Reviewed, UniProtKB/Swiss-Prot Q13094 (LCP2_HUMAN)

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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Subcellular location	CytoplasmProbable.
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.
Sequence similarities	Contains 1 SH2 domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	immune response Ref.1 Traceable author statement. Source: ProtInc transmembrane receptor protein tyrosine kinase signaling pathway Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.1 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCK	P08631	1	EBI-346946,EBI-346340

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 533

533

Lymphocyte cytosolic protein 2

PRO_0000084368

Regions

Domain

422 – 530

109

SH2

Compositional bias

133 – 136

4

Poly-Glu

Compositional bias

198 – 201

4

Poly-Pro

Amino acid modifications

Modified residue

23

1

Phosphotyrosine By similarity

Modified residue

173

1

Phosphotyrosine

Modified residue

207

1

Phosphoserine

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

533

Helix Strand Turn

Details...

Beta strand

1 – 4

4

Helix

9 – 12

4

Turn

17 – 19

3

Helix

20 – 26

7

Helix

30 – 38

9

Helix

43 – 47

5

Helix

51 – 54

4

Turn

59 – 61

3

Helix

62 – 73

12

Helix

237 – 239

3

Sequences

	Sequence		Length	Mass (Da)
	Q13094-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C5D22F31D36200C8	FASTA	533	60,188
	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

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: 7706237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Leukemia.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U20158 mRNA. Translation: AAC50135.1.
BC016618 mRNA. Translation: AAH16618.1.

PIR

A56110.

RefSeq

NP_005556.1.

UniGene

Hs.304475

3D structure databases

PDBMSD

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13094.

PTM databases

PhosphoSite

Q13094.

Genome annotation databases

Ensembl

ENSG00000043462. Homo sapiens. [Contig view]

GeneID

3937.

KEGG

hsa:3937.

Organism-specific databases

H-InvDB

HIX0005402.
HIX0005403.

HGNC

HGNC:6529. LCP2.

HPA

CAB004574.

MIM

601603. gene.

PharmGKB

PA30313.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q13094.

HOVERGEN

Q13094.

Gene expression databases

ArrayExpress

Q13094.

CleanEx

HS_LCP2.

GermOnline

ENSG00000043462. Homo sapiens.

Family and domain databases

InterPro

IPR001660. SAM.
IPR011510. SAM_2.
IPR000980. SH2.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

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

PRINTS

PR00401. SH2DOMAIN.

ProDom

PD000093. SH2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

PROSITE

PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

15461.

SOURCE

Search...

Entry information

Entry name

LCP2_HUMAN

Accession

Primary (citable) accession number: Q13094

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	November 4, 2008
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)