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Protein

Lymphocyte cytosolic protein 2

Gene

Lcp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  • cytokine secretion Source: MGI
  • immune response Source: GO_Central
  • intracellular signal transduction Source: GO_Central
  • mast cell activation Source: MGI
  • positive regulation of protein kinase activity Source: Ensembl
  • T cell receptor signaling pathway Source: MGI
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-202433. Generation of second messenger molecules.
R-MMU-2424491. DAP12 signaling.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1321402. Lcp2.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytosol Source: MGI
  • plasma membrane raft Source: MGI
  • TCR signalosome Source: MGI
Complete GO annotation...

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 – 231PhosphotyrosineCombined sources
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei210 – 2101PhosphoserineCombined sources
Modified residuei410 – 4101PhosphoserineBy similarity

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

EPDiQ60787.
MaxQBiQ60787.
PaxDbiQ60787.
PRIDEiQ60787.

PTM databases

iPTMnetiQ60787.
PhosphoSiteiQ60787.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ60787.
CleanExiMM_LCP2.
ExpressionAtlasiQ60787. baseline and differential.
GenevisibleiQ60787. MM.

Interactioni

Subunit structurei

Interacts with SHB. Interacts with PRAM1 (By similarity). Interacts with SLA (PubMed:10662792). Interacts with the adapter proteins GRB2 and FYB. Interacts with CBLB (PubMed:10646608). Interacts (via SH2 domain) with CD6 (via tyrosine phosphorylated C-terminus) (PubMed:16914752, PubMed:24584089).By similarity4 Publications

Protein-protein interaction databases

BioGridi201124. 1 interaction.
IntActiQ60787. 4 interactions.
MINTiMINT-8013600.
STRINGi10090.ENSMUSP00000126796.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OEBX-ray1.76C/D231-243[»]
2ETZNMR-B143-148[»]
2EU0NMR-B143-148[»]
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

eggNOGiENOG410IFFN. Eukaryota.
ENOG4111KZ2. LUCA.
GeneTreeiENSGT00530000063094.
HOVERGENiHBG006247.
InParanoidiQ60787.
KOiK07361.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
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

        10         20         30         40         50
MALKNVPFRS EVLAWNSDNL ADYFRKLNYR DCEKAVKKYH IDGARFLNLT
60 70 80 90 100
ENDIQKFPKL RMPLLSKLSQ DINKNEERRS IFTRKPQIPR FLEETESHEE
110 120 130 140 150
DDGGWSSFED DYESPNDDDP DGEDDGDYES PNEEEQALVD DAADYEPPPS
160 170 180 190 200
NNEEALQSSI LPPNSFHNTN SMYIDRPPTG KVSQQPPVPP LRPKPALPPL
210 220 230 240 250
PTGRNHSPLS PPHPNHEEPS RSGNNKTAKL PAPSIDRSTK PPLDRSLAPL
260 270 280 290 300
DREPFILGKK PPFSDKPSAP LGREHLPKIQ KPPLPPAMDR HERNERLGPV
310 320 330 340 350
TTRKPPVPRH GRGPDRREND EDDVHQRPLP QPSLPSMSSN TFPSRSVQPS
360 370 380 390 400
SKNTFPLAHM PGAFSESNIG FQQSASLPPY FSQGPGNRPP LRSEGRNLPL
410 420 430 440 450
PVPNRPQPPS PGEEETPLDE EWYVSYITRP EAEAALRKIN QDGTFLVRDS
460 470 480 490 500
SKKTANNPYV LMVLYKDKVY NIQIRYQEES QVYLLGTGLR GKEDFLSVSD
510 520 530
IIDYFRKMPL LLIDGKNRGS RYQCTLTHAA GCL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OEBX-ray1.76C/D231-243[»]
2ETZNMR-B143-148[»]
2EU0NMR-B143-148[»]
ProteinModelPortaliQ60787.
SMRiQ60787. Positions 1-83, 358-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201124. 1 interaction.
IntActiQ60787. 4 interactions.
MINTiMINT-8013600.
STRINGi10090.ENSMUSP00000126796.

PTM databases

iPTMnetiQ60787.
PhosphoSiteiQ60787.

Proteomic databases

EPDiQ60787.
MaxQBiQ60787.
PaxDbiQ60787.
PRIDEiQ60787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3937.
MGIiMGI:1321402. Lcp2.

Phylogenomic databases

eggNOGiENOG410IFFN. Eukaryota.
ENOG4111KZ2. LUCA.
GeneTreeiENSGT00530000063094.
HOVERGENiHBG006247.
InParanoidiQ60787.
KOiK07361.

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-202433. Generation of second messenger molecules.
R-MMU-2424491. DAP12 signaling.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.

Miscellaneous databases

EvolutionaryTraceiQ60787.
NextBioi290720.
PROiQ60787.
SOURCEiSearch...

Gene expression databases

BgeeiQ60787.
CleanExiMM_LCP2.
ExpressionAtlasiQ60787. baseline and differential.
GenevisibleiQ60787. MM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "CD6 regulates T-cell responses through activation-dependent recruitment of the positive regulator SLP-76."
    Hassan N.J., Simmonds S.J., Clarkson N.G., Hanrahan S., Puklavec M.J., Bomb M., Barclay A.N., Brown M.H.
    Mol. Cell. Biol. 26:6727-6738(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD6.
  9. "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.
  10. "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].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  12. "Quantitative proteomics analysis of signalosome dynamics in primary T cells identifies the surface receptor CD6 as a Lat adaptor-independent TCR signaling hub."
    Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A., Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R., Yamasaki S., Saito T., Malissen M., Aebersold R., Gstaiger M., Malissen B.
    Nat. Immunol. 15:384-392(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD6.

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: March 16, 2016
This is version 134 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

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.