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P28068

- DMB_HUMAN

UniProt

P28068 - DMB_HUMAN

Protein

HLA class II histocompatibility antigen, DM beta chain

Gene

HLA-DMB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Plays a critical role in catalyzing the release of class II-associated invariant chain peptide (CLIP) from newly synthesized MHC class II molecules and freeing the peptide binding site for acquisition of antigenic peptides. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO.3 Publications

    GO - Molecular functioni

    1. MHC class II protein complex binding Source: UniProt

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProt
    2. immune response Source: InterPro
    3. MHC class II protein complex assembly Source: UniProt
    4. peptide antigen assembly with MHC class II protein complex Source: UniProt
    5. positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: UniProt
    6. positive regulation of T cell proliferation Source: UniProt

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HLA class II histocompatibility antigen, DM beta chain
    Alternative name(s):
    MHC class II antigen DMB
    Really interesting new gene 7 protein
    Gene namesi
    Name:HLA-DMB
    Synonyms:DMB, RING7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4935. HLA-DMB.

    Subcellular locationi

    Late endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Lysosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: Localizes to late endocytic compartment. Associates with lysosome membranes.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. late endosome membrane Source: UniProtKB-SubCell
    3. lysosomal membrane Source: Reactome
    4. MHC class II protein complex Source: UniProt

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane, MHC II

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi248 – 2481Y → A: Abolishes targeting to endosomes and results in relocalization to the cell membrane. 1 Publication
    Mutagenesisi251 – 2511L → A: Abolishes targeting to endosomes and results in relocalization to the cell membrane. 1 Publication

    Organism-specific databases

    PharmGKBiPA35059.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 263245HLA class II histocompatibility antigen, DM beta chainPRO_0000018960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 97
    Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
    Disulfide bondi135 ↔ 192

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP28068.
    PRIDEiP28068.

    PTM databases

    PhosphoSiteiP28068.

    Expressioni

    Gene expression databases

    ArrayExpressiP28068.
    BgeeiP28068.
    CleanExiHS_HLA-DMB.
    GenevestigatoriP28068.

    Organism-specific databases

    HPAiHPA012298.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha chain (DMA) and a beta chain (DMB).2 Publications

    Protein-protein interaction databases

    BioGridi109354. 6 interactions.
    DIPiDIP-6185N.
    IntActiP28068. 7 interactions.
    MINTiMINT-1539801.
    STRINGi9606.ENSP00000393646.

    Structurei

    Secondary structure

    1
    263
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 3211
    Beta strandi33 – 353
    Beta strandi37 – 4610
    Beta strandi49 – 557
    Turni56 – 594
    Beta strandi60 – 634
    Beta strandi67 – 693
    Helixi70 – 8112
    Helixi84 – 918
    Helixi93 – 10917
    Beta strandi116 – 1216
    Beta strandi128 – 14316
    Beta strandi146 – 1516
    Beta strandi154 – 1563
    Beta strandi170 – 1723
    Beta strandi174 – 1829
    Beta strandi190 – 1956
    Beta strandi199 – 2013
    Beta strandi203 – 2075

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HDMX-ray2.50B19-218[»]
    2BC4X-ray2.27B/D19-256[»]
    4FQXX-ray2.60D19-211[»]
    4GBXX-ray3.00D19-211[»]
    4I0PX-ray3.20B/F21-211[»]
    ProteinModelPortaliP28068.
    SMRiP28068. Positions 21-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28068.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 218200LumenalSequence AnalysisAdd
    BLAST
    Topological domaini240 – 26324CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei219 – 23921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini114 – 20895Ig-like C1-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 11294Beta-1Add
    BLAST
    Regioni113 – 20795Beta-2Add
    BLAST
    Regioni208 – 21811Connecting peptideSequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi248 – 2514YXXZ motif

    Domaini

    The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic residue) motif mediates the targeting to the lysosomal compartments.

    Sequence similaritiesi

    Belongs to the MHC class II family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG40558.
    HOVERGENiHBG007327.
    InParanoidiP28068.
    KOiK06752.
    OMAiDCATHTQ.
    PhylomeDBiP28068.
    TreeFamiTF335727.

    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]
    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.

    P28068-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL    50
    LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQKDTLMQRL RNGLQNCATH 100
    TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR 150
    KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP 200
    EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSYTP 250
    LPGSNYSEGW HIS 263
    Length:263
    Mass (Da):28,943
    Last modified:August 1, 1992 - v1
    Checksum:i9B50F6CC22B3A4BA
    GO

