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Reviewed, UniProtKB/Swiss-Prot Q13094 (LCP2_HUMAN)

Last modified February 9, 2010. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Involved in T-cell antigen receptor mediated signaling.

Subunit structure

Interacts with SLA. Interacts with CBLB By similarity. Interacts with the adapter proteins GRB2 and FYB. Interacts with SHB. Interacts with PRAM1. Ref.5 Ref.6

Subcellular location

Cytoplasm Probable.

Tissue specificity

Highly expressed in spleen, thymus, and peripheral blood leukocytes. Highly expressed also in T-cell and monocytic cell lines, expressed at lower level in B-cell lines. Not detected in fibroblast or neuroblasatoma cell lines.

Domain

The SH2 domain mediates interaction with SHB.

Post-translational modification

Phosphorylated after T-cell receptor activation by ZAP-70. Ref.7 Ref.8 Ref.9 Ref.10

Sequence similarities

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainSH2 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processimmune response Ref.1

Traceable author statement. Source: ProtInc

transmembrane receptor protein tyrosine kinase signaling pathway Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

   Molecular functionprotein binding Ref.1

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HCKP086311EBI-346946,EBI-346340

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Lymphocyte cytosolic protein 2
PRO_0000084368

Regions

Domain15 – 8167SAM
Domain422 – 530109SH2
Compositional bias133 – 1364Poly-Glu
Compositional bias198 – 2014Poly-Pro

Amino acid modifications

Modified residue231Phosphotyrosine By similarity
Modified residue1731Phosphotyrosine Ref.8
Modified residue2071Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Secondary structure

.................. 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13094-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C5D22F31D36200C8

FASTA53360,188
        10         20         30         40         50         60 
MALRNVPFRS EVLGWDPDSL ADYFKKLNYK DCEKAVKKYH IDGARFLNLT ENDIQKFPKL 

        70         80         90        100        110        120 
RVPILSKLSQ EINKNEERRS IFTRKPQVPR FPEETESHEE DNGGWSSFEE DDYESPNDDQ 

       130        140        150        160        170        180 
DGEDDGDYES PNEEEEAPVE DDADYEPPPS NDEEALQNSI LPAKPFPNSN SMYIDRPPSG 

       190        200        210        220        230        240 
KTPQQPPVPP QRPMAALPPP PAGRNHSPLP PPQTNHEEPS RSRNHKTAKL PAPSIDRSTK 

       250        260        270        280        290        300 
PPLDRSLAPF DREPFTLGKK PPFSDKPSIP AGRSLGEHLP KIQKPPLPPT TERHERSSPL 

       310        320        330        340        350        360 
PGKKPPVPKH GWGPDRREND EDDVHQRPLP QPALLPMSSN TFPSRSTKPS PMNPLPSSHM 

       370        380        390        400        410        420 
PGAFSESNSS FPQSASLPPY FSQGPSNRPP IRAEGRNFPL PLPNKPRPPS PAEEENSLNE 

       430        440        450        460        470        480 
EWYVSYITRP EAEAALRKIN QDGTFLVRDS SKKTTTNPYV LMVLYKDKVY NIQIRYQKES 

       490        500        510        520        530 
QVYLLGTGLR GKEDFLSVSD IIDYFRKMPL LLIDGKNRGS RYQCTLTHAA GYP 

« 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: 7706237] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Leukemia.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[5]"PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells."
Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F., Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.
J. Biol. Chem. 276:22375-22381(2001) [PubMed: 11301322] [Abstract]
Cited for: INTERACTION WITH PRAM1.
[6]"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
Eur. J. Biochem. 269:3279-3288(2002) [PubMed: 12084069] [Abstract]
Cited for: INTERACTION WITH SHB.
[7]"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: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, MASS SPECTROMETRY.
Tissue: T-cell.
[8]"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.
Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-173 AND SER-207, MASS SPECTROMETRY.
Tissue: T-cell.
[9]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, MASS SPECTROMETRY.
Tissue: Platelet.
[10]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, MASS SPECTROMETRY.
Tissue: T-cell.
[11]"Solution structure of the N-terminal SAM-domain of human lymphocyte cytosolic protein 2."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-83.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20158 mRNA. Translation: AAC50135.1.
BT007273 mRNA. Translation: AAP35937.1.
CH471062 Genomic DNA. Translation: EAW61479.1.
BC016618 mRNA. Translation: AAH16618.1.
IPIIPI00297169.
PIRA56110.
RefSeqNP_005556.1.
UniGeneHs.304475

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3HNMR-B232-241[»]
1YWOX-ray1.81P185-194[»]
2EAPNMR-A1-83[»]
2RORNMR-B122-136[»]
SMRQ13094. Positions 406-530.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13094. 2 interactions.
STRINGQ13094.

PTM databases

PhosphoSiteQ13094.

Proteomic databases

PRIDEQ13094.

Genome annotation databases

EnsemblENST00000046794; ENSP00000046794; ENSG00000043462; Homo sapiens. [Genome view]
GeneID3937.
KEGGhsa:3937.
UCSCuc003man.1. human.

Organism-specific databases

CTD3937.
GeneCardsGC05M169607.
H-InvDBHIX0005402.
HIX0005403.
HGNCHGNC:6529. LCP2.
HPACAB004574.
MIM601603. gene.
PharmGKBPA30313.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13343.
HOGENOMHBG715822.
HOVERGENQ13094.
InParanoidQ13094.
OMACEKAVKK.
OrthoDBEOG9616QC.

Enzyme and pathway databases

Pathway_Interaction_DBfcer1pathway. Fc-epsilon receptor I signaling in mast cells.
tcrjnkpathway. JNK signaling in the CD4+ TCR pathway.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressQ13094.
BgeeQ13094.
CleanExHS_LCP2.
GenevestigatorQ13094.
GermOnlineENSG00000043462. Homo sapiens.

Family and domain databases

InterProIPR001660. SAM.
IPR011510. SAM_2.
IPR010993. SAM_homology.
IPR000980. SH2.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF07647. SAM_2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00454. SAM. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
PROSITEPS50105. SAM_DOMAIN. False negative.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio15461.
SOURCESearch...

Entry information

Entry nameLCP2_HUMAN
AccessionPrimary (citable) accession number: Q13094
Secondary accession number(s): Q53XV4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents