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Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)

 SYNE1_HUMAN             Reviewed;        8797 AA.
Q8NF91; B3W695; E7EQI5; H0Y4C0; O94890; Q3ZCV0; Q5JV19; Q5JV22;
Q8N9P7; Q8TCP1; Q8WWW6; Q8WWW7; Q8WXF6; Q96N17; Q9C0A7; Q9H525;
Q9H526; Q9NS36; Q9NU50; Q9UJ06; Q9UJ07; Q9ULF8;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
28-NOV-2012, sequence version 4.
20-JUN-2018, entry version 174.
RecName: Full=Nesprin-1;
AltName: Full=Enaptin;
AltName: Full=KASH domain-containing protein 1;
Short=KASH1;
AltName: Full=Myocyte nuclear envelope protein 1;
Short=Myne-1;
AltName: Full=Nuclear envelope spectrin repeat protein 1;
AltName: Full=Synaptic nuclear envelope protein 1;
Short=Syne-1;
Name=SYNE1; Synonyms=C6orf98, KIAA0796, KIAA1262, KIAA1756, MYNE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 8758-LEU--CYS-8763, AND
VARIANTS VAL-7302 AND ALA-8323.
TISSUE=Heart, Placenta, Skeletal muscle, Spleen, and Testis;
PubMed=11792814;
Zhang Q., Skepper J.N., Yang F., Davies J.D., Hegyi L., Roberts R.G.,
Weissberg P.L., Ellis J.A., Shanahan C.M.;
"Nesprins: a novel family of spectrin-repeat-containing proteins that
localize to the nuclear membrane in multiple tissues.";
J. Cell Sci. 114:4485-4498(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
VARIANTS THR-4596; MET-5015; VAL-7302 AND ALA-8323.
TISSUE=Heart, Spleen, and Testis;
PubMed=12408964; DOI=10.1006/geno.2002.6859;
Zhang Q., Ragnauth C., Greener M.J., Shanahan C.M., Roberts R.G.;
"The nesprins are giant actin-binding proteins, orthologous to
Drosophila melanogaster muscle protein MSP-300.";
Genomics 80:473-481(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND VARIANT ALA-8323.
PubMed=11801724;
Mislow J.M.K., Kim M.S., Davis D.B., McNally E.M.;
"Myne-1, a spectrin repeat transmembrane protein of the myocyte inner
nuclear membrane, interacts with lamin A/C.";
J. Cell Sci. 115:61-70(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
TISSUE=Ovary;
PubMed=18709643; DOI=10.1002/ijc.23763;
Marme A., Zimmermann H.P., Moldenhauer G., Schorpp-Kistner M.,
Muller C., Keberlein O., Giersch A., Kretschmer J., Seib B.,
Spiess E., Hunziker A., Merchan F., Moller P., Hahn U., Kurek R.,
Marme F., Bastert G., Wallwiener D., Ponstingl H.;
"Loss of Drop1 expression already at early tumor stages in a wide
range of human carcinomas.";
Int. J. Cancer 123:2048-2056(2008).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
TISSUE=Cerebellum;
PubMed=15093733; DOI=10.1016/j.yexcr.2004.01.014;
Padmakumar V.C., Abraham S., Braune S., Noegel A.A., Tunggal B.,
Karakesisoglou I., Korenbaum E.;
"Enaptin, a giant actin-binding protein, is an element of the nuclear
membrane and the actin cytoskeleton.";
Exp. Cell Res. 295:330-339(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9), AND VARIANTS VAL-7302
AND ALA-8323.
Zhang Q., Shanahan C.M.;
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GSRP-56).
TISSUE=Testis;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-856 (ISOFORM 1).
TISSUE=Kidney;
PubMed=12808039; DOI=10.1091/mbc.E02-07-0446;
Gough L.L., Fan J., Chu S., Winnick S., Beck K.A.;
"Golgi localization of Syne-1.";
Mol. Biol. Cell 14:2410-2424(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-778 AND 2901-3476
(ISOFORM 1).
TISSUE=Adrenal gland, and Teratocarcinoma;
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-8797 (ISOFORM 5).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 743-8797 (ISOFORM 6).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4219-8797 (ISOFORM 7), AND
VARIANTS THR-4596 AND MET-5015.
