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P28068

- DMB_HUMAN

UniProt

P28068 - DMB_HUMAN

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Protein

HLA class II histocompatibility antigen, DM beta chain

Gene
HLA-DMB, DMB, RING7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 218200Lumenal Reviewed predictionAdd
BLAST
Transmembranei219 – 23921Helical; Reviewed predictionAdd
BLAST
Topological domaini240 – 26324Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 263245HLA class II histocompatibility antigen, DM beta chainPRO_0000018960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 972 Publications
Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
Disulfide bondi135 ↔ 1922 Publications

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.

Miscellaneous databases

EvolutionaryTraceiP28068.

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 peptide Reviewed predictionAdd
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.

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

« Hide 'large scale' publications
  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: September 3, 2014
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

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

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