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Plectin (PCN) (PLTN) (Plectin-1) (Plectin-6)

 PLEC_MOUSE              Reviewed;        4691 AA.
Q9QXS1; E9QN87; Q6S384; Q6S389; Q6S394; Q9CS65; Q9QUT2; Q9QXQ8;
Q9QXQ9; Q9QXR0; Q9QXR1; Q9QXR2; Q9QXR3; Q9QXR4; Q9QXR5; Q9QXR6;
Q9QXR7; Q9QXR8; Q9QXR9; Q9QXS0; Q9QXS2; Q9QXS3;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 3.
18-JUL-2018, entry version 177.
RecName: Full=Plectin;
Short=PCN;
Short=PLTN;
AltName: Full=Plectin-1;
AltName: Full=Plectin-6;
Name=Plec; Synonyms=Plec1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=14672974; DOI=10.1101/gr.1225204;
Zhang T., Haws P., Wu Q.;
"Multiple variable first exons: a mechanism for cell- and tissue-
specific gene regulation.";
Genome Res. 14:79-89(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-964, ALTERNATIVE SPLICING, AND TISSUE
SPECIFICITY.
TISSUE=Brain, Embryo, Heart, Kidney, Skeletal muscle, and Testis;
PubMed=10556294; DOI=10.1093/hmg/8.13.2461;
Fuchs P., Zoerer M., Rezniczek G.A., Spazierer D., Oehler S.,
Castanon M.J., Hauptmann R., Wiche G.;
"Unusual 5' transcript complexity of plectin isoforms: novel tissue-
specific exons modulate actin binding activity.";
Hum. Mol. Genet. 8:2461-2472(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-812.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
PROTEIN SEQUENCE OF 629-633, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
INTERACTION WITH FER.
PubMed=12200133; DOI=10.1016/S0006-291X(02)02007-7;
Lunter P.C., Wiche G.;
"Direct binding of plectin to Fer kinase and negative regulation of
its catalytic activity.";
Biochem. Biophys. Res. Commun. 296:904-910(2002).
[7]
INTERACTION WITH SYNE3.
PubMed=16330710; DOI=10.1083/jcb.200506083;
Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N.,
Janssen H., van den Bout I., Raymond K., Sonnenberg A.;
"Nesprin-3, a novel outer nuclear membrane protein, associates with
the cytoskeletal linker protein plectin.";
J. Cell Biol. 171:799-810(2005).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2788; TYR-3040;
TYR-3369; TYR-3797 AND TYR-4622, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT TYR-26 (ISOFORM PLEC-1A), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-823, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4633, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[14]
INTERACTION WITH TOR1A.
PubMed=18827015; DOI=10.1242/jcs.029454;
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D.,
Li Y., Wiche G., Sonnenberg A., Breakefield X.O.;
"TorsinA binds the KASH domain of nesprins and participates in linkage
between nuclear envelope and cytoskeleton.";
J. Cell Sci. 121:3476-3486(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4393 AND SER-4396,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4389 AND SER-4393,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728; SER-1055; THR-4037;
SER-4389; SER-4391; SER-4392; SER-4393; SER-4396; SER-4620; SER-4625;
SER-4629; THR-4630; SER-4633 AND SER-4649, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
INTERACTION WITH DST.
PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010;
Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F.,
Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G.,
Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L.,
Borradori L.;
"BPAG1 isoform-b: complex distribution pattern in striated and heart
muscle and association with plectin and alpha-actinin.";
Exp. Cell Res. 316:297-313(2010).
[20]
TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK;
BFSP1; BFSP2; ANK2; PRX; VIM AND SPECTRIN.
PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J.,
Rao P.V.;
"Periaxin is required for hexagonal geometry and membrane organization
of mature lens fibers.";
Dev. Biol. 357:179-190(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1733; LYS-2644 AND LYS-3060,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[22]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4634 AND ARG-4647, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 181-417, AND INTERACTION
WITH VIM.
PubMed=15128297; DOI=10.1111/j.1432-1033.2004.04095.x;
Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.;
"Actin-binding domain of mouse plectin. Crystal structure and binding
to vimentin.";
Eur. J. Biochem. 271:1873-1884(2004).
-!- FUNCTION: Interlinks intermediate filaments with microtubules and
microfilaments and anchors intermediate filaments to desmosomes or
hemidesmosomes. May be involved not only in the cross-linking and
stabilization of cytoskeletal intermediate filaments network, but
also in the regulation of their dynamics.
