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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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiR-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:95896. H2-D1.

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

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...)2 Publications1
Disulfide bondi125 ↔ 188PROSITE-ProRule annotation1 Publication
Glycosylationi200N-linked (GlcNAc...)Curated1
Disulfide bondi227 ↔ 283PROSITE-ProRule annotation1 Publication
Glycosylationi280N-linked (GlcNAc...)1 Publication1
Cross-linki353Glycyl 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

EPDiP01899.
PaxDbiP01899.
PRIDEiP01899.

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

DIPiDIP-6121N.
IntActiP01899. 2 interactors.
MINTiMINT-85762.
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 strandi131 – 142Combined sources12
Beta strandi145 – 150Combined sources6
Beta strandi157 – 159Combined sources3
Helixi162 – 174Combined sources13
Helixi177 – 185Combined sources9
Helixi187 – 198Combined sources12
Helixi200 – 203Combined sources4
Beta strandi210 – 219Combined sources10
Beta strandi222 – 235Combined sources14
Beta strandi238 – 243Combined sources6
Beta strandi246 – 248Combined sources3
Beta strandi250 – 254Combined sources5
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[»]
5SWSX-ray2.86A25-304[»]
5SWZX-ray2.65A/F/K/P25-304[»]
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.
OMAiKTHITHY.
OrthoDBiEOG091G09OH.
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.
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]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. 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 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
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[»]
5SWSX-ray2.86A25-304[»]
5SWZX-ray2.65A/F/K/P25-304[»]
ProteinModelPortaliP01899.
SMRiP01899.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6121N.
IntActiP01899. 2 interactors.
MINTiMINT-85762.
STRINGi10090.ENSMUSP00000134570.

Proteomic databases

EPDiP01899.
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

eggNOGiENOG410II5V. Eukaryota.
ENOG4111K8F. LUCA.
GeneTreeiENSGT00760000118960.
HOVERGENiHBG016709.
KOiK06751.
OMAiKTHITHY.
OrthoDBiEOG091G09OH.
PhylomeDBiP01899.
TreeFamiTF336617.

Enzyme and pathway databases

ReactomeiR-MMU-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

EvolutionaryTraceiP01899.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000073411.
CleanExiMM_H2-D1.
ExpressionAtlasiP01899. baseline and differential.
GenevisibleiP01899. MM.

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.
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]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 167 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

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 one 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.