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P26718

- NKG2D_HUMAN

UniProt

P26718 - NKG2D_HUMAN

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Protein
NKG2-D type II integral membrane protein
Gene
KLRK1, D12S2489E, NKG2D
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Function as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8+ T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4.6 Publications

GO - Molecular functioni

  1. MHC class Ib receptor activity Source: Ensembl
  2. carbohydrate binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. receptor activity Source: ProtInc

GO - Biological processi

  1. T cell costimulation Source: BHF-UCL
  2. cell differentiation Source: UniProtKB-KW
  3. cellular response to lipopolysaccharide Source: Ensembl
  4. defense response to Gram-positive bacterium Source: Ensembl
  5. innate immune response Source: Reactome
  6. natural killer cell activation Source: BHF-UCL
  7. positive regulation of interferon-gamma production Source: Ensembl
  8. positive regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
  9. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  10. regulation of immune response Source: Reactome
  11. signal transduction Source: ProtInc
  12. stimulatory C-type lectin receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Differentiation, Immunity, Innate immunity

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_147694. DAP12 interactions.
REACT_147814. DAP12 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
NKG2-D type II integral membrane protein
Alternative name(s):
Killer cell lectin-like receptor subfamily K member 1
NK cell receptor D
NKG2-D-activating NK receptor
CD_antigen: CD314
Gene namesi
Name:KLRK1
Synonyms:D12S2489E, NKG2D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18788. KLRK1.

Subcellular locationi

Cell membrane; Single-pass type II membrane protein
Note: Colocalized with HCST on the cell surface.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5151Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei52 – 7221Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini73 – 216144Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. external side of plasma membrane Source: Ensembl
  3. integral component of membrane Source: ProtInc
  4. integral component of plasma membrane Source: ProtInc
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661R → A: Inhibits association with the HCST signaling dimer. 1 Publication

Organism-specific databases

PharmGKBiPA128394594.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216NKG2-D type II integral membrane protein
PRO_0000046665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi96 ↔ 105
Disulfide bondi99 ↔ 110
Disulfide bondi127 ↔ 211
Glycosylationi131 – 1311N-linked (GlcNAc...) Reviewed prediction
Glycosylationi163 – 1631N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi189 ↔ 203
Glycosylationi202 – 2021N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP26718.
PRIDEiP26718.

PTM databases

PhosphoSiteiP26718.

Expressioni

Tissue specificityi

Expressed in natural killer (NK) cells, CD8+ alpha-beta and gamma-delta T-cells. Expressed on essentially all CD56+CD3- NK cells from freshly isolated PBMC. Expressed in interferon-producing killer dendritic cells (IKDCs).3 Publications

Inductioni

Up-regulated by interleukin IL15 in primary NK cells.1 Publication

Gene expression databases

BgeeiP26718.
CleanExiHS_KLRK1.
GenevestigatoriP26718.

Organism-specific databases

HPAiCAB021896.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Heterohexamer composed of two subunits of KLRK1 and four subunits of HCST/DAP10. Interacts (via transmembrane domain) with HCST/DAP10 (via transmembrane domain); the interaction is required for KLRK1 NK cell surface and induces NK cell-mediated cytotoxicity. Does not interact with TYROBP.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MICAQ299832EBI-458344,EBI-1031130

Protein-protein interaction databases

BioGridi116576. 2 interactions.
DIPiDIP-31100N.
IntActiP26718. 4 interactions.
MINTiMINT-8289618.
STRINGi9606.ENSP00000240618.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi94 – 963
Beta strandi103 – 1064
Beta strandi109 – 11810
Helixi120 – 1289
Turni129 – 1313
Beta strandi133 – 1353
Turni140 – 1434
Helixi144 – 1485
Beta strandi153 – 1597
Turni161 – 1633
Beta strandi166 – 1683
Beta strandi176 – 1783
Beta strandi180 – 1823
Beta strandi185 – 1939
Turni194 – 1963
Beta strandi197 – 2015
Beta strandi207 – 2137

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYRX-ray2.70A/B80-216[»]
1KCGX-ray2.60A/B93-216[»]
1MPUX-ray2.50A80-216[»]
4PDCX-ray1.99A/B/C/D93-215[»]
ProteinModelPortaliP26718.
SMRiP26718. Positions 88-215.

Miscellaneous databases

EvolutionaryTraceiP26718.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 213116C-type lectin
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG315914.
HOGENOMiHOG000220925.
HOVERGENiHBG052629.
InParanoidiP26718.
KOiK06728.
PhylomeDBiP26718.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced.

