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Plastin-2 (L-plastin) (LC64P) (Lymphocyte cytosolic protein 1) (LCP-1)

 PLSL_HUMAN              Reviewed;         627 AA.
P13796; B2R613; B4DUA0; Q5TBN4;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 6.
12-SEP-2018, entry version 212.
RecName: Full=Plastin-2;
AltName: Full=L-plastin;
AltName: Full=LC64P;
AltName: Full=Lymphocyte cytosolic protein 1;
Short=LCP-1;
Name=LCP1; Synonyms=PLS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-533.
PubMed=2252891; DOI=10.1021/bi00488a017;
Zu Y., Shigesada K., Nishida E., Kubota I., Kohno M., Hanaoka M.,
Namba Y.;
"65-kilodalton protein phosphorylated by interleukin 2 stimulation
bears two putative actin-binding sites and two calcium-binding
sites.";
Biochemistry 29:8319-8324(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLU-533.
TISSUE=Amygdala, and Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLU-533.
TISSUE=Lymph, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-627 (ISOFORM 1), PARTIAL PROTEIN
SEQUENCE, AND VARIANT GLU-533.
PubMed=3211125; DOI=10.1128/MCB.8.11.4659;
Lin C.-S., Aebersold R.H., Kent S.B., Varma M., Leavitt J.;
"Molecular cloning and characterization of plastin, a human leukocyte
protein expressed in transformed human fibroblasts.";
Mol. Cell. Biol. 8:4659-4668(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-140 (ISOFORM 1), AND SEQUENCE
REVISION.
PubMed=2378651; DOI=10.1128/MCB.10.4.1818;
Lin C.-S., Aebersold R.H., Leavitt J.;
"Correction of the N-terminal sequences of the human plastin isoforms
by using anchored polymerase chain reaction: identification of a
potential calcium-binding domain.";
Mol. Cell. Biol. 10:1818-1821(1990).
[8]
PROTEIN SEQUENCE OF 2-14; 20-31; 184-192 AND 534-541, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-627.
PubMed=8428952;
Lin C.-S., Park T., Chen Z.P., Leavitt J.;
"Human plastin genes. Comparative gene structure, chromosome location,
and differential expression in normal and neoplastic cells.";
J. Biol. Chem. 268:2781-2792(1993).
[10]
PROTEIN SEQUENCE OF 264-283; 517-533 AND 593-609, AND VARIANT GLU-533.
PubMed=2111166; DOI=10.1021/bi00456a030;
Zu Y., Kohno M., Kubota I., Nishida E., Hanaoka M., Namba Y.;
"Characterization of interleukin 2 stimulated 65-kilodalton
phosphoprotein in human T cells.";
Biochemistry 29:1055-1062(1990).
[11]
PROTEIN SEQUENCE OF 590-611, AND TISSUE SPECIFICITY.
PubMed=3261603; DOI=10.1021/bi00410a037;
Matsushima K., Shiroo M., Kung H.F., Copeland T.D.;
"Purification and characterization of a cytosolic 65-kilodalton
phosphoprotein in human leukocytes whose phosphorylation is augmented
by stimulation with interleukin 1.";
Biochemistry 27:3765-3770(1988).
[12]
INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
TRANSLOCATION WITH BCL6.
PubMed=10469447;
DOI=10.1002/(SICI)1098-2264(199910)26:2<97::AID-GCC1>3.3.CO;2-0;
Galiegue-Zouitina S., Quief S., Hildebrand M.P., Denis C.,
Detourmignies L., Lai J.L., Kerckaert J.P.;
"Nonrandom fusion of L-plastin(LCP1) and LAZ3(BCL6) genes by
t(3;13)(q27;q14) chromosome translocation in two cases of B-cell non-
Hodgkin lymphoma.";
Genes Chromosomes Cancer 26:97-105(1999).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[14]
FUNCTION, ACTIN-BINDING, INTERACTION WITH ACTIN FIBERS, SUBCELLULAR
LOCATION, MUTAGENESIS OF SER-5, AND PHOSPHORYLATION AT SER-5.
PubMed=16636079; DOI=10.1242/jcs.02874;
Janji B., Giganti A., De Corte V., Catillon M., Bruyneel E., Lentz D.,
Plastino J., Gettemans J., Friederich E.;
"Phosphorylation on Ser5 increases the F-actin-binding activity of L-
plastin and promotes its targeting to sites of actin assembly in
cells.";
J. Cell Sci. 119:1947-1960(2006).
[15]
SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-5, PHOSPHORYLATION
AT SER-5, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17294403; DOI=10.1002/eji.200636320;
Wabnitz G.H., Koecher T., Lohneis P., Stober C., Konstandin M.H.,
Funk B., Sester U., Wilm M., Klemke M., Samstag Y.;
"Costimulation induced phosphorylation of L-plastin facilitates
surface transport of the T cell activation molecules CD69 and CD25.";
Eur. J. Immunol. 37:649-662(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; TYR-28; SER-30;
SER-257 AND SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-88; LYS-294;
LYS-297; LYS-361; LYS-472; LYS-542 AND LYS-579, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-257; SER-290;
THR-291; THR-353; SER-406 AND SER-474, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
STRUCTURE BY NMR OF 513-627.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the fourth CH domain from human L-plastin.";
Submitted (JUN-2006) to the PDB data bank.
[25]
VARIANT SER-608, CHARACTERIZATION OF VARIANT SER-608, FUNCTION, AND
INTERACTION WITH ACTIN.
PubMed=28493397; DOI=10.1002/humu.23246;
UK10K;
Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D.,
Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M.,
Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G.,
FitzPatrick D.R.;
"A recurrent de novo mutation in ACTG1 causes isolated ocular
coloboma.";
Hum. Mutat. 38:942-946(2017).
-!- FUNCTION: Actin-binding protein (PubMed:16636079, PubMed:17294403,
PubMed:28493397). Plays a role in the activation of T-cells in
response to costimulation through TCR/CD3 and CD2 or CD28
(PubMed:17294403). Modulates the cell surface expression of
IL2RA/CD25 and CD69 (PubMed:17294403).
{ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403,
ECO:0000269|PubMed:28493397}.
-!- SUBUNIT: Monomer. Interacts with AIF1 (By similarity). Interacts
with actin (PubMed:28493397). {ECO:0000250|UniProtKB:Q61233,
ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:28493397}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:16636079}. Cell junction
{ECO:0000269|PubMed:17294403}. Cell projection
{ECO:0000269|PubMed:16636079}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:Q61233, ECO:0000269|PubMed:16636079};
Peripheral membrane protein {ECO:0000250|UniProtKB:Q61233};
Cytoplasmic side {ECO:0000250|UniProtKB:Q61233}. Note=Relocalizes
to the immunological synapse between peripheral blood T-
lymphocytes and antibody-presenting cells in response to
costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403).
Associated with the actin cytoskeleton at membrane ruffles.
Relocalizes to actin-rich cell projections upon serine
phosphorylation (PubMed:16636079). {ECO:0000250|UniProtKB:Q61233,
ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13796-1; Sequence=Displayed;
Name=2;
IsoId=P13796-2; Sequence=VSP_056450, VSP_056451;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in intestinal microvilli, hair cell
stereocilia, and fibroblast filopodia, in spleen and other lymph
node-containing organs. Expressed in peripheral blood T-
lymphocytes, neutrophils, monocytes, B-lymphocytes, and myeloid
cells. {ECO:0000269|PubMed:3261603}.
-!- PTM: Phosphorylated on a serine residue in response to
costimulation through TCR/CD3 and CD2 or CD28. Serine
phosphorylation promotes association with the actin cytoskeleton
and targeting to peripheral cell projections.
{ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403}.
-!- DISEASE: Note=Chromosomal aberrations involving LCP1 is a cause of
B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation
t(3;13)(q27;q14), with BCL6. {ECO:0000269|PubMed:10469447}.
-!- DISEASE: Note=Defects in LCP1 has been found in a patient with
isolated coloboma, a defect of the eye characterized by the
absence of ocular structures due to abnormal morphogenesis of the
optic cup and stalk, and the fusion of the fetal fissure (optic
fissure). Isolated colobomas may be associated with an abnormally
small eye (microphthalmia) or small cornea.
{ECO:0000269|PubMed:28493397}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LCP1ID95.html";
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EMBL; J02923; AAA63236.1; -; mRNA.
EMBL; AK300556; BAG62262.1; -; mRNA.
EMBL; AK312393; BAG35310.1; -; mRNA.
EMBL; AL137141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08757.1; -; Genomic_DNA.
EMBL; BC007673; AAH07673.1; -; mRNA.
EMBL; BC010271; AAH10271.1; -; mRNA.
EMBL; M22300; AAB02845.1; -; mRNA.
EMBL; AH002870; AAA59529.1; -; Genomic_DNA.
EMBL; M34426; AAA36184.1; -; mRNA.
CCDS; CCDS9403.1; -. [P13796-1]
PIR; A35836; A35836.
RefSeq; NP_002289.2; NM_002298.4. [P13796-1]
RefSeq; XP_005266431.1; XM_005266374.1. [P13796-1]
UniGene; Hs.381099; -.
UniGene; Hs.658408; -.
PDB; 2D85; NMR; -; A=517-627.
PDB; 5JOJ; NMR; -; A=1-97.
PDB; 5JOL; NMR; -; A=1-82.
PDBsum; 2D85; -.
PDBsum; 5JOJ; -.
PDBsum; 5JOL; -.
ProteinModelPortal; P13796; -.
SMR; P13796; -.
BioGrid; 110128; 23.
DIP; DIP-34767N; -.
ELM; P13796; -.
IntAct; P13796; 9.
MINT; P13796; -.
STRING; 9606.ENSP00000315757; -.
iPTMnet; P13796; -.
PhosphoSitePlus; P13796; -.
SwissPalm; P13796; -.
BioMuta; LCP1; -.
DMDM; 308153685; -.
EPD; P13796; -.
MaxQB; P13796; -.
PaxDb; P13796; -.
PeptideAtlas; P13796; -.
PRIDE; P13796; -.
ProteomicsDB; 52986; -.
DNASU; 3936; -.
Ensembl; ENST00000323076; ENSP00000315757; ENSG00000136167. [P13796-1]
Ensembl; ENST00000398576; ENSP00000381581; ENSG00000136167. [P13796-1]
GeneID; 3936; -.
KEGG; hsa:3936; -.
UCSC; uc001vba.5; human. [P13796-1]
CTD; 3936; -.
DisGeNET; 3936; -.
EuPathDB; HostDB:ENSG00000136167.13; -.
GeneCards; LCP1; -.
H-InvDB; HIX0130592; -.
HGNC; HGNC:6528; LCP1.
HPA; CAB020673; -.
HPA; HPA019493; -.
MIM; 153430; gene.
neXtProt; NX_P13796; -.
OpenTargets; ENSG00000136167; -.
PharmGKB; PA30312; -.
eggNOG; KOG0046; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00390000005691; -.
HOGENOM; HOG000213447; -.
HOVERGEN; HBG003082; -.
InParanoid; P13796; -.
KO; K17276; -.
OMA; MFDECKD; -.
OrthoDB; EOG091G03YP; -.
PhylomeDB; P13796; -.
TreeFam; TF300680; -.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P13796; -.
ChiTaRS; LCP1; human.
EvolutionaryTrace; P13796; -.
GeneWiki; LCP1; -.
GenomeRNAi; 3936; -.
PRO; PR:P13796; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136167; Expressed in 176 organ(s), highest expression level in blood.
CleanEx; HS_LCP1; -.
ExpressionAtlas; P13796; baseline and differential.
Genevisible; P13796; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005884; C:actin filament; IMP:UniProtKB.
GO; GO:0032432; C:actin filament bundle; IMP:UniProtKB.
GO; GO:0030054; C:cell junction; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0030175; C:filopodium; IMP:UniProtKB.
GO; GO:0005925; C:focal adhesion; IMP:UniProtKB.
GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0002102; C:podosome; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IMP:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; NAS:UniProtKB.
GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IPI:ARUK-UCL.
GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0071803; P:positive regulation of podosome assembly; IMP:UniProtKB.
GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
GO; GO:0033157; P:regulation of intracellular protein transport; IDA:UniProtKB.
GO; GO:0002286; P:T cell activation involved in immune response; IDA:UniProtKB.
CDD; cd00014; CH; 2.
