Q60787 (LCP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Lcp2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine secretion Inferred from mutant phenotype PubMed 15153494. Source: MGI mast cell activation Inferred from mutant phenotype PubMed 15153494. Source: MGI
Cellular_component	cytosol Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 533

533

Lymphocyte cytosolic protein 2

PRO_0000084369

Regions

Domain

12 – 78

67

SAM

Domain

422 – 530

109

SH2

Amino acid modifications

Modified residue

23

1

Phosphotyrosine Ref.8

Modified residue

207

1

Phosphoserine By similarity

Modified residue

210

1

Phosphoserine Ref.9

Experimental info

Sequence conflict

306

1

P → S in AAC52189. Ref.1

Secondary structure

1

.

.

.

533

Helix Strand Turn

Details...

Helix

237 – 239

3

Sequences

	Sequence		Length	Mass (Da)
	Q60787 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 50AEA025EF0DAD01	FASTA	533	60,238
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Macrophage.
+	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.

IPI

IPI00311477.

PIR

B56110.

RefSeq

NP_034826.2. NM_010696.3.

UniGene

Mm.265350.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OEB	X-ray	1.76	C/D	231-243	[»]
2ETZ	NMR	-	B	142-149	[»]
2EU0	NMR	-	B	142-149	[»]

ProteinModelPortal

Q60787.

SMR

Q60787. Positions 1-83, 358-517.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q60787. 2 interactions.

PTM databases

PhosphoSite

Q60787.

Proteomic databases

PaxDb

Q60787.

PRIDE

Q60787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000169878; ENSMUSP00000126796; ENSMUSG00000002699.

GeneID

16822.

KEGG

mmu:16822.

Organism-specific databases

CTD

3937.

MGI

MGI:1321402. Lcp2.

Phylogenomic databases

eggNOG

NOG43557.

GeneTree

ENSGT00530000063094.

HOVERGEN

HBG006247.

InParanoid

Q922M0.

KO

K07361.

OrthoDB

EOG4F1X2Z.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

ArrayExpress

Q60787.

Bgee

Q60787.

CleanEx

MM_LCP2.

Genevestigator

Q60787.

GermOnline

ENSMUSG00000002699. Mus musculus.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
3.30.505.10. 1 hit.

InterPro

IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR000980. SH2.
[Graphical view]

Pfam

PF07647. SAM_2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

SMART

SM00454. SAM. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS50105. SAM_DOMAIN. False negative.
PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q60787.

NextBio

290720.

SOURCE

Search...

Entry information

Entry name

LCP2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program