Isoform 1 (identifier: P26718-1) [UniParc]FASTAAdd to Basket

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

MGWIRGRRSR HSWEMSEFHN YNLDLKKSDF STRWQKQRCP VVKSKCRENA    50
SPFFFCCFIA VAMGIRFIIM VAIWSAVFLN SLFNQEVQIP LTESYCGPCP 100
KNWICYKNNC YQFFDESKNW YESQASCMSQ NASLLKVYSK EDQDLLKLVK 150
SYHWMGLVHI PTNGSWQWED GSILSPNLLT IIEMQKGDCA LYASSFKGYI 200
ENCSTPNTYI CMQRTV 216
Length:216
Mass (Da):25,274
Last modified:August 1, 1992 - v1
Checksum:iC22F6BD533D7800E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721A → T in allele NKG2-D*02. 4 Publications
Corresponds to variant rs2255336 [ dbSNP | Ensembl ].
VAR_013295
Natural varianti177 – 1771N → S.
Corresponds to variant rs2306182 [ dbSNP | Ensembl ].
VAR_030738

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861K → R in BAF84709. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54870 mRNA. Translation: CAA38652.1.
AJ001687, AJ001688, AJ001689 Genomic DNA. Translation: CAA04925.1.
AF461811 mRNA. Translation: AAL65233.1.
AF260135 mRNA. Translation: AAF86973.1.
AF260136 mRNA. Translation: AAF86974.1.
AK292059 mRNA. Translation: BAF84748.1.
AK292020 mRNA. Translation: BAF84709.1.
AC022075 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96178.1.
BC039836 mRNA. Translation: AAH39836.1.
CCDSiCCDS8623.1. [P26718-1]
PIRiPT0375.
RefSeqiNP_001186734.1. NM_001199805.1.
NP_031386.2. NM_007360.3.
UniGeneiHs.387787.

Genome annotation databases

EnsembliENST00000240618; ENSP00000240618; ENSG00000213809.
ENST00000540818; ENSP00000446003; ENSG00000213809.
GeneIDi100528032.
22914.
KEGGihsa:100528032.
hsa:22914.
UCSCiuc001qyc.3. human. [P26718-1]

Polymorphism databases

DMDMi128370.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Functional Glycomics Gateway - Glycan Binding

NKG-2D

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54870 mRNA. Translation: CAA38652.1 .
AJ001687 , AJ001688 , AJ001689 Genomic DNA. Translation: CAA04925.1 .
AF461811 mRNA. Translation: AAL65233.1 .
AF260135 mRNA. Translation: AAF86973.1 .
AF260136 mRNA. Translation: AAF86974.1 .
AK292059 mRNA. Translation: BAF84748.1 .
AK292020 mRNA. Translation: BAF84709.1 .
AC022075 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96178.1 .
BC039836 mRNA. Translation: AAH39836.1 .
CCDSi CCDS8623.1. [P26718-1 ]
PIRi PT0375.
RefSeqi NP_001186734.1. NM_001199805.1.
NP_031386.2. NM_007360.3.
UniGenei Hs.387787.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HYR X-ray 2.70 A/B 80-216 [» ]
1KCG X-ray 2.60 A/B 93-216 [» ]
1MPU X-ray 2.50 A 80-216 [» ]
4PDC X-ray 1.99 A/B/C/D 93-215 [» ]
ProteinModelPortali P26718.
SMRi P26718. Positions 88-215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116576. 2 interactions.
DIPi DIP-31100N.
IntActi P26718. 4 interactions.
MINTi MINT-8289618.
STRINGi 9606.ENSP00000240618.

PTM databases

PhosphoSitei P26718.

Polymorphism databases

DMDMi 128370.

Proteomic databases

PaxDbi P26718.
PRIDEi P26718.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000240618 ; ENSP00000240618 ; ENSG00000213809 .
ENST00000540818 ; ENSP00000446003 ; ENSG00000213809 .
GeneIDi 100528032.
22914.
KEGGi hsa:100528032.
hsa:22914.
UCSCi uc001qyc.3. human. [P26718-1 ]

Organism-specific databases

CTDi 100528032.
22914.
GeneCardsi GC12M010524.
H-InvDB HIX0020427.
HGNCi HGNC:18788. KLRK1.
HPAi CAB021896.
MIMi 611817. gene.
neXtProti NX_P26718.
PharmGKBi PA128394594.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315914.
HOGENOMi HOG000220925.
HOVERGENi HBG052629.
InParanoidi P26718.
KOi K06728.
PhylomeDBi P26718.
TreeFami TF336674.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_147694. DAP12 interactions.
REACT_147814. DAP12 signaling.

Miscellaneous databases

EvolutionaryTracei P26718.
GeneWikii KLRK1.
NextBioi 43595.
PROi P26718.
SOURCEi Search...

