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Protein

Major histocompatibility complex class I-related gene protein

Gene

MR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antigen-presenting molecule specialized in presenting microbial vitamin B metabolites. Involved in the development and expansion of a small population of T-cells expressing an invariant T-cell receptor alpha chain called mucosal-associated invariant T-cells (MAIT). MAIT lymphocytes are preferentially located in the gut lamina propria and therefore may be involved in monitoring commensal flora or serve as a distress signal. Expression and MAIT cell recognition seem to be ligand-dependent.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651Pathogen-derived ligand

GO - Molecular functioni

  • antigen binding Source: GO_Central
  • MHC class I receptor activity Source: UniProtKB
  • peptide antigen binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Major histocompatibility complex class I-related gene protein
Short name:
MHC class I-related gene protein
Alternative name(s):
Class I histocompatibility antigen-like protein
Gene namesi
Name:MR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4975. MR1.

Subcellular locationi

Isoform 3 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 302280ExtracellularSequence AnalysisAdd
BLAST
Transmembranei303 – 32321HelicalSequence AnalysisAdd
BLAST
Topological domaini324 – 34118CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, MHC I, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651K → R: Fails to refold in the presence of 6-FP.
Mutagenesisi169 – 1691Q → L: Able to activate mouse MAIT cells. 1 Publication
Mutagenesisi283 – 2831C → G: No effect on cell surface expression. 1 Publication

Organism-specific databases

PharmGKBiPA29309.

Chemistry

DrugBankiDB00098. Antithymocyte globulin.

Polymorphism and mutation databases

BioMutaiMR1.
DMDMi74751679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 341319Major histocompatibility complex class I-related gene proteinPRO_0000344441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)1 Publication
Disulfide bondi120 ↔ 183PROSITE-ProRule annotation1 Publication
Disulfide bondi222 ↔ 278PROSITE-ProRule annotation1 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ95460.
PRIDEiQ95460.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ95460.
CleanExiHS_MR1.
GenevisibleiQ95460. HS.

Interactioni

Subunit structurei

Heterodimerizes with B2M, this interaction is required for surface expression. Associated with the peptide-loading complex, TAPBP, CALR and PDIA3. Isoform 3/MR1B homodimerizes and doesn't associates with B2M nor proteins of the peptide-loading complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FATE1Q969F03EBI-10280401,EBI-743099

Protein-protein interaction databases

BioGridi109385. 13 interactions.
DIPiDIP-59986N.
IntActiQ95460. 1 interaction.
STRINGi9606.ENSP00000356552.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 3612Combined sources
Beta strandi39 – 413Combined sources
Beta strandi43 – 508Combined sources
Beta strandi53 – 597Combined sources
Turni60 – 623Combined sources
Beta strandi66 – 694Combined sources
Helixi70 – 734Combined sources
Helixi78 – 10629Combined sources
Beta strandi113 – 12210Combined sources
Beta strandi128 – 1369Combined sources
Beta strandi139 – 1457Combined sources
Turni146 – 1494Combined sources
Beta strandi150 – 1556Combined sources
Helixi156 – 16611Combined sources
Helixi169 – 18012Combined sources
Helixi182 – 19312Combined sources
Helixi195 – 1984Combined sources
Beta strandi205 – 2128Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi218 – 23013Combined sources
Beta strandi233 – 2386Combined sources
Turni239 – 2413Combined sources
Helixi244 – 2463Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi260 – 2678Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi285 – 2906Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GUPX-ray3.20A/C23-292[»]
4L4TX-ray2.00A/C23-292[»]
4L4VX-ray1.90A/C23-292[»]
4LCWX-ray2.40A/C23-292[»]
4NQCX-ray2.50A/C23-292[»]
4NQDX-ray2.20A/C23-292[»]
4NQEX-ray2.10A/C23-292[»]
4PJ5X-ray2.00A/C23-292[»]
4PJ7X-ray2.50A/C23-292[»]
4PJ8X-ray3.30A23-292[»]
4PJ9X-ray2.00A23-292[»]
4PJAX-ray2.68A/C23-292[»]
4PJBX-ray2.85A/C23-292[»]
4PJCX-ray2.50A/C23-292[»]
4PJDX-ray2.78A/C23-292[»]
4PJEX-ray1.95A/C23-292[»]
4PJFX-ray2.45A/C23-292[»]
4PJGX-ray2.40A/C23-292[»]
4PJHX-ray2.00A/C23-292[»]
4PJIX-ray2.50A/C23-292[»]
4PJXX-ray2.25A/C23-292[»]
ProteinModelPortaliQ95460.
SMRiQ95460. Positions 23-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini203 – 29997Ig-like C1-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 201179Ligand-bindingAdd
BLAST
Regioni23 – 10987Alpha-1Add
BLAST
Regioni110 – 20192Alpha-2Add
BLAST
Regioni202 – 29392Alpha-3Add
BLAST
Regioni294 – 3029Connecting peptide

Domaini

The alpha-3 region and to a lesser extent the transmembrane and cytosolic domains regulate surface expression. The alpha-3 region mediates interaction with B2M (PubMed:23051753).1 Publication
The ligand-binding groove is ideally suited to present small organic compounds that can originate from vitamins rather than antigenic peptides.1 Publication

Sequence similaritiesi

Belongs to the MHC class I family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42056.
GeneTreeiENSGT00760000118960.
HOGENOMiHOG000296917.
HOVERGENiHBG016709.
InParanoidiQ95460.
OMAiTWMKNGE.
OrthoDBiEOG7JT6WQ.
PhylomeDBiQ95460.
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.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 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]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q95460-1) [UniParc]FASTAAdd to basket

Also known as: MR1A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGELMAFLLP LIIVLMVKHS DSRTHSLRYF RLGVSDPIHG VPEFISVGYV
60 70 80 90 100
DSHPITTYDS VTRQKEPRAP WMAENLAPDH WERYTQLLRG WQQMFKVELK
110 120 130 140 150
RLQRHYNHSG SHTYQRMIGC ELLEDGSTTG FLQYAYDGQD FLIFNKDTLS
160 170 180 190 200
WLAVDNVAHT IKQAWEANQH ELLYQKNWLE EECIAWLKRF LEYGKDTLQR
210 220 230 240 250
TEPPLVRVNR KETFPGVTAL FCKAHGFYPP EIYMTWMKNG EEIVQEIDYG
260 270 280 290 300
DILPSGDGTY QAWASIELDP QSSNLYSCHV EHCGVHMVLQ VPQESETIPL
310 320 330 340
VMKAVSGSIV LVIVLAGVGV LVWRRRPREQ NGAIYLPTPD R
Length:341
Mass (Da):39,366
Last modified:February 1, 1997 - v1
Checksum:i2990C1F3F0A1CAD9
GO
Isoform 2 (identifier: Q95460-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-154: Missing.

Show »
Length:296
Mass (Da):34,278
Checksum:i05ABC9CD4189F639
GO
Isoform 3 (identifier: Q95460-3) [UniParc]FASTAAdd to basket

Also known as: MR1B, MR1D

The sequence of this isoform differs from the canonical sequence as follows:
     203-294: Missing.

Show »
Length:249
Mass (Da):28,973
Checksum:iDED2E979686D6A8A
GO
Isoform 4 (identifier: Q95460-4) [UniParc]FASTAAdd to basket

Also known as: MR1C

The sequence of this isoform differs from the canonical sequence as follows:
     202-220: EPPLVRVNRKETFPGVTAL → GKEKEKASFPHCLNNCFYT
     221-341: Missing.

Show »
Length:220
Mass (Da):25,933
Checksum:i529688A56159C475
GO
Isoform 5 (identifier: Q95460-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     202-328: Missing.

Note: No experimental confirmation available.
Show »
Length:214
Mass (Da):25,190
Checksum:iB84A09E70B280E74
GO

Sequence cautioni

The sequence AAD01443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171M → V in BAF83063 (PubMed:14702039).Curated
Sequence conflicti200 – 2001R → G in BAD96630 (Ref. 4) Curated
Sequence conflicti315 – 3151L → P in BAD96630 (Ref. 4) Curated

Polymorphismi

Several individuals from different ethnic background were analyzed for polymorphism. MR1 was identical in all individuals analyzed, except one. MR1 is not polymorphic.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391H → R.1 Publication
Corresponds to variant rs2236410 [ dbSNP | Ensembl ].
VAR_045608
Natural varianti63 – 631R → Q.
Corresponds to variant rs3897433 [ dbSNP | Ensembl ].
VAR_045609
Natural varianti77 – 771A → V.
Corresponds to variant rs3897434 [ dbSNP | Ensembl ].
VAR_045610

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei110 – 15445Missing in isoform 2. 1 PublicationVSP_034755Add
BLAST
Alternative sequencei202 – 328127Missing in isoform 5. 1 PublicationVSP_043479Add
BLAST
Alternative sequencei202 – 22019EPPLV…GVTAL → GKEKEKASFPHCLNNCFYT in isoform 4. 1 PublicationVSP_034756Add
BLAST
Alternative sequencei203 – 29492Missing in isoform 3. 2 PublicationsVSP_034757Add
BLAST
Alternative sequencei221 – 341121Missing in isoform 4. 1 PublicationVSP_034758Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22963 mRNA. Translation: AAC50174.1.
AJ249778 mRNA. Translation: CAB77667.1.
AK290374 mRNA. Translation: BAF83063.1.
AK304645 mRNA. Translation: BAG65423.1.
AK222910 mRNA. Translation: BAD96630.1.
AL356267 Genomic DNA. Translation: CAH72302.1.
AL356267 Genomic DNA. Translation: CAH72303.1.
AL356267 Genomic DNA. Translation: CAH72304.1.
AL356267 Genomic DNA. Translation: CAH72305.1.
CH471067 Genomic DNA. Translation: EAW91097.1.
CH471067 Genomic DNA. Translation: EAW91098.1.
CH471067 Genomic DNA. Translation: EAW91095.1.
BC012485 mRNA. Translation: AAH12485.1.
AF010446 mRNA. Translation: AAD01442.1.
AF010447 mRNA. Translation: AAD01443.1. Different initiation.
AF031469 mRNA. Translation: AAD01933.1.
AF039526 Genomic DNA. Translation: AAD02172.1.
AH006983 Genomic DNA. Translation: AAC72900.1.
AF223407 Genomic DNA. Translation: AAF40170.1.
CCDSiCCDS1342.1. [Q95460-1]
CCDS53440.1. [Q95460-3]
CCDS53441.1. [Q95460-5]
CCDS53442.1. [Q95460-2]
PIRiA57136.
RefSeqiNP_001181928.1. NM_001194999.1. [Q95460-2]
NP_001181929.1. NM_001195000.1. [Q95460-3]
NP_001181964.1. NM_001195035.1. [Q95460-5]
NP_001522.1. NM_001531.2. [Q95460-1]
UniGeneiHs.13500.

Genome annotation databases

EnsembliENST00000282990; ENSP00000282990; ENSG00000153029. [Q95460-3]
ENST00000367579; ENSP00000356551; ENSG00000153029. [Q95460-2]
ENST00000367580; ENSP00000356552; ENSG00000153029.
ENST00000434571; ENSP00000388504; ENSG00000153029. [Q95460-5]
ENST00000614012; ENSP00000477563; ENSG00000153029.
ENST00000617803; ENSP00000478976; ENSG00000153029. [Q95460-3]
GeneIDi3140.
KEGGihsa:3140.
UCSCiuc001gop.3. human. [Q95460-4]
uc001goq.2. human. [Q95460-1]
uc001gor.2. human. [Q95460-2]
uc001gos.2. human. [Q95460-3]
uc010pns.2. human. [Q95460-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22963 mRNA. Translation: AAC50174.1.
AJ249778 mRNA. Translation: CAB77667.1.
AK290374 mRNA. Translation: BAF83063.1.
AK304645 mRNA. Translation: BAG65423.1.
AK222910 mRNA. Translation: BAD96630.1.
AL356267 Genomic DNA. Translation: CAH72302.1.
AL356267 Genomic DNA. Translation: CAH72303.1.
AL356267 Genomic DNA. Translation: CAH72304.1.
AL356267 Genomic DNA. Translation: CAH72305.1.
CH471067 Genomic DNA. Translation: EAW91097.1.
CH471067 Genomic DNA. Translation: EAW91098.1.
CH471067 Genomic DNA. Translation: EAW91095.1.
BC012485 mRNA. Translation: AAH12485.1.
AF010446 mRNA. Translation: AAD01442.1.
AF010447 mRNA. Translation: AAD01443.1. Different initiation.
AF031469 mRNA. Translation: AAD01933.1.
AF039526 Genomic DNA. Translation: AAD02172.1.
AH006983 Genomic DNA. Translation: AAC72900.1.
AF223407 Genomic DNA. Translation: AAF40170.1.
CCDSiCCDS1342.1. [Q95460-1]
CCDS53440.1. [Q95460-3]
CCDS53441.1. [Q95460-5]
CCDS53442.1. [Q95460-2]
PIRiA57136.
RefSeqiNP_001181928.1. NM_001194999.1. [Q95460-2]
NP_001181929.1. NM_001195000.1. [Q95460-3]
NP_001181964.1. NM_001195035.1. [Q95460-5]
NP_001522.1. NM_001531.2. [Q95460-1]
UniGeneiHs.13500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GUPX-ray3.20A/C23-292[»]
4L4TX-ray2.00A/C23-292[»]
4L4VX-ray1.90A/C23-292[»]
4LCWX-ray2.40A/C23-292[»]
4NQCX-ray2.50A/C23-292[»]
4NQDX-ray2.20A/C23-292[»]
4NQEX-ray2.10A/C23-292[»]
4PJ5X-ray2.00A/C23-292[»]
4PJ7X-ray2.50A/C23-292[»]
4PJ8X-ray3.30A23-292[»]
4PJ9X-ray2.00A23-292[»]
4PJAX-ray2.68A/C23-292[»]
4PJBX-ray2.85A/C23-292[»]
4PJCX-ray2.50A/C23-292[»]
4PJDX-ray2.78A/C23-292[»]
4PJEX-ray1.95A/C23-292[»]
4PJFX-ray2.45A/C23-292[»]
4PJGX-ray2.40A/C23-292[»]
4PJHX-ray2.00A/C23-292[»]
4PJIX-ray2.50A/C23-292[»]
4PJXX-ray2.25A/C23-292[»]
ProteinModelPortaliQ95460.
SMRiQ95460. Positions 23-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109385. 13 interactions.
DIPiDIP-59986N.
IntActiQ95460. 1 interaction.
STRINGi9606.ENSP00000356552.

Chemistry

DrugBankiDB00098. Antithymocyte globulin.

Polymorphism and mutation databases

BioMutaiMR1.
DMDMi74751679.

Proteomic databases

PaxDbiQ95460.
PRIDEiQ95460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282990; ENSP00000282990; ENSG00000153029. [Q95460-3]
ENST00000367579; ENSP00000356551; ENSG00000153029. [Q95460-2]
ENST00000367580; ENSP00000356552; ENSG00000153029.
ENST00000434571; ENSP00000388504; ENSG00000153029. [Q95460-5]
ENST00000614012; ENSP00000477563; ENSG00000153029.
ENST00000617803; ENSP00000478976; ENSG00000153029. [Q95460-3]
GeneIDi3140.
KEGGihsa:3140.
UCSCiuc001gop.3. human. [Q95460-4]
uc001goq.2. human. [Q95460-1]
uc001gor.2. human. [Q95460-2]
uc001gos.2. human. [Q95460-3]
uc010pns.2. human. [Q95460-5]

Organism-specific databases

CTDi3140.
GeneCardsiGC01P181003.
HGNCiHGNC:4975. MR1.
MIMi600764. gene.
neXtProtiNX_Q95460.
PharmGKBiPA29309.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42056.
GeneTreeiENSGT00760000118960.
HOGENOMiHOG000296917.
HOVERGENiHBG016709.
InParanoidiQ95460.
OMAiTWMKNGE.
OrthoDBiEOG7JT6WQ.
PhylomeDBiQ95460.
TreeFamiTF336617.

