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UniProtKB/Swiss-Prot entry Q15149


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PLEC1_HUMAN
Primary accession number Q15149
Secondary accession numbers Q15148 Q16640 Q6S376 Q6S377 Q6S378 Q6S379 Q6S380 Q6S381 Q6S382 Q6S383
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on October 14, 2008 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 108)
Name and origin of the protein
Protein name Plectin-1
Synonyms PLTN
PCN
Hemidesmosomal protein 1
HD1
Gene name
Name: PLEC1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1073/pnas.93.9.4278; PubMed=8633055 [NCBI, ExPASy, EBI, Israel, Japan]
Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.;
"Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24).";
Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), AND DISEASE.
PubMed=8698233 [NCBI, ExPASy, EBI, Israel, Japan]
McLean W.H.I., Pulkkinen L., Smith F.J.D., Rugg E.L., Lane E.B., Bullrich F., Burgeson R.E., Amano S., Hudson D.L., Owaribe K., McGrath J.A., McMillan J.R., Eady R.A.J., Leigh I.M., Christiano A.M., Uitto J.;
"Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization.";
Genes Dev. 10:1724-1735(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
DOI=10.1101/gr.1225204; PubMed=14672974 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04406; PubMed=16421571 [NCBI, ExPASy, EBI, Israel, Japan]
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[5]
PROTEIN SEQUENCE OF 14-21; 209-227; 237-248; 301-316; 329-336; 350-365; 372-417; 510-517; 588-597; 631-675; 697-706; 714-724; 734-740; 751-764; 857-869; 897-908; 927-934; 1029-1037; 1045-1052; 1076-1088; 1131-1139; 1166-1175; 1187-1210; 1216-1224; 1227-1243; 1251-1266; 1274-1291; 1318-1335; 1338-1344; 1351-1364; 1366-1382; 1411-1438; 1473-1479; 1499-1508; 1554-1563; 1596-1603; 1606-1616; 1628-1638; 1649-1657; 1671-1679; 1699-1709; 1732-1744; 1783-1792; 1825-1833; 1846-1854; 1867-1875; 1888-1908; 1976-1994; 2006-2014; 2048-2055; 2058-2068; 2079-2087; 2098-2108; 2130-2139; 2142-2150; 2172-2182; 2199-2217; 2310-2316; 2319-2329; 2340-2348; 2361-2379; 2402-2409; 2420-2429; 2432-2442; 2462-2473; 2483-2503; 2512-2521; 2565-2575; 2587-2594; 2651-2663; 2685-2693; 2705-2761; 2768-2787; 2795-2821; 2833-2841; 2847-2881; 2885-2903; 2942-2968; 2979-3007; 3028-3039; 3045-3053; 3095-3106; 3109-3127; 3132-3139; 3146-3154; 3175-3183; 3213-3231; 3244-3259; 3270-3285; 3289-3297; 3317-3335; 3356-3368; 3374-3384; 3424-3436; 3447-3469; 3477-3485; 3506-3513; 3519-3540; 3544-3568; 3601-3637; 3648-3661; 3667-3676; 3686-3702; 3739-3749; 3771-3781; 3784-3804; 3839-3878; 3887-3897; 3926-3963; 3969-3999; 4004-4018; 4027-4060; 4084-4091; 4122-4138; 4159-4167; 4179-4205; 4278-4296; 4339-4348; 4354-4360; 4384-4401; 4429-4447; 4467-4475; 4492-4500; 4543-4551; 4590-4627 AND 4668-4684, PHOSPHORYLATION AT SER-4385, AND MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; SER-1435; SER-4386; THR-4402; SER-4613 AND THR-4623, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1721; SER-4386 AND SER-4389, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4611, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4615, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, AND MASS SPECTROMETRY.
TISSUE=Hepatocyte;
DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.;
"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.";