-!- SUBUNIT: Homodimer or homotetramer (By similarity). Interacts (via
actin-binding domain) with SYNE3 (PubMed:16330710). Interacts (via
calponin-homology (CH) 1 domain) with VIM (via rod region)
(PubMed:15128297). Interacts (via N-terminus) with DST isoform 2
(via N-terminus) (PubMed:19932097). Interacts with FER
(PubMed:12200133). Interacts with TOR1A (PubMed:18827015).
Interacts with ANK3 (By similarity). Identified in complexes that
contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and
spectrin (PubMed:21745462). {ECO:0000250,
ECO:0000250|UniProtKB:P30427, ECO:0000269|PubMed:12200133,
ECO:0000269|PubMed:15128297, ECO:0000269|PubMed:16330710,
ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19932097,
ECO:0000269|PubMed:21745462}.
-!- INTERACTION:
P62158:CALM3 (xeno); NbExp=11; IntAct=EBI-16145475, EBI-397435;
P16144:ITGB4 (xeno); NbExp=4; IntAct=EBI-16145475, EBI-948678;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
hemidesmosome {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=16;
Name=PLEC-1,2A;
IsoId=Q9QXS1-1; Sequence=Displayed;
Name=PLEC-1;
IsoId=Q9QXS1-2; Sequence=VSP_005048;
Name=PLEC-1A;
IsoId=Q9QXS1-3; Sequence=VSP_005036, VSP_005045, VSP_005048;
Note=Contains a phosphoserine at position 21. Contains a
phosphotyrosine at position 26. {ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:19131326, ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079};
Name=PLEC-1B,2A;
IsoId=Q9QXS1-4; Sequence=VSP_005037, VSP_005045;
Name=PLEC-1B;
IsoId=Q9QXS1-5; Sequence=VSP_005037, VSP_005045, VSP_005048;
Name=PLEC-0,1C;
IsoId=Q9QXS1-6; Sequence=VSP_005039, VSP_005047, VSP_005048;
Name=PLEC-0,1C,2A;
IsoId=Q9QXS1-7; Sequence=VSP_005039, VSP_005047;
Name=PLEC-0,1C,2A,3A;
IsoId=Q9QXS1-8; Sequence=VSP_005039, VSP_005047, VSP_005049;
Name=PLEC-1D,2A;
IsoId=Q9QXS1-9; Sequence=VSP_005032, VSP_005041;
Name=PLEC-1D;
IsoId=Q9QXS1-10; Sequence=VSP_005032, VSP_005041, VSP_005048;
Name=PLEC-1E,2A;
IsoId=Q9QXS1-11; Sequence=VSP_005033, VSP_005042;
Name=PLEC-1E;
IsoId=Q9QXS1-12; Sequence=VSP_005033, VSP_005042, VSP_005048;
Name=PLEC-1F;
IsoId=Q9QXS1-13; Sequence=VSP_005034, VSP_005043, VSP_005048;
Name=PLEC-1G;
IsoId=Q9QXS1-14; Sequence=VSP_005038, VSP_005046, VSP_005048;
Name=PLEC-1H;
IsoId=Q9QXS1-15; Sequence=VSP_005040;
Name=PLEC-1I;
IsoId=Q9QXS1-16; Sequence=VSP_005035, VSP_005044;
-!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein
level) (PubMed:21745462). Expressed at high levels in lung, brain,
small intestine, muscle, heart and skin with lower levels found in
kidney, liver, uterus, spleen and salivary gland
(PubMed:10556294). {ECO:0000269|PubMed:10556294,
ECO:0000269|PubMed:21745462}.
-!- DOMAIN: The N-terminus interacts with actin, the C-terminus with
vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the
N- and the C-terminus can bind integrin beta-4.
-!- PTM: Phosphorylated by CDK1; regulates dissociation from
intermediate filaments during mitosis. Isoform PLEC-1A is
phosphorylated on Ser-21. Isoform PLEC-1A is phosphorylated on
Tyr-26.
-!- SIMILARITY: Belongs to the plakin or cytolinker family.
{ECO:0000305}.
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EMBL; AY480033; AAR95666.1; -; mRNA.
EMBL; AY480038; AAR95671.1; -; mRNA.
EMBL; AY480043; AAR95676.1; -; mRNA.
EMBL; AC110211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF188006; AAF18066.1; -; mRNA.
EMBL; AF188007; AAF18067.1; -; mRNA.
EMBL; AF188008; AAF18068.1; -; mRNA.
EMBL; AF188009; AAF18069.1; -; mRNA.
EMBL; AF188010; AAF18070.1; -; mRNA.
EMBL; AF188011; AAF18071.1; -; mRNA.
EMBL; AF188012; AAF18072.1; -; mRNA.
EMBL; AF188013; AAF18073.1; -; mRNA.
EMBL; AF188014; AAF18074.1; -; mRNA.
