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Protein

Natural killer cell receptor 2B4

Gene

Cd244

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor (PubMed:8326140, PubMed:12734329, PubMed:19648922, PubMed:20962259). Activating function implicates association with SH2D1A and FYN. Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2. Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis (PubMed:8326140, PubMed:15169881, PubMed:15998796, PubMed:22683124). Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (PubMed:15905190). Regulation of NK cell activity by adapters Sh2d1b and Sh2d1b2 is reported conflictingly (PubMed:16127454, PubMed:16425036). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1. At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells (By similarity). Involved in the regulation of CD8+ T-cell proliferation; expression on activated T-cells and binding to CD488 provides costimulatory-like function for neighboring T-cells (PubMed:11739483). Inhibits inflammatory responses in dendritic cells (DCs) (PubMed:25643613).By similarity2 Publications8 Publications

GO - Molecular functioni

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • myeloid dendritic cell activation Source: UniProtKB
  • natural killer cell activation involved in immune response Source: UniProtKB
  • positive regulation of CD8-positive, alpha-beta T cell proliferation Source: UniProtKB
  • positive regulation of granzyme B production Source: MGI
  • positive regulation of inositol phosphate biosynthetic process Source: MGI
  • positive regulation of interferon-gamma secretion Source: MGI
  • positive regulation of interleukin-8 secretion Source: MGI
  • positive regulation of natural killer cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-202733. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
Natural killer cell receptor 2B4
Alternative name(s):
NK cell type I receptor protein 2B4
Short name:
NKR2B4
Non-MHC restricted killing associated
SLAM family member 4
Short name:
SLAMF4
Signaling lymphocytic activation molecule 4
CD_antigen: CD244
Gene namesi
Name:Cd244
Synonyms:2b4, Nmrk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:109294. Cd244.

Subcellular locationi

  • Membrane Curated; Single-pass type I membrane protein Curated
  • Cell membrane Curated

  • Note: Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 226207ExtracellularSequence analysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence analysisAdd
BLAST
Topological domaini248 – 397150CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • external side of plasma membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi266 – 2661Y → F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-325, F-344 and F-369. 1 Publication
Mutagenesisi266 – 2661Y → F: Decreases downstream phosphorylation of CBL and VAV1. 1 Publication
Mutagenesisi325 – 3251Y → F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-344 and F-369. 1 Publication
Mutagenesisi325 – 3251Y → F: Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-344 and F-369. 1 Publication
Mutagenesisi344 – 3441Y → F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-325 and F-369. 1 Publication
Mutagenesisi344 – 3441Y → F: Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-325 and F-369. 1 Publication
Mutagenesisi369 – 3691Y → F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-325 and F-344. 1 Publication
Mutagenesisi369 – 3691Y → F: Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-325 and F-344. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 397378Natural killer cell receptor 2B4PRO_0000014669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 1192 Publications
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi154 ↔ 196By similarity
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence analysis
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence analysis
Modified residuei266 – 2661Phosphotyrosine ProbableBy similarity1 Publication
Modified residuei325 – 3251Phosphotyrosine; by FYN ProbableBy similarity1 Publication
Modified residuei344 – 3441Phosphotyrosine Probable1 Publication
Modified residuei369 – 3691Phosphotyrosine; by FYN Probable1 Publication

Post-translational modificationi

N-linked glycosylation is essential for the binding to its ligand CD48. Also O-glycosylated, in contrast, O-linked sialylation has a negative impact on ligand binding (By similarity).By similarity
Phosphorylated by FYN and CSK at tyrosine residues following activation. Coligation with inhibitory receptors such as KIR2DL1 inhibits phosphorylation upon contact of NK cells with sensitive target cells.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ07763.
MaxQBiQ07763.
PaxDbiQ07763.
PRIDEiQ07763.

PTM databases

iPTMnetiQ07763.
PhosphoSiteiQ07763.

Expressioni

Tissue specificityi

Expressed in natural killer (NK) cells, T cells and dendritic cells.2 Publications

Gene expression databases

BgeeiQ07763.
CleanExiMM_CD244.
ExpressionAtlasiQ07763. baseline and differential.
GenevisibleiQ07763. MM.

Interactioni

Subunit structurei

Interacts with CD48 (PubMed:9841922, PubMed:15905190). Interacts (via phosphorylated ITSM 1-4) with SH2D1A/SAP (via SH2 domain); SH2D1A probably mediates association with FYN. Interacts (via phosphorylated ITSM 3) with PTPN11/SHP-2, INPP5D/SHIP1, PTPN6/SHP-1 and CSK; binding of SH2D1A prevents association with PTPN11, PTPN6 and CSK. Interacts weakly (via phosphorylated ITSM 2) with PTPN11 and CSK. Interacts with SH2D1B and SH2D1B2. Interacts with MHC class I proteins; the interaction is proposed to prevent self-killing of NK cells (By similarity).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201792. 2 interactions.
STRINGi10090.ENSMUSP00000004829.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 317Combined sources
Beta strandi37 – 393Combined sources
Beta strandi50 – 567Combined sources
Beta strandi60 – 623Combined sources
Beta strandi63 – 7311Combined sources
Beta strandi76 – 783Combined sources
Helixi79 – 835Combined sources
Beta strandi85 – 873Combined sources
Turni89 – 913Combined sources
Beta strandi94 – 985Combined sources
Helixi101 – 1033Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi117 – 12711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2KNMR-A21-129[»]
2PTTX-ray1.63B19-129[»]
2PTUX-ray2.38A/B/C/D19-129[»]
ProteinModelPortaliQ07763.
SMRiQ07763. Positions 21-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 129108Ig-like 1Add
BLAST
Domaini131 – 21585Ig-like 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi264 – 2696ITSM 1By similarity
Motifi323 – 3286ITSM 2By similarity
Motifi342 – 3476ITSM 3By similarity
Motifi367 – 3726ITSM 4By similarity

Domaini

The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3).By similarity1 Publication

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKYZ. Eukaryota.
ENOG410Y74Q. LUCA.
GeneTreeiENSGT00510000049238.
HOVERGENiHBG050850.
InParanoidiQ07763.
KOiK06582.
OMAiTIYEDVK.
OrthoDBiEOG7QVM45.
TreeFamiTF334964.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR024304. NK_rcpt_2B4.
IPR024303. NK_rcpt_2B4_Ig_dom.
[Graphical view]
PANTHERiPTHR12080:SF56. PTHR12080:SF56. 1 hit.
PfamiPF11465. Receptor_2B4. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q07763-1) [UniParc]FASTAAdd to basket

Also known as: m2B4L

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
MLGQAVLFTT FLLLRAHQGQ DCPDSSEEVV GVSGKPVQLR PSNIQTKDVS
60 70 80 90 100
VQWKKTEQGS HRKIEILNWY NDGPSWSNVS FSDIYGFDYG DFALSIKSAK
110 120 130 140 150
LQDSGHYLLE ITNTGGKVCN KNFQLLILDH VETPNLKAQW KPWTNGTCQL
160 170 180 190 200
FLSCLVTKDD NVSYALYRGS TLISNQRNST HWENQIDASS LHTYTCNVSN
210 220 230 240 250
RASWANHTLN FTHGCQSVPS NFRFLPFGVI IVILVTLFLG AIICFCVWTK
260 270 280 290 300
KRKQLQFSPK EPLTIYEYVK DSRASRDQQG CSRASGSPSA VQEDGRGQRE
310 320 330 340 350
LDRRVSEVLE QLPQQTFPGD RGTMYSMIQC KPSDSTSQEK CTVYSVVQPS
360 370 380 390
RKSGSKKRNQ NSSLSCTVYE EVGNPWLKAH NPARLSRREL ENFDVYS
Length:397
Mass (Da):44,836
Last modified:July 27, 2011 - v3
Checksum:i0E2F0D946F7B63A7
GO
Isoform 2 (identifier: Q07763-2) [UniParc]FASTAAdd to basket

Also known as: m2B4S

The sequence of this isoform differs from the canonical sequence as follows:
     309-340: LEQLPQQTFPGDRGTMYSMIQCKPSDSTSQEK → MFSSLLAFLLHQFPGSTQRGKEKRERAEKNGK
     341-397: Missing.

