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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

BioCyciZFISH:G66-31236-MONOMER.
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)DescriptionActionsGraphical viewLength
Topological domaini30 – 227ExtracellularSequence analysisAdd BLAST198
Transmembranei228 – 248HelicalSequence analysisAdd BLAST21
Topological domaini249 – 266CytoplasmicSequence analysisAdd BLAST18

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

DisGeNETi3127.
OpenTargetsiENSG00000198502.
PharmGKBiPA35076.

Polymorphism and mutation databases

BioMutaiHLA-DRB5.
DMDMi74754558.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_500014310630 – 266HLA class II histocompatibility antigen, DR beta 5 chainAdd BLAST237

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 108
Glycosylationi48N-linked (GlcNAc...)1 Publication1
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

BgeeiENSG00000198502.
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 interactors.
IntActiQ30154. 6 interactors.
MINTiMINT-6630223.
STRINGi9606.ENSP00000364114.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 47Combined sources12
Turni48 – 51Combined sources4
Beta strandi52 – 61Combined sources10
Beta strandi64 – 70Combined sources7
Turni71 – 73Combined sources3
Beta strandi75 – 80Combined sources6
Helixi81 – 83Combined sources3
Helixi84 – 91Combined sources8
Helixi94 – 101Combined sources8
Helixi103 – 106Combined sources4
Helixi108 – 115Combined sources8
Helixi116 – 118Combined sources3
Turni119 – 121Combined sources3
Beta strandi127 – 132Combined sources6
Beta strandi137 – 154Combined sources18
Beta strandi157 – 166Combined sources10
Beta strandi169 – 173Combined sources5
Beta strandi180 – 182Combined sources3
Beta strandi184 – 192Combined sources9
Beta strandi199 – 205Combined sources7
Beta strandi213 – 218Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ30154.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini126 – 214Ig-like C1-typeSequence analysisAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 124Beta-1Sequence analysisAdd BLAST95
Regioni125 – 227Beta-2Sequence analysisAdd BLAST103

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.
OMAiFLGKAEC.
OrthoDBiEOG091G15IU.
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)DescriptionActionsGraphical viewLength
Sequence conflicti139Q → E AA sequence (PubMed:6576979).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06095114K → M.Corresponds to variant rs1064587dbSNPEnsembl.1
Natural variantiVAR_06095214K → Q.Corresponds to variant rs701884dbSNPEnsembl.1
Natural variantiVAR_06095314K → V in allele DRB5*02:02; requires 2 nucleotide substitutions. 1
Natural variantiVAR_05035520M → T.Corresponds to variant rs17211043dbSNPEnsembl.1
Natural variantiVAR_03987128L → S.3 Publications1
Natural variantiVAR_05035633R → Q.Corresponds to variant rs34716432dbSNPEnsembl.1
Natural variantiVAR_06095435R → C in allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05. Corresponds to variant rs1136744dbSNPEnsembl.1
Natural variantiVAR_05035741K → T.Corresponds to variant rs200581589dbSNPEnsembl.1
Natural variantiVAR_06095557H → Q.Corresponds to variant rs202185589dbSNPEnsembl.1
Natural variantiVAR_06095659D → 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 rs41546317dbSNPEnsembl.1
Natural variantiVAR_06095759D → H.Corresponds to variant rs707955dbSNPEnsembl.1
Natural variantiVAR_05035862N → H.Corresponds to variant rs1059576dbSNPEnsembl.1
Natural variantiVAR_06095866D → 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 rs77853982dbSNPEnsembl.1
Natural variantiVAR_06095966D → Y in allele DRB5*01:14. Corresponds to variant rs77853982dbSNPEnsembl.1
Natural variantiVAR_06096067L → 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 rs1059580dbSNPEnsembl.1
Natural variantiVAR_06096187A → E in allele DRB5*01:13. 1
Natural variantiVAR_06096289Y → S in allele DRB5*01:12. Corresponds to variant rs41541218dbSNPEnsembl.1
Natural variantiVAR_06096496F → 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 rs41562819dbSNPEnsembl.1
Natural variantiVAR_06096396F → L in allele DRB5*02:05. Corresponds to variant rs41562819dbSNPEnsembl.1
Natural variantiVAR_06096599D → E.Corresponds to variant rs41559913dbSNPEnsembl.1
Natural variantiVAR_06096699D → G.Corresponds to variant rs41545413dbSNPEnsembl.1
Natural variantiVAR_06096799D → H.Corresponds to variant rs41547217dbSNPEnsembl.1
Natural variantiVAR_06096899D → N in allele DRB5*01:09. Corresponds to variant rs41547217dbSNPEnsembl.1
Natural variantiVAR_06096999D → 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. 1
Natural variantiVAR_06097099D → R in allele DRB5*01:12; requires 2 nucleotide substitutions. 1
Natural variantiVAR_060971100R → 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. 1
Natural variantiVAR_060972100R → G.Corresponds to variant rs41551116dbSNPEnsembl.1
Natural variantiVAR_060973100R → T in allele DRB5*01:03. Corresponds to variant rs41544215dbSNPEnsembl.1
Natural variantiVAR_060974103A → E in allele DRB5*01:12. Corresponds to variant rs1059598dbSNPEnsembl.1
Natural variantiVAR_060975103A → L in allele DRB5*01:04; requires 2 nucleotide substitutions. 1
Natural variantiVAR_050359106T → N.Corresponds to variant rs115817940dbSNPEnsembl.1
Natural variantiVAR_060976107Y → V in allele DRB5*01:12; requires 2 nucleotide substitutions. 1
Natural variantiVAR_060977114V → A in allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05. Corresponds to variant rs1136778dbSNPEnsembl.1
Natural variantiVAR_060978115G → V in allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05. Corresponds to variant rs41556512dbSNPEnsembl.1
Natural variantiVAR_039872154G → A.2 PublicationsCorresponds to variant rs113395425dbSNPEnsembl.1
Natural variantiVAR_060979164S → G in allele DRB5*02:02. Corresponds to variant rs1059633dbSNPEnsembl.1
Natural variantiVAR_060980186T → I in allele DRB5*02:02. Corresponds to variant rs41559420dbSNPEnsembl.1
Natural variantiVAR_060981232V → I in allele DRB5*02:02. Corresponds to variant rs41553512dbSNPEnsembl.1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109372. 15 interactors.
IntActiQ30154. 6 interactors.
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.
DisGeNETi3127.
GeneCardsiHLA-DRB5.
HGNCiHGNC:4953. HLA-DRB5.
HPAiHPA043151.
MIMi604776. gene.
neXtProtiNX_Q30154.
OpenTargetsiENSG00000198502.
PharmGKBiPA35076.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWG3. Eukaryota.
ENOG410YI0S. LUCA.
GeneTreeiENSGT00760000118970.
HOVERGENiHBG012730.
InParanoidiQ30154.
KOiK06752.
OMAiFLGKAEC.
OrthoDBiEOG091G15IU.
PhylomeDBiQ30154.
TreeFamiTF336626.

Enzyme and pathway databases

BioCyciZFISH:G66-31236-MONOMER.
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

BgeeiENSG00000198502.
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...

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: November 2, 2016
This is version 148 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.