DRB5*01:11, allele DRB5*02:02 and allele DRB5*02:03.
Corresponds to variant rs41562819 [ dbSNP | Ensembl ].
VAR_060964
Natural varianti96 – 961F → L in allele DRB5*02:05.
Corresponds to variant rs41562819 [ dbSNP | Ensembl ].
VAR_060963
Natural varianti99 – 991D → E.
Corresponds to variant rs41559913 [ dbSNP | Ensembl ].
VAR_060965
Natural varianti99 – 991D → G.
Corresponds to variant rs41545413 [ dbSNP | Ensembl ].
VAR_060966
Natural varianti99 – 991D → H.
Corresponds to variant rs41547217 [ dbSNP | Ensembl ].
VAR_060967
Natural varianti99 – 991D → N in allele DRB5*01:09.
Corresponds to variant rs41547217 [ dbSNP | Ensembl ].
VAR_060968
Natural varianti99 – 991D → Q in allele DRB5*01:06, allele DRB5*01:11, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05; requires 2 nucleotide substitutions.
VAR_060969
Natural varianti99 – 991D → R in allele DRB5*01:12; requires 2 nucleotide substitutions.
VAR_060970
Natural varianti100 – 1001R → A in allele DRB5*01:06, allele DRB5*01:11, allele DRB5*02:02, allele DRB5*02:03 and allele DRB5*02:04; requires 2 nucleotide substitutions.
VAR_060971
Natural varianti100 – 1001R → G.
Corresponds to variant rs41551116 [ dbSNP | Ensembl ].
VAR_060972
Natural varianti100 – 1001R → T in allele DRB5*01:03.
Corresponds to variant rs41544215 [ dbSNP | Ensembl ].
VAR_060973
Natural varianti103 – 1031A → E in allele DRB5*01:12.
Corresponds to variant rs1059598 [ dbSNP | Ensembl ].
VAR_060974
Natural varianti103 – 1031A → L in allele DRB5*01:04; requires 2 nucleotide substitutions.
VAR_060975
Natural varianti106 – 1061T → N.
Corresponds to variant rs115817940 [ dbSNP | Ensembl ].
VAR_050359
Natural varianti107 – 1071Y → V in allele DRB5*01:12; requires 2 nucleotide substitutions.
VAR_060976
Natural varianti114 – 1141V → A in allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05.
Corresponds to variant rs1136778 [ dbSNP | Ensembl ].
VAR_060977
Natural varianti115 – 1151G → V in allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05.
Corresponds to variant rs41556512 [ dbSNP | Ensembl ].
VAR_060978
Natural varianti154 – 1541G → A.2 Publications
Corresponds to variant rs113395425 [ dbSNP | Ensembl ].
VAR_039872
Natural varianti164 – 1641S → G in allele DRB5*02:02.
Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
VAR_060979
Natural varianti186 – 1861T → I in allele DRB5*02:02.
Corresponds to variant rs41559420 [ dbSNP | Ensembl ].
VAR_060980
Natural varianti232 – 2321V → I in allele DRB5*02:02.
Corresponds to variant rs41553512 [ dbSNP | Ensembl ].
VAR_060981

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20429 mRNA. Translation: AAA59822.1.
M35159 Genomic DNA. Translation: AAA59791.1.
AL713966 Genomic DNA. Translation: CAI18079.1.
AK314834 mRNA. Translation: BAG37353.1.
BC009234 mRNA. Translation: AAH09234.1.
U31770 mRNA. Translation: AAB63983.1.
U59685 Genomic DNA. Translation: AAB52229.1.
M16954 mRNA. Translation: AAA36276.1.
M16955 mRNA. Translation: AAA36277.1.
M17377 mRNA. Translation: AAA59818.1.
X87210 Genomic DNA. No translation available.
FN430425 Genomic DNA. Translation: CAZ86696.1.
Z83201 Genomic DNA. Translation: CAB05668.1.
AF122887 Genomic DNA. Translation: AAD31766.1.
AJ271159 Genomic DNA. Translation: CAB71144.1.
AY141137 Genomic DNA. Translation: AAN28924.1.
AJ427352 Genomic DNA. Translation: CAD20460.1.
AY457037 Genomic DNA. Translation: AAR20446.2.
Y09342 Genomic DNA. Translation: CAA70524.1.
Y13727 Genomic DNA. Translation: CAA74055.1.
M91001 Genomic DNA. No translation available.
CCDSiCCDS4751.1.
PIRiB27060.
B28043.
B28756.
C32526.
D25239.
I68733.
PT0169.
PT0170.
PT0171.
RefSeqiNP_002116.2. NM_002125.3.
UniGeneiHs.485130.
Hs.534322.
Hs.696211.
Hs.736560.