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6922-8797 (ISOFORM 1), AND
VARIANTS VAL-7302 AND ALA-8323.
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[15]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 8406-8797 (ISOFORM 1).
Ma F.-R., Zhu L.-P.;
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[17]
SUBUNIT, AND INTERACTION WITH EMD AND LMNA.
PubMed=12163176; DOI=10.1016/S0014-5793(02)03105-8;
Mislow J.M., Holaska J.M., Kim M.S., Lee K.K., Segura-Totten M.,
Wilson K.L., McNally E.M.;
"Nesprin-1alpha self-associates and binds directly to emerin and lamin
A in vitro.";
FEBS Lett. 525:135-140(2002).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8223; THR-8274; SER-8277
AND SER-8280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[19]
ALTERNATIVE SPLICING (ISOFORM GSRP-56), SUBCELLULAR LOCATION (ISOFORM
GSRP-56), INTERACTION WITH TRPV2 (ISOFORM GSRP-56), AND TISSUE
SPECIFICITY (ISOFORM GSRP-56).
PubMed=16875688; DOI=10.1016/j.yexcr.2006.06.026;
Kobayashi Y., Katanosaka Y., Iwata Y., Matsuoka M., Shigekawa M.,
Wakabayashi S.;
"Identification and characterization of GSRP-56, a novel Golgi-
localized spectrin repeat-containing protein.";
Exp. Cell Res. 312:3152-3164(2006).
[20]
INVOLVEMENT IN SCAR8.
PubMed=17159980; DOI=10.1038/ng1927;
Gros-Louis F., Dupre N., Dion P., Fox M.A., Laurent S., Verreault S.,
Sanes J.R., Bouchard J.-P., Rouleau G.A.;
"Mutations in SYNE1 lead to a newly discovered form of autosomal
recessive cerebellar ataxia.";
Nat. Genet. 39:80-85(2007).
[21]
FUNCTION, DOMAIN, AND INTERACTION WITH SUN1 AND SUN2.
PubMed=18396275; DOI=10.1016/j.yexcr.2008.02.022;
Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.;
"Structural requirements for the assembly of LINC complexes and their
function in cellular mechanical stiffness.";
Exp. Cell Res. 314:1892-1905(2008).
[22]
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).
[23]
TISSUE SPECIFICITY, AND INTERACTION WITH SYNE3.
PubMed=22518138; DOI=10.1155/2012/736524;
Taranum S., Sur I., Muller R., Lu W., Rashmi R.N., Munck M.,
Neumann S., Karakesisoglou I., Noegel A.A.;
"Cytoskeletal interactions at the nuclear envelope mediated by
nesprins.";
Int. J. Cell Biol. 2012:736524-736524(2012).
[24]
SPECTRIN REPEATS.
PubMed=23671687; DOI=10.1371/journal.pone.0063633;
Autore F., Pfuhl M., Quan X., Williams A., Roberts R.G.,
Shanahan C.M., Fraternali F.;
"Large-scale modelling of the divergent spectrin repeats in nesprins:
giant modular proteins.";
PLoS ONE 8:E63633-E63633(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8223 AND THR-8360, 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).
[26]
X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 8769-8797 IN COMPLEX WITH
SUN2, AND SUBUNIT.
PubMed=22632968; DOI=10.1016/j.cell.2012.03.046;
Sosa B.A., Rothballer A., Kutay U., Schwartz T.U.;
"LINC complexes form by binding of three KASH peptides to domain
interfaces of trimeric SUN proteins.";
Cell 149:1035-1047(2012).
[27]
VARIANTS COLORECTAL CANCER [LARGE SCALE ANALYSIS] MET-3671; ASP-4210;
HIS-4223; ARG-5507 AND HIS-8468.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[28]
VARIANTS EDMD4 HIS-8095; LEU-8387 AND LYS-8461.
PubMed=17761684; DOI=10.1093/hmg/ddm238;
Zhang Q., Bethmann C., Worth N.F., Davies J.D., Wasner C., Feuer A.,
Ragnauth C.D., Yi Q., Mellad J.A., Warren D.T., Wheeler M.A.,
Ellis J.A., Skepper J.N., Vorgerd M., Schlotter-Weigel B.,
Weissberg P.L., Roberts R.G., Wehnert M., Shanahan C.M.;
"Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss
muscular dystrophy and are critical for nuclear envelope integrity.";
Hum. Mol. Genet. 16:2816-2833(2007).
[29]
VARIANTS ARG-655; THR-3088 AND SER-3892.
PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644;
Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E.,
van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C.,
Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S.,
Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T.,
Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M.,
Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A.,
van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.;
"Identification of pathogenic gene variants in small families with
intellectually disabled siblings by exome sequencing.";
J. Med. Genet. 50:802-811(2013).
[30]
VARIANT SER-1062.
PubMed=25787250; DOI=10.1073/pnas.1503696112;
Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
Bjoerklund P., Lifton R.P.;
"Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
insulin-producing adenomas.";
Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
-!- FUNCTION: Multi-isomeric modular protein which forms a linking
network between organelles and the actin cytoskeleton to maintain
the subcellular spatial organization. As a component of the LINC
(LInker of Nucleoskeleton and Cytoskeleton) complex involved in
the connection between the nuclear lamina and the cytoskeleton.
The nucleocytoplasmic interactions established by the LINC complex
play an important role in the transmission of mechanical forces
across the nuclear envelope and in nuclear movement and
positioning. May be involved in nucleus-centrosome attachment and
nuclear migration in neural progenitors implicating LINC complex
association with SUN1/2 and probably association with cytoplasmic
dynein-dynactin motor complexes; SYNE1 and SYNE2 may act
redundantly. Required for centrosome migration to the apical cell
surface during early ciliogenesis. May be involved in nuclear
remodeling during sperm head formation in spermatogenenis; a
probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei
to posterior cytoskeletal structures such as the manchette.
{ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:11792814,
ECO:0000269|PubMed:18396275}.
-!- SUBUNIT: Core component of LINC complexes which are composed of
inner nuclear membrane SUN domain-containing proteins coupled to
outer nuclear membrane KASH domain-containing nesprins. SUN and
KASH domain-containing proteins seem to bind each other
promiscuously; however, differentially expression of LINC complex
constituents can give rise to specific assemblies. At least
SUN1/2-containing core LINC complexes are proposed to be hexameric
composed of three protomers of each KASH and SUN domain-containing
protein. The SUN2:SYNE1/KASH1 LINC complex is a heterohexamer; the
homotrimeric cloverleave-like conformation of the SUN domain is a
prerequisite for LINC complex formation in which three separate
SYNE1/KASH1 peptides bind at the interface of adjacent SUN
domains. Self-associates. Interacts with SYNE3. Interacts with
SPAG4/SUN4. May interact with MUSK. Interacts with F-actin via its
N-terminal domain. Interacts with EMD and LMNA in vitro.
{ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:12163176,
ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:22518138}.
-!- INTERACTION:
Q9NRI5:DISC1; NbExp=6; IntAct=EBI-928867, EBI-529989;
P50402:EMD; NbExp=5; IntAct=EBI-10760352, EBI-489887;
O94901:SUN1; NbExp=2; IntAct=EBI-6170938, EBI-2796904;
Q9UH99:SUN2; NbExp=3; IntAct=EBI-928867, EBI-1044964;
-!- SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000305};
Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm,
cytoskeleton. Cytoplasm, myofibril, sarcomere. Note=The largest
part of the protein is cytoplasmic, while its C-terminal part is
associated with the nuclear envelope, most probably the outer
nuclear membrane. In skeletal and smooth muscles, a significant
amount is found in the sarcomeres. In myoblasts, relocalized from
the nuclear envelope to the nucleus and cytoplasm during cell
differentiation.
-!- SUBCELLULAR LOCATION: Isoform GSRP-56: Golgi apparatus
{ECO:0000269|PubMed:16875688}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1; Synonyms=Nesprin-1 Giant, Enaptin;
IsoId=Q8NF91-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q8NF91-2; Sequence=VSP_007130;
Name=3; Synonyms=Alpha;
IsoId=Q8NF91-3; Sequence=VSP_007132, VSP_007144;
Name=4;
IsoId=Q8NF91-4; Sequence=VSP_007134, VSP_007139, VSP_007140,
VSP_007144;
Name=5;
IsoId=Q8NF91-5; Sequence=VSP_007135, VSP_007136;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q8NF91-6; Sequence=VSP_007137, VSP_007138;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q8NF91-7; Sequence=VSP_007141, VSP_007142;
Note=No experimental confirmation available.;
Name=8; Synonyms=Beta 2;
IsoId=Q8NF91-8; Sequence=VSP_007131;
Name=9; Synonyms=Alpha 2;
IsoId=Q8NF91-9; Sequence=VSP_007133, VSP_007143, VSP_007144;
Name=10; Synonyms=drop1;
IsoId=Q8NF91-10; Sequence=VSP_057478, VSP_057479, VSP_057480;
Note=Lost in uterus, cervix, kidney, lung, thyroid and pancreas
carcinomas, already at early tumor stages.
{ECO:0000269|PubMed:18709643};
Name=11; Synonyms=myne-1, 131kDa;
IsoId=Q8NF91-11; Sequence=VSP_057476;
Note=Muscle-specific.;
Name=GSRP-56; Synonyms=56kDa;
IsoId=Q8NF91-12; Sequence=VSP_057477, VSP_057481, VSP_057482;
Note=Interacts with TRPV2. {ECO:0000269|PubMed:16875688};
-!- TISSUE SPECIFICITY: Expressed in HeLa, A431, A172 and HaCaT cells
(at protein level). Widely expressed. Highly expressed in skeletal
and smooth muscles, heart, spleen, peripheral blood leukocytes,
pancreas, cerebellum, stomach, kidney and placenta. Isoform GSRP-
56 is predominantly expressed in heart and skeletal muscle (at
protein level). {ECO:0000269|PubMed:11792814,
ECO:0000269|PubMed:11801724, ECO:0000269|PubMed:15093733,
ECO:0000269|PubMed:16875688, ECO:0000269|PubMed:22518138}.
-!- DOMAIN: The KASH domain, which contains a transmembrane domain,
mediates the nuclear envelope targeting and is involved in the
binding to SUN1 and SUN2 through recognition of their SUN domains.
{ECO:0000269|PubMed:18396275}.
-!- PTM: The disulfid bond with SUN1 or SUN2 is required for stability
of the respective LINC complex under tensile forces.
{ECO:0000250|UniProtKB:Q8WXH0}.
-!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 8 (SCAR8)
[MIM:610743]: Spinocerebellar ataxia is a clinically and
genetically heterogeneous group of cerebellar disorders. Patients
show progressive incoordination of gait and often poor
coordination of hands, speech and eye movements, due to
degeneration of the cerebellum with variable involvement of the
brainstem and spinal cord. SCAR8 is an autosomal recessive form.
{ECO:0000269|PubMed:17159980}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Emery-Dreifuss muscular dystrophy 4, autosomal dominant
(EDMD4) [MIM:612998]: A form of Emery-Dreifuss muscular dystrophy,
a degenerative myopathy characterized by weakness and atrophy of
muscle without involvement of the nervous system, early
contractures of the elbows, Achilles tendons and spine, and
cardiomyopathy associated with cardiac conduction defects.
{ECO:0000269|PubMed:17761684}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC02992.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH39121.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAM95335.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin.; Evidence={ECO:0000305};
Sequence=BAB71097.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
Sequence=BAC04284.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAD28486.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Enaptin entry;
URL="https://en.wikipedia.org/wiki/Enaptin";
-----------------------------------------------------------------------
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EMBL; AY061755; AAL33798.1; -; mRNA.
EMBL; AY061756; AAL33799.1; -; mRNA.
EMBL; AY184203; AAO27771.1; -; mRNA.
EMBL; AY184206; AAO27774.1; -; mRNA.
EMBL; AF535142; AAN03486.1; -; mRNA.
EMBL; AF444779; AAL38031.1; -; mRNA.
EMBL; FM162565; CAQ57272.1; -; mRNA.
EMBL; AF495910; AAN60442.1; -; mRNA.
EMBL; AL049548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL589963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL078582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL357081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL450401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF458330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039121; AAH39121.1; ALT_INIT; mRNA.
EMBL; AY135172; AAM95335.1; ALT_SEQ; mRNA.
EMBL; AY183142; AAO23669.1; -; mRNA.
EMBL; AK056122; BAB71097.1; ALT_SEQ; mRNA.
EMBL; AK094094; BAC04284.1; ALT_INIT; mRNA.
EMBL; AB051543; BAB21847.1; -; mRNA.
EMBL; AL713682; CAD28486.2; ALT_INIT; mRNA.
EMBL; AB033088; BAA86576.1; -; mRNA.
EMBL; AB018339; BAA34516.2; -; mRNA.
EMBL; AF043290; AAC02992.2; ALT_INIT; mRNA.
CCDS; CCDS5235.1; -. [Q8NF91-4]
CCDS; CCDS5236.2; -. [Q8NF91-1]
RefSeq; NP_001334631.1; NM_001347702.1.
RefSeq; NP_149062.1; NM_033071.3.
RefSeq; NP_892006.3; NM_182961.3. [Q8NF91-1]
UniGene; Hs.12967; -.
PDB; 4DXR; X-ray; 2.32 A; B=8769-8797.
PDBsum; 4DXR; -.
ProteinModelPortal; Q8NF91; -.
SMR; Q8NF91; -.
BioGrid; 116928; 38.
CORUM; Q8NF91; -.
IntAct; Q8NF91; 22.
MINT; Q8NF91; -.
STRING; 9606.ENSP00000356224; -.
CarbonylDB; Q8NF91; -.
iPTMnet; Q8NF91; -.
PhosphoSitePlus; Q8NF91; -.
BioMuta; SYNE1; -.
DMDM; 425906075; -.
EPD; Q8NF91; -.
MaxQB; Q8NF91; -.
PaxDb; Q8NF91; -.
PeptideAtlas; Q8NF91; -.
PRIDE; Q8NF91; -.
ProteomicsDB; 73268; -.
ProteomicsDB; 73269; -. [Q8NF91-2]
ProteomicsDB; 73270; -. [Q8NF91-3]
ProteomicsDB; 73271; -. [Q8NF91-4]
ProteomicsDB; 73272; -. [Q8NF91-5]
ProteomicsDB; 73273; -. [Q8NF91-6]
ProteomicsDB; 73274; -. [Q8NF91-7]
ProteomicsDB; 73275; -. [Q8NF91-8]
ProteomicsDB; 73276; -. [Q8NF91-9]
Ensembl; ENST00000367253; ENSP00000356222; ENSG00000131018. [Q8NF91-6]
Ensembl; ENST00000367255; ENSP00000356224; ENSG00000131018. [Q8NF91-1]
Ensembl; ENST00000413186; ENSP00000414510; ENSG00000131018. [Q8NF91-5]
GeneID; 23345; -.
KEGG; hsa:23345; -.
UCSC; uc003qot.5; human. [Q8NF91-1]
UCSC; uc003qov.4; human.
CTD; 23345; -.
DisGeNET; 23345; -.
EuPathDB; HostDB:ENSG00000131018.22; -.
GeneCards; SYNE1; -.
GeneReviews; SYNE1; -.
HGNC; HGNC:17089; SYNE1.
HPA; HPA019113; -.
MalaCards; SYNE1; -.
MIM; 608441; gene.
MIM; 610743; phenotype.
MIM; 612998; phenotype.
neXtProt; NX_Q8NF91; -.
OpenTargets; ENSG00000131018; -.
Orphanet; 98853; Autosomal dominant Emery-Dreifuss muscular dystrophy.
Orphanet; 88644; Autosomal recessive ataxia, Beauce type.
Orphanet; 319332; Autosomal recessive myogenic arthrogryposis multiplex congenita.
PharmGKB; PA134975331; -.
eggNOG; KOG0516; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00900000140842; -.
HOVERGEN; HBG066187; -.
InParanoid; Q8NF91; -.
KO; K19326; -.
OMA; QVRCAEG; -.
OrthoDB; EOG091G0007; -.
TreeFam; TF329280; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
ChiTaRS; SYNE1; human.
GeneWiki; Enaptin; -.
GenomeRNAi; 23345; -.
PRO; PR:Q8NF91; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000131018; -.
ExpressionAtlas; Q8NF91; baseline and differential.
Genevisible; Q8NF91; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:BHF-UCL.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0030017; C:sarcomere; IDA:MGI.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005521; F:lamin binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0090286; P:cytoskeletal anchoring at nuclear membrane; IDA:UniProtKB.
GO; GO:0007030; P:Golgi organization; IDA:UniProtKB.
GO; GO:0042692; P:muscle cell differentiation; IDA:UniProtKB.
GO; GO:0090292; P:nuclear matrix anchoring at nuclear membrane; IDA:UniProtKB.
GO; GO:0006997; P:nucleus organization; NAS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR012315; KASH.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR002017; Spectrin_repeat.
InterPro; IPR030265; SYNE1.
PANTHER; PTHR44867; PTHR44867; 1.
Pfam; PF00307; CH; 2.
Pfam; PF10541; KASH; 1.
Pfam; PF00435; Spectrin; 10.
SMART; SM00033; CH; 2.
SMART; SM01249; KASH; 1.
SMART; SM00150; SPEC; 45.
SUPFAM; SSF47576; SSF47576; 2.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS51049; KASH; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Differentiation;
Disease mutation; Disulfide bond; Emery-Dreifuss muscular dystrophy;
Golgi apparatus; Membrane; Neurodegeneration; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Spermatogenesis;
Transmembrane; Transmembrane helix.
CHAIN 1 8797 Nesprin-1.
/FTId=PRO_0000163591.
TOPO_DOM 1 8746 Cytoplasmic. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
TRANSMEM 8747 8767 Helical; Anchor for type IV membrane
protein. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
TOPO_DOM 8768 8797 Perinuclear space. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
DOMAIN 27 134 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 178 283 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 314 397 Spectrin 1.
REPEAT 398 502 Spectrin 2.
REPEAT 503 609 Spectrin 3.
REPEAT 610 703 Spectrin 4.
REPEAT 704 815 Spectrin 5.
REPEAT 816 923 Spectrin 6.
REPEAT 924 1024 Spectrin 7.
REPEAT 1025 1122 Spectrin 8.
REPEAT 1123 1246 Spectrin 9.
REPEAT 1247 1335 Spectrin 10.
REPEAT 1336 1444 Spectrin 11.
REPEAT 1445 1550 Spectrin 12.
REPEAT 1551 1653 Spectrin 13.
REPEAT 1654 1763 Spectrin 14.
REPEAT 1764 1879 Spectrin 15.
REPEAT 1880 1976 Spectrin 16.
REPEAT 1977 2081 Spectrin 17.
REPEAT 2082 2195 Spectrin 18.
REPEAT 2196 2303 Spectrin 19.
REPEAT 2304 2401 Spectrin 20.
REPEAT 2402 2513 Spectrin 21.
REPEAT 2514 2619 Spectrin 22.
REPEAT 2620 2731 Spectrin 23.
REPEAT 2732 2838 Spectrin 24.
REPEAT 2839 2962 Spectrin 25.
REPEAT 2963 3062 Spectrin 26.
REPEAT 3063 3171 Spectrin 27.
REPEAT 3172 3275 Spectrin 28.
REPEAT 3276 3387 Spectrin 29.
REPEAT 3388 3490 Spectrin 30.
REPEAT 3491 3593 Spectrin 31.
REPEAT 3594 3720 Spectrin 32.
REPEAT 3721 3814 Spectrin 33.
REPEAT 3815 3920 Spectrin 34.
REPEAT 3921 4028 Spectrin 35.
REPEAT 4029 4139 Spectrin 36.
REPEAT 4140 4235 Spectrin 37.
REPEAT 4236 4339 Spectrin 38.
REPEAT 4340 4451 Spectrin 39.
REPEAT 4452 4560 Spectrin 40.
REPEAT 4561 4669 Spectrin 41.
REPEAT 4670 4776 Spectrin 42.
REPEAT 4777 4882 Spectrin 43.
REPEAT 4883 4991 Spectrin 44.
REPEAT 4992 5099 Spectrin 45.
REPEAT 5100 5209 Spectrin 46.
REPEAT 5210 5318 Spectrin 47.
REPEAT 5319 5424 Spectrin 48.
REPEAT 5425 5522 Spectrin 49.
REPEAT 5523 5630 Spectrin 50.
REPEAT 5631 5736 Spectrin 51.
REPEAT 5737 5842 Spectrin 52.
REPEAT 5962 6071 Spectrin 53.
REPEAT 6072 6178 Spectrin 54.
REPEAT 6374 6485 Spectrin 55.
REPEAT 6486 6581 Spectrin 56.
REPEAT 6582 6691 Spectrin 57.
REPEAT 6692 6795 Spectrin 58.
REPEAT 6796 6902 Spectrin 59.
REPEAT 6903 7020 Spectrin 60.
REPEAT 7021 7128 Spectrin 61.
REPEAT 7129 7237 Spectrin 62.
REPEAT 7238 7350 Spectrin 63.
REPEAT 7351 7454 Spectrin 64.
REPEAT 7455 7558 Spectrin 65.
REPEAT 7559 7671 Spectrin 66.
REPEAT 7672 7783 Spectrin 67.
REPEAT 7784 7883 Spectrin 68.
REPEAT 7884 7997 Spectrin 69.
REPEAT 7998 8106 Spectrin 70.
REPEAT 8107 8216 Spectrin 71.
REPEAT 8329 8438 Spectrin 72.
REPEAT 8439 8548 Spectrin 73.
REPEAT 8549 8666 Spectrin 74.
DOMAIN 8738 8797 KASH. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
REGION 1 289 Actin-binding.
COILED 314 8666 {ECO:0000255}.
COMPBIAS 8663 8729 Ser-rich.
MOD_RES 732 732 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZWR6}.
MOD_RES 2270 2270 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6ZWR6}.
MOD_RES 5657 5657 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZWR6}.
MOD_RES 8223 8223 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:24275569}.
MOD_RES 8274 8274 Phosphothreonine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 8277 8277 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 8280 8280 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 8305 8305 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZWR6}.
MOD_RES 8360 8360 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
DISULFID 8774 8774 Interchain (C-563 in SUN2); alternate.
{ECO:0000250|UniProtKB:Q8WXH0}.
DISULFID 8774 8774 Interchain (with C-657 in SUN1);
alternate.
{ECO:0000250|UniProtKB:Q8WXH0}.
VAR_SEQ 1 7843 Missing (in isoform 9).
{ECO:0000303|Ref.6}.
/FTId=VSP_007133.
VAR_SEQ 1 7838 Missing (in isoform 3).
{ECO:0000303|PubMed:11792814}.
/FTId=VSP_007132.
VAR_SEQ 1 7658 Missing (in isoform 11).
{ECO:0000303|PubMed:11801724}.
/FTId=VSP_057476.
VAR_SEQ 1 5585 Missing (in isoform 8).
{ECO:0000303|Ref.6}.
/FTId=VSP_007131.
VAR_SEQ 1 5476 Missing (in isoform 2).
{ECO:0000303|PubMed:11792814}.
/FTId=VSP_007130.
VAR_SEQ 1 2918 Missing (in isoform GSRP-56).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057477.
VAR_SEQ 103 103 K -> KSMHRGSP (in isoform 4).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_007134.
VAR_SEQ 297 313 Missing (in isoform 10).
{ECO:0000303|PubMed:18709643}.
/FTId=VSP_057478.
VAR_SEQ 1437 1443 DIKTMEM -> EYVIDKS (in isoform 5).
{ECO:0000303|PubMed:11214970}.
/FTId=VSP_007135.
VAR_SEQ 1444 8797 Missing (in isoform 5).
{ECO:0000303|PubMed:11214970}.
/FTId=VSP_007136.
VAR_SEQ 1702 1725 LQNEVVSQASFYSKLLQLKESLFS -> SSRKCEEGKNKML
FVTVTLFKIIK (in isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_007137.
VAR_SEQ 1726 8797 Missing (in isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_007138.
VAR_SEQ 3049 3049 C -> W (in isoform 10).
{ECO:0000303|PubMed:18709643}.
/FTId=VSP_057479.
VAR_SEQ 3050 8797 Missing (in isoform 10).
{ECO:0000303|PubMed:18709643}.
/FTId=VSP_057480.
VAR_SEQ 3325 3394 ALLSVKQEKEIQMKMIVTRGESVLQNTSPEGIPTIQQQLQS
VKDMWASLLSAGIRCKSQLEGALSKWTSY -> VCIFTQKY
LQPTEFVFLKISRLHPPGVMMSHSLHDKSQMLCECNAVCLG
CTCQRIPESSDPGCFPKNKIK (in isoform GSRP-
56). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_057481.
VAR_SEQ 3395 8797 Missing (in isoform GSRP-56).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057482.
VAR_SEQ 3620 3641 Missing (in isoform 4).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_007139.
VAR_SEQ 3912 3967 Missing (in isoform 4).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_007140.
VAR_SEQ 5571 5580 TLLEESKEID -> VTLGKIIFKK (in isoform 7).
{ECO:0000303|PubMed:10574462}.
/FTId=VSP_007141.
VAR_SEQ 5581 8797 Missing (in isoform 7).
{ECO:0000303|PubMed:10574462}.
/FTId=VSP_007142.
VAR_SEQ 7844 7874 AKASHESKASEIEYKLGKVNDRWQHLLDLIA -> MVVAED
LSALRMAEDGCVDADLPDCNCDVTR (in isoform 9).
{ECO:0000303|Ref.6}.
/FTId=VSP_007143.
VAR_SEQ 8325 8325 S -> SDVMIPESPEAYVKLTENAIKNTS (in isoform
3, isoform 4 and isoform 9).
{ECO:0000303|PubMed:11792814,
ECO:0000303|PubMed:15093733,
ECO:0000303|Ref.6}.
/FTId=VSP_007144.
VARIANT 655 655 Q -> R (found in a patient with mild
intellectual disability, spastic
paraplegia, axon neuropathy and
leukoencephalopathy; unknown pathological
significance; dbSNP:rs9397509).
{ECO:0000269|PubMed:24123876}.
/FTId=VAR_056211.
VARIANT 885 885 L -> V (in dbSNP:rs17082709).
/FTId=VAR_056212.
VARIANT 1035 1035 V -> A (in dbSNP:rs214976).
/FTId=VAR_056213.
VARIANT 1062 1062 R -> S. {ECO:0000269|PubMed:25787250}.
/FTId=VAR_074190.
VARIANT 2030 2030 S -> G (in dbSNP:rs35763277).
/FTId=VAR_056214.
VARIANT 2795 2795 A -> V (in dbSNP:rs214950).
/FTId=VAR_056215.
VARIANT 3088 3088 A -> T (found in a patient with mild
intellectual disability, spastic
paraplegia, axon neuropathy and
leukoencephalopathy; unknown pathological
significance; dbSNP:rs398123005).
{ECO:0000269|PubMed:24123876}.
/FTId=VAR_070561.
VARIANT 3671 3671 V -> M (in a colorectal cancer sample;
somatic mutation; dbSNP:rs567753957).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036250.
VARIANT 3874 3874 K -> T (in dbSNP:rs13210127).
/FTId=VAR_056216.
VARIANT 3892 3892 L -> S (found in a patient with mild
intellectual disability, spastic
paraplegia, axon neuropathy and
leukoencephalopathy; unknown pathological
significance; dbSNP:rs180727534).
{ECO:0000269|PubMed:24123876}.
/FTId=VAR_070562.
VARIANT 3954 3954 S -> T (in dbSNP:rs7775119).
/FTId=VAR_056217.
VARIANT 4060 4060 E -> D (in dbSNP:rs4645434).
/FTId=VAR_056218.
VARIANT 4121 4121 K -> N (in dbSNP:rs28385621).
/FTId=VAR_056219.
VARIANT 4121 4121 K -> R (in dbSNP:rs9479297).
/FTId=VAR_056220.
VARIANT 4203 4203 E -> K (in dbSNP:rs2130262).
/FTId=VAR_056221.
VARIANT 4210 4210 E -> D (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036251.
VARIANT 4223 4223 R -> H (in a colorectal cancer sample;
somatic mutation; dbSNP:rs140492158).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036252.
VARIANT 4546 4546 V -> I (in dbSNP:rs4870093).
/FTId=VAR_056222.
VARIANT 4596 4596 S -> T (in dbSNP:rs6911096).
{ECO:0000269|PubMed:10574462,
ECO:0000269|PubMed:12408964}.
/FTId=VAR_056223.
VARIANT 4944 4944 L -> M (in dbSNP:rs2306916).
/FTId=VAR_056224.
VARIANT 5015 5015 L -> M (in dbSNP:rs2306916).
{ECO:0000269|PubMed:10574462,
ECO:0000269|PubMed:12408964}.
/FTId=VAR_056225.
VARIANT 5377 5377 M -> L (in dbSNP:rs35987150).
/FTId=VