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Protein

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

Gene

H2-D1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. beta-2-microglobulin binding Source: MGI
  2. peptide antigen binding Source: MGI
  3. poly(A) RNA binding Source: MGI
  4. receptor binding Source: MGI
  5. TAP binding Source: MGI
  6. T cell receptor 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
Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_300990. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_308964. ER-Phagosome pathway.
REACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
REACT_341075. ER-Phagosome pathway.
REACT_342269. Endosomal/Vacuolar pathway.
REACT_349056. Interferon gamma signaling.

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 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:95896. H2-D1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 309285ExtracellularSequence AnalysisAdd
BLAST
Transmembranei310 – 33122HelicalSequence AnalysisAdd
BLAST
Topological domaini332 – 36231CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: MGI
  3. endoplasmic reticulum exit site Source: MGI
  4. external side of plasma membrane Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. Golgi apparatus Source: MGI
  7. Golgi medial cisterna Source: MGI
  8. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  9. membrane Source: MGI
  10. MHC class I protein complex Source: MGI
  11. phagocytic vesicle membrane Source: Reactome
  12. plasma membrane Source: MGI
Complete GO annotation...

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. 1 Publication
Mutagenesisi350 – 3523SQS → AQG in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361. 2 Publications
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. 3 Publications

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 ↔ 188PROSITE-ProRule annotation1 Publication
Glycosylationi200 – 2001N-linked (GlcNAc...)Curated
Disulfide bondi227 ↔ 283PROSITE-ProRule annotation1 Publication
Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
Modified residuei353 – 3531Phosphoserine; alternateBy similarity
Cross-linki353 – 353Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei356 – 3561PhosphoserineBy similarity

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, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP01899.
PaxDbiP01899.
PRIDEiP01899.

Expressioni

Gene expression databases

BgeeiP01899.
CleanExiMM_H2-D1.
ExpressionAtlasiP01899. baseline and differential.
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 – 3610Combined sources
Beta strandi39 – 413Combined sources
Beta strandi45 – 528Combined sources
Beta strandi55 – 617Combined sources
Beta strandi64 – 663Combined sources
Beta strandi70 – 734Combined sources
Helixi74 – 785Combined sources
Helixi81 – 10828Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi131 – 14212Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 17413Combined sources
Helixi177 – 1859Combined sources
Helixi187 – 19812Combined sources
Helixi200 – 2034Combined sources
Beta strandi210 – 21910Combined sources
Beta strandi222 – 23514Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi265 – 27410Combined sources
Helixi278 – 2803Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi294 – 2963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PG2X-ray2.80A25-299[»]
ProteinModelPortaliP01899.
SMRiP01899. Positions 25-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01899.

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.
KOiK06751.
OMAiHRYLANG.
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

        10         20         30         40         50
MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LEEPRYISVG
60 70 80 90 100
YVDNKEFVRF DSDAENPRYE PRAPWMEQEG PEYWERETQK AKGQEQWFRV
110 120 130 140 150
SLRNLLGYYN QSAGGSHTLQ QMSGCDLGSD WRLLRGYLQF AYEGRDYIAL
160 170 180 190 200
NEDLKTWTAA DMAAQITRRK WEQSGAAEHY KAYLEGECVE WLHRYLKNGN
210 220 230 240 250
ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT WQLNGEELTQ
260 270 280 290 300
DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP
310 320 330 340 350
PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS
360
QSSEMSLRDC KA
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.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PG2X-ray2.80A25-299[»]
ProteinModelPortaliP01899.
SMRiP01899. Positions 25-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP01899.
PaxDbiP01899.
PRIDEiP01899.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi14964.
MGIiMGI:95896. H2-D1.

Phylogenomic databases

eggNOGiNOG42056.
HOVERGENiHBG016709.
KOiK06751.
OMAiHRYLANG.
OrthoDBiEOG7JT6WQ.
PhylomeDBiP01899.
TreeFamiTF336617.

Enzyme and pathway databases

ReactomeiREACT_300990. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_308964. ER-Phagosome pathway.
REACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
REACT_341075. ER-Phagosome pathway.
REACT_342269. Endosomal/Vacuolar pathway.
REACT_349056. Interferon gamma signaling.

Miscellaneous databases

EvolutionaryTraceiP01899.
NextBioi287322.
PROiP01899.
SOURCEiSearch...

Gene expression databases

BgeeiP01899.
CleanExiMM_H2-D1.
ExpressionAtlasiP01899. baseline and differential.
GenevestigatoriP01899.

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]
ProtoNetiSearch...

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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C3H.
  2. Girgis K.R., Capra D.J., Stroynowski I.
    Submitted (APR-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(1995) [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(1981) [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(1980) [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(1981) [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(1984) [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(2006) [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(2008) [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(2008) [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(1993) [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(1999) [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: April 1, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.