    Polymorphismi

    The following alleles of DMB are known: DMB*01:01, DMB*01:02, DMB*01:03, DMB*01:04 (DMB3.4), DMB*01:05, DMB*01:06, and DMB*01:07. The sequence shown is that of DMB*01:01.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281T → A in allele DMB*01:07.
    Corresponds to variant rs17583782 [ dbSNP | Ensembl ].
    VAR_050360
    Natural varianti45 – 451S → F in allele DMB*01:06.
    Corresponds to variant rs41560814 [ dbSNP | Ensembl ].
    VAR_016752
    Natural varianti49 – 491D → V in allele DMB*01:07.
    Corresponds to variant rs17617333 [ dbSNP | Ensembl ].
    VAR_050361
    Natural varianti71 – 711S → N in allele DMB*01:07.
    Corresponds to variant rs17617321 [ dbSNP | Ensembl ].
    VAR_050362
    Natural varianti162 – 1621A → E in allele DMB*01:02 and allele DMB*01:06.
    VAR_016753
    Natural varianti162 – 1621A → V in allele DMB*01:04 and allele DMB*01:05.
    VAR_016754
    Natural varianti197 – 1971I → T in allele DMB*01:03, allele DMB*01:04 and allele DMB*01:06. 1 Publication
    Corresponds to variant rs1042337 [ dbSNP | Ensembl ].
    VAR_016755

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z23139 mRNA. Translation: CAA80670.1.
    U15085 mRNA. Translation: AAB60387.1.
    X76776 Genomic DNA. Translation: CAA54171.1.
    X87344 Genomic DNA. Translation: CAA60782.1.
    AY645722 mRNA. Translation: AAV97947.1.
    AL662845 Genomic DNA. Translation: CAI17490.1.
    AL645941 Genomic DNA. Translation: CAI18108.1.
    AL935042 Genomic DNA. Translation: CAI18685.1.
    BX088556 Genomic DNA. Translation: CAM26271.1.
    BX927138 Genomic DNA. Translation: CAQ08457.1.
    CR936913 Genomic DNA. Translation: CAQ08780.1.
    CR759798 Genomic DNA. Translation: CAQ09462.1.
    CR752645 Genomic DNA. Translation: CAQ09834.1.
    CH471081 Genomic DNA. Translation: EAX03657.1.
    BC027175 mRNA. Translation: AAH27175.1.
    Z24750 Genomic DNA. No translation available.
    Z24751 Genomic DNA. No translation available.
    U00700 Genomic DNA. Translation: AAA03296.1.
    U16762 Genomic DNA. Translation: AAC50514.1.
    AF134890 Genomic DNA. Translation: AAD30279.1.
    AF072680 Genomic DNA. Translation: AAC26112.1.
    CCDSiCCDS4760.1.
    PIRiI37533.
    RefSeqiNP_002109.2. NM_002118.4.
    UniGeneiHs.351279.

    Genome annotation databases

    EnsembliENST00000383231; ENSP00000372718; ENSG00000241674.
    ENST00000395312; ENSP00000378723; ENSG00000242092.
    ENST00000412948; ENSP00000413471; ENSG00000241296.
    ENST00000418107; ENSP00000398890; ENSG00000242574.
    ENST00000424822; ENSP00000414817; ENSG00000234154.
    ENST00000428420; ENSP00000393646; ENSG00000239329.
    ENST00000440078; ENSP00000411321; ENSG00000226264.
    ENST00000450897; ENSP00000408453; ENSG00000242386.
    GeneIDi3109.
    KEGGihsa:3109.

    Polymorphism databases

    DMDMi133160.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z23139 mRNA. Translation: CAA80670.1 .
    U15085 mRNA. Translation: AAB60387.1 .
    X76776 Genomic DNA. Translation: CAA54171.1 .
    X87344 Genomic DNA. Translation: CAA60782.1 .
    AY645722 mRNA. Translation: AAV97947.1 .
    AL662845 Genomic DNA. Translation: CAI17490.1 .
    AL645941 Genomic DNA. Translation: CAI18108.1 .
    AL935042 Genomic DNA. Translation: CAI18685.1 .
    BX088556 Genomic DNA. Translation: CAM26271.1 .
    BX927138 Genomic DNA. Translation: CAQ08457.1 .
    CR936913 Genomic DNA. Translation: CAQ08780.1 .
    CR759798 Genomic DNA. Translation: CAQ09462.1 .
    CR752645 Genomic DNA. Translation: CAQ09834.1 .
    CH471081 Genomic DNA. Translation: EAX03657.1 .
    BC027175 mRNA. Translation: AAH27175.1 .
    Z24750 Genomic DNA. No translation available.
    Z24751 Genomic DNA. No translation available.
    U00700 Genomic DNA. Translation: AAA03296.1 .
    U16762 Genomic DNA. Translation: AAC50514.1 .
    AF134890 Genomic DNA. Translation: AAD30279.1 .
    AF072680 Genomic DNA. Translation: AAC26112.1 .
    CCDSi CCDS4760.1.
    PIRi I37533.
    RefSeqi NP_002109.2. NM_002118.4.
    UniGenei Hs.351279.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HDM X-ray 2.50 B 19-218 [» ]
    2BC4 X-ray 2.27 B/D 19-256 [» ]
    4FQX X-ray 2.60 D 19-211 [» ]
    4GBX X-ray 3.00 D 19-211 [» ]
    4I0P X-ray 3.20 B/F 21-211 [» ]
    ProteinModelPortali P28068.
    SMRi P28068. Positions 21-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109354. 6 interactions.
    DIPi DIP-6185N.
    IntActi P28068. 7 interactions.
    MINTi MINT-1539801.
    STRINGi 9606.ENSP00000393646.

    PTM databases

    PhosphoSitei P28068.

    Polymorphism databases

    DMDMi 133160.

    Proteomic databases

    PaxDbi P28068.
    PRIDEi P28068.

    Protocols and materials databases

    DNASUi 3109.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000383231 ; ENSP00000372718 ; ENSG00000241674 .
    ENST00000395312 ; ENSP00000378723 ; ENSG00000242092 .
    ENST00000412948 ; ENSP00000413471 ; ENSG00000241296 .
    ENST00000418107 ; ENSP00000398890 ; ENSG00000242574 .
    ENST00000424822 ; ENSP00000414817 ; ENSG00000234154 .
    ENST00000428420 ; ENSP00000393646 ; ENSG00000239329 .
    ENST00000440078 ; ENSP00000411321 ; ENSG00000226264 .
    ENST00000450897 ; ENSP00000408453 ; ENSG00000242386 .
    GeneIDi 3109.
    KEGGi hsa:3109.

    Organism-specific databases

    CTDi 3109.
    GeneCardsi GC06M032903.
    GC06Mi32885.
    GC06Mj32824.
    GC06Mk32880.
    GC06Ml33056.
    GC06Mm32935.
    GC06Mn32831.
    GC06Mo32992.
    H-InvDB HIX0166396.
    HIX0207613.
    HIX0207705.
    HIX0207762.
    HGNCi HGNC:4935. HLA-DMB.
    HPAi HPA012298.
    MIMi 142856. gene.
    neXtProti NX_P28068.
    PharmGKBi PA35059.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40558.
    HOVERGENi HBG007327.
    InParanoidi P28068.
    KOi K06752.
    OMAi DCATHTQ.
    PhylomeDBi P28068.
    TreeFami TF335727.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.

    Miscellaneous databases

    EvolutionaryTracei P28068.
    GeneWikii HLA-DMB.
    GenomeRNAii 3109.
    NextBioi 12337.
    PROi P28068.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28068.
    Bgeei P28068.
    CleanExi HS_HLA-DMB.
    Genevestigatori P28068.

    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 ]
    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

    1. "A new human HLA class II-related locus, DM."
      Kelly A.P., Monaco J.J., Cho S., Trowsdale J.
      Nature 353:571-573(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMB*01:01).
    2. "Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene organization of all six class II families in the human major histocompatibility complex."
      Radley E., Alderton R.P., Kelly A., Trowsdale J., Beck S.
      J. Biol. Chem. 269:18834-18838(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*01:01).
    3. "Evolutionary dynamics of non-coding sequences within the class II region of the human MHC."
      Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L., Trowsdale J.
      J. Mol. Biol. 255:1-13(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*01:01).
    4. "Identification of a novel HLA-DMB allele (DMB*0107) in the Korean population."
      Gu H., Moon S.-M., Kim J.-J., Ryu H.-J., Kwack K., Kimm K., Lee J.-K., Oh B.
      Tissue Antigens 65:393-394(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMB*01:07).
    5. "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], VARIANT THR-197.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 DMB*01:01).
      Tissue: Lymph.
    8. "Limited polymorphism in HLA-DM does not involve the peptide binding groove."
      Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.
      Immunogenetics 39:56-58(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-207 (ALLELES DMB*01:02 AND DMB*01:03).
    9. "Characterization of HLA-DMB polymorphism."
      Carrington M., Yeager M., Mann D.
      Immunogenetics 38:446-449(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-200 (ALLELE DMB*01:04).
    10. "Three HLA-DMB variants in Korean patients with autoimmune diseases."
      Kim T.-G., Carrington M., Choi H.B., Kim H.Y., Han H.
      Hum. Immunol. 46:58-60(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-207 (ALLELE DMB*01:05).
      Tissue: Blood.
    11. "The nucleotide sequence of a new DMB allele, DMB*0106."
      McTernan C.L., Mijovic C.H., Cockram C.S., Barnett A.H.
      Tissue Antigens 55:470-472(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-112 AND 152-207 (ALLELE DMB*01:06).
    12. "Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM."
      Weber D.A., Evavold B.D., Jensen P.E.
      Science 274:618-620(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Targeting signal and subcellular compartments involved in the intracellular trafficking of HLA-DMB."
      Copier J., Kleijmeer M.J., Ponnambalam S., Oorschot V., Potter P., Trowsdale J., Kelly A.
      J. Immunol. 157:1017-1027(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-248 AND LEU-251.
    14. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
      Tissue: Plasma.
    15. "The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation."
      Mosyak L., Zaller D.M., Wiley D.C.
      Immunity 9:377-383(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-218 IN COMPLEX WITH DMA, FUNCTION, SUBUNIT, DISULFIDE BONDS.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 19-218 IN COMPLEX WITH DMA, FUNCTION, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiDMB_HUMAN
    AccessioniPrimary (citable) accession number: P28068
    Secondary accession number(s): O77936
    , Q13012, Q29751, Q58ZE2, Q5SNZ8, Q5STC4, Q9XRX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 146 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

    Keywords - Technical termi

    3D-structure, Complete proteome, 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