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P01899 (HA11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
H-2 class I histocompatibility antigen, D-B alpha chain

Short name=H-2D(B)
Gene names
Name:H2-D1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the presentation of foreign antigens to the immune system.

Subunit structure

Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Interacts with murid herpesvirus 4 protein K3 (mK3). Ref.8 Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3). This modification causes the protein to be targeted for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) system. Ubiquitination occurs on lysine, as well as serine and threonine residues present in the cytoplasmic tail. Serine and threonine residues are subject to ubiquitination via ester bonds instead of the usual isopeptide linkage.

Sequence similarities

Belongs to the MHC class I family.

Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Sequence caution

The sequence AAA39580.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.5
Chain25 – 362338H-2 class I histocompatibility antigen, D-B alpha chain
PRO_0000018923

Regions

Topological domain25 – 309285Extracellular Potential
Transmembrane310 – 33122Helical; Potential
Topological domain332 – 36231Cytoplasmic Potential
Domain209 – 29789Ig-like C1-type
Region25 – 11490Alpha-1
Region115 – 20692Alpha-2
Region207 – 29892Alpha-3
Region299 – 30911Connecting peptide

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation2001N-linked (GlcNAc...) Probable
Glycosylation2801N-linked (GlcNAc...) Ref.7
Disulfide bond125 ↔ 188 Ref.12
Disulfide bond227 ↔ 283 Ref.12
Cross-link353Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin) Probable

Experimental info

Mutagenesis551K → R in K-less, no effect on ubiquitination; when associated with R-92, R-155, R-170, R-197, R-210, R-220, R-267 and R-277. Ref.8
Mutagenesis921K → R in K-less, no effect on ubiquitination; when associated with R-55, R-155, R-170, R-197, R-210, R-220, R-267 and R-277. Ref.8
Mutagenesis1551K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-170, R-197, R-210, R-220, R-267 and R-277. Ref.8
Mutagenesis1701K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-197, R-210, R-220, R-267 and R-277. Ref.8
Mutagenesis1971K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-210, R-220, R-267 and R-277. Ref.8
Mutagenesis2101K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-220, R-267 and R-277. Ref.8
Mutagenesis2201K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-267 and R-277. Ref.8
Mutagenesis2671K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-220 and R-277. Ref.8
Mutagenesis2771K → R in K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-220 and R-267. Ref.8
Mutagenesis3321K → R in Ld KCST-less, strongly impairs ubiquitination; when associated with I-337; R-340; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated I-337; R-340; 350-A--A-352; A-356 and 360-R-R-361. Ref.8 Ref.9 Ref.10
Mutagenesis3371T → I in Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; R-340; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated R-332; R-340; 350-A--A-352; A-356 and 360-R-R-361. Ref.8 Ref.9 Ref.10
Mutagenesis3401K → R in Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; 350-A--A-352; A-356 and 360-R-R-361. Ref.8 Ref.9 Ref.10
Mutagenesis350 – 3567SQSSEMS → AQGAEMA in Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337 and 360-R-R-361. Ref.8 Ref.9 Ref.10
Mutagenesis350 – 3523SQS → AQG in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361. Ref.9 Ref.10
Mutagenesis3561S → A in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340 and A-356. Ref.9 Ref.10
Mutagenesis360 – 3612CK → RR in Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; R-340 and 350-A--A-356. In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; 350-A--A-352; A-356 and 360-R-R-361.

Secondary structure

....................................................... 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01899 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 6EE6AEF97263FA71

FASTA36240,836
        10         20         30         40         50         60 
MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LEEPRYISVG YVDNKEFVRF 

        70         80         90        100        110        120 
DSDAENPRYE PRAPWMEQEG PEYWERETQK AKGQEQWFRV SLRNLLGYYN QSAGGSHTLQ 

       130        140        150        160        170        180 
QMSGCDLGSD WRLLRGYLQF AYEGRDYIAL NEDLKTWTAA DMAAQITRRK WEQSGAAEHY 

       190        200        210        220        230        240 
KAYLEGECVE WLHRYLKNGN ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT 

       250        260        270        280        290        300 
WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP 

       310        320        330        340        350        360 
PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS QSSEMSLRDC 


KA 

« Hide

References

[1]"DNA sequence analysis of the C3H H-2Kk and H-2Dk loci. Evolutionary relationships to H-2 genes from four other mouse strains."
Watts S., Vogel J.M., Harriman W.D., Itoh T., Stauss H.J., Goodenow R.S.
J. Immunol. 139:3878-3885(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C3H.
[2]Girgis K.R., Capra D.J., Stroynowski I.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NOD/LT.
[3]"Nucleotide sequences of three H-2K and three H-2D complementary DNA clones coding mouse class I MHC heavy chain proteins."
Wang M., Stepkowski S.M., Hebert J.S., Tian L., Yu J., Kahan B.D.
Ann. Transplant. 1:26-31(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/10.
[4]"The complete amino acid sequence of the murine transplantation antigen H-2Db as deduced by molecular cloning."
Reyes A.A., Schold M., Wallace R.B.
Immunogenetics 16:1-9(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-362.
[5]"Primary structure of murine major histocompatibility complex alloantigens. Amino acid sequence of the NH2-terminal ninety-eight residues of the H-2Db glycoprotein."
Maloy W.L., Nathenson S.G., Coligan J.E.
J. Biol. Chem. 256:2863-2872(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-122.
[6]"Primary structure of the H-2Db alloantigen. II. Additional amino acid sequence information, localization of a third site of glycosylation and evidence for K and D region specific sequences."
Maloy W.L., Coligan J.E.
Immunogenetics 16:11-22(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 253-308 AND 332-358.
[7]"Oligosaccharide microheterogeneity of the murine major histocompatibility antigens. Reproducible site-specific patterns of sialylation and branching in asparagine-linked oligosaccharides."
Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., Hart G.W.
J. Biol. Chem. 260:4046-4054(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-110 AND ASN-280.
[8]"Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3."
Wang X., Herr R.A., Chua W.J., Lybarger L., Wiertz E.J., Hansen T.H.
J. Cell Biol. 177:613-624(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH MURID HERPESVIRUS 4 K3, MUTAGENESIS OF LYS-55; LYS-92; LYS-155; LYS-170; LYS-197; LYS-210; LYS-220; LYS-267; LYS-277; LYS-332; THR-337; LYS-340; 350-SER--SER-356 AND 360-CYS-LYS-361.
[9]"Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates."
Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J., Hansen T.H.
J. Cell Biol. 187:655-668(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT SER-353, INTERACTION WITH MURID HERPESVIRUS 4 K3, MUTAGENESIS OF LYS-332; THR-337; LYS-340; 350-SER--SER-352; SER-356 AND 360-CYS-LYS-361.
[10]"Role of the RING-CH domain of viral ligase mK3 in ubiquitination of non-lysine and lysine MHC I residues."
Herr R.A., Harris J., Fang S., Wang X., Hansen T.H.
Traffic 10:1301-1317(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH MURID HERPESVIRUS 4 K3, MUTAGENESIS OF LYS-332; THR-337; LYS-340; 350-SER--SER-352; SER-356 AND 360-CYS-LYS-361.
[11]"The three-dimensional structure of H-2Db at 2.4-A resolution: implications for antigen-determinant selection."