EMBL; AF188015; AAF18075.1; -; mRNA.
EMBL; AF188016; AAF18076.1; -; mRNA.
EMBL; AF188017; AAF18077.1; -; mRNA.
EMBL; AF188018; AAF18078.1; -; mRNA.
EMBL; AF188019; AAF18079.1; -; mRNA.
EMBL; AF188020; AAF18080.1; -; mRNA.
EMBL; AF188021; AAF18081.1; -; mRNA.
EMBL; AF188022; AAF18082.1; -; mRNA.
EMBL; AF188023; AAF18083.1; -; mRNA.
EMBL; AK017743; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS37113.1; -. [Q9QXS1-13]
CCDS; CCDS37114.1; -. [Q9QXS1-2]
CCDS; CCDS37115.1; -. [Q9QXS1-14]
CCDS; CCDS37116.1; -. [Q9QXS1-3]
CCDS; CCDS49644.1; -. [Q9QXS1-5]
CCDS; CCDS49645.1; -. [Q9QXS1-4]
CCDS; CCDS49646.1; -. [Q9QXS1-10]
CCDS; CCDS49647.1; -. [Q9QXS1-1]
CCDS; CCDS49648.1; -. [Q9QXS1-12]
CCDS; CCDS49649.1; -. [Q9QXS1-8]
PIR; D59404; D59404.
RefSeq; NP_001157012.1; NM_001163540.1. [Q9QXS1-1]
RefSeq; NP_001157014.1; NM_001163542.1. [Q9QXS1-8]
RefSeq; NP_001157021.1; NM_001163549.1. [Q9QXS1-4]
RefSeq; NP_001157675.1; NM_001164203.1.
RefSeq; NP_035247.2; NM_011117.2. [Q9QXS1-6]
RefSeq; NP_958791.2; NM_201389.2. [Q9QXS1-2]
RefSeq; NP_958796.2; NM_201394.2. [Q9QXS1-3]
UniGene; Mm.234912; -.
PDB; 1SH5; X-ray; 2.00 A; A/B=181-417.
PDB; 1SH6; X-ray; 2.00 A; A=181-417.
PDB; 4Q57; X-ray; 1.80 A; B=181-411.
PDBsum; 1SH5; -.
PDBsum; 1SH6; -.
PDBsum; 4Q57; -.
ProteinModelPortal; Q9QXS1; -.
SMR; Q9QXS1; -.
BioGrid; 202243; 13.
DIP; DIP-32004N; -.
IntAct; Q9QXS1; 9.
MINT; Q9QXS1; -.
STRING; 10090.ENSMUSP00000073124; -.
iPTMnet; Q9QXS1; -.
PhosphoSitePlus; Q9QXS1; -.
SwissPalm; Q9QXS1; -.
PaxDb; Q9QXS1; -.
PeptideAtlas; Q9QXS1; -.
PRIDE; Q9QXS1; -.
Ensembl; ENSMUST00000023226; ENSMUSP00000023226; ENSMUSG00000022565. [Q9QXS1-3]
Ensembl; ENSMUST00000054449; ENSMUSP00000057158; ENSMUSG00000022565. [Q9QXS1-4]
Ensembl; ENSMUST00000071869; ENSMUSP00000071765; ENSMUSG00000022565. [Q9QXS1-12]
Ensembl; ENSMUST00000072692; ENSMUSP00000072478; ENSMUSG00000022565. [Q9QXS1-14]
Ensembl; ENSMUST00000073418; ENSMUSP00000073124; ENSMUSG00000022565. [Q9QXS1-1]
Ensembl; ENSMUST00000074834; ENSMUSP00000074383; ENSMUSG00000022565. [Q9QXS1-13]
Ensembl; ENSMUST00000076442; ENSMUSP00000075772; ENSMUSG00000022565. [Q9QXS1-2]
Ensembl; ENSMUST00000089610; ENSMUSP00000087037; ENSMUSG00000022565. [Q9QXS1-8]
Ensembl; ENSMUST00000169108; ENSMUSP00000126068; ENSMUSG00000022565. [Q9QXS1-10]
Ensembl; ENSMUST00000169714; ENSMUSP00000126526; ENSMUSG00000022565. [Q9QXS1-5]
GeneID; 18810; -.
KEGG; mmu:18810; -.