Note: No experimental confirmation available.
Show »
Length:340
Mass (Da):38,397
Checksum:i0D5275A1A354FC1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381Q → P in AAF91290 (PubMed:10941850).Curated
Sequence conflicti156 – 1561V → A in AAF91290 (PubMed:10941850).Curated
Sequence conflicti166 – 1661L → FW in AAA16353 (PubMed:8228228).Curated
Sequence conflicti362 – 3621S → Y in AAA16353 (PubMed:8228228).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei309 – 34032LEQLP…TSQEK → MFSSLLAFLLHQFPGSTQRG KEKRERAEKNGK in isoform 2. 1 PublicationVSP_010401Add
BLAST
Alternative sequencei341 – 39757Missing in isoform 2. 1 PublicationVSP_010402Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19057 mRNA. Translation: AAA16353.1.
AF234831 mRNA. Translation: AAF91290.1.
AF082803 mRNA. Translation: AAC34859.1.
AK137505 mRNA. Translation: BAE23386.1.
CCDSiCCDS35778.1. [Q07763-1]
PIRiI49443.
RefSeqiNP_061199.2. NM_018729.2. [Q07763-1]
UniGeneiMm.2299.

Genome annotation databases

EnsembliENSMUST00000004829; ENSMUSP00000004829; ENSMUSG00000004709. [Q07763-1]
GeneIDi18106.
KEGGimmu:18106.
UCSCiuc007dor.1. mouse. [Q07763-2]
uc007dos.1. mouse. [Q07763-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19057 mRNA. Translation: AAA16353.1.
AF234831 mRNA. Translation: AAF91290.1.
AF082803 mRNA. Translation: AAC34859.1.
AK137505 mRNA. Translation: BAE23386.1.
CCDSiCCDS35778.1. [Q07763-1]
PIRiI49443.
RefSeqiNP_061199.2. NM_018729.2. [Q07763-1]
UniGeneiMm.2299.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2KNMR-A21-129[»]
2PTTX-ray1.63B19-129[»]
2PTUX-ray2.38A/B/C/D19-129[»]
ProteinModelPortaliQ07763.
SMRiQ07763. Positions 21-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201792. 2 interactions.
STRINGi10090.ENSMUSP00000004829.

PTM databases

iPTMnetiQ07763.
PhosphoSiteiQ07763.

Proteomic databases

EPDiQ07763.
MaxQBiQ07763.
PaxDbiQ07763.
PRIDEiQ07763.

Protocols and materials databases

DNASUi18106.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004829; ENSMUSP00000004829; ENSMUSG00000004709. [Q07763-1]
GeneIDi18106.
KEGGimmu:18106.
UCSCiuc007dor.1. mouse. [Q07763-2]
uc007dos.1. mouse. [Q07763-1]

Organism-specific databases

CTDi51744.
MGIiMGI:109294. Cd244.

Phylogenomic databases

eggNOGiENOG410IKYZ. Eukaryota.
ENOG410Y74Q. LUCA.
GeneTreeiENSGT00510000049238.
HOVERGENiHBG050850.
InParanoidiQ07763.
KOiK06582.
OMAiTIYEDVK.
OrthoDBiEOG7QVM45.
TreeFamiTF334964.

Enzyme and pathway databases

ReactomeiR-MMU-202733. Cell surface interactions at the vascular wall.

Miscellaneous databases

EvolutionaryTraceiQ07763.
PROiQ07763.
SOURCEiSearch...