Young A.C.M., Zhang W., Sacchettini J.C., Nathenson S.G.
Cell 76:39-50(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-296.
[12]"Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex."
Tissot A.C., Ciatto C., Mittl P.R., Grutter M.G., Pluckthun A.
J. Mol. Biol. 302:873-885(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 24-304, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18523 Genomic DNA. Translation: AAA53200.1.
L36068 mRNA. Translation: AAA89206.1.
U47325 mRNA. Translation: AAB17603.1.
K00129 mRNA. Translation: AAA39580.1. Different initiation.
PIRB60854.
HLMSDB. I56002.
RefSeqNP_034510.3. NM_010380.3.
UniGeneMm.439675.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZ9X-ray2.80A26-299[»]
1CE6X-ray2.90A25-298[»]
1FFNX-ray2.70A/D26-298[»]
1FFOX-ray2.65A/D26-298[»]
1FFPX-ray2.60A/D26-298[»]
1FG2X-ray2.75A/D/G/J25-304[»]
1HOCX-ray2.40A25-296[»]
1INQX-ray2.20A25-299[»]
1JPFX-ray2.18A25-304[»]
1JPGX-ray2.20A25-304[»]
1JUFX-ray2.00A25-299[»]
1N3NX-ray3.00A/C/E/G25-304[»]
1N5AX-ray2.85A/D/G/J25-300[»]
1QLFX-ray2.65A25-300[»]
1S7UX-ray2.20A/D/G/J25-362[»]
1S7VX-ray2.20A/D25-362[»]
1S7WX-ray2.40A/D/G/J25-362[»]
1S7XX-ray2.41A/D/G/J25-362[»]
1WBXX-ray1.90A25-300[»]
1WBYX-ray2.30A25-300[»]
1YN6X-ray2.20A26-298[»]
1YN7X-ray2.20A26-298[»]
1ZHBX-ray2.70A/D/G/J25-300[»]
2CIIX-ray2.55A25-299[»]
2F74X-ray2.70A/D25-300[»]
2VE6X-ray2.65A/D/G/J25-301[»]
2ZOKX-ray2.10A/C/E/G25-299[»]
2ZOLX-ray2.70A/C25-299[»]
3BUYX-ray2.60A26-300[»]
3CC5X-ray1.91A/D25-300[»]
3CCHX-ray2.60A/D/G/J25-300[»]
3CH1X-ray2.30A/D/G/J25-300[»]
3CPLX-ray2.50A/C25-299[»]
3FTGX-ray2.60A25-304[»]
3L3HX-ray2.70A26-300[»]
3PQYX-ray3.19A/F/K/P26-300[»]
3QUKX-ray2.41A/D25-362[»]
3QULX-ray2.00A/D/G/J25-362[»]
3TBSX-ray2.49A/D25-362[»]
3TBTX-ray2.30A/D/G/J25-362[»]
3TBVX-ray2.10A/C/E/G25-362[»]
3TBWX-ray2.15A/C/E/G25-362[»]
3TBYX-ray2.50A/D/G/J25-362[»]
4HUUX-ray2.00A/D25-304[»]
4HUVX-ray2.50A/D25-304[»]
4HUWX-ray3.16A/C/E/G25-304[»]
4HUXX-ray2.20A25-304[»]
4HV8X-ray2.00A/C25-304[»]
4IHOX-ray2.80A/D25-300[»]
4L8BX-ray2.20A25-304[»]
4L8CX-ray2.80A/C/E/G25-304[»]
4L8DX-ray1.90A/C25-304[»]
4NSKX-ray2.60A25-362[»]
ProteinModelPortalP01899.
SMRP01899. Positions 25-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6121N.
IntActP01899. 2 interactions.
MINTMINT-85762.

Proteomic databases

PaxDbP01899.
PRIDEP01899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000172785; ENSMUSP00000134570; ENSMUSG00000073411.
GeneID14964.
KEGGmmu:14964.
UCSCuc008chg.1. mouse.

Organism-specific databases

CTD14964.
MGIMGI:95896. H2-D1.

Phylogenomic databases

eggNOGNOG42056.
HOVERGENHBG016709.
InParanoidP01899.
KOK06751.
OMAYYLTHEC.
OrthoDBEOG7JT6WQ.
PhylomeDBP01899.
TreeFamTF336617.

Enzyme and pathway databases

ReactomeREACT_102124. Immune System.
REACT_98458. Immune System.

Gene expression databases

ArrayExpressP01899.
BgeeP01899.
CleanExMM_H2-D1.
GenevestigatorP01899.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
IPR010579. MHC_I_a_C.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]
PRINTSPR01638. MHCCLASSI.
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01899.
NextBio287322.
PROP01899.
SOURCESearch...

Entry information

Entry nameHA11_MOUSE
AccessionPrimary (citable) accession number: P01899
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot