H2-D1
entrez
14964
canonical
uniprot
P01899
canonical
ensembl
ENSMUSG00000073411
resolver
ensp
ENSMUSP00000134570
resolver
enst
ENSMUST00000172785
resolver
genesymbol
H2-D1
resolver
genesymbol_syn
D(b) gene
resolver
uniprot
Q792Z7
resolver
uniprot_entry
HA11_MOUSE
resolver
uniprot_entry
Q792Z7_MOUSE
resolver
amino_acid_sequence
MGAMAPRTLLLLLAAALAPTQTRAGPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAMAIIGAVVAFVMKRRRNTGGKGGDYALAPGSQSSEMSLRDCKA
uniprot
proteins
function
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
uniprot
proteins
mass_dalton
40836
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 92; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 155; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 170; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 197; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 210; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 220; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 267; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 277; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 332; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"; MUTAGEN 337; /note="T->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."; /evidence="ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"; MUTAGEN 340; /note="K->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."; /evidence="ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"; MUTAGEN 350..356; /note="SQSSEMS->AQGAEMA: In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337 and 360-R-R-361."; /evidence="ECO:0000269|PubMed:17502423"; MUTAGEN 350..352; /note="SQS->AQG: In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361."; /evidence="ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"; MUTAGEN 356; /note="S->A: In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340 and A-356."; /evidence="ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"; MUTAGEN 360..361; /note="CK->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."; /evidence="ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915}.
uniprot
proteins
protein_family
MHC class I family
uniprot
proteins
pubmed
10993729
uniprot
proteins
pubmed
17502423
uniprot
proteins
pubmed
19531064
uniprot
proteins
pubmed
19951915
uniprot
proteins
pubmed
3680952
uniprot
proteins
pubmed
3980466
uniprot
proteins
pubmed
7118211
uniprot
proteins
pubmed
7118212
uniprot
proteins
pubmed
7225204
uniprot
proteins
pubmed
7506996
uniprot
proteins
pubmed
9869916
uniprot
proteins
sequence_length
362
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 310..331; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins