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P01899

- HA11_MOUSE

UniProt

P01899 - HA11_MOUSE

Protein

H-2 class I histocompatibility antigen, D-B alpha chain

Gene

H2-D1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. peptide antigen binding Source: InterPro
    2. protein binding Source: MGI

    GO - Biological processi

    1. antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent Source: MGI
    2. immune response Source: InterPro
    3. positive regulation of T cell mediated cytotoxicity Source: MGI

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_197102. ER-Phagosome pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    H-2 class I histocompatibility antigen, D-B alpha chain
    Short name:
    H-2D(B)
    Gene namesi
    Name:H2-D1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:95896. H2-D1.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    3. MHC class I protein complex Source: UniProtKB-KW
    4. phagocytic vesicle membrane Source: Reactome
    5. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane, MHC I

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551K → 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. 1 Publication
    Mutagenesisi92 – 921K → 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. 1 Publication
    Mutagenesisi155 – 1551K → 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. 1 Publication
    Mutagenesisi170 – 1701K → 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. 1 Publication
    Mutagenesisi197 – 1971K → 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. 1 Publication
    Mutagenesisi210 – 2101K → 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. 1 Publication
    Mutagenesisi220 – 2201K → 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. 1 Publication
    Mutagenesisi267 – 2671K → 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. 1 Publication
    Mutagenesisi277 – 2771K → 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. 1 Publication
    Mutagenesisi332 – 3321K → 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. 3 Publications
    Mutagenesisi337 – 3371T → 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. 3 Publications
    Mutagenesisi340 – 3401K → 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. 3 Publications
    Mutagenesisi350 – 3567SQSSEMS → AQGAEMA in Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337 and 360-R-R-361.
    Mutagenesisi350 – 3523SQS → AQG in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361.
    Mutagenesisi356 – 3561S → A in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340 and A-356. 2 Publications
    Mutagenesisi360 – 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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 362338H-2 class I histocompatibility antigen, D-B alpha chainPRO_0000018923Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)2 Publications
    Disulfide bondi125 ↔ 1881 PublicationPROSITE-ProRule annotation
    Glycosylationi200 – 2001N-linked (GlcNAc...)Curated
    Disulfide bondi227 ↔ 2831 PublicationPROSITE-ProRule annotation
    Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
    Cross-linki353 – 353Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    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.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP01899.
    PaxDbiP01899.
    PRIDEiP01899.

    Expressioni

    Gene expression databases

    ArrayExpressiP01899.
    BgeeiP01899.
    CleanExiMM_H2-D1.
    GenevestigatoriP01899.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Interacts with murid herpesvirus 4 protein K3 (mK3).3 Publications

    Protein-protein interaction databases

    DIPiDIP-6121N.
    IntActiP01899. 2 interactions.
    MINTiMINT-85762.

    Structurei

    Secondary structure

    1
    362
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 3610
    Beta strandi39 – 413
    Beta strandi45 – 528
    Beta strandi55 – 617
    Beta strandi64 – 663
    Beta strandi70 – 734
    Helixi74 – 785
    Helixi81 – 10828
    Beta strandi113 – 1153
    Beta strandi118 – 12710
    Beta strandi131 – 14212
    Beta strandi145 – 1506
    Beta strandi157 – 1593
    Helixi162 – 17413
    Helixi177 – 1859
    Helixi187 – 19812
    Helixi200 – 2034
    Beta strandi210 – 21910
    Beta strandi222 – 23514
    Beta strandi238 – 2436
    Beta strandi246 – 2483
    Beta strandi250 – 2545
    Beta strandi261 – 2633
    Beta strandi265 – 27410
    Helixi278 – 2803
    Beta strandi281 – 2866
    Beta strandi290 – 2923
    Beta strandi294 – 2963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    3WS3X-ray2.34A/C26-298[»]
    3WS6X-ray1.98A/B26-300[»]
    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-ray2.60A25-300[»]
    ProteinModelPortaliP01899.
    SMRiP01899. Positions 25-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01899.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 309285ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini332 – 36231CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei310 – 33122HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini209 – 29789Ig-like C1-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 11490Alpha-1Add
    BLAST
    Regioni115 – 20692Alpha-2Add
    BLAST
    Regioni207 – 29892Alpha-3Add
    BLAST
    Regioni299 – 30911Connecting peptideAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MHC class I family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42056.
    HOVERGENiHBG016709.
    InParanoidiP01899.
    KOiK06751.
    OMAiWDEETEE.
    OrthoDBiEOG7JT6WQ.
    PhylomeDBiP01899.
    TreeFamiTF336617.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. 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]
    PfamiPF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    PF06623. MHC_I_C. 1 hit.
    [Graphical view]
    PRINTSiPR01638. MHCCLASSI.
    SMARTiSM00407. IGc1. 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.

    P01899-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LEEPRYISVG    50
    YVDNKEFVRF DSDAENPRYE PRAPWMEQEG PEYWERETQK AKGQEQWFRV 100
    SLRNLLGYYN QSAGGSHTLQ QMSGCDLGSD WRLLRGYLQF AYEGRDYIAL 150
    NEDLKTWTAA DMAAQITRRK WEQSGAAEHY KAYLEGECVE WLHRYLKNGN 200
    ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT WQLNGEELTQ 250
    DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP 300
    PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS 350
    QSSEMSLRDC KA 362
    Length:362
    Mass (Da):40,836
    Last modified:January 1, 1990 - v2
    Checksum:i6EE6AEF97263FA71
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18523 Genomic DNA. Translation: AAA53200.1.
    L36068 mRNA. Translation: AAA89206.1.
    U47325 mRNA. Translation: AAB17603.1.
    K00129 mRNA. Translation: AAA39580.1. Different initiation.
    CCDSiCCDS57074.1.
    PIRiB60854.
    I56002. HLMSDB.
    RefSeqiNP_034510.3. NM_010380.3.
    UniGeneiMm.439675.

    Genome annotation databases

    EnsembliENSMUST00000172785; ENSMUSP00000134570; ENSMUSG00000073411.
    GeneIDi14964.
    KEGGimmu:14964.
    UCSCiuc008chg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18523 Genomic DNA. Translation: AAA53200.1 .
    L36068 mRNA. Translation: AAA89206.1 .
    U47325 mRNA. Translation: AAB17603.1 .
    K00129 mRNA. Translation: AAA39580.1 . Different initiation.
    CCDSi CCDS57074.1.
    PIRi B60854.
    I56002. HLMSDB.
    RefSeqi NP_034510.3. NM_010380.3.
    UniGenei Mm.439675.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BZ9 X-ray 2.80 A 26-299 [» ]
    1CE6 X-ray 2.90 A 25-298 [» ]
    1FFN X-ray 2.70 A/D 26-298 [» ]
    1FFO X-ray 2.65 A/D 26-298 [» ]
    1FFP X-ray 2.60 A/D 26-298 [» ]
    1FG2 X-ray 2.75 A/D/G/J 25-304 [» ]
    1HOC X-ray 2.40 A 25-296 [» ]
    1INQ X-ray 2.20 A 25-299 [» ]
    1JPF X-ray 2.18 A 25-304 [» ]
    1JPG X-ray 2.20 A 25-304 [» ]
    1JUF X-ray 2.00 A 25-299 [» ]
    1N3N X-ray 3.00 A/C/E/G 25-304 [» ]
    1N5A X-ray 2.85 A/D/G/J 25-300 [» ]
    1QLF X-ray 2.65 A 25-300 [» ]
    1S7U X-ray 2.20 A/D/G/J 25-362 [» ]
    1S7V X-ray 2.20 A/D 25-362 [» ]
    1S7W X-ray 2.40 A/D/G/J 25-362 [» ]
    1S7X X-ray 2.41 A/D/G/J 25-362 [» ]
    1WBX X-ray 1.90 A 25-300 [» ]
    1WBY X-ray 2.30 A 25-300 [» ]
    1YN6 X-ray 2.20 A 26-298 [» ]
    1YN7 X-ray 2.20 A 26-298 [» ]
    1ZHB X-ray 2.70 A/D/G/J 25-300 [» ]
    2CII X-ray 2.55 A 25-299 [» ]
    2F74 X-ray 2.70 A/D 25-300 [» ]
    2VE6 X-ray 2.65 A/D/G/J 25-301 [» ]
    2ZOK X-ray 2.10 A/C/E/G 25-299 [» ]
    2ZOL X-ray 2.70 A/C 25-299 [» ]
    3BUY X-ray 2.60 A 26-300 [» ]
    3CC5 X-ray 1.91 A/D 25-300 [» ]
    3CCH X-ray 2.60 A/D/G/J 25-300 [» ]
    3CH1 X-ray 2.30 A/D/G/J 25-300 [» ]
    3CPL X-ray 2.50 A/C 25-299 [» ]
    3FTG X-ray 2.60 A 25-304 [» ]
    3L3H X-ray 2.70 A 26-300 [» ]
    3PQY X-ray 3.19 A/F/K/P 26-300 [» ]
    3QUK X-ray 2.41 A/D 25-362 [» ]
    3QUL X-ray 2.00 A/D/G/J 25-362 [» ]
    3TBS X-ray 2.49 A/D 25-362 [» ]
    3TBT X-ray 2.30 A/D/G/J 25-362 [» ]
    3TBV X-ray 2.10 A/C/E/G 25-362 [» ]
    3TBW X-ray 2.15 A/C/E/G 25-362 [» ]
    3TBY X-ray 2.50 A/D/G/J 25-362 [» ]
    3WS3 X-ray 2.34 A/C 26-298 [» ]
    3WS6 X-ray 1.98 A/B 26-300 [» ]
    4HUU X-ray 2.00 A/D 25-304 [» ]
    4HUV X-ray 2.50 A/D 25-304 [» ]
    4HUW X-ray 3.16 A/C/E/G 25-304 [» ]
    4HUX X-ray 2.20 A 25-304 [» ]
    4HV8 X-ray 2.00 A/C 25-304 [» ]
    4IHO X-ray 2.80 A/D 25-300 [» ]
    4L8B X-ray 2.20 A 25-304 [» ]
    4L8C X-ray 2.80 A/C/E/G 25-304 [» ]
    4L8D X-ray 1.90 A/C 25-304 [» ]
    4NSK X-ray 2.60 A 25-300 [» ]
    ProteinModelPortali P01899.
    SMRi P01899. Positions 25-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6121N.
    IntActi P01899. 2 interactions.
    MINTi MINT-85762.

    Proteomic databases

    MaxQBi P01899.
    PaxDbi P01899.
    PRIDEi P01899.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000172785 ; ENSMUSP00000134570 ; ENSMUSG00000073411 .
    GeneIDi 14964.
    KEGGi mmu:14964.
    UCSCi uc008chg.1. mouse.

    Organism-specific databases

    CTDi 14964.
    MGIi MGI:95896. H2-D1.

    Phylogenomic databases

    eggNOGi NOG42056.
    HOVERGENi HBG016709.
    InParanoidi P01899.
    KOi K06751.
    OMAi WDEETEE.
    OrthoDBi EOG7JT6WQ.
    PhylomeDBi P01899.
    TreeFami TF336617.

    Enzyme and pathway databases

    Reactomei REACT_197102. ER-Phagosome pathway.

    Miscellaneous databases

    EvolutionaryTracei P01899.
    NextBioi 287322.
    PROi P01899.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01899.
    Bgeei P01899.
    CleanExi MM_H2-D1.
    Genevestigatori P01899.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. 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 ]
    Pfami PF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    PF06623. MHC_I_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01638. MHCCLASSI.
    SMARTi SM00407. IGc1. 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. "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.

    Entry informationi

    Entry nameiHA11_MOUSE
    AccessioniPrimary (citable) accession number: P01899
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3