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P01911

- 2B1F_HUMAN

UniProt

P01911 - 2B1F_HUMAN

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Protein

HLA class II histocompatibility antigen, DRB1-15 beta chain

Gene

HLA-DRB1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. MHC class II protein complex binding Source: UniProt
  2. peptide antigen binding Source: UniProt

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. interferon-gamma-mediated signaling pathway Source: Reactome
  4. polysaccharide assembly with MHC class II protein complex Source: UniProt
  5. T cell costimulation Source: Reactome
  6. T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.
REACT_25078. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
HLA class II histocompatibility antigen, DRB1-15 beta chain
Alternative name(s):
DW2.2/DR2.2
MHC class II antigen DRB1*15
Gene namesi
Name:HLA-DRB1
Synonyms:HLA-DRB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4948. HLA-DRB1.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Golgi apparatustrans-Golgi network membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Lysosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Late endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication
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.

Topology

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

GO - Cellular componenti

  1. cell surface Source: UniProt
  2. clathrin-coated endocytic vesicle membrane Source: Reactome
  3. endocytic vesicle membrane Source: Reactome
  4. ER to Golgi transport vesicle membrane Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. Golgi membrane Source: Reactome
  7. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  8. late endosome membrane Source: UniProtKB
  9. lysosomal membrane Source: UniProtKB
  10. membrane Source: UniProtKB
  11. MHC class II protein complex Source: UniProt
  12. plasma membrane Source: Reactome
  13. trans-Golgi network membrane Source: Reactome
  14. transport vesicle membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35072.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29292 PublicationsAdd
BLAST
Chaini30 – 266237HLA class II histocompatibility antigen, DRB1-15 beta chainPRO_0000080744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 108
Glycosylationi48 – 481N-linked (GlcNAc...)
Disulfide bondi146 ↔ 202
Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP01911.
PRIDEiP01911.

Expressioni

Gene expression databases

BgeeiP01911.
CleanExiHS_HLA-DRB1.
ExpressionAtlasiP01911. baseline and differential.
GenevestigatoriP01911.

Organism-specific databases

HPAiCAB015400.
CAB034021.

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.

Protein-protein interaction databases

BioGridi109368. 24 interactions.
IntActiP01911. 1 interaction.

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 – 929Combined sources
Helixi94 – 10613Combined sources
Helixi108 – 1158Combined sources
Turni116 – 1216Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi142 – 15413Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1929Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi213 – 2186Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX2X-ray2.60B/E32-222[»]
1YMMX-ray3.50B30-227[»]
2WBJX-ray3.00B/F30-227[»]
ProteinModelPortaliP01911.
SMRiP01911. Positions 32-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01911.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the MHC class II family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG012730.
InParanoidiP01911.
KOiK06752.
OMAiERISCGI.
PhylomeDBiP01911.

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]
SUPFAMiSSF54452. 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.

P01911-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT
60 70 80 90 100
ERVRFLDRYF YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA
110 120 130 140 150
RAAVDTYCRH NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG
160 170 180 190 200
FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG DWTFQTLVML ETVPRSGEVY
210 220 230 240 250
TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF
260
RNQKGHSGLQ PTGFLS
Length:266
Mass (Da):29,966
Last modified:January 15, 2008 - v2
Checksum:i3B5912820A4654BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191T → A in AAI08923. (PubMed:15489334)Curated
Sequence conflicti154 – 1541G → A in AAA59801. (PubMed:3476943)Curated
Sequence conflicti171 – 1711M → G AA sequence (PubMed:6947956)Curated
Sequence conflicti179 – 1802NG → D AA sequence (PubMed:6947956)Curated

Polymorphismi

The following alleles of DRB1-15 are known: DRB1*15:01, DRB1*15:02, DRB1*15:03, DRB1*15:04, DRB1*15:05, DRB1*15:06, DRB1*15:07, DRB1*15:08, DRB1*15:09, DRB1*15:10, DRB1*15:11, DRB1*15:12, DRB1*15:13, DRB1*15:14, DRB1*15:15, DRB1*15:16, DRB1*15:18, DRB1*15:19, DRB1*15:20, DRB1*15:21, DRB1*15:22, DRB1*15:23, DRB1*15:24, DRB1*15:25, DRB1*15:26, DRB1*15:27, DRB1*15:28, DRB1*15:29, DRB1*15:30, DRB1*15:31 and DRB1*15:32. The sequence shown is that of DRB1*15:01.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51K → R.
Corresponds to variant rs9270305 [ dbSNP | Ensembl ].
VAR_050364
Natural varianti55 – 551F → Y.
Corresponds to variant rs16822516 [ dbSNP | Ensembl ].
VAR_050365
Natural varianti59 – 591Y → H in allele DRB1*15:03.
VAR_038162
Natural varianti96 – 961I → F in allele DRB1*15:04.
Corresponds to variant rs17886918 [ dbSNP | Ensembl ].
VAR_038163
Natural varianti106 – 1061T → N.
Corresponds to variant rs9269941 [ dbSNP | Ensembl ].
VAR_050366
Natural varianti115 – 1151V → G in allele DRB1*15:02.
Corresponds to variant rs17885482 [ dbSNP | Ensembl ].
VAR_038164
Natural varianti164 – 1641G → S.
Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
VAR_050367
Natural varianti169 – 1691A → T.
Corresponds to variant rs2308768 [ dbSNP | Ensembl ].
VAR_050368
Natural varianti236 – 2361V → M.
Corresponds to variant rs2230816 [ dbSNP | Ensembl ].
VAR_050369
Natural varianti262 – 2621T → R.
Corresponds to variant rs9269744 [ dbSNP | Ensembl ].
VAR_050370

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20430 mRNA. Translation: AAA59831.1.
AY663395 Genomic DNA. Translation: AAU87979.1.
AY663406 Genomic DNA. Translation: AAU88008.1.
AY663411 Genomic DNA. Translation: AAU88023.1.
AY663414 Genomic DNA. Translation: AAU88033.1.
AY961072 mRNA. Translation: AAX63460.1.
AY961073 mRNA. Translation: AAX63461.1.
AL713966 Genomic DNA. Translation: CAI18081.1.
BC033827 mRNA. Translation: AAH33827.1.
BC108922 mRNA. Translation: AAI08923.1.
M28584 mRNA. Translation: AAA59681.1.
M16957 mRNA. Translation: AAA36279.1.
M17378 mRNA. Translation: AAA59801.1.
CCDSiCCDS47409.1.
PIRiI68734. HLHUWB.
RefSeqiNP_002115.2. NM_002124.3.
UniGeneiHs.534322.
Hs.696211.
Hs.736560.

Genome annotation databases

EnsembliENST00000360004; ENSP00000353099; ENSG00000196126.
GeneIDi3123.
KEGGihsa:3123.
UCSCiuc003obp.4. human.

Polymorphism databases

DMDMi166214928.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20430 mRNA. Translation: AAA59831.1 .
AY663395 Genomic DNA. Translation: AAU87979.1 .
AY663406 Genomic DNA. Translation: AAU88008.1 .
AY663411 Genomic DNA. Translation: AAU88023.1 .
AY663414 Genomic DNA. Translation: AAU88033.1 .
AY961072 mRNA. Translation: AAX63460.1 .
AY961073 mRNA. Translation: AAX63461.1 .
AL713966 Genomic DNA. Translation: CAI18081.1 .
BC033827 mRNA. Translation: AAH33827.1 .
BC108922 mRNA. Translation: AAI08923.1 .
M28584 mRNA. Translation: AAA59681.1 .
M16957 mRNA. Translation: AAA36279.1 .
M17378 mRNA. Translation: AAA59801.1 .
CCDSi CCDS47409.1.
PIRi I68734. HLHUWB.
RefSeqi NP_002115.2. NM_002124.3.
UniGenei Hs.534322.
Hs.696211.
Hs.736560.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BX2 X-ray 2.60 B/E 32-222 [» ]
1YMM X-ray 3.50 B 30-227 [» ]
2WBJ X-ray 3.00 B/F 30-227 [» ]
ProteinModelPortali P01911.
SMRi P01911. Positions 32-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109368. 24 interactions.
IntActi P01911. 1 interaction.

Polymorphism databases

DMDMi 166214928.

Proteomic databases

MaxQBi P01911.
PRIDEi P01911.

Protocols and materials databases

DNASUi 3123.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360004 ; ENSP00000353099 ; ENSG00000196126 .
GeneIDi 3123.
KEGGi hsa:3123.
UCSCi uc003obp.4. human.

Organism-specific databases

CTDi 3123.
GeneCardsi GC06M032546.
HGNCi HGNC:4948. HLA-DRB1.
HPAi CAB015400.
CAB034021.
MIMi 142857. gene.
neXtProti NX_P01911.
PharmGKBi PA35072.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG012730.
InParanoidi P01911.
KOi K06752.
OMAi ERISCGI.
PhylomeDBi P01911.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.
REACT_25078. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSi HLA-DRB1. human.
EvolutionaryTracei P01911.
GeneWikii HLA-DRB1.
GenomeRNAii 3123.
NextBioi 12394.
PROi P01911.
SOURCEi Search...

Gene expression databases

Bgeei P01911.
CleanExi HS_HLA-DRB1.
ExpressionAtlasi P01911. baseline and differential.
Genevestigatori P01911.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProi 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 ]
Pfami PF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view ]
ProDomi PD000328. MHC_II_b_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view ]
SUPFAMi SSF54452. SSF54452. 1 hit.
PROSITEi PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01).
    Tissue: B-cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*15:01; DRB1*15:02 AND DRB1*15:03).
  3. "Group-specific amplification of cDNA from DRB1 genes. Complete coding sequences of partially defined alleles and identification of the new alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."
    Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., de Pablo R., Garcia-Sanchez F., Vicario J.L.
    Hum. Immunol. 67:1008-1016(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*15:03 AND DRB1*15:04).
    Tissue: Blood.
  4. "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*15:01).
  5. "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] (ALLELES DRB1*15:01 AND DRB1*15:02).
    Tissue: Leukocyte.
  6. "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] OF 11-266 (ALLELE DRB1*15:02).
    Tissue: Lymphoblast.
  7. "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 (ALLELE DRB1*15:01).
    Tissue: Lymphoblast.
  8. "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*15:01).
    Tissue: Lymphoblast.
  9. "Primary structure of class II human histocompatibility antigens. 1st communication. Amino acid sequence of the N-terminal 198 residues of the beta chain of a HLA-Dw2,2;DR2,2-alloantigen."
    Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G., Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-228.
    Tissue: Lymphoblast.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-64.
    Tissue: B-cell.
  11. "Invariant chain structure and MHC class II function."
    Cresswell P.
    Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor."
    Hahn M., Nicholson M.J., Pyrdol J., Wucherpfennig K.W.
    Nat. Immunol. 6:490-496(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 30-227.

Entry informationi

Entry namei2B1F_HUMAN
AccessioniPrimary (citable) accession number: P01911
Secondary accession number(s): Q29790
, Q29975, Q30142, Q30166, Q32MY7, Q56FN9, Q5Y7B0, Q5Y7B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 15, 2008
Last modified: November 26, 2014
This is version 126 of the entry and version 2 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

Miscellaneous

The chain shown constituted about 70% of a pool of at least seven similar beta chains.

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

External Data

Dasty 3