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Q60787

- LCP2_MOUSE

UniProt

Q60787 - LCP2_MOUSE

Protein

Lymphocyte cytosolic protein 2

Gene

Lcp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Involved in T-cell antigen receptor mediated signaling.1 Publication

    GO - Biological processi

    1. cytokine secretion Source: MGI
    2. mast cell activation Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225768. Generation of second messenger molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lymphocyte cytosolic protein 2
    Alternative name(s):
    SH2 domain-containing leukocyte protein of 76 kDa
    SLP-76 tyrosine phosphoprotein
    Short name:
    SLP76
    Gene namesi
    Name:Lcp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1321402. Lcp2.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 533533Lymphocyte cytosolic protein 2PRO_0000084369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Phosphotyrosine2 Publications
    Modified residuei207 – 2071PhosphoserineBy similarity
    Modified residuei210 – 2101Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated after T-cell receptor activation by ZAP70, ITK and TXK, which leads to the up-regulation of Th1 preferred cytokine IL-2. SYK-dependent phosphorylation is required for recruitment of PI3K signaling components By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ60787.
    PaxDbiQ60787.
    PRIDEiQ60787.

    PTM databases

    PhosphoSiteiQ60787.

    Expressioni

    Tissue specificityi

    Highly expressed in spleen, thymus, and peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiQ60787.
    BgeeiQ60787.
    CleanExiMM_LCP2.
    GenevestigatoriQ60787.

    Interactioni

    Subunit structurei

    Interacts with SHB. Interacts with PRAM1 By similarity. Interacts with SLA. Interacts with the adapter proteins GRB2 and FYB. Interacts with CBLB.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi201124. 1 interaction.
    IntActiQ60787. 4 interactions.
    MINTiMINT-8013600.

    Structurei

    Secondary structure

    1
    533
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi237 – 2393

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OEBX-ray1.76C/D231-243[»]
    2ETZNMR-B142-149[»]
    2EU0NMR-B142-149[»]
    ProteinModelPortaliQ60787.
    SMRiQ60787. Positions 1-83, 358-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60787.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 7867SAMAdd
    BLAST
    Domaini422 – 530109SH2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SH2 domain mediates interaction with SHB.By similarity

    Sequence similaritiesi

    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG43557.
    GeneTreeiENSGT00530000063094.
    HOVERGENiHBG006247.
    InParanoidiQ922M0.
    KOiK07361.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR000980. SH2.
    [Graphical view]
    PfamiPF07647. SAM_2. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    SMARTiSM00454. SAM. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60787-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALKNVPFRS EVLAWNSDNL ADYFRKLNYR DCEKAVKKYH IDGARFLNLT    50
    ENDIQKFPKL RMPLLSKLSQ DINKNEERRS IFTRKPQIPR FLEETESHEE 100
    DDGGWSSFED DYESPNDDDP DGEDDGDYES PNEEEQALVD DAADYEPPPS 150
    NNEEALQSSI LPPNSFHNTN SMYIDRPPTG KVSQQPPVPP LRPKPALPPL 200
    PTGRNHSPLS PPHPNHEEPS RSGNNKTAKL PAPSIDRSTK PPLDRSLAPL 250
    DREPFILGKK PPFSDKPSAP LGREHLPKIQ KPPLPPAMDR HERNERLGPV 300
    TTRKPPVPRH GRGPDRREND EDDVHQRPLP QPSLPSMSSN TFPSRSVQPS 350
    SKNTFPLAHM PGAFSESNIG FQQSASLPPY FSQGPGNRPP LRSEGRNLPL 400
    PVPNRPQPPS PGEEETPLDE EWYVSYITRP EAEAALRKIN QDGTFLVRDS 450
    SKKTANNPYV LMVLYKDKVY NIQIRYQEES QVYLLGTGLR GKEDFLSVSD 500
    IIDYFRKMPL LLIDGKNRGS RYQCTLTHAA GCL 533
    Length:533
    Mass (Da):60,238
    Last modified:July 27, 2011 - v2
    Checksum:i50AEA025EF0DAD01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti306 – 3061P → S in AAC52189. (PubMed:7706237)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20159 mRNA. Translation: AAC52189.1.
    AK036727 mRNA. Translation: BAC29553.1.
    AK170491 mRNA. Translation: BAE41833.1.
    CH466604 Genomic DNA. Translation: EDL23730.1.
    BC006948 mRNA. Translation: AAH06948.1.
    CCDSiCCDS48768.1.
    PIRiB56110.
    RefSeqiNP_034826.2. NM_010696.3.
    UniGeneiMm.265350.

    Genome annotation databases

    EnsembliENSMUST00000169878; ENSMUSP00000126796; ENSMUSG00000002699.
    GeneIDi16822.
    KEGGimmu:16822.
    UCSCiuc007ikv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20159 mRNA. Translation: AAC52189.1 .
    AK036727 mRNA. Translation: BAC29553.1 .
    AK170491 mRNA. Translation: BAE41833.1 .
    CH466604 Genomic DNA. Translation: EDL23730.1 .
    BC006948 mRNA. Translation: AAH06948.1 .
    CCDSi CCDS48768.1.
    PIRi B56110.
    RefSeqi NP_034826.2. NM_010696.3.
    UniGenei Mm.265350.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OEB X-ray 1.76 C/D 231-243 [» ]
    2ETZ NMR - B 142-149 [» ]
    2EU0 NMR - B 142-149 [» ]
    ProteinModelPortali Q60787.
    SMRi Q60787. Positions 1-83, 358-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201124. 1 interaction.
    IntActi Q60787. 4 interactions.
    MINTi MINT-8013600.

    PTM databases

    PhosphoSitei Q60787.

    Proteomic databases

    MaxQBi Q60787.
    PaxDbi Q60787.
    PRIDEi Q60787.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169878 ; ENSMUSP00000126796 ; ENSMUSG00000002699 .
    GeneIDi 16822.
    KEGGi mmu:16822.
    UCSCi uc007ikv.1. mouse.

    Organism-specific databases

    CTDi 3937.
    MGIi MGI:1321402. Lcp2.

    Phylogenomic databases

    eggNOGi NOG43557.
    GeneTreei ENSGT00530000063094.
    HOVERGENi HBG006247.
    InParanoidi Q922M0.
    KOi K07361.

    Enzyme and pathway databases

    Reactomei REACT_188185. DAP12 signaling.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225768. Generation of second messenger molecules.

    Miscellaneous databases

    EvolutionaryTracei Q60787.
    NextBioi 290720.
    PROi Q60787.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60787.
    Bgeei Q60787.
    CleanExi MM_LCP2.
    Genevestigatori Q60787.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR000980. SH2.
    [Graphical view ]
    Pfami PF07647. SAM_2. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    SMARTi SM00454. SAM. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells."
      Jackman J.K., Motto D.G., Sun Q., Tanemoto M., Turck C.W., Peltz G.A., Koretzky G.A., Findell P.R.
      J. Biol. Chem. 270:7029-7032(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell lymphoma.
    2. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Bone.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "Resting lymphocyte kinase (Rlk/Txk) targets lymphoid adaptor SLP-76 in the cooperative activation of interleukin-2 transcription in T-cells."
      Schneider H., Guerette B., Guntermann C., Rudd C.E.
      J. Biol. Chem. 275:3835-3840(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY TXK.
    6. "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
      Sosinowski T., Pandey A., Dixit V.M., Weiss A.
      J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA.
    7. Cited for: INTERACTION WITH CBLB.
    8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    9. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLCP2_MOUSE
    AccessioniPrimary (citable) accession number: Q60787
    Secondary accession number(s): Q922M0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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

    External Data

    Dasty 3