UCSC; uc007wir.2; mouse. [Q9QXS1-3]
UCSC; uc007wis.2; mouse. [Q9QXS1-14]
UCSC; uc007wit.2; mouse. [Q9QXS1-1]
UCSC; uc007wiu.2; mouse. [Q9QXS1-5]
UCSC; uc007wiv.2; mouse. [Q9QXS1-10]
UCSC; uc007wiw.2; mouse. [Q9QXS1-2]
UCSC; uc007wiz.2; mouse. [Q9QXS1-12]
UCSC; uc007wja.2; mouse. [Q9QXS1-13]
UCSC; uc007wjb.2; mouse. [Q9QXS1-6]
UCSC; uc007wjd.2; mouse. [Q9QXS1-4]
UCSC; uc011zuq.1; mouse. [Q9QXS1-8]
CTD; 5339; -.
MGI; MGI:1277961; Plec.
eggNOG; KOG0516; Eukaryota.
eggNOG; KOG3344; Eukaryota.
eggNOG; COG5045; LUCA.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00760000119163; -.
HOVERGEN; HBG053616; -.
InParanoid; Q9QXS1; -.
KO; K10388; -.
OMA; SEYFTAE; -.
OrthoDB; EOG091G0012; -.
Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-MMU-446107; Type I hemidesmosome assembly.
EvolutionaryTrace; Q9QXS1; -.
PRO; PR:Q9QXS1; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022565; -.
CleanEx; MM_PLEC1; -.
ExpressionAtlas; Q9QXS1; baseline and differential.
Genevisible; Q9QXS1; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0043292; C:contractile fiber; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0030056; C:hemidesmosome; ISS:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
GO; GO:0016528; C:sarcoplasm; ISO:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0030506; F:ankyrin binding; ISO:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
GO; GO:0008307; F:structural constituent of muscle; ISO:MGI.
GO; GO:0031581; P:hemidesmosome assembly; ISS:UniProtKB.
GO; GO:0007584; P:response to nutrient; ISO:MGI.
CDD; cd00014; CH; 2.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 3.90.1290.10; -; 6.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR035915; Plakin_repeat_sf.
InterPro; IPR030269; Plectin.
InterPro; IPR001101; Plectin_repeat.
InterPro; IPR005326; S10_plectin_N.
InterPro; IPR001452; SH3_domain.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR036388; WH-like_DNA-bd_sf.
PANTHER; PTHR44968:SF2; PTHR44968:SF2; 1.
Pfam; PF00307; CH; 2.
Pfam; PF00681; Plectin; 18.
Pfam; PF03501; S10_plectin; 1.
SMART; SM00033; CH; 2.
SMART; SM00250; PLEC; 35.
SMART; SM00150; SPEC; 6.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF75399; SSF75399; 8.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Cell junction; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Methylation; Phosphoprotein;
Reference proteome; Repeat; SH3 domain.
CHAIN 1 4691 Plectin.
/FTId=PRO_0000078136.
DOMAIN 185 293 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 306 411 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 653 727 Spectrin 1.
REPEAT 748 832 Spectrin 2.
REPEAT 845 938 Spectrin 3.
DOMAIN 949 1006 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REPEAT 1323 1423 Spectrin 4.
REPEAT 2795 2832 Plectin 1.
REPEAT 2833 2870 Plectin 2.
REPEAT 2871 2908 Plectin 3.
REPEAT 2909 2946 Plectin 4.
REPEAT 2947 2984 Plectin 5.
REPEAT 2988 3022 Plectin 6.
REPEAT 3123 3160 Plectin 7.
REPEAT 3161 3198 Plectin 8.
REPEAT 3199 3236 Plectin 9.
REPEAT 3237 3274 Plectin 10.
REPEAT 3275 3312 Plectin 11.
REPEAT 3315 3350 Plectin 12.
REPEAT 3492 3529 Plectin 13.
REPEAT 3530 3567 Plectin 14.
REPEAT 3568 3605 Plectin 15.
REPEAT 3606 3643 Plectin 16.
REPEAT 3647 3681 Plectin 17.
REPEAT 3827 3864 Plectin 18.
REPEAT 3865 3902 Plectin 19.
REPEAT 3903 3940 Plectin 20.
REPEAT 3941 3978 Plectin 21.
REPEAT 3982 4015 Plectin 22.
REPEAT 4070 4107 Plectin 23.
REPEAT 4108 4145 Plectin 24.
REPEAT 4146 4183 Plectin 25.
REPEAT 4184 4221 Plectin 26.
REPEAT 4225 4259 Plectin 27.
REPEAT 4272 4312 Plectin 28.
REPEAT 4415 4452 Plectin 29.
REPEAT 4453 4490 Plectin 30.
REPEAT 4491 4528 Plectin 31.
REPEAT 4529 4566 Plectin 32.
REPEAT 4567 4604 Plectin 33.
REGION 1 1478 Globular 1. {ECO:0000250}.
REGION 181 411 Actin-binding.