CDD; cd00051; EFh; 1.
Gene3D; 1.10.418.10; -; 4.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF00307; CH; 4.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00033; CH; 4.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF47576; SSF47576; 1.
PROSITE; PS00019; ACTININ_1; 2.
PROSITE; PS00020; ACTININ_2; 2.
PROSITE; PS50021; CH; 4.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Calcium; Cell junction; Cell membrane; Cell projection;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Disease mutation; Membrane; Metal-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 627 Plastin-2.
/FTId=PRO_0000073743.
DOMAIN 9 44 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 49 84 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 120 236 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 264 375 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 394 503 Calponin-homology (CH) 3.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 515 624 Calponin-homology (CH) 4.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
CA_BIND 22 33 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 62 73 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 106 379 Actin-binding 1.
REGION 380 624 Actin-binding 2.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.8}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16636079,
ECO:0000269|PubMed:17294403}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 28 28 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 88 88 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 124 124 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 291 291 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 294 294 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 297 297 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 353 353 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 361 361 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 472 472 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 579 579 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 25 MARGSVSDEEMMELREAFAKVDTDG -> MCAEDGDSKFSM
SISMNSPFLEILH (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056450.
VAR_SEQ 26 456 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056451.
VARIANT 24 24 D -> E.
/FTId=VAR_001371.
VARIANT 533 533 K -> E (in dbSNP:rs4941543).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2111166,
ECO:0000269|PubMed:2252891,
ECO:0000269|PubMed:3211125}.
/FTId=VAR_024398.
VARIANT 544 544 P -> A (in dbSNP:rs17067725).
/FTId=VAR_030826.
VARIANT 608 608 N -> S (found in a patient with isolated
coloboma; increases interaction with
actin). {ECO:0000269|PubMed:28493397}.
/FTId=VAR_079850.
MUTAGEN 5 5 S->A: Abolishes phosphorylation and
reduces the cell surface expression of
CD69 and IL2RA. Reduces association with
the actin cytoskeleton.
{ECO:0000269|PubMed:16636079,
ECO:0000269|PubMed:17294403}.
MUTAGEN 5 5 S->E: Promotes association with the actin
cytoskeleton.
{ECO:0000269|PubMed:16636079,
ECO:0000269|PubMed:17294403}.
CONFLICT 611 611 M -> T (in Ref. 11; AA sequence).
{ECO:0000305}.
HELIX 8 21 {ECO:0000244|PDB:5JOJ}.
STRAND 27 29 {ECO:0000244|PDB:5JOJ}.
HELIX 31 40 {ECO:0000244|PDB:5JOJ}.
HELIX 47 59 {ECO:0000244|PDB:5JOJ}.
STRAND 61 63 {ECO:0000244|PDB:5JOL}.
TURN 64 66 {ECO:0000244|PDB:5JOL}.
HELIX 71 80 {ECO:0000244|PDB:5JOJ}.
HELIX 85 94 {ECO:0000244|PDB:5JOJ}.
HELIX 520 532 {ECO:0000244|PDB:2D85}.
HELIX 545 548 {ECO:0000244|PDB:2D85}.
HELIX 550 559 {ECO:0000244|PDB:2D85}.
TURN 566 568 {ECO:0000244|PDB:2D85}.
HELIX 576 593 {ECO:0000244|PDB:2D85}.
HELIX 601 604 {ECO:0000244|PDB:2D85}.
TURN 605 607 {ECO:0000244|PDB:2D85}.
HELIX 609 612 {ECO:0000244|PDB:2D85}.
HELIX 615 620 {ECO:0000244|PDB:2D85}.
TURN 621 623 {ECO:0000244|PDB:2D85}.
SEQUENCE 627 AA; 70288 MW; 668E4AA6A3FC7B58 CRC64;
MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV REITENLMAT
GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE
EEKYAFVNWI NKALENDPDC RHVIPMNPNT NDLFNAVGDG IVLCKMINLS VPDTIDERTI
NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI
ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY
HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP
KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL
SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVELGKNQ AKFSLVGIGG
QDLNEGNRTL TLALIWQLMR RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAKKSSSISS
FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL
PEDLVEVNPK MVMTVFACLM GKGMKRV


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