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P01899

- HA11_MOUSE

UniProt

P01899 - HA11_MOUSE

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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: 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. peptide antigen binding Source: RefGenome
  2. protein binding Source: MGI
  3. receptor binding Source: RefGenome

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_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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 309285Extracellular Reviewed prediction
Add
BLAST
Transmembranei310 – 33122Helical; Reviewed prediction
Add
BLAST
Topological domaini332 – 36231Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 Publication
Add
BLAST
Chaini25 – 362338H-2 class I histocompatibility antigen, D-B alpha chain
PRO_0000018923Add
BLAST

Amino acid modifications

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

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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP01899.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the MHC class I family.

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: September 3, 2014
This is version 142 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

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