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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: -Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processImmunity

Enzyme and pathway databases

ReactomeiR-MMU-1236974 ER-Phagosome pathway
R-MMU-1236977 Endosomal/Vacuolar pathway
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-6798695 Neutrophil degranulation
R-MMU-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:95896 H2-D1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 309ExtracellularSequence analysisAdd BLAST285
Transmembranei310 – 331HelicalSequence analysisAdd BLAST22
Topological domaini332 – 362CytoplasmicSequence analysisAdd BLAST31

Keywords - Cellular componenti

Membrane, MHC I

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi55K → 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 Publication1
Mutagenesisi92K → 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 Publication1
Mutagenesisi155K → 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 Publication1
Mutagenesisi170K → 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 Publication1
Mutagenesisi197K → 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 Publication1
Mutagenesisi210K → 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 Publication1
Mutagenesisi220K → 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 Publication1
Mutagenesisi267K → 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 Publication1
Mutagenesisi277K → 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 Publication1
Mutagenesisi332K → 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 Publications1
Mutagenesisi337T → 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 Publications1
Mutagenesisi340K → 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 Publications1
Mutagenesisi350 – 356SQSSEMS → AQGAEMA in Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337 and 360-R-R-361. 1 Publication7
Mutagenesisi350 – 352SQS → AQG in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361. 2 Publications3
Mutagenesisi356S → A in Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340 and A-356. 2 Publications1
Mutagenesisi360 – 361CK → 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 Publications2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001892325 – 362H-2 class I histocompatibility antigen, D-B alpha chainAdd BLAST338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi110N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi125 ↔ 188PROSITE-ProRule annotation1 Publication
Glycosylationi200N-linked (GlcNAc...) asparagineCurated1
Disulfide bondi227 ↔ 283PROSITE-ProRule annotation1 Publication
Glycosylationi280N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei353Phosphoserine; alternateBy similarity1
Cross-linki353Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei356PhosphoserineBy similarity1

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

EPDiP01899
PaxDbiP01899
PRIDEiP01899

PTM databases

iPTMnetiP01899
PhosphoSitePlusiP01899

Expressioni

Gene expression databases

BgeeiENSMUSG00000073411
CleanExiMM_H2-D1
ExpressionAtlasiP01899 baseline and differential
GenevisibleiP01899 MM

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200150, 1 interactor
DIPiDIP-6121N
IntActiP01899, 2 interactors
MINTiP01899
STRINGi10090.ENSMUSP00000134570

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 36Combined sources10
Beta strandi39 – 41Combined sources3
Beta strandi45 – 52Combined sources8
Beta strandi55 – 61Combined sources7
Beta strandi64 – 66Combined sources3
Beta strandi70 – 73Combined sources4
Helixi74 – 78Combined sources5
Helixi81 – 108Combined sources28
Beta strandi113 – 115Combined sources3
Beta strandi118 – 127Combined sources10
Beta strandi129 – 131Combined sources3
Beta strandi133 – 142Combined sources10
Beta strandi145 – 150Combined sources6
Beta strandi157 – 159Combined sources3
Helixi162 – 174Combined sources13
Helixi176 – 185Combined sources10
Helixi187 – 203Combined sources17
Beta strandi210 – 218Combined sources9
Turni219 – 221Combined sources3
Beta strandi222 – 235Combined sources14
Beta strandi238 – 243Combined sources6
Beta strandi246 – 248Combined sources3
Helixi249 – 251Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi261 – 263Combined sources3
Beta strandi265 – 274Combined sources10
Helixi278 – 280Combined sources3
Beta strandi281 – 286Combined sources6
Beta strandi290 – 292Combined sources3
Beta strandi294 – 296Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5E8NX-ray2.25A/D/G/J25-300[»]
5E8OX-ray1.98A/D25-300[»]
5E8PX-ray2.00A/D25-300[»]
5JWDX-ray2.50A25-298[»]
5JWEX-ray2.40A/C/E/G25-300[»]
5M00X-ray1.95A25-300[»]
5M01X-ray1.95A25-300[»]
5M02X-ray1.75A25-300[»]
5MZMX-ray2.40A/D25-300[»]
5OPIX-ray3.30A25-300[»]
5SWSX-ray2.86A25-304[»]
5SWZX-ray2.65A/F/K/P25-304[»]
5TILX-ray2.83A/D25-300[»]
5TJEX-ray3.20A/C25-300[»]
5WLGX-ray2.10A/F25-302[»]
5WLIX-ray2.20A/D/G/J25-302[»]
ProteinModelPortaliP01899
SMRiP01899
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01899

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini209 – 297Ig-like C1-typeAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 114Alpha-1Add BLAST90
Regioni115 – 206Alpha-2Add BLAST92
Regioni207 – 298Alpha-3Add BLAST92
Regioni299 – 309Connecting peptideAdd BLAST11

Sequence similaritiesi

Belongs to the MHC class I family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II5V Eukaryota
ENOG4111K8F LUCA
GeneTreeiENSGT00760000118960
HOVERGENiHBG016709
KOiK06751
OMAiVPGYYNQ
OrthoDBiEOG091G09OH
PhylomeDBiP01899
TreeFamiTF336617

Family and domain databases

Gene3Di2.60.40.10, 1 hit
3.30.500.10, 1 hit
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003006 Ig/MHC_CS
IPR003597 Ig_C1-set
IPR011161 MHC_I-like_Ag-recog
IPR037055 MHC_I-like_Ag-recog_sf
IPR011162 MHC_I/II-like_Ag-recog
IPR001039 MHC_I_a_a1/a2
IPR010579 MHC_I_a_C
PfamiView protein in Pfam
PF07654 C1-set, 1 hit
PF00129 MHC_I, 1 hit
PF06623 MHC_I_C, 1 hit
PRINTSiPR01638 MHCCLASSI
SMARTiView protein in SMART
SM00407 IGc1, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
SSF54452 SSF54452, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00290 IG_MHC, 1 hit

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 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

Similar proteinsi

Entry informationi

Entry nameiHA11_MOUSE
AccessioniPrimary (citable) accession number: P01899
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: May 23, 2018
This is version 180 of the entry and version 2 of the sequence. See 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

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