Genome annotation databases

EnsembliENST00000374975; ENSP00000364114; ENSG00000198502.
GeneIDi3127.
KEGGihsa:3127.
UCSCiuc003obj.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20429 mRNA. Translation: AAA59822.1.
M35159 Genomic DNA. Translation: AAA59791.1.
AL713966 Genomic DNA. Translation: CAI18079.1.
AK314834 mRNA. Translation: BAG37353.1.
BC009234 mRNA. Translation: AAH09234.1.
U31770 mRNA. Translation: AAB63983.1.
U59685 Genomic DNA. Translation: AAB52229.1.
M16954 mRNA. Translation: AAA36276.1.
M16955 mRNA. Translation: AAA36277.1.
M17377 mRNA. Translation: AAA59818.1.
X87210 Genomic DNA. No translation available.
FN430425 Genomic DNA. Translation: CAZ86696.1.
Z83201 Genomic DNA. Translation: CAB05668.1.
AF122887 Genomic DNA. Translation: AAD31766.1.
AJ271159 Genomic DNA. Translation: CAB71144.1.
AY141137 Genomic DNA. Translation: AAN28924.1.
AJ427352 Genomic DNA. Translation: CAD20460.1.
AY457037 Genomic DNA. Translation: AAR20446.2.
Y09342 Genomic DNA. Translation: CAA70524.1.
Y13727 Genomic DNA. Translation: CAA74055.1.
M91001 Genomic DNA. No translation available.
CCDSiCCDS4751.1.
PIRiB27060.
B28043.
B28756.
C32526.
D25239.
I68733.
PT0169.
PT0170.
PT0171.
RefSeqiNP_002116.2. NM_002125.3.
UniGeneiHs.485130.
Hs.534322.
Hs.696211.
Hs.736560.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FV1X-ray1.90B/E30-219[»]
1H15X-ray3.10B/E30-219[»]
1HQRX-ray3.20B30-219[»]
1ZGLX-ray2.80B/E/H/K30-221[»]
ProteinModelPortaliQ30154.
SMRiQ30154. Positions 30-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109372. 15 interactions.
IntActiQ30154. 6 interactions.
MINTiMINT-6630223.
STRINGi9606.ENSP00000364114.

Polymorphism and mutation databases

BioMutaiHLA-DRB5.
DMDMi74754558.

Proteomic databases

EPDiQ30154.
PaxDbiQ30154.
PeptideAtlasiQ30154.
PRIDEiQ30154.

Protocols and materials databases

DNASUi3127.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374975; ENSP00000364114; ENSG00000198502.
GeneIDi3127.
KEGGihsa:3127.
UCSCiuc003obj.4. human.

Organism-specific databases

CTDi3127.
GeneCardsiHLA-DRB5.
HGNCiHGNC:4953. HLA-DRB5.
HPAiHPA043151.
MIMi604776. gene.
neXtProtiNX_Q30154.
PharmGKBiPA35076.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWG3. Eukaryota.
ENOG410YI0S. LUCA.
GeneTreeiENSGT00760000118970.
HOVERGENiHBG012730.
InParanoidiQ30154.
KOiK06752.
OMAiNIFECHF.
OrthoDBiEOG7PS1GV.
PhylomeDBiQ30154.
TreeFamiTF336626.

Enzyme and pathway databases

ReactomeiR-HSA-202424. Downstream TCR signaling.
R-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-202430. Translocation of ZAP-70 to Immunological synapse.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-389948. PD-1 signaling.
R-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiHLA-DRB5. human.
EvolutionaryTraceiQ30154.
GeneWikiiHLA-DRB5.
GenomeRNAii3127.
PROiQ30154.
SOURCEiSearch...

Gene expression databases

BgeeiQ30154.
GenevisibleiQ30154. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011162. MHC_I/II-like_Ag-recog.
IPR014745. MHC_II_a/b_N.
IPR000353. MHC_II_b_N.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]
ProDomiPD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Polymorphism of human Ia antigens generated by reciprocal intergenic exchange between two DR beta loci."
    Wu S., Saunders T.L., Bach F.H.
    Nature 324:676-679(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-28 AND ALA-154.
  2. "cDNA cloning and sequencing reveals that the electrophoretically constant DR beta 2 molecules, as well as the variable DR beta 1 molecules, from HLA-DR2 subtypes have different amino acid sequences including a hypervariable region for a functionally important epitope."
    Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.
    J. Immunol. 138:2953-2959(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-28.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB5*01:01).
  4. "A novel DRB1 allele in DR2-positive American blacks."
    Demopulos J.T., Hodge T.W., Wooten V., Acton R.T.
    Hum. Immunol. 30:41-44(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-28.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB5*01:01).
    Tissue: Stomach.
  6. "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 DRB5*01:01).
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB5*01:01).
    Tissue: B-cellImported.
  8. "Diversity associated with the second expressed HLA-DRB locus in the human population."
    Robbins F., Hurley C.K., Tang T., Yao H., Lin Y.S., Wade J., Goeken N., Hartzman R.J.
    Immunogenetics 46:104-110(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-140 (ALLELE DRB5*01:04), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DRB5*02:04).
    Tissue: Blood.
  9. "HLA-DR2 subtypes form an additional supertypic family of DR beta alleles."
    Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.
    Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELES DRB5*01:01 AND DRB5*01:02).
  10. "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, VARIANT ALA-154.
  11. "Primary structure of human class II histocompatibility antigens 3rd communication. Amino acid sequence comparison between DR and DC subclass antigens derived from a lymphoblastoid B cell line homozygous at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1)."
    Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E., Koelbel S., Egert G., Wernet P., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-148 AND 158-178.
  12. "Characterization of a new HLA-DRB5 allele (DRB5*0105) by PCR-SSP and direct sequencing."
    Poli F., Bianchi P., Crespiatico L., Terragna C., van den Berg-Loonen E., Sirchia G.
    Tissue Antigens 47:338-340(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-122 (ALLELE DRB5*01:05).
  13. "New sequences found during routine HLA typing."
    Anholts J.D.H.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB5*01:14).
    Tissue: Blood.
  14. "Sequence of a new HLA-DR allele, DRB5*0106."
    Kervaire B., Tiercy J.
    Eur. J. Immunogenet. 24:225-228(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:06).
  15. Hurley C.K.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:03).
    Tissue: Blood.
  16. "Identification of a new DRB5*02 variant allele by PCR-SSP and SBT."
    Carter V., Day S., Dunn P.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*02:05).
  17. "Novel HLA-DRB5 allele found by sequence based typing."
    Greville W.D., Chapman G., Hogbin J.-P., Velickovic Z.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:11).
  18. "Identification of a new HLA-DRB5 allele, DRB5*0112, by routine PCR-SSP."
    Atkinson D.C., Jobson S.E., Dunn P.P., Briggs D.C.
    Tissue Antigens 62:554-555(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:12).
  19. "Identification of a new allele, HLA-DRB5*0113, through three different molecular biology techniques."
    Garino E., Berrino M., Bertinetto F., Caropreso P., Chidichimo R., Dametto E., Fasano M.E., Frisaldi E., Mazzola G., Tondat F., Boccadoro M., Bruno B., Amoroso A.
    Tissue Antigens 67:427-429(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:13).
  20. "Identification of novel DRB1*11 (DRB1*11013, DRB1*1129), DRB1*08 (DRB1*0816) and DRB5* (DRB5*0107) alleles."
    Buyse I.M., Couture C., Hashemi-Tavoularis S.
    Tissue Antigens 50:678-681(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB5*01:07).
  21. "Identification of novel DRB1*13 (DRB1*1333), DRB1*04 (DRB1*0426) and DRB5* (DRB5*0109) alleles."
    Buyse I.M., Ouellet S., Hashemi-Tavoularis S.
    Tissue Antigens 51:658-662(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB5*01:09).
  22. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB5*02:03).
  23. "Invariant chain structure and MHC class II function."
    Cresswell P.
    Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48.
    Tissue: Liver.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX WITH MBP PEPTIDE, SUBUNIT, DISULFIDE BONDS.
  33. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX WITH MPB PEPTIDE AND STREPTOCOCCUS PYOGENES SPEC PEPTIDE, SUBUNIT, DISULFIDE BONDS.
  34. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX EPSTEIN-BARR VIRUS BALF5 PEPTIDE, SUBUNIT, DISULFIDE BONDS.
  35. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-221 OF HLA-DRA/HLA-DRB5 HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND TRAC, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiDRB5_HUMAN
AccessioniPrimary (citable) accession number: Q30154
Secondary accession number(s): B2RBV6
, C7C4X3, O00157, O00283, O46700, Q29703, Q29787, Q29788, Q30126, Q30150, Q30199, Q6SJR2, Q7M2H9, Q8HWS7, Q8WLR5, Q9MY54, Q9XRX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

HLA-DRB3, HLA-DRB4 and HLA-DRB5 may represent a unique gene.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.