Miscellaneous databases

ChiTaRSiMR1. human.
GeneWikiiMajor_histocompatibility_complex,_class_I-related.
GenomeRNAii3140.
NextBioi12452.
PROiQ95460.
SOURCEiSearch...

Gene expression databases

BgeeiQ95460.
CleanExiHS_MR1.
GenevisibleiQ95460. HS.

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.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 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

« Hide 'large scale' publications
  1. "A gene outside the human MHC related to classical HLA class I genes."
    Hashimoto K., Hirai M., Kurosawa Y.
    Science 269:693-695(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, TOPOLOGY.
    Tissue: Thymus.
  2. "A study on the polymorphism of human MHC class I-related MR1 gene and identification of an MR1-like pseudogene."
    Parra-Cuadrado J.F., Navarro P., Mirones I., Setien F., Oteo M., Martinez-Naves E.
    Tissue Antigens 56:170-172(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM.
    Tissue: Peripheral blood.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
    Tissue: Tongue and Uterus.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney proximal tubule.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  8. "Genomics, isoforms, expression, and phylogeny of the MHC class I-related MR1 gene."
    Riegert P., Wanner V., Bahram S.
    J. Immunol. 161:4066-4077(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, NUCLEOTIDE SEQUENCE [MRNA] OF 5-341 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 6-229 (ISOFORM 4), TOPOLOGY, ALTERNATIVE SPLICING.
  9. "Expanded genomic organization of conserved mammalian MHC class I-related genes, human MR1 and its murine ortholog."
    Yamaguchi H., Kurosawa Y., Hashimoto K.
    Biochem. Biophys. Res. Commun. 250:558-564(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-341.
    Tissue: Placenta.
  10. "Unrelated expression patterns of MHC class Ia, Ib and TCRA molecules."
    Han M., Robinson M.A.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-109, VARIANT ARG-39.
  11. "Biochemical features of the MHC-related protein 1 consistent with an immunological function."
    Miley M.J., Truscott S.M., Yu Y.Y., Gilfillan S., Fremont D.H., Hansen T.H., Lybarger L.
    J. Immunol. 170:6090-6098(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION AT ASN-107, INTERACTION WITH B2M; TAPBP; CALR AND PDIA3, MUTAGENESIS OF CYS-283.
  12. "Novel MHC class I-related molecule MR1 affects MHC class I expression in 293T cells."
    Aldemir H.
    Biochem. Biophys. Res. Commun. 366:328-334(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH B2M.
  13. "MR1 antigen presentation to mucosal-associated invariant T cells was highly conserved in evolution."
    Huang S., Martin E., Kim S., Yu L., Soudais C., Fremont D.H., Lantz O., Hansen T.H.
    Proc. Natl. Acad. Sci. U.S.A. 106:8290-8295(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLN-169.
  14. "MR1B, a natural spliced isoform of the MHC-related 1 protein, is expressed as homodimers at the cell surface and activates MAIT cells."
    Lion J., Debuysscher V., Wlodarczyk A., Hodroge A., Serriari N.E., Choteau L., Ouled-haddou H., Plistat M., Lassoued K., Lantz O., Treiner E.
    Eur. J. Immunol. 43:1363-1373(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM 3), SUBUNIT (ISOFORM 3).
  15. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-292 IN COMPLEX WITH VITAMIN B9 METABOLITE, LIGAND-BINDING SITES, DISULFIDE BONDS.

Entry informationi

Entry nameiHMR1_HUMAN
AccessioniPrimary (citable) accession number: Q95460
Secondary accession number(s): A8K2V9
, B4E3B1, O97985, O97986, Q53GM1, Q95HB8, Q9MY23, Q9NPL2, Q9TQB3, Q9TQB9, Q9TQK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: February 1, 1997
Last modified: July 22, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

MR1 is detected in an open versus folded conformation. Only the folded MR1 conformer activates MAIT cells.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.