Gene expression databases

Bgeei P26718.
CleanExi HS_KLRK1.
Genevestigatori P26718.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells."
    Houchins J.P., Yabe T., McSherry C., Bach F.H.
    J. Exp. Med. 173:1017-1020(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The genomic organization of NKG2C, E, F, and D receptor genes in the human natural killer gene complex."
    Glienke J., Sobanov Y., Brostjan C., Steffens C., Nguyen C., Lehrach H., Hofer E., Francis F.
    Immunogenetics 48:163-173(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification and characterization of the NKG2D gene from large granular lymphocytic leukemia (LGL) cells."
    Kothapalli R., Kusmartseva I., Loughran T.P. Jr.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Conservation and variation in human and common chimpanzee CD94 and NKG2 genes."
    Shum B.P., Flodin L.R., Muir D.G., Rajalingam R., Khakoo S.I., Cleland S., Guethlein L.A., Uhrberg M., Parham P.
    J. Immunol. 168:240-252(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-72.
  5. "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], VARIANT THR-72.
    Tissue: Spleen and Stomach.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-72.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-72.
  8. "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 1).
    Tissue: Testis.
  9. "An activating immunoreceptor complex formed by NKG2D and DAP10."
    Wu J., Song Y., Bakker A.B.H., Bauer S., Spies T., Lanier L.L., Phillips J.H.
    Science 285:730-732(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOTOXICITY ACTIVATION, INTERACTION WITH HCST, SUBCELLULAR LOCATION.
  10. "DAP10 and DAP12 form distinct, but functionally cooperative, receptor complexes in natural killer cells."
    Wu J., Cherwinski H., Spies T., Phillips J.H., Lanier L.L.
    J. Exp. Med. 192:1059-1068(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCST, SUBCELLULAR LOCATION.
  11. "Costimulation of CD8alphabeta T cells by NKG2D via engagement by MIC induced on virus-infected cells."
    Groh V., Rhinehart R., Randolph-Habecker J., Topp M.S., Riddell S.R., Spies T.
    Nat. Immunol. 2:255-260(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOTOXICITY ACTIVATION AND VIRAL INFECTION, FUNCTION AS A RECEPTOR FOR MICA.
  12. "UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells."
    Sutherland C.L., Chalupny N.J., Schooley K., VandenBos T., Kubin M., Cosman D.
    J. Immunol. 168:671-679(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RECEPTOR FOR MICA; MICB; ULBP1; ULBP2, ULBP3, INDUCTION.
  13. "Lymphocyte activation via NKG2D: towards a new paradigm in immune recognition?"
    Vivier E., Tomasello E., Paul P.
    Curr. Opin. Immunol. 14:306-311(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, ALTERNATIVE SPLICING.
  14. "Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D."
    Bacon L., Eagle R.A., Meyer M., Easom N., Young N.T., Trowsdale J.
    J. Immunol. 173:1078-1084(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOTOXICITY ACTIVATION, FUNCTION AS A RECEPTOR FOR RAET1E; RAET1G AND ULBP2.
  15. "A Structural basis for the association of DAP12 with mouse, but not human, NKG2D."
    Rosen D.B., Araki M., Hamerman J.A., Chen T., Yamamura T., Lanier L.L.
    J. Immunol. 173:2470-2478(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCST, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  16. "The activating NKG2D receptor assembles in the membrane with two signaling dimers into a hexameric structure."
    Garrity D., Call M.E., Feng J., Wucherpfennig K.W.
    Proc. Natl. Acad. Sci. U.S.A. 102:7641-7646(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF ARG-66.
  17. "Interferon-producing killer dendritic cells provide a link between innate and adaptive immunity."
    Chan C.W., Crafton E., Fan H.-N., Flook J., Yoshimura K., Skarica M., Brockstedt D., Dubensky T.W., Stins M.F., Lanier L.L., Pardoll D.M., Housseau F.
    Nat. Med. 12:207-213(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  18. "Regulation of immune cell function and differentiation by the NKG2D receptor."
    Zafirova B., Wensveen F.M., Gulin M., Polic B.
    Cell. Mol. Life Sci. 68:3519-3529(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
  19. "Regulation of ligands for the NKG2D activating receptor."
    Raulet D.H., Gasser S., Gowen B.G., Deng W., Jung H.
    Annu. Rev. Immunol. 31:413-441(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION AS A RECEPTOR FOR MHC CLASS I-RELATED GLYCOPROTEINS.
  20. "Activation of NK cells and T cells by NKG2D, a receptor for stress-inducible MICA."
    Bauer S., Groh V., Wu J., Steinle A., Phillips J.H., Lanier L.L., Spies T.
    Science 285:727-729(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 89-216 IN COMPLEX WITH MICA, TISSUE SPECIFICITY.
  21. "Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3."
    Radaev S., Rostro B., Brooks A.G., Colonna M., Sun P.D.
    Immunity 15:1039-1049(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 93-216 IN COMPLEX WITH ULBP3.
  22. "Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands."
    McFarland B.J., Kortemme T., Yu S.F., Baker D., Strong R.K.
    Structure 11:411-422(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-215.

Entry informationi

Entry nameiNKG2D_HUMAN
AccessioniPrimary (citable) accession number: P26718
Secondary accession number(s): A8K7K5, A8K7P4, Q9NR41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 140 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

Is not capable of signal transduction by itself, but operates through the adapter protein HCST (1 Publication and 1 Publication). Some families of ligands for human and mouse KLRK1 receptors have been characterized being very similar in structure and highly likely to be orthologs. In humans, an additional distinct subfamily of ligands (MICA and MICB) differs structurally, having an extra MHC alpha 3-like domain (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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