Proteomics 5:3589-3599(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1721; THR-2814; THR-4030; SER-4382; SER-4384; SER-4385; SER-4386; THR-4411 AND SER-4620, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435; SER-4384; SER-4396; SER-4613 AND SER-4620, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3362 AND TYR-4155, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1644 AND SER-2755, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-720 AND SER-1435, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4384; SER-4385; SER-4386; SER-4389; SER-4392; TYR-4393; SER-4396; SER-4613; SER-4622; THR-4623; SER-4626; THR-4628; SER-4642 AND SER-4658, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[20]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
DOI=10.1016/j.jmb.2007.02.090; PubMed=17397861 [NCBI, ExPASy, EBI, Israel, Japan]
Sonnenberg A., Rojas A.M., de Pereda J.M.;
"The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain.";
J. Mol. Biol. 368:1379-1391(2007).
[21]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
DOI=10.1016/S0969-2126(03)00090-X; PubMed=12791251 [NCBI, ExPASy, EBI, Israel, Japan]
Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.;
"Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4.";
Structure 11:615-625(2003).
[22]
VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
DOI=10.1093/hmg/5.10.1539; PubMed=8894687 [NCBI, ExPASy, EBI, Israel, Japan]
Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J.;
"Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy.";
Hum. Mol. Genet. 5:1539-1546(1996).
[23]
VARIANT MD-EBS LEU-429 INS.
PubMed=11159198 [NCBI, ExPASy, EBI, Israel, Japan]
Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W., Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J., Hintner H.;
"A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency.";
Am. J. Pathol. 158:617-625(2001).
[24]
VARIANT O-EBS TRP-2110.
DOI=10.1046/j.0022-202x.2001.01591.x; PubMed=11851880 [NCBI, ExPASy, EBI, Israel, Japan]
Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A., Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.;
"A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations.";
J. Invest. Dermatol. 118:87-93(2002).
[25]
INVOLVEMENT IN EBS-PA.
DOI=10.1111/j.1523-1747.2003.12639.x; PubMed=14675180 [NCBI, ExPASy, EBI, Israel, Japan]
Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P., De Raeve L., Meneguzzi G.;
"Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin.";
J. Invest. Dermatol. 121:1344-1348(2003).
Comments
  • FUNCTION: Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. 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. Interacts with Nesprin-3 (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
  • ALTERNATIVE PRODUCTS: 9 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsPlectin-6
    Isoform IDQ15149-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsPlectin-1
    Isoform IDQ15149-2
    Features which should be applied to build the isoform sequence: VSP_005030.
    Name3
    Isoform IDQ15149-3
    Features which should be applied to build the isoform sequence: VSP_005030, VSP_005031.
    Name4
    SynonymsPlectin-11
    Isoform IDQ15149-4
    Note: Phosphorylated on 'Ser-21'. Phosphorylated on 'Tyr-26' (By similarity).
    Features which should be applied to build the isoform sequence: VSP_023510.
    Name5
    SynonymsPlectin-8
    Isoform IDQ15149-5
    Features which should be applied to build the isoform sequence: VSP_037103, VSP_037106.
    Name6
    SynonymsPlectin-10
    Isoform IDQ15149-6
    Features which should be applied to build the isoform sequence: VSP_037104, VSP_037105.
    Name7
    SynonymsPlectin-7
    Isoform IDQ15149-7
    Features which should be applied to build the isoform sequence: VSP_037100, VSP_037109.
    Name8
    SynonymsPlectin-3
    Isoform IDQ15149-8
    Features which should be applied to build the isoform sequence: VSP_037101, VSP_037108.
    Name9
    SynonymsPlectin-2
    Isoform IDQ15149-9
    Features which should be applied to build the isoform sequence: VSP_037102, VSP_037107.
  • TISSUE SPECIFICITY: Widely expressed with highest levels in muscle, heart, placenta and spinal cord.
  • 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 CDC2; regulates dissociation from intermediate filaments during mitosis (By similarity). Phosphorylated upon DNA damage, probably by ATM or ATR. Isoform 4 is phosphorylated on 'Tyr-26' (By similarity). Isoform 4 is phosphorylated on 'Ser-21'.
  • DISEASE: Defects in PLEC1 are the cause of epidermolysis bullosa simplex with pyloric atresia (EBS-PA) [MIM:612138]. EBS-PA is an autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD-EBS.
  • DISEASE: Defects in PLEC1 are the cause of epidermolysis bullosa simplex with muscular dystrophy (MD-EBS) [MIM:226670]. MD-EBS is an autosomal recessive disorder characterized by epidermal blister formation at the level of the hemidesmosome and associated with late-onset muscular dystrophy.
  • DISEASE: Defects in PLEC1 are the cause of epidermolysis bullosa simplex Ogna type (O-EBS) [MIM:131950]; also called epidermolysis bullosa simplex 1. O-EBS is a form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates.
  • SIMILARITY: Belongs to the plakin or cytolinker family.
  • SIMILARITY: Contains 1 actin-binding domain.
  • SIMILARITY: Contains 2 CH (calponin-homology) domains.
  • SIMILARITY: Contains 33 plectin repeats.
  • SIMILARITY: Contains 4 spectrin repeats.
  • WEB RESOURCE: Name=Wikipedia; Note=Plectin entry; URL="http://en.wikipedia.org/wiki/Plectin";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z54367; CAA91196.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U53204; AAB05427.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U63610; AAB05428.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U63609; AAB05428.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X97053; CAA65765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480044; AAR95677.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480045; AAR95678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480046; AAR95679.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480047; AAR95680.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480048; AAR95681.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480049; AAR95682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480050; AAR95683.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY480051; AAR95684.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC109322; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
IPI IPI00014898; -.
IPI00186711; -.
IPI00398002; -.
IPI00398779; -.
PIR C59404; A59404.
G02520; G02520.
RefSeq NP_000436.2; -.
NP_958780.1; -.
NP_958781.1; -.
NP_958782.1; -.
NP_958783.1; -.
NP_958784.1; -.
NP_958785.1; -.
NP_958786.1; -.
UniGene Hs.434248
3D structure databases
PDB
1MB8; X-ray; 2.15 A; A=175-403.[ExPASy / RCSB / EBI]
2ODU; X-ray; 2.30 A; A=409-640.[ExPASy / RCSB / EBI]
2ODV; X-ray; 2.05 A; A=409-640.[ExPASy / RCSB / EBI]
3F7P; X-ray; 2.75 A; A/B=175-403.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MB8; -.
2ODU; -.
2ODV; -.
3F7P; -.
ModBase Q15149.
PTM databases
PhosphoSite Q15149; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
GeneCards GC08M145061; -.
GC08M145062; -.
H-InvDB HIX0055497; -.
HGNC HGNC:9069; PLEC1.
GenAtlas PLEC1.
HPA CAB003847; -.
MIM 131950; phenotype. [NCBI / EBI]
226670; phenotype. [NCBI / EBI]
601282; gene. [NCBI / EBI]
612138; phenotype. [NCBI / EBI]
Orphanet 257; Epidermolysis bullosa simplex - limb girdle muscular dystrophy.
158684; Epidermolysis bullosa simplex - pyloric atresia.
79401; Epidermolysis bullosa simplex, Ogna type.
304; Epidermolysis bullosa, epidermolytic.
PharmGKB PA33399; -.
Gene expression databases
ArrayExpress Q15149; -.
Bgee Q15149; -.
CleanEx HS_PLEC1; -.
GermOnline ENSG00000178209; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886; Cellular component: plasma membrane (non-traceable author statement from ProtInc).
GO:0003779; Molecular function: actin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008307; Molecular function: structural constituent of muscle (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001589; Actinin_actin-bd_CS.
IPR001715; Calponin_act_bd.
IPR015622; Plectin.
IPR001101; Plectin_repeat.
IPR005326; S10_plectin_N.
IPR018159; Spectrin/alpha-actinin.
Graphical view of domain structure.
Gene3D G3DSA:1.10.418.10; Calponin-homology; 2.
PANTHER PTHR11915:SF52; Plectin; 1.
Pfam PF00307; CH; 2.
PF00681; Plectin; 17.
PF03501; S10_plectin; 1.
Pfam graphical view of domain structure.
ProDom PD006662; S10_plectin_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00033; CH; 2.
SM00250; PLEC; 32.
SM00150; SPEC; 7.
SMART graphical view of domain structure.
PROSITE PS00019; ACTININ_1; 1.
PS00020; ACTININ_2; 1.
PS50021; CH; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q15149; -.
Genome annotation databases
Ensembl ENSG00000178209; Homo sapiens. [Contig view]
GeneID 5339; -.
Phylogenomic databases
HOGENOM Q15149; -.
HOVERGEN Q15149; -.
OMA Q15149; DVFEKAT.
Other
NextBio 20680; -.
SOURCE PLEC1; Homo sapiens.
ProtoNet Q15149.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Epidermolysis bullosa; Phosphoprotein; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   4684  4684     Plectin-1. PRO_0000078135
DOMAIN   175    400  226     Actin-binding. 
DOMAIN   179    282  104     CH 1. 
DOMAIN   295    397  103     CH 2. 
REPEAT   645    710  66     Spectrin 1. 
REPEAT   740    824  85     Spectrin 2. 
REPEAT   837    930  94     Spectrin 3. 
REPEAT   1315   1415  101     Spectrin 4. 
REPEAT   2826   2863  38     Plectin 1. 
REPEAT   2864   2901  38     Plectin 2. 
REPEAT   2902   2939  38     Plectin 3. 
REPEAT   2940   2977  38     Plectin 4. 
REPEAT   2981   3015  35     Plectin 5. 
REPEAT   3116   3153  38     Plectin 6. 
REPEAT   3154   3191  38     Plectin 7. 
REPEAT   3192   3229  38     Plectin 8. 
REPEAT   3230   3267  38     Plectin 9. 
REPEAT   3268   3305  38     Plectin 10. 
REPEAT   3306   3343  38     Plectin 11. 
REPEAT   3485   3522  38     Plectin 12. 
REPEAT   3523   3560  38     Plectin 13. 
REPEAT   3561   3598  38     Plectin 14. 
REPEAT   3599   3636  38     Plectin 15. 
REPEAT   3640   3674  35     Plectin 16. 
REPEAT   3820   3857  38     Plectin 17. 
REPEAT   3858   3895  38     Plectin 18. 
REPEAT   3896   3933  38     Plectin 19. 
REPEAT   3934   3971  38     Plectin 20. 
REPEAT   3975   4008  34     Plectin 21. 
REPEAT   4063   4100  38     Plectin 22. 
REPEAT   4101   4138  38     Plectin 23. 
REPEAT   4139   4176  38     Plectin 24. 
REPEAT   4177   4214  38     Plectin 25. 
REPEAT   4218   4252  35     Plectin 26. 
REPEAT   4265   4305  41     Plectin 27. 
REPEAT   4319   4356  38     Plectin 28. 
REPEAT   4408   4445  38     Plectin 29. 
REPEAT   4446   4483  38     Plectin 30. 
REPEAT   4484   4521  38     Plectin 31. 
REPEAT   4522   4559  38     Plectin 32. 
REPEAT   4560   4597  38     Plectin 33. 
REGION   1   1470  1470     Globular 1. 
REGION   1471   2755  1285     Central fibrous rod domain. 
REGION   2756   4684  1929     Globular 2. 
REGION   4250   4300  51     Binding to intermediate filaments (By similarity). 
REGION   4625   4640  16     4 X 4 AA tandem repeats of G-S-R-X. 
COILED   1469   2756  1288     Potential. 
MOD_RES   125    125        Phosphoserine. 
MOD_RES   149    149        Phosphoserine. 
MOD_RES   720    720        Phosphoserine. 
MOD_RES   782    782        Phosphoserine. 
MOD_RES   1435   1435        Phosphoserine. 
MOD_RES   1644   1644        Phosphoserine. 
MOD_RES   1721   1721        Phosphoserine. 
MOD_RES   1732   1732        Phosphoserine. 
MOD_RES   2755   2755        Phosphoserine. 
MOD_RES   2814   2814        Phosphothreonine. 
MOD_RES   3033   3033        Phosphotyrosine (By similarity). 
MOD_RES   3362   3362        Phosphotyrosine. 
MOD_RES   4030   4030        Phosphothreonine. 
MOD_RES   4155   4155        Phosphotyrosine. 
MOD_RES   4382   4382        Phosphoserine. 
MOD_RES   4384   4384        Phosphoserine. 
MOD_RES   4385   4385        Phosphoserine. 
MOD_RES   4386   4386        Phosphoserine. 
MOD_RES   4389   4389        Phosphoserine. 
MOD_RES   4390   4390        Phosphoserine (By similarity). 
MOD_RES   4391   4391        Phosphoserine (By similarity). 
MOD_RES   4392   4392        Phosphoserine. 
MOD_RES   4393   4393        Phosphotyrosine. 
MOD_RES   4396   4396        Phosphoserine. 
MOD_RES   4402   4402        Phosphothreonine. 
MOD_RES   4411   4411        Phosphothreonine. 
MOD_RES   4539   4539        Phosphothreonine; by CDC2 (By similarity). 
MOD_RES   4611   4611        Phosphotyrosine. 
MOD_RES   4613   4613        Phosphoserine. 
MOD_RES   4615   4615        Phosphotyrosine. 
MOD_RES   4620   4620        Phosphoserine. 
MOD_RES   4622   4622        Phosphoserine. 
MOD_RES   4623   4623        Phosphothreonine. 
MOD_RES   4626   4626        Phosphoserine. 
MOD_RES   4628   4628        Phosphothreonine. 
MOD_RES   4642   4642        Phosphoserine. 
MOD_RES   4658   4658        Phosphoserine. 
VAR_SEQ   1    174        MVAGMLMPRDQLRAIYEVLFREGVMVAKKDRRPRSLHPHV PGVTNLQVMRAMASLRARGLVRETFAWCHFYWYLTNEGIA HLRQYLHLPPEIVPASLQRVRRPVAMVMPARRTPHVQAVQ GPLGSPPKRGPLPTEEQRVYRRKELEEVSPETPVVPATTQ RTLARPGPEPAPAT -> MSGEDAEVRAVSEDVSNGSSGSPSPGDTLPWNLGKTQRSR RSGGGAGSNGSVLDPAERAVIRIA (in isoform 2 and isoform 3). VSP_005030
VAR_SEQ   1    174        MVAGMLMPRDQLRAIYEVLFREGVMVAKKDRRPRSLHPHV PGVTNLQVMRAMASLRARGLVRETFAWCHFYWYLTNEGIA HLRQYLHLPPEIVPASLQRVRRPVAMVMPARRTPHVQAVQ GPLGSPPKRGPLPTEEQRVYRRKELEEVSPETPVVPATTQ RTLARPGPEPAPAT -> MSQHQLRVPQPEGLGRKRTSSEDNLYLAVLRASEGKK (in isoform 4). VSP_023510
VAR_SEQ   1    169        Missing (in isoform 7). VSP_037100
VAR_SEQ   1    159        Missing (in isoform 8). VSP_037101
VAR_SEQ   1    151        Missing (in isoform 9). VSP_037102
VAR_SEQ   1    137        Missing (in isoform 5). VSP_037103
VAR_SEQ   1    133        Missing (in isoform 6). VSP_037104
VAR_SEQ   134    174        TEEQRVYRRKELEEVSPETPVVPATTQRTLARPGPE PAPAT -> MSGAGGAFASPREVLLERPCWLDGGCEPARRGYLYQ QLCCV (in isoform 6). VSP_037105
VAR_SEQ   138    174        RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT -> MEPSGSLFPSLVVVGHVVTLAAVWHWRRGRRWAQDEQ (in isoform 5). VSP_037106
VAR_SEQ   152    174        TPVVPATTQRTLARPGPEPAPAT -> MAGPLPDEQDFIQAYEEVREKYK (in isoform 9). VSP_037107
VAR_SEQ   160    174        QRTLARPGPEPAPAT -> MDPSRAIQNEISSLK (in isoform 8). VSP_037108
VAR_SEQ   170    174        PAPAT -> MKIVP (in isoform 7). VSP_037109
VAR_SEQ   409    412        Missing (in isoform 3). VSP_005031
VARIANT   429    429  1     L -> LL (in MD-EBS). VAR_011336
VARIANT   641    641  1     A -> V (in dbSNP:rs11136336 [NCBI]). VAR_053585 
VARIANT   1003   1005  3     Missing (in MD-EBS). VAR_011337
VARIANT   2110   2110  1     R -> W (in O-EBS). VAR_015817 
VARIANT   2150   2150  1     R -> W (in dbSNP:rs34893635 [NCBI]). VAR_053586 
VARIANT   2194   2194  1     A -> V (in dbSNP:rs7002002 [NCBI]). VAR_053587 
VARIANT   2791   2791  1     S -> P (in dbSNP:rs7833924 [NCBI]). VAR_053588 
VARIANT   2821   2821  1     R -> W (in dbSNP:rs35723243 [NCBI]). VAR_053589 
VARIANT   2969   2969  1     R -> H (in dbSNP:rs6558407 [NCBI]). VAR_053590 
VARIANT   3162   3162  1     V -> I (in dbSNP:rs35027700 [NCBI]). VAR_053591 
VARIANT   3171   3171  1     A -> V (in dbSNP:rs35858667 [NCBI]). VAR_053592 
VARIANT   3486   3486  1     T -> M (in dbSNP:rs34725742 [NCBI]). VAR_053593 
VARIANT   3490   3490  1     G -> A (in dbSNP:rs35261863 [NCBI]). VAR_053594 
CONFLICT   71     71        Y -> F (in Ref. 1; CAA91196). 
CONFLICT   94     94        P -> A (in Ref. 1; CAA91196). 
CONFLICT   139    139        V -> L (in Ref. 1; CAA91196). 
CONFLICT   185    185        F -> S (in Ref. 1; CAA91196). 
CONFLICT   259    259        N -> D (in Ref. 2; AAB05427/AAB05428). 
CONFLICT   550    550        N -> H (in Ref. 1; CAA91196). 
CONFLICT   560    560        V -> I (in Ref. 1; CAA91196). 
CONFLICT   706    706        R -> Q (in Ref. 1; CAA91196). 
CONFLICT   886    886        Y -> N (in Ref. 1; CAA91196). 
CONFLICT   1002   1002        A -> V (in Ref. 1; CAA91196). 
CONFLICT   1309   1309        V -> L (in Ref. 2; AAB05427/AAB05428). 
CONFLICT   1321   1321        L -> V (in Ref. 2; AAB05427/AAB05428). 
CONFLICT   1334   1334        V -> L (in Ref. 2; AAB05427/AAB05428). 
CONFLICT   1534   1534        M -> I (in Ref. 1; CAA91196). 
CONFLICT   1662   1662        A -> T (in Ref. 2; AAB05427/AAB05428). 
CONFLICT   1688   1690        RLR -> WLC (in Ref. 1; CAA91196). 
CONFLICT   1767   1767        E -> Q (in Ref. 1; CAA91196). 
CONFLICT   1789   1789        A -> L (in Ref. 1; CAA91196). 
CONFLICT   1910   1910        R -> K (in Ref. 1; CAA91196). 
CONFLICT   2154   2154        K -> N (in Ref. 2; AAB05427/AAB05428/CAA65765 and 3; AAR95680/AAR95682/AAR95683). 
CONFLICT   2160   2160        R -> S (in Ref. 1; CAA91196). 
CONFLICT   2215   2215        Q -> R (in Ref. 1; CAA91196). 
CONFLICT   2244   2244        S -> A (in Ref. 1; CAA91196 and 2; AAB05427/AAB05428/CAA65765). 
CONFLICT   3027   3027        K -> E (in Ref. 2; AAB05427/AAB05428). 
CONFLICT   3310   3310        A -> E (in Ref. 1; CAA91196). 
CONFLICT   3361   3361        L -> F (in Ref. 1; CAA91196). 
CONFLICT   3408   3408        L -> F (in Ref. 1; CAA91196). 
CONFLICT   3447   3447        A -> S (in Ref. 1; CAA91196). 
CONFLICT   3531   3531        A -> G (in Ref. 1; CAA91196). 
CONFLICT   3580   3580        S -> R (in Ref. 1; CAA91196). 
CONFLICT   3589   3589        Q -> K (in Ref. 1; CAA91196). 
CONFLICT   3596   3596        Q -> E (in Ref. 1; CAA91196). 
CONFLICT   3616   3616        H -> N (in Ref. 1; CAA91196). 
CONFLICT   3686   3686        A -> V (in Ref. 1; CAA91196). 
CONFLICT   3786   3786        A -> G (in Ref. 1; CAA91196). 
CONFLICT   3808   3808        R -> K (in Ref. 1; CAA91196). 
CONFLICT   3816   3816        A -> G (in Ref. 1; CAA91196). 
CONFLICT   3821   3821        C -> F (in Ref. 1; CAA91196). 
CONFLICT   3915   3915        Q -> K (in Ref. 1; CAA91196). 
CONFLICT   3999   3999        R -> K (in Ref. 1; CAA91196). 
CONFLICT   4007   4007        T -> S (in Ref. 1; CAA91196). 
CONFLICT   4467   4467        F -> L (in Ref. 1; CAA91196). 
HELIX   175    193  19      
TURN   203    209  7      
HELIX   211    221  11      
HELIX   233    249  17      
HELIX   259    263  5      
HELIX   267    282  16      
HELIX   297    308  12      
TURN   309    311  3      
HELIX   322    324  3      
HELIX   328    337  10      
HELIX   339    341  3      
HELIX   344    347  4      
HELIX   352    367  16      
HELIX   375    378  4      
STRAND   380    382  3      
HELIX   385    398  14      
HELIX   414    440  27      
HELIX   448    463  16      
HELIX   466    489  24      
STRAND   490    492  3      
HELIX   500    564  65      
HELIX   572    598  27      
HELIX   604    629  26      
Sequence information
Length: 4684 AA [This is the length of the unprocessed precursor] Molecular weight: 531791 Da [This is the MW of the unprocessed precursor] CRC64: 04772E4F70A304C8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLRARGL 

        70         80         90        100        110        120 
VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV RRPVAMVMPA RRTPHVQAVQ 

       130        140        150        160        170        180 
GPLGSPPKRG PLPTEEQRVY RRKELEEVSP ETPVVPATTQ RTLARPGPEP APATDERDRV 

       190        200        210        220        230        240 
QKKTFTKWVN KHLIKAQRHI SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV 

       250        260        270        280        290        300 
QIALDYLRHR QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK 

       310        320        330        340        350        360 
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ TNLENLDQAF 

       370        380        390        400        410        420 
SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP RVPDVQDGVR ANELQLRWQE 

       430        440        450        460        470        480 
YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE IEILWSQFLK FKEMELPAKE ADKNRSKGIY 

       490        500        510        520        530        540 
QSLEGAVQAG QLKVPPGYHP LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM 

       550        560        570        580        590        600 
EAGLCEEQLN QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR 

       610        620        630        640        650        660 
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR RPELEDSTLR 

       670        680        690        700        710        720 
YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ SIEEFRAKIE RARSDEGQLS 

       730        740        750        760        770        780 
PATRGAYRDC LGRLDLQYAK LLNSSKARLR SLESLHSFVA AATKELMWLN EKEEEEVGFD 

       790        800        810        820        830        840 
WSDRNTNMTA KKESYSALMR ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ 

       850        860        870        880        890        900 
WSWMLQLCCC IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL 

       910        920        930        940        950        960 
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC DYKQVEVTVH 

       970        980        990       1000       1010       1020 
KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ EAQEAVTRLE AQHQALVTLW 

      1030       1040       1050       1060       1070       1080 
HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT FRTLKPEEQR QALHSLELHY QAFLRDSQDA 

      1090       1100       1110       1120       1130       1140 
GGFGPEDRLM AEREYGSCSH HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT 

      1150       1160       1170       1180       1190       1200 
VHRLRLPLDK EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL 

      1210       1220       1230       1240       1250       1260 
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK EAQAVPATLP 

      1270       1280       1290       1300       1310       1320 
ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL QQRHGERDVE VERWRERVAQ 

      1330       1340       1350       1360       1370       1380 
LLERWQAVLA QTDVRQRELE QLGRQLRYYR ESADPLGAWL QDARRRQEQI QAMPLADSQA 

      1390       1400       1410       1420       1430       1440 
VREQLRQEQA LLEEIERHGE KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP 

      1450       1460       1470       1480       1490       1500 
KVQSGSESVI QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA 

      1510       1520       1530       1540       1550       1560 
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ QKRSIQEELQ 

      1570       1580       1590       1600       1610       1620 
QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA TERQRGGAEG ELQALRARAE 

      1630       1640       1650       1660       1670       1680 
EAEAQKRQAQ EEAERLRRQV QDESQRKRQA EVELASRVKA EAEAAREKQR ALQALEELRL 

      1690       1700       1710       1720       1730       1740 
QAEEAERRLR QAEVERARQV QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV 

      1750       1760       1770       1780       1790       1800 
AQLREEAERR AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE 

      1810       1820       1830       1840       1850       1860 
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ ELIRLRAETE 

      1870       1880       1890       1900       1910       1920 
QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE MEVLLASKAR AEEESRSTSE 

      1930       1940       1950       1960       1970       1980 
KSKQRLEAEA GRFRELAEEA ARLRALAEEA KRQRQLAEED AARQRAEAER VLAEKLAAIG 

      1990       2000       2010       2020       2030       2040 
EATRLKTEAE IALKEKEAEN ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD 

      2050       2060       2070       2080       2090       2100 
SELERQKGLV EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE 

      2110       2120       2130       2140       2150       2160 
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER LKAKVEEARR 

      2170       2180       2190       2200       2210       2220 
LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ ELQQTLQQEQ SVLDQLRGEA 

      2230       2240       2250       2260       2270       2280 
EAARRAAEEA EEARVQAERE AAQSRRQVEE AERLKQSAEE QAQARAQAQA AAEKLRKEAE 

      2290       2300       2310       2320       2330       2340 
QEAARRAQAE QAALRQKQAA DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN 

      2350       2360       2370       2380       2390       2400 
LLDEELQRLK AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ 

      2410       2420       2430       2440       2450       2460 
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK EKMQAVQEAT 

      2470       2480       2490       2500       2510       2520 
RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG FQRTLEAERQ RQLEMSAEAE 

      2530       2540       2550       2560       2570       2580 
RLKLRVAEMS RAQARAEEDA QRFRKQAEEI GEKLHRTELA TQEKVTLVQT LEIQRQQSDH 

      2590       2600       2610       2620       2630       2640 
DAERLREAIA ELEREKEKLQ QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL 

      2650       2660       2670       2680       2690       2700 
QRERFIEQEK AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE 

      2710       2720       2730       2740       2750       2760 
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE EVTASQVAAT 

      2770       2780       2790       2800       2810       2820 
KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI LSAEELQRLA QGHTTVDELA 

      2830       2840       2850       2860       2870       2880 
RREDVRHYLQ GRSSIAGLLL KATNEKLSVY AALQRQLLSP GTALILLEAQ AASGFLLDPV 

      2890       2900       2910       2920       2930       2940 
RNRRLTVNEA VKEGVVGPEL HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI 

      2950       2960       2970       2980       2990       3000 
RLLEAQIATG GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT 

      3010       3020       3030       3040       3050       3060 
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP FGKFQGKTVT 

      3070       3080       3090       3100       3110       3120 
IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV EEQEQKGRLC FEGLRSLVPA 

      3130       3140       3150       3160       3170       3180 
AELLESRVID RELYQQLQRG ERSVRDVAEV DTVRRALRGA NVIAGVWLEE AGQKLSIYNA 

      3190       3200       3210       3220       3230       3240 
LKKDLLPSDM AVALLEAQAG TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT 

      3250       3260       3270       3280       3290       3300 
GYRDPYTGQS VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL 

      3310       3320       3330       3340       3350       3360 
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS EKAARARQEE 

      3370       3380       3390       3400       3410       3420 
LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT AEQRQELLRQ FRTGKVTVEK 

      3430       3440       3450       3460       3470       3480 
VIKILITIVE EVETLRQERL SFSGLRAPVP ASELLASGVL SRAQFEQLKD GKTTVKDLSE 

      3490       3500       3510       3520       3530       3540 
LGSVRTLLQG SGCLAGIYLE DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR 

      3550       3560       3570       3580       3590       3600 
NQRLYVHEAV KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR 

      3610       3620       3630       3640       3650       3660 
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF DPNTHENLTY 

      3670       3680       3690       3700       3710       3720 
RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET RRAFEETQID IPGGGSHGGS 

      3730       3740       3750       3760       3770       3780 
TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV TKERMIIIII EIIEKTEIIR QQGLASYDYV 

      3790       3800       3810       3820       3830       3840 
RRRLTAEDLF EARIISLETY NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT 

      3850       3860       3870       3880       3890       3900 
LSIYQALKKG LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS 

      3910       3920       3930       3940       3950       3960 
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR LGFHLPLEVA 

      3970       3980       3990       4000       4010       4020 
YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR CRRDDGTGQL LLPLSDARKL 

      4030       4040       4050       4060       4070       4080 
TFRGLRKQIT MEELVRSQVM DEATALQLRE GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT 

      4090       4100       4110       4120       4130       4140 
KERLSVYQAM KKGIIRPGTA FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK 

      4150       4160       4170       4180       4190       4200 
LLSAERAVTG YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV 

      4210       4220       4230       4240       4250       4260 
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ TGLCLLPLKE 

      4270       4280       4290       4300       4310       4320 
KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI DHQTYLELSE QECEWEEITI 

      4330       4340       4350       4360       4370       4380 
SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL IDRSALDQYR AGTLSITEFA DMLSGNAGGF 

      4390       4400       4410       4420       4430       4440 
RSRSSSVGSS SSYPISPAVS RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV 

      4450       4460       4470       4480       4490       4500 
DNITGQRLLE AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR 

      4510       4520       4530       4540       4550       4560 
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ RGTVDARTAQ 

      4570       4580       4590       4600       4610       4620 
KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL LEAAAQSTKG YYSPYSVSGS 

      4630       4640       4650       4660       4670       4680 
GSTAGSRTGS RTGSRAGSRR GSFDATGSGF SMTFSSSSYS SSGYGRRYAS GSSASLGGPE 


SAVA 

Q15149 in FASTA format

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