Gene expression databases

BgeeiQ07763.
CleanExiMM_CD244.
ExpressionAtlasiQ07763. baseline and differential.
GenevisibleiQ07763. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR024304. NK_rcpt_2B4.
IPR024303. NK_rcpt_2B4_Ig_dom.
[Graphical view]
PANTHERiPTHR12080:SF56. PTHR12080:SF56. 1 hit.
PfamiPF11465. Receptor_2B4. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the 2B4 gene encoding a molecule associated with non-MHC-restricted killing mediated by activated natural killer cells and T cells."
    Mathew P.A., Garni-Wagner B.A., Land K., Takashima A., Stoneman E., Bennett M., Kumar V.
    J. Immunol. 151:5328-5337(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. "Polymorphism in the 2B4 gene of inbred mouse strains."
    Kumaresan P.R., Huynh V.T., Mathew P.A.
    Immunogenetics 51:758-761(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: A.CA.
  3. "Characterization of genomic structure and alternative splicing of the murine NK cell receptor 2B4."
    Stepp S.E., Schatzle J.D., Bennett M., Kumar V., Mathew P.A.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone.
  5. "A novel function-associated molecule related to non-MHC-restricted cytotoxicity mediated by activated natural killer cells and T cells."
    Garni-Wagner B.A., Purohit A., Mathew P.A., Bennett M., Kumar V.
    J. Immunol. 151:60-70(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "2B4, the natural killer and T cell immunoglobulin superfamily surface protein, is a ligand for CD48."
    Brown M.H., Boles K., van der Merwe P.A., Kumar V., Mathew P.A., Barclay A.N.
    J. Exp. Med. 188:2083-2090(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD48.
  7. "Regulation of CD8(+) T cell proliferation by 2B4/CD48 interactions."
    Kambayashi T., Assarsson E., Chambers B.J., Ljunggren H.G.
    J. Immunol. 167:6706-6710(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The NK cell receptor 2B4 augments antigen-specific T cell cytotoxicity through CD48 ligation on neighboring T cells."
    Lee K.M., Bhawan S., Majima T., Wei H., Nishimura M.I., Yagita H., Kumar V.
    J. Immunol. 170:4881-4885(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Molecular dissection of 2B4 signaling: implications for signal transduction by SLAM-related receptors."
    Chen R., Relouzat F., Roncagalli R., Aoukaty A., Tan R., Latour S., Veillette A.
    Mol. Cell. Biol. 24:5144-5156(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN ITSM MOTIF, PHOSPHORYLATION AT TYR-266; TYR-325; TYR-344 AND TYR-369, MUTAGENESIS OF TYR-266; TYR-325; TYR-344 AND TYR-369.
  10. "Regulation of natural cytotoxicity by the adaptor SAP and the Src-related kinase Fyn."
    Bloch-Queyrat C., Fondaneche M.C., Chen R., Yin L., Relouzat F., Veillette A., Fischer A., Latour S.
    J. Exp. Med. 202:181-192(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Negative regulation of natural killer cell function by EAT-2, a SAP-related adaptor."
    Roncagalli R., Taylor J.E., Zhang S., Shi X., Chen R., Cruz-Munoz M.E., Yin L., Latour S., Veillette A.
    Nat. Immunol. 6:1002-1010(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SH2D1A; SH2D1B AND SH2D1B2.
  12. "Requirement of homotypic NK-cell interactions through 2B4(CD244)/CD48 in the generation of NK effector functions."
    Lee K.M., Forman J.P., McNerney M.E., Stepp S., Kuppireddi S., Guzior D., Latchman Y.E., Sayegh M.H., Yagita H., Park C.K., Oh S.B., Wuelfing C., Schatzle J., Mathew P.A., Sharpe A.H., Kumar V.
    Blood 107:3181-3188(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CD48.
  13. "Identification and characterization of two related murine genes, Eat2a and Eat2b, encoding single SH2-domain adapters."
    Calpe S., Erdos E., Liao G., Wang N., Rietdijk S., Simarro M., Scholtz B., Mooney J., Lee C.H., Shin M.S., Rajnavoelgyi E., Schatzle J., Morse H.C. III, Terhorst C., Lanyi A.
    Immunogenetics 58:15-25(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 129/SvJ and C57BL/6.
  14. "Essential function for SAP family adaptors in the surveillance of hematopoietic cells by natural killer cells."
    Dong Z., Cruz-Munoz M.E., Zhong M.C., Chen R., Latour S., Veillette A.
    Nat. Immunol. 10:973-980(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The adapters EAT-2A and -2B are positive regulators of CD244- and CD84-dependent NK cell functions in the C57BL/6 mouse."
    Wang N., Calpe S., Westcott J., Castro W., Ma C., Engel P., Schatzle J.D., Terhorst C.
    J. Immunol. 185:5683-5687(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The adaptor SAP controls NK cell activation by regulating the enzymes Vav-1 and SHIP-1 and by enhancing conjugates with target cells."
    Dong Z., Davidson D., Perez-Quintero L.A., Kurosaki T., Swat W., Veillette A.
    Immunity 36:974-985(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. Cited for: TISSUE SPECIFICITY, FUNCTION.
  18. "NMR structure of the natural killer cell receptor 2B4 (CD244): implications for ligand recognition."
    Ames J.B., Vyas V., Lusin J.D., Mariuzza R.
    Biochemistry 44:6416-6423(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 21-129, DISULFIDE BOND.
  19. "Structure of natural killer receptor 2B4 bound to CD48 reveals basis for heterophilic recognition in signaling lymphocyte activation molecule family."
    Velikovsky C.A., Deng L., Chlewicki L.K., Fernandez M.M., Kumar V., Mariuzza R.A.
    Immunity 27:572-584(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 19-129 ALONE AND IN COMPLEX WITH CD48, DISULFIDE BOND.

Entry informationi

Entry nameiCD244_MOUSE
AccessioniPrimary (citable) accession number: Q07763
Secondary accession number(s): O88654, Q3UV86, Q9JIE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.