REGION 1479 2762 Central fibrous rod domain.
{ECO:0000250}.
REGION 2763 4691 Globular 2. {ECO:0000250}.
REGION 4257 4307 Binding to intermediate filaments.
{ECO:0000250}.
REGION 4632 4647 4 X 4 AA tandem repeats of G-S-R-X.
COILED 1477 1697 {ECO:0000255}.
COILED 1729 2764 {ECO:0000255}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 823 823 Phosphothreonine.
{ECO:0000244|PubMed:17208939}.
MOD_RES 1055 1055 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1443 1443 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 1729 1729 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 1733 1733 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2639 2639 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 2644 2644 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2781 2781 Phosphoserine.
{ECO:0000250|UniProtKB:P30427}.
MOD_RES 2788 2788 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 2809 2809 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 2893 2893 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 3040 3040 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 3060 3060 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 3098 3098 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 3369 3369 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 3427 3427 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 3792 3792 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 3797 3797 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 4037 4037 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4061 4061 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4389 4389 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 4391 4391 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4392 4392 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4393 4393 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 4396 4396 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 4397 4397 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4398 4398 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4399 4399 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4400 4400 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4403 4403 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4413 4413 Phosphoserine.
{ECO:0000250|UniProtKB:P30427}.
MOD_RES 4418 4418 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4546 4546 Phosphothreonine; by CDK1.
{ECO:0000250|UniProtKB:Q9JI55}.
MOD_RES 4614 4614 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4620 4620 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4622 4622 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 4623 4623 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
MOD_RES 4625 4625 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4629 4629 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4630 4630 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4633 4633 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 4634 4634 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 4647 4647 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 4649 4649 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4682 4682 Phosphoserine.
{ECO:0000250|UniProtKB:Q15149}.
VAR_SEQ 1 242 Missing (in isoform PLEC-1H).
{ECO:0000305}.
/FTId=VSP_005040.
VAR_SEQ 1 66 MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLHPHVP
GVTNLQVMRAMASLKARGLVRETFA -> MSGEDSEVRPVA
VAEGSSNGSSGSPSPGDTLPWNLGKTQRSRRSGGGSVGNGS
VLDPAERAVIRIA (in isoform PLEC-0,1C,
isoform PLEC-0,1C,2A,3A and isoform PLEC-
0,1C,2A). {ECO:0000305}.
/FTId=VSP_005039.
VAR_SEQ 1 44 MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLHPHVP
GVT -> MAGTWAAKGVFTSQREVLLERPCWLDGGCEQVRR
GYLYGQLCCV (in isoform PLEC-1G).
{ECO:0000305}.
/FTId=VSP_005038.
VAR_SEQ 1 37 MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH ->
MSQHRLRVPEPEGLGSKRTSSEDNLYLAVLRASEGKK (in
isoform PLEC-1A). {ECO:0000305}.
/FTId=VSP_005036.
VAR_SEQ 1 37 MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH ->
MEPSGSLFPSLVVVGHVVTLAAVWHWRKGHRQAKDEQ (in
isoform PLEC-1B and isoform PLEC-1B,2A).
{ECO:0000305}.
/FTId=VSP_005037.
VAR_SEQ 1 33 MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRP -> MNET
VCRRKLSPSGSTNTLSRLRGTSVTCTKTS (in isoform
PLEC-1I). {ECO:0000305}.
/FTId=VSP_005035.
VAR_SEQ 1 28 MVAGMLMPLDRLRAIYEVLFREGVMVAK -> MAHLLTSGP
PPDEQDFIQAYEEVREKYK (in isoform PLEC-1F).
{ECO:0000305}.
/FTId=VSP_005034.
VAR_SEQ 1 15 MVAGMLMPLDRLRAI -> MDPSRAIQHEISSLK (in
isoform PLEC-1E and isoform PLEC-1E,2A).
{ECO:0000305}.
/FTId=VSP_005033.
VAR_SEQ 1 5 MVAGM -> MKIVP (in isoform PLEC-1D and
isoform PLEC-1D,2A). {ECO:0000305}.
/FTId=VSP_005032.
VAR_SEQ 6 180 Missing (in isoform PLEC-1D and isoform
PLEC-1D,2A). {ECO:0000305}.
/FTId=VSP_005041.
VAR_SEQ 16 180 Missing (in isoform PLEC-1E and isoform
PLEC-1E,2A). {ECO:0000305}.
/FTId=VSP_005042.
VAR_SEQ 29 180 Missing (in isoform PLEC-1F).
{ECO:0000305}.
/FTId=VSP_005043.
VAR_SEQ 34 180 Missing (in isoform PLEC-1I).
