Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O43561

- LAT_HUMAN

UniProt

O43561 - LAT_HUMAN

Protein

Linker for activation of T-cells family member 1

Gene

LAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase binding Source: UniProtKB
    3. SH3/SH2 adaptor activity Source: HGNC

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. calcium-mediated signaling Source: HGNC
    3. Fc-epsilon receptor signaling pathway Source: Reactome
    4. immune response Source: HGNC
    5. innate immune response Source: Reactome
    6. integrin-mediated signaling pathway Source: HGNC
    7. intracellular signal transduction Source: HGNC
    8. mast cell degranulation Source: UniProtKB-KW
    9. platelet activation Source: Reactome
    10. positive regulation of signal transduction Source: GOC
    11. Ras protein signal transduction Source: HGNC
    12. regulation of T cell activation Source: HGNC
    13. T cell activation Source: UniProtKB
    14. T cell receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Adaptive immunity, Immunity, Mast cell degranulation

    Enzyme and pathway databases

    ReactomeiREACT_12623. Generation of second messenger molecules.
    REACT_147814. DAP12 signaling.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_163936. Fc epsilon receptor (FCERI) signaling.
    REACT_1695. GPVI-mediated activation cascade.
    SignaLinkiO43561.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Linker for activation of T-cells family member 1
    Alternative name(s):
    36 kDa phospho-tyrosine adapter protein
    Short name:
    pp36
    p36-38
    Gene namesi
    Name:LAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:18874. LAT.

    Subcellular locationi

    Cell membrane 2 Publications; Single-pass type III membrane protein 2 Publications
    Note: Present in lipid rafts.

    GO - Cellular componenti

    1. COP9 signalosome Source: UniProtKB
    2. immunological synapse Source: HGNC
    3. integral component of membrane Source: HGNC
    4. mast cell granule Source: GOC
    5. membrane raft Source: HGNC
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261C → A: Reduces palmitoylation; abolishes localization to lipid rafts. 1 Publication
    Mutagenesisi29 – 291C → A: Reduces palmitoylation; impairs localization to lipid rafts. 1 Publication
    Mutagenesisi161 – 1611Y → F: Abolishes interaction with PLCG1. 1 Publication
    Mutagenesisi200 – 2001Y → F: Abolishes interaction with GRB2 and PIK3R1; when associated with F-220. 1 Publication
    Mutagenesisi220 – 2201Y → F: Abolishes interaction with GRB2 and PIK3R1; when associated with F-200. 1 Publication

    Organism-specific databases

    PharmGKBiPA38728.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 262262Linker for activation of T-cells family member 1PRO_0000083325Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi26 – 261S-palmitoyl cysteine1 Publication
    Lipidationi29 – 291S-palmitoyl cysteine1 Publication
    Modified residuei39 – 391Phosphothreonine1 Publication
    Modified residuei40 – 401Phosphoserine1 Publication
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei43 – 431Phosphoserine1 Publication
    Modified residuei84 – 841Phosphoserine1 Publication
    Modified residuei101 – 1011Phosphoserine2 Publications
    Modified residuei106 – 1061Phosphoserine1 Publication
    Modified residuei110 – 1101PhosphotyrosineCurated
    Modified residuei156 – 1561PhosphotyrosineCurated
    Modified residuei161 – 1611PhosphotyrosineCurated
    Modified residuei200 – 2001Phosphotyrosine1 Publication
    Modified residuei220 – 2201PhosphotyrosineCurated
    Modified residuei224 – 2241Phosphoserine1 Publication
    Modified residuei240 – 2401Phosphoserine1 Publication
    Modified residuei241 – 2411Phosphoserine1 Publication
    Modified residuei255 – 2551Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated by ITK leading to the recruitment of VAV1 to LAT-containing complexes.
    Palmitoylation of Cys-26 and Cys-29 is required for raft targeting and efficient phosphorylation.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiO43561.
    PaxDbiO43561.
    PRIDEiO43561.

    PTM databases

    PhosphoSiteiO43561.

    Expressioni

    Tissue specificityi

    Expressed in thymus, T-cells, NK cells, mast cells and, at lower levels, in spleen. Present in T-cells but not B-cells (at protein level).2 Publications

    Gene expression databases

    BgeeiO43561.
    CleanExiHS_LAT.
    GenevestigatoriO43561.

    Organism-specific databases

    HPAiCAB002223.
    CAB012978.
    HPA011157.

    Interactioni

    Subunit structurei

    When phosphorylated, interacts directly with the PIK3R1 subunit of phosphoinositide 3-kinase and the SH2 domains of GRB2, GRAP, GRAP2, PLCG1 and PLCG2. Interacts indirectly with CBL, SOS, VAV, and LCP2. Interacts with SHB, SKAP2 and CLNK By similarity. Interacts with FCGR1A. Interacts with GRB2, PLCG1 and THEMIS upon TCR activation in thymocytes By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRB2P6299312EBI-1222766,EBI-401755
    LCKP062392EBI-1222766,EBI-1348
    PIK3R1P279864EBI-1222766,EBI-79464
    PLCG1P084874EBI-8070286,EBI-8013886From a different organism.
    PLCG1P191746EBI-1222766,EBI-79387
    PTPN1P180313EBI-1222766,EBI-968788

    Protein-protein interaction databases

    BioGridi117971. 31 interactions.
    DIPiDIP-29231N.
    IntActiO43561. 15 interactions.
    MINTiMINT-2836977.
    STRINGi9606.ENSP00000354119.

    Structurei

    3D structure databases

    ProteinModelPortaliO43561.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44ExtracellularSequence Analysis
    Topological domaini28 – 262235CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni161 – 1644Interaction with PLCG1
    Regioni200 – 2034Interaction with GRB2, GRAP2 and PIK3R1
    Regioni220 – 2234Interaction with GRB2, GRAP2 and PIK3R1

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41822.
    HOGENOMiHOG000081810.
    HOVERGENiHBG018198.
    KOiK07362.
    OMAiGSHRMPS.
    PhylomeDBiO43561.

    Family and domain databases

    InterProiIPR008359. Linker_for_activat_Tcells_prot.
    [Graphical view]
    PANTHERiPTHR15586. PTHR15586. 1 hit.
    PfamiPF15234. LAT. 1 hit.
    [Graphical view]
    PRINTSiPR01781. LATPROTEIN.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43561-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MEEAILVPCV LGLLLLPILA MLMALCVHCH RLPGSYDSTS SDSLYPRGIQ    50
    FKRPHTVAPW PPAYPPVTSY PPLSQPDLLP IPRSPQPLGG SHRTPSSRRD 100
    SDGANSVASY ENEGASGIRG AQAGWGVWGP SWTRLTPVSL PPEPACEDAD 150
    EDEDDYHNPG YLVVLPDSTP ATSTAAPSAP ALSTPGIRDS AFSMESIDDY 200
    VNVPESGESA EASLDGSREY VNVSQELHPG AAKTEPAALS SQEAEEVEEE 250
    GAPDYENLQE LN 262
    Length:262
    Mass (Da):27,930
    Last modified:June 1, 1998 - v1
    Checksum:iBCD80AE7DCA64153
    GO
    Isoform 2 (identifier: O43561-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         114-142: Missing.

    Show »
    Length:233
    Mass (Da):24,985
    Checksum:i0832E2D2B4220BC6
    GO
    Isoform 3 (identifier: O43561-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEATAASWQVAVPVLGGASRPLGPRGAASLLRAPLQM
         114-142: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:269
    Mass (Da):28,568
    Checksum:i00A1E5FD10A258FE
    GO
    Isoform 4 (identifier: O43561-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         83-83: Missing.
         114-142: Missing.

    Show »
    Length:232
    Mass (Da):24,829
    Checksum:iAFA91E716FEBE1CE
    GO
    Isoform 5 (identifier: O43561-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         83-83: Missing.

    Show »
    Length:261
    Mass (Da):27,774
    Checksum:i0108E1F423BFE30E
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEATAASWQVAVPVLGGASR PLGPRGAASLLRAPLQM in isoform 3. CuratedVSP_054758
    Alternative sequencei83 – 831Missing in isoform 4 and isoform 5. 1 PublicationVSP_054759
    Alternative sequencei114 – 14229Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_004303Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036906 mRNA. Translation: AAC39637.1.
    AF036905 mRNA. Translation: AAC39636.1.
    AJ223280 mRNA. Translation: CAA11218.1.
    FN432832 mRNA. Translation: CBA11533.1.
    AC109460 Genomic DNA. No translation available.
    CH471267 Genomic DNA. Translation: EAW52027.1.
    CH471267 Genomic DNA. Translation: EAW52028.1.
    BC011563 mRNA. Translation: AAH11563.1.
    CCDSiCCDS10647.1. [O43561-1]
    CCDS32425.1. [O43561-2]
    CCDS45455.1. [O43561-4]
    CCDS53999.1. [O43561-3]
    RefSeqiNP_001014987.1. NM_001014987.1. [O43561-2]
    NP_001014988.1. NM_001014988.1. [O43561-4]
    NP_001014989.2. NM_001014989.1. [O43561-3]
    NP_055202.1. NM_014387.3. [O43561-1]
    UniGeneiHs.632179.

