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P26718 (NKG2D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KLRK1
Synonyms:D12S2489E, NKG2D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.12 Ref.14 Ref.18 Ref.19

Subunit structure

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. Ref.9 Ref.10 Ref.15 Ref.16

Subcellular location

Cell membrane; Single-pass type II membrane protein. Note: Colocalized with HCST on the cell surface. Ref.9 Ref.10 Ref.15

Tissue specificity

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). Ref.15 Ref.17 Ref.20

Induction

Up-regulated by interleukin IL15 in primary NK cells. Ref.12

Miscellaneous

Is not capable of signal transduction by itself, but operates through the adapter protein HCST (Ref.9 and Ref.16). 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 (Ref.19).

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Differentiation
Immunity
Innate immunity
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Traceable author statement PubMed 18676862. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

natural killer cell activation

Traceable author statement PubMed 18676862. Source: BHF-UCL

positive regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

positive regulation of natural killer cell mediated cytotoxicity

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

stimulatory C-type lectin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay Ref.9Ref.15. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Traceable author statement Ref.2. Source: ProtInc

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionMHC class Ib receptor activity

Inferred from electronic annotation. Source: Ensembl

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

receptor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MICAQ299832EBI-458344,EBI-1031130

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced.
Isoform 1 (identifier: P26718-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216NKG2-D type II integral membrane protein
PRO_0000046665

Regions

Topological domain1 – 5151Cytoplasmic Potential
Transmembrane52 – 7221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain73 – 216144Extracellular Potential
Domain98 – 213116C-type lectin

Amino acid modifications

Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Disulfide bond96 ↔ 105
Disulfide bond99 ↔ 110
Disulfide bond127 ↔ 211
Disulfide bond189 ↔ 203

Natural variations

Natural variant721A → T in allele NKG2-D*02. Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs2255336 [ dbSNP | Ensembl ].
VAR_013295
Natural variant1771N → S.
Corresponds to variant rs2306182 [ dbSNP | Ensembl ].
VAR_030738

Experimental info

Mutagenesis661R → A: Inhibits association with the HCST signaling dimer. Ref.16
Sequence conflict1861K → R in BAF84709. Ref.5

Secondary structure

............................. 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: C22F6BD533D7800E

FASTA21625,274
        10         20         30         40         50         60 
MGWIRGRRSR HSWEMSEFHN YNLDLKKSDF STRWQKQRCP VVKSKCRENA SPFFFCCFIA 

        70         80         90        100        110        120 
VAMGIRFIIM VAIWSAVFLN SLFNQEVQIP LTESYCGPCP KNWICYKNNC YQFFDESKNW 

       130        140        150        160        170        180 
YESQASCMSQ NASLLKVYSK EDQDLLKLVK SYHWMGLVHI PTNGSWQWED GSILSPNLLT 

       190        200        210 
IIEMQKGDCA LYASSFKGYI ENCSTPNTYI CMQRTV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPT0375.
RefSeqNP_001186734.1. NM_001199805.1.
NP_031386.2. NM_007360.3.
UniGeneHs.387787.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYRX-ray2.70A/B80-216[»]
1KCGX-ray2.60A/B93-216[»]
1MPUX-ray2.50A80-216[»]
ProteinModelPortalP26718.
SMRP26718. Positions 88-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116576. 2 interactions.
DIPDIP-31100N.
IntActP26718. 4 interactions.
MINTMINT-8289618.
STRING9606.ENSP00000240618.

PTM databases

PhosphoSiteP26718.

Polymorphism databases

DMDM128370.

Proteomic databases

PaxDbP26718.
PRIDEP26718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240618; ENSP00000240618; ENSG00000213809.
ENST00000540818; ENSP00000446003; ENSG00000213809.
GeneID100528032.
22914.
KEGGhsa:100528032.
hsa:22914.
UCSCuc001qyc.3. human. [P26718-1]

Organism-specific databases

CTD100528032.
22914.
GeneCardsGC12M010524.
H-InvDBHIX0020427.
HGNCHGNC:18788. KLRK1.
HPACAB021896.
MIM611817. gene.
neXtProtNX_P26718.
PharmGKBPA128394594.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315914.
HOGENOMHOG000220925.
HOVERGENHBG052629.
InParanoidP26718.
KOK06728.
PhylomeDBP26718.
TreeFamTF336674.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP26718.
CleanExHS_KLRK1.
GenevestigatorP26718.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26718.
GeneWikiKLRK1.
NextBio43595.
PROP26718.
SOURCESearch...

Entry information

Entry nameNKG2D_HUMAN
AccessionPrimary (citable) accession number: P26718
Secondary accession number(s): A8K7K5, A8K7P4, Q9NR41
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries