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Q13094 (LCP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismHomo sapiens (Human) [Reference 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.6 Ref.7

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 neuroblastoma cell lines.

Domain

The SH2 domain mediates interaction with SHB.

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. Ref.9 Ref.11

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_0000084368

Regions

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

Amino acid modifications

Modified residue231Phosphotyrosine By similarity
Modified residue2071Phosphoserine Ref.8 Ref.10

Natural variations

Natural variant4101S → C. Ref.3
Corresponds to variant rs34192428 [ dbSNP | Ensembl ].
VAR_070803

Experimental info

Sequence conflict191S → G in BAF85579. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13094 [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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-410.
Tissue: Trachea.
[4]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].
[5]"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].
Tissue: Prostate.
[6]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRAM1.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHB.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase."
Shim E.K., Moon C.S., Lee G.Y., Ha Y.J., Chae S.K., Lee J.R.
FEBS Lett. 575:35-40(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY SYK.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[11]"Sequential phosphorylation of SLP-76 at tyrosine 173 is required for activation of T and mast cells."
Sela M., Bogin Y., Beach D., Oellerich T., Lehne J., Smith-Garvin J.E., Okumura M., Starosvetsky E., Kosoff R., Libman E., Koretzky G., Kambayashi T., Urlaub H., Wienands J., Chernoff J., Yablonski D.
EMBO J. 30:3160-3172(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ITK.
[12]"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.
AK292890 mRNA. Translation: BAF85579.1.
CH471062 Genomic DNA. Translation: EAW61479.1.
BC016618 mRNA. Translation: AAH16618.1.
PIRA56110.
RefSeqNP_005556.1. NM_005565.3.
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[»]
ProteinModelPortalQ13094.
SMRQ13094. Positions 1-83, 413-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110129. 25 interactions.
DIPDIP-31812N.
IntActQ13094. 27 interactions.
MINTMINT-110432.
STRING9606.ENSP00000046794.

PTM databases

PhosphoSiteQ13094.

Polymorphism databases

DMDM10720065.

Proteomic databases

PaxDbQ13094.
PRIDEQ13094.

Protocols and materials databases

DNASU3937.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000046794; ENSP00000046794; ENSG00000043462.
GeneID3937.
KEGGhsa:3937.
UCSCuc003man.1. human.

Organism-specific databases

CTD3937.
GeneCardsGC05M169673.
H-InvDBHIX0005402.
HGNCHGNC:6529. LCP2.
HPACAB004574.
HPA036396.
HPA036397.
MIM601603. gene.
neXtProtNX_Q13094.
PharmGKBPA30313.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43557.
HOGENOMHOG000049173.
HOVERGENHBG006247.
InParanoidQ13094.
KOK07361.
OMANSMYIDR.
OrthoDBEOG7FJH09.
PhylomeDBQ13094.
TreeFamTF326567.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ13094.

Gene expression databases

ArrayExpressQ13094.
BgeeQ13094.
CleanExHS_LCP2.
GenevestigatorQ13094.

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

EvolutionaryTraceQ13094.
GeneWikiLymphocyte_cytosolic_protein_2.
GenomeRNAi3937.
NextBio15461.
PROQ13094.
SOURCESearch...

Entry information

Entry nameLCP2_HUMAN
AccessionPrimary (citable) accession number: Q13094
Secondary accession number(s): A8KA25, Q53XV4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

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