    Genome annotation databases

    EnsembliENST00000360872; ENSP00000354119; ENSG00000213658. [O43561-1]
    ENST00000395456; ENSP00000378841; ENSG00000213658. [O43561-2]
    ENST00000395461; ENSP00000378845; ENSG00000213658. [O43561-3]
    ENST00000454369; ENSP00000398793; ENSG00000213658. [O43561-4]
    ENST00000564277; ENSP00000457036; ENSG00000213658. [O43561-4]
    ENST00000566177; ENSP00000456761; ENSG00000213658. [O43561-5]
    GeneIDi27040.
    KEGGihsa:27040.
    UCSCiuc002dsb.3. human. [O43561-2]
    uc002dsc.3. human.
    uc002dsd.3. human. [O43561-1]
    uc010vdj.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036906 mRNA. Translation: AAC39637.1 .
    AF036905 mRNA. Translation: AAC39636.1 .
    AJ223280 mRNA. Translation: CAA11218.1 .
    FN432832 mRNA. Translation: CBA11533.1 .
    AC109460 Genomic DNA. No translation available.
    CH471267 Genomic DNA. Translation: EAW52027.1 .
    CH471267 Genomic DNA. Translation: EAW52028.1 .
    BC011563 mRNA. Translation: AAH11563.1 .
    CCDSi CCDS10647.1. [O43561-1 ]
    CCDS32425.1. [O43561-2 ]
    CCDS45455.1. [O43561-4 ]
    CCDS53999.1. [O43561-3 ]
    RefSeqi NP_001014987.1. NM_001014987.1. [O43561-2 ]
    NP_001014988.1. NM_001014988.1. [O43561-4 ]
    NP_001014989.2. NM_001014989.1. [O43561-3 ]
    NP_055202.1. NM_014387.3. [O43561-1 ]
    UniGenei Hs.632179.

    3D structure databases

    ProteinModelPortali O43561.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117971. 31 interactions.
    DIPi DIP-29231N.
    IntActi O43561. 15 interactions.
    MINTi MINT-2836977.
    STRINGi 9606.ENSP00000354119.

    Chemistry

    ChEMBLi CHEMBL5779.

    PTM databases

    PhosphoSitei O43561.

    Proteomic databases

    MaxQBi O43561.
    PaxDbi O43561.
    PRIDEi O43561.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360872 ; ENSP00000354119 ; ENSG00000213658 . [O43561-1 ]
    ENST00000395456 ; ENSP00000378841 ; ENSG00000213658 . [O43561-2 ]
    ENST00000395461 ; ENSP00000378845 ; ENSG00000213658 . [O43561-3 ]
    ENST00000454369 ; ENSP00000398793 ; ENSG00000213658 . [O43561-4 ]
    ENST00000564277 ; ENSP00000457036 ; ENSG00000213658 . [O43561-4 ]
    ENST00000566177 ; ENSP00000456761 ; ENSG00000213658 . [O43561-5 ]
    GeneIDi 27040.
    KEGGi hsa:27040.
    UCSCi uc002dsb.3. human. [O43561-2 ]
    uc002dsc.3. human.
    uc002dsd.3. human. [O43561-1 ]
    uc010vdj.2. human.

    Organism-specific databases

    CTDi 27040.
    GeneCardsi GC16P028998.
    HGNCi HGNC:18874. LAT.
    HPAi CAB002223.
    CAB012978.
    HPA011157.
    MIMi 602354. gene.
    neXtProti NX_O43561.
    PharmGKBi PA38728.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41822.
    HOGENOMi HOG000081810.
    HOVERGENi HBG018198.
    KOi K07362.
    OMAi GSHRMPS.
    PhylomeDBi O43561.

    Enzyme and pathway databases

    Reactomei REACT_12623. Generation of second messenger molecules.
    REACT_147814. DAP12 signaling.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_163936. Fc epsilon receptor (FCERI) signaling.
    REACT_1695. GPVI-mediated activation cascade.
    SignaLinki O43561.

    Miscellaneous databases

    GeneWikii Linker_of_activated_T_cells.
    GenomeRNAii 27040.
    NextBioi 35483432.
    PROi O43561.
    SOURCEi Search...

    Gene expression databases

    Bgeei O43561.
    CleanExi HS_LAT.
    Genevestigatori O43561.

    Family and domain databases

    InterProi IPR008359. Linker_for_activat_Tcells_prot.
    [Graphical view ]
    PANTHERi PTHR15586. PTHR15586. 1 hit.
    Pfami PF15234. LAT. 1 hit.
    [Graphical view ]
    PRINTSi PR01781. LATPROTEIN.
    ProtoNeti Search...

    Publicationsi

    1. "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
      Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
      Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 32-47 AND 219-233, PHOSPHORYLATION AT TYR-200, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-200 AND TYR-220, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PIK3R1; GRB2; GRAP AND PLCG1.
      Tissue: Leukemia.
    2. "Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells."
      Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F., Ryan J.C., Tasken K., Imboden J.B., Vaage J.T.
      J. Exp. Med. 187:1157-1161(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Thymus.
    3. "Inactivation of pre-B cell receptor-mediated tumor suppression by aberrant splicing in Ph+ acute lymphoblastic leukemia."
      Muschen M.
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Bone marrow.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon.
    7. "LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation."
      Zhang W., Trible R.P., Samelson L.E.
      Immunity 9:239-246(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-26 AND CYS-29, MUTAGENESIS OF CYS-26 AND CYS-29.
    8. "Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells."
      Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.
      J. Biol. Chem. 274:28050-28057(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    9. "A role for the adaptor protein LAT in human NK cell-mediated cytotoxicity."
      Jevremovic D., Billadeau D.D., Schoon R.A., Dick C.J., Irvin B.J., Zhang W., Samelson L.E., Abraham R.T., Leibson P.J.
      J. Immunol. 162:2453-2456(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NK CELLS, INTERACTION WITH PLCG1.
    10. "Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell antigen receptor-mediated signaling."
      Zhang W., Trible R.P., Zhu M., Liu S.K., McGlade C.J., Samelson L.E.
      J. Biol. Chem. 275:23355-23361(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2; GRAP2 AND PLCG1.
    11. "The adapter protein LAT enhances fcgamma receptor-mediated signal transduction in myeloid cells."
      Tridandapani S., Lyden T.W., Smith J.L., Carter J.E., Coggeshall K.M., Anderson C.L.
      J. Biol. Chem. 275:20480-20487(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCGR1A.
    12. "Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
      Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
      J. Biol. Chem. 275:33427-33434(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH LCP2; SKAP2; GRB2; PLCG2 AND CBL.
    13. "Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells."
      Paz P.E., Wang S., Clarke H., Lu X., Stokoe D., Abo A.
      Biochem. J. 356:461-471(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1 AND PLCG1, MUTAGENESIS OF TYR-161.
    14. "Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
      Baker J.E., Majeti R., Tangye S.G., Weiss A.
      Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
    15. "Phosphorylation of the linker for activation of T-cells by Itk promotes recruitment of Vav."
      Perez-Villar J.J., Whitney G.S., Sitnick M.T., Dunn R.J., Venkatesan S., O'Day K., Schieven G.L., Lin T.A., Kanner S.B.
      Biochemistry 41:10732-10740(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ITK.
    16. "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
      Lin J., Weiss A.
      J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
    17. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "LAT: a T lymphocyte adapter protein that couples the antigen receptor to downstream signaling pathways."
      Sommers C.L., Samelson L.E., Love P.E.
      Bioessays 26:61-67(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN T-CELLS.
    19. Cited for: TISSUE SPECIFICITY.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-101 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39; SER-40; SER-41; SER-43; SER-101; SER-106; SER-240; SER-241 AND TYR-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiLAT_HUMAN
    AccessioniPrimary (citable) accession number: O43561
    Secondary accession number(s): B7WPI0
    , C7C5T6, G5E9K3, O43919
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 136 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

    Engagement of killer inhibitory receptors (KIR) disrupts the interaction of PLCG1 with LAT and blocks target cell-induced activation of PLC, maybe by inducing the dephosphorylation of LAT.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3