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Q13094

- LCP2_HUMAN

UniProt

Q13094 - LCP2_HUMAN

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Protein

Lymphocyte cytosolic protein 2

Gene

LCP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in T-cell antigen receptor mediated signaling.

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cytokine secretion Source: Ensembl
  3. Fc-epsilon receptor signaling pathway Source: Reactome
  4. immune response Source: ProtInc
  5. innate immune response Source: Reactome
  6. mast cell activation Source: Ensembl
  7. platelet activation Source: Reactome
  8. T cell receptor signaling pathway Source: Reactome
  9. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12623. Generation of second messenger molecules.
REACT_147814. DAP12 signaling.
REACT_163701. FCERI mediated MAPK activation.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_1695. GPVI-mediated activation cascade.
SignaLinkiQ13094.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6529. LCP2.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30313.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 533533Lymphocyte cytosolic protein 2PRO_0000084368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231PhosphotyrosineBy similarity
Modified residuei207 – 2071Phosphoserine2 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.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13094.
PaxDbiQ13094.
PRIDEiQ13094.

PTM databases

PhosphoSiteiQ13094.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ13094.
CleanExiHS_LCP2.
ExpressionAtlasiQ13094. baseline and differential.
GenevestigatoriQ13094.

Organism-specific databases

HPAiCAB004574.
HPA036396.
HPA036397.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005332EBI-346946,EBI-297353
FYBO151175EBI-346946,EBI-1753267
GRAP2O7579111EBI-346946,EBI-740418
Grap2O891003EBI-346946,EBI-642151From a different organism.
GRB2P629937EBI-346946,EBI-401755
MAP4K3Q8IVH85EBI-346946,EBI-1758170
Map4k3Q99JP02EBI-346946,EBI-5324222From a different organism.
NCK1P1633314EBI-346946,EBI-389883
PLCG1P084875EBI-346946,EBI-8013886From a different organism.
PLCG1P191743EBI-346946,EBI-79387
STAMQ927833EBI-346946,EBI-752333
STAM2O758863EBI-346946,EBI-373258
VAV1P154989EBI-346946,EBI-625518

Protein-protein interaction databases

BioGridi110129. 26 interactions.
DIPiDIP-31812N.
IntActiQ13094. 28 interactions.
MINTiMINT-110432.
STRINGi9606.ENSP00000046794.

Structurei

Secondary structure

533
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 44
Helixi9 – 124
Turni17 – 193
Helixi20 – 267
Helixi30 – 389
Helixi43 – 475
Helixi51 – 544
Turni59 – 613
Helixi62 – 7312
Helixi237 – 2393

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3HNMR-B232-241[»]
1YWOX-ray1.81P185-194[»]
2EAPNMR-A1-83[»]
2RORNMR-B122-136[»]
ProteinModelPortaliQ13094.
SMRiQ13094. Positions 1-83, 413-517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 8167SAMAdd
BLAST
Domaini422 – 530109SH2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi133 – 1364Poly-Glu
Compositional biasi198 – 2014Poly-Pro

Domaini

The SH2 domain mediates interaction with SHB.

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG43557.
GeneTreeiENSGT00530000063094.
HOGENOMiHOG000049173.
HOVERGENiHBG006247.
InParanoidiQ13094.
KOiK07361.
OMAiNSMYIDR.
OrthoDBiEOG7FJH09.
PhylomeDBiQ13094.
TreeFamiTF326567.

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.

Q13094-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALRNVPFRS EVLGWDPDSL ADYFKKLNYK DCEKAVKKYH IDGARFLNLT
60 70 80 90 100
ENDIQKFPKL RVPILSKLSQ EINKNEERRS IFTRKPQVPR FPEETESHEE
110 120 130 140 150
DNGGWSSFEE DDYESPNDDQ DGEDDGDYES PNEEEEAPVE DDADYEPPPS
160 170 180 190 200
NDEEALQNSI LPAKPFPNSN SMYIDRPPSG KTPQQPPVPP QRPMAALPPP
210 220 230 240 250
PAGRNHSPLP PPQTNHEEPS RSRNHKTAKL PAPSIDRSTK PPLDRSLAPF
260 270 280 290 300
DREPFTLGKK PPFSDKPSIP AGRSLGEHLP KIQKPPLPPT TERHERSSPL
310 320 330 340 350
PGKKPPVPKH GWGPDRREND EDDVHQRPLP QPALLPMSSN TFPSRSTKPS
360 370 380 390 400
PMNPLPSSHM PGAFSESNSS FPQSASLPPY FSQGPSNRPP IRAEGRNFPL
410 420 430 440 450
PLPNKPRPPS PAEEENSLNE EWYVSYITRP EAEAALRKIN QDGTFLVRDS
460 470 480 490 500
SKKTTTNPYV LMVLYKDKVY NIQIRYQKES QVYLLGTGLR GKEDFLSVSD
510 520 530
IIDYFRKMPL LLIDGKNRGS RYQCTLTHAA GYP
Length:533
Mass (Da):60,188
Last modified:November 1, 1996 - v1
Checksum:iC5D22F31D36200C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191S → G in BAF85579. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti410 – 4101S → C.1 Publication
Corresponds to variant rs34192428 [ dbSNP | Ensembl ].
VAR_070803

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS47339.1.
PIRiA56110.
RefSeqiNP_005556.1. NM_005565.3.
UniGeneiHs.304475.

Genome annotation databases

EnsembliENST00000046794; ENSP00000046794; ENSG00000043462.
GeneIDi3937.
KEGGihsa:3937.
UCSCiuc003man.1. human.

Polymorphism databases

DMDMi10720065.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS47339.1.
PIRi A56110.
RefSeqi NP_005556.1. NM_005565.3.
UniGenei Hs.304475.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H3H NMR - B 232-241 [» ]
1YWO X-ray 1.81 P 185-194 [» ]
2EAP NMR - A 1-83 [» ]
2ROR NMR - B 122-136 [» ]
ProteinModelPortali Q13094.
SMRi Q13094. Positions 1-83, 413-517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110129. 26 interactions.
DIPi DIP-31812N.
IntActi Q13094. 28 interactions.
MINTi MINT-110432.
STRINGi 9606.ENSP00000046794.

PTM databases

PhosphoSitei Q13094.

Polymorphism databases

DMDMi 10720065.

Proteomic databases

MaxQBi Q13094.
PaxDbi Q13094.
PRIDEi Q13094.

Protocols and materials databases

DNASUi 3937.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000046794 ; ENSP00000046794 ; ENSG00000043462 .
GeneIDi 3937.
KEGGi hsa:3937.
UCSCi uc003man.1. human.

Organism-specific databases

CTDi 3937.
GeneCardsi GC05M169673.
H-InvDB HIX0005402.
HGNCi HGNC:6529. LCP2.
HPAi CAB004574.
HPA036396.
HPA036397.
MIMi 601603. gene.
neXtProti NX_Q13094.
PharmGKBi PA30313.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43557.
GeneTreei ENSGT00530000063094.
HOGENOMi HOG000049173.
HOVERGENi HBG006247.
InParanoidi Q13094.
KOi K07361.
OMAi NSMYIDR.
OrthoDBi EOG7FJH09.
PhylomeDBi Q13094.
TreeFami TF326567.

Enzyme and pathway databases

Reactomei REACT_12623. Generation of second messenger molecules.
REACT_147814. DAP12 signaling.
REACT_163701. FCERI mediated MAPK activation.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_1695. GPVI-mediated activation cascade.
SignaLinki Q13094.

Miscellaneous databases

EvolutionaryTracei Q13094.
GeneWikii Lymphocyte_cytosolic_protein_2.
GenomeRNAii 3937.
NextBioi 15461.
PROi Q13094.
SOURCEi Search...

Gene expression databases

Bgeei Q13094.
CleanExi HS_LCP2.
ExpressionAtlasi Q13094. baseline and differential.
Genevestigatori Q13094.

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

« 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], 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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  11. 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.

Entry informationi

Entry nameiLCP2_HUMAN
AccessioniPrimary (citable) accession number: Q13094
Secondary accession number(s): A8KA25, Q53XV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3