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P26718

- NKG2D_HUMAN

UniProt

P26718 - NKG2D_HUMAN

Protein

NKG2-D type II integral membrane protein

Gene

KLRK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    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. carbohydrate binding Source: InterPro
    2. MHC class Ib receptor activity Source: Ensembl
    3. protein binding Source: UniProtKB
    4. receptor activity Source: ProtInc

    GO - Biological processi

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

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

    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

    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 proteinPRO_0000046665Add
    BLAST

    Amino acid modifications

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

    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.6 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

    1
    216
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26718.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5151CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini73 – 216144ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei52 – 7221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini98 – 213116C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861K → R in BAF84709. (PubMed:14702039)Curated

    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 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

    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: October 1, 2014
    This is version 141 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 (PubMed:10426994 and PubMed:15894612). 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 (PubMed:23298206).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