{ECO:0000305}.
/FTId=VSP_005044.
VAR_SEQ 38 180 Missing (in isoform PLEC-1A, isoform
PLEC-1B and isoform PLEC-1B,2A).
{ECO:0000305}.
/FTId=VSP_005045.
VAR_SEQ 45 180 Missing (in isoform PLEC-1G).
{ECO:0000305}.
/FTId=VSP_005046.
VAR_SEQ 67 180 Missing (in isoform PLEC-0,1C, isoform
PLEC-0,1C,2A and isoform PLEC-
0,1C,2A,3A). {ECO:0000305}.
/FTId=VSP_005047.
VAR_SEQ 202 206 Missing (in isoform PLEC-1, isoform PLEC-
1A, isoform PLEC-1B, isoform PLEC-1D,
isoform PLEC-1E, isoform PLEC-1G, isoform
PLEC-1F and isoform PLEC-0,1C).
{ECO:0000305}.
/FTId=VSP_005048.
VAR_SEQ 239 239 E -> ERDVIRSVRLPRE (in isoform PLEC-
0,1C,2A,3A). {ECO:0000305}.
/FTId=VSP_005049.
CONFLICT 2535 2535 A -> V (in Ref. 1; AAR95666/AAR95671/
AAR95676). {ECO:0000305}.
HELIX 181 199 {ECO:0000244|PDB:4Q57}.
HELIX 205 207 {ECO:0000244|PDB:1SH5}.
TURN 214 220 {ECO:0000244|PDB:4Q57}.
HELIX 222 232 {ECO:0000244|PDB:4Q57}.
HELIX 244 260 {ECO:0000244|PDB:4Q57}.
HELIX 270 274 {ECO:0000244|PDB:4Q57}.
HELIX 278 292 {ECO:0000244|PDB:4Q57}.
HELIX 294 296 {ECO:0000244|PDB:4Q57}.
HELIX 308 319 {ECO:0000244|PDB:4Q57}.
TURN 320 322 {ECO:0000244|PDB:4Q57}.
HELIX 333 335 {ECO:0000244|PDB:4Q57}.
HELIX 339 348 {ECO:0000244|PDB:4Q57}.
HELIX 350 352 {ECO:0000244|PDB:4Q57}.
HELIX 355 360 {ECO:0000244|PDB:4Q57}.
HELIX 363 378 {ECO:0000244|PDB:4Q57}.
HELIX 386 389 {ECO:0000244|PDB:4Q57}.
STRAND 390 393 {ECO:0000244|PDB:4Q57}.
HELIX 396 408 {ECO:0000244|PDB:4Q57}.
SEQUENCE 4691 AA; 534188 MW; 91A09EC8181137D1 CRC64;
MVAGMLMPLD RLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLKARGL
VRETFAWCHF YWYLTNEGID HLRQYLHLPP EIVPASLQRV RRPVAMVIPA RRRSPHVQTM
QGPLGCPPKR GPLPAEDPAR EERQVYRRKE REEGAPETPV VSATTVGTLA RPGPEPAPAT
DERDRVQKKT FTKWVNKHLI KHWRAEAQRH ISDLYEDLRD GHNLISLLEV LSGDSLPREK
GRMRFHKLQN VQIALDYLRH RQVKLVNIRN DDIADGNPKL TLGLIWTIIL HFQISDIQVS
GQSEDMTAKE KLLLWSQRMV EGYQGLRCDN FTTSWRDGRL FNAIIHRHKP MLIDMNKVYR
QTNLENLDQA FSVAERDLGV TRLLDPEDVD VPQPDEKSII TYVSSLYDAM PRVPGAQDGV
RANELQLRWQ EYRELVLLLL QWIRHHTAAF EERKFPSSFE EIEILWCQFL KFKETELPAK
EADKNRSKVI YQSLEGAVQA GQLKIPPGYH PLDVEKEWGK LHVAILEREK QLRSEFERLE
CLQRIVSKLQ MEAGLCEEQL NQADALLQSD IRLLASGKVA QRAGEVERDL DKADGMIRLL
FNDVQTLKDG RHPQGEQMYR RVYRLHERLV AIRTEYNLRL KAGVGAPVTQ VTLQSTQRRP
ELEDSTLRYL QDLLAWVEEN QRRIDSAEWG VDLPSVEAQL GSHRGMHQSI EEFRAKIERA
RNDESQLSPA TRGAYRDCLG RLDLQYAKLL NSSKARLRSL ESLHGFVAAA TKELMWLNEK
EEEEVGFDWS DRNTNMAAKK ESYSALMREL EMKEKKIKEI QNTGDRLLRE DHPARPTVES
FQAALQTQWS WMLQLCCCIE AHLKENTAYF QFFSDVREAE EQLQKLQETL RRKYSCDRTI
TVTRLEDLLQ DAQDEKEQLN EYKGHLSGLA KRAKAIVQLK PRNPAHPVRG HVPLIAVCDY
KQVEVTVHKG DQCQLVGPAQ PSHWKVLSGS SSEAAVPSVC FLVPPPNQEA QEAVARLEAQ
HQALVTLWHQ LHVDMKSLLA WQSLSRDIQL IRSWSLVTFR TLKPEEQRQA LRNLELHYQA
FLRDSQDAGG FGPEDRLVAE REYGSCSRHY QQLLQSLEQG EQEESRCQRC ISELKDIRLQ
LEACETRTVH RLRLPLDKDP ARECAQRIAE QQKAQAEVEG LGKGVARLSA EAEKVLALPE
PSPAAPTLRS ELELTLGKLE QVRSLSAIYL EKLKTISLVI RSTQGAEEVL KTHEEQLKEA
QAVPATLQEL EATKASLKKL RAQAEAQQPV FNTLRDELRG AQEVGERLQQ RHGERDVEVE
RWRERVTQLL ERWQAVLAQT DVRQRELEQL GRQLRYYRES ADPLSAWLQD AKRRQEQIQA
VPIANCQAAR EQLRQEKALL EEIERHGEKV EECQKFAKQY INAIKDYELQ LITYKAQLEP
VASPAKKPKV QSGSESVIQE YVDLRTRYSE LTTLTSQYIK FISETLRRME EEERLAEQQR
AEERERLAEV EAALEKQRQL AEAHAQAKAQ AELEAQELQR RMQEEVARRE EAAVDAQQQK
RSIQEELQHL RQSSEAEIQA KAQQVEAAER SRMRIEEEIR VVRLQLETTE RQRGGAEGEL
QALRARAEEA EAQKRQAQEE AERLRRQVQD ESQRKRQAEA ELALRVKAEA EAAREKQRAL
QALDELRLQA EEAERRLRQA EAERARQVQV ALETAQRSAE VELQSKRASF AEKTAQLERT
LQEEHVTVAQ LREEAERRAQ QQAEAERARE EAERELERWQ LKANEALRLR LQAEEVAQQK
SLAQADAEKQ KEEAEREARR RGKAEEQAVR QRELAEQELE KQRQLAEGTA QQRLAAEQEL
IRLRAETEQG EQQRQLLEEE LARLQHEATA ATQKRQELEA ELAKVRAEME VLLASKARAE
EESRSTSEKS KQRLEAEAGR FRELAEEAAR LRALAEEAKR QRQLAEEDAA RQRAEAERVL
TEKLAAISEA TRLKTEAEIA LKEKEAENER LRRLAEDEAF QRRRLEEQAA LHKADIEERL
AQLRKASESE LERQKGLVED TLRQRRQVEE EIMALKVSFE KAAAGKAELE LELGRIRSNA
EDTMRSKEQA ELEAARQRQL AAEEEQRRRE AEERVQRSLA AEEEAARQRK VALEEVERLK
AKVEEARRLR ERAEQESARQ LQLAQEAAQK RLQAEEKAHA FVVQQREEEL QQTLQQEQNM
LDRLRSEAEA ARRAAEEAEE AREQAEREAA QSRKQVEEAE RLKQSAEEQA QAQAQAQAAA
EKLRKEAEQE AARRAQAEQA ALKQKQAADA EMEKHKKFAE QTLRQKAQVE QELTTLRLQL
EETDHQKSIL DEELQRLKAE VTEAARQRSQ VEEELFSVRV QMEELGKLKA RIEAENRALI
LRDKDNTQRF LEEEAEKMKQ VAEEAARLSV AAQEAARLRQ LAEEDLAQQR ALAEKMLKEK
MQAVQEATRL KAEAELLQQQ KELAQEQARR LQEDKEQMAQ QLVEETQGFQ RTLEAERQRQ
LEMSAEAERL KLRMAEMSRA QARAEEDAQR FRKQAEEIGE KLHRTELATQ EKVTLVQTLE
IQRQQSDHDA ERLREAIAEL EREKEKLKQE AKLLQLKSEE MQTVQQEQIL QETQALQKSF
LSEKDSLLQR ERFIEQEKAK LEQLFQDEVA KAKQLREEQQ RQQQQMEQEK QELMASMEEA
RRRQREAEEG VRRKQEELQH LEQQRQQQEK LLAEENQRLR ERLQRLEEEH RAALAHSEIA
TTQAASTKAL PNGRDAPDGP SVEAEPEYTF EGLRQKVPAQ QLQEAGILSQ EELQRLAQGH
TTVAELTQRE DVYRYLKGRS SIAGLLLKPT NEKLSVYTAL QRQLLSPGTA LILLEAQAAS
GFLLDPVRNR RLTVNEAVKE GVVGPELHHK LLSAERAVTG YKDPYTGEQI SLFQAMKKDL
IVRDHGVRLL EAQIATGGII DPVHSHRVPV DVAYKRGYFD EEMNRILSDP SDDTKGFFDP
NTHENLTYLQ LLERCVEDPE TGLRLLPLTD KAAKGGELVY TDTEARDVFE KATVSAPFGK
FQGRTVTIWE IINSEYFTAE QRRDLLQQFR TGHITVEKII KIVITVVEEH ERKGQLCFEG
LRALVPAAEL LDSGVISHEL YQQLQRGERS VREVAEADSV RQALRGTNVI AGVWLEEAGQ
KLSIYEALKK DLLQPEVAVA LLEAQAGTGH IIDPATSARL TVDEAVRAGL VGPELHEKLL
SAEKAVTGYR DPYSGQSVSL FQALKKGLIP REQGLRLLDA QLSTGGIVDP SKSHRVPLDV
AYARGYLDKE TNRALTSPRD DARVYHDPST QEPVTYSQLQ QRCRSDQLTG LSLLPLSEKA
VRARQEEVYS ELQARETLEQ AKVEVPVGSF KGRAMTVWEL ISSEYFTEEQ RQELLRQFRT
GKVTVEKVIK IVITIVEEVE TRRQERLSFS GLRAPVPASE LLDAKILSRA QFDQLKDGKT
SVKELSEVGS VRTLLQGSGC LAGIYLEDSK EKVTIYEAMR RGLLRPSTAT LLLEAQAATG
FLVDPVRNQR LYVHEAVKAG VVGPELHEKL LSAEKAVTGY KDPYSGNTIS LFQAMKKGLV
LRDHAIRLLE AQVATGGIID PVHSHRLPVD VAYQRGYFDE EMNRVLADPS DDTKGFFDPN
THENLTYLQL LERCVEDPET GLRLLPLKGA EKTEVVETTQ VYTEEETRRA FEETQIDIPG
GGSHGGSSMS LWEVMQSNMI PEDQRARLMA DFQAGRVTKE RMIIIIIEII EKTEIIRQQN
LASYDYVRRR LTAEDLYEAR IISLETYNLF REGTKNLREV LEMESAWRYL YGTGAVAGVY
LPGSRQTLTI YQALKKGLLS AEVARLLLEA QAATGFLLDP VKGERLTVDE AVRKGLVGPE
LHDRLLSAER AVTGYRDPYT EQTISLFQAM KKELIPAEEA LRLLDAQLAT GGIVDPRLGF
HLPLEVAYQR GYLNKDTHDQ LSEPSEVRSY VDPSTDERLS YTQLLKRCRR DDPSGQMLLL
LSDARKLTFR GLRKQITVEE LVRSQVMDEA TALQLQEGLT SIEEVTKNLQ KFLEGTSCIA
GVFVDATKER LSVYQAMKKG IIRPGTAFEL LEAQAATGYV IDPIKGLKLT VEEAVRMGIV
GPEFKDKLLS AERAVTGYKD PYSGKLISLF QAMKKGLILK DHGIRLLEAQ IATGGIIDPE
ESHRLPVEVA YKRGLFDEEM NEILTDPSDD TKGFFDPNTE ENLTYLQLME RCITDPQTGL
CLLPLKEKKR ERKTSSKSSV RKRRVVIVDP ETGKEMSVYE AYRKGLIDHQ TYLELSEQEC
EWEEITISSS DGVVKSMIID RRSGRQYDID DAITKNLIDR SALDQYRAGT LSITEFADML
SGNAGGFRSR SSSVGSSSSY PISSAGPRTQ LASWSDPTEE TGPVAGILDT ETLEKVSITE
AMHRNLVDNI TGQRLLEAQA CTGGIIDPST GERFPVTEAV NKGLVDKIMV DRINLAQKAF
CGFEDPRTKT KMSAAQALKK GWLYYEAGQR FLEVQYLTGG LIEPDTPGRV SLDEALQRGT
VDARTAQKLR DVSAYSKYLT CPKTKLKISY KDALDRSMVE EGTGLRLLEA AAQSSKGYYS
PYSVSGSGST AGSRTGSRTG SRAGSRRGSF DATGSGFSMT FSSSSYSSSG YGRRYASGPS
ASLGGPESAV A


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