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Q60787 (LCP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lymphocyte cytosolic protein 2
Alternative name(s):
SH2 domain-containing leukocyte protein of 76 kDa
SLP-76 tyrosine phosphoprotein
Short name=SLP76
Gene names
Name:Lcp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in T-cell antigen receptor mediated signaling. Ref.5

Subunit structure

Interacts with SHB. Interacts with PRAM1 By similarity. Interacts with SLA. Interacts with the adapter proteins GRB2 and FYB. Interacts with CBLB. Ref.6 Ref.7

Subcellular location

Cytoplasm Probable.

Tissue specificity

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

Domain

The SH2 domain mediates interaction with SHB By similarity.

Post-translational modification

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. Ref.5

Sequence similarities

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Lymphocyte cytosolic protein 2
PRO_0000084369

Regions

Domain12 – 7867SAM
Domain422 – 530109SH2

Amino acid modifications

Modified residue231Phosphotyrosine Ref.8
Modified residue2071Phosphoserine By similarity
Modified residue2101Phosphoserine Ref.9

Experimental info

Sequence conflict3061P → S in AAC52189. Ref.1

Secondary structure

... 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60787 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 50AEA025EF0DAD01

FASTA53360,238
        10         20         30         40         50         60 
MALKNVPFRS EVLAWNSDNL ADYFRKLNYR DCEKAVKKYH IDGARFLNLT ENDIQKFPKL 

        70         80         90        100        110        120 
RMPLLSKLSQ DINKNEERRS IFTRKPQIPR FLEETESHEE DDGGWSSFED DYESPNDDDP 

       130        140        150        160        170        180 
DGEDDGDYES PNEEEQALVD DAADYEPPPS NNEEALQSSI LPPNSFHNTN SMYIDRPPTG 

       190        200        210        220        230        240 
KVSQQPPVPP LRPKPALPPL PTGRNHSPLS PPHPNHEEPS RSGNNKTAKL PAPSIDRSTK 

       250        260        270        280        290        300 
PPLDRSLAPL DREPFILGKK PPFSDKPSAP LGREHLPKIQ KPPLPPAMDR HERNERLGPV 

       310        320        330        340        350        360 
TTRKPPVPRH GRGPDRREND EDDVHQRPLP QPSLPSMSSN TFPSRSVQPS SKNTFPLAHM 

       370        380        390        400        410        420 
PGAFSESNIG FQQSASLPPY FSQGPGNRPP LRSEGRNLPL PVPNRPQPPS PGEEETPLDE 

       430        440        450        460        470        480 
EWYVSYITRP EAEAALRKIN QDGTFLVRDS SKKTANNPYV LMVLYKDKVY NIQIRYQEES 

       490        500        510        520        530 
QVYLLGTGLR GKEDFLSVSD IIDYFRKMPL LLIDGKNRGS RYQCTLTHAA GCL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b."
Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.
Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS48768.1.
PIRB56110.
RefSeqNP_034826.2. NM_010696.3.
UniGeneMm.265350.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OEBX-ray1.76C/D231-243[»]
2ETZNMR-B142-149[»]
2EU0NMR-B142-149[»]
ProteinModelPortalQ60787.
SMRQ60787. Positions 1-83, 358-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201124. 1 interaction.
IntActQ60787. 4 interactions.
MINTMINT-8013600.

PTM databases

PhosphoSiteQ60787.

Proteomic databases

MaxQBQ60787.
PaxDbQ60787.
PRIDEQ60787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169878; ENSMUSP00000126796; ENSMUSG00000002699.
GeneID16822.
KEGGmmu:16822.
UCSCuc007ikv.1. mouse.

Organism-specific databases

CTD3937.
MGIMGI:1321402. Lcp2.

Phylogenomic databases

eggNOGNOG43557.
GeneTreeENSGT00530000063094.
HOVERGENHBG006247.
InParanoidQ922M0.
KOK07361.

Gene expression databases

ArrayExpressQ60787.
BgeeQ60787.
CleanExMM_LCP2.
GenevestigatorQ60787.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
3.30.505.10. 1 hit.
InterProIPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR000980. SH2.
[Graphical view]
PfamPF07647. SAM_2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTSM00454. SAM. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60787.
NextBio290720.
PROQ60787.
SOURCESearch...

Entry information

Entry nameLCP2_MOUSE
AccessionPrimary (citable) accession number: Q60787
Secondary accession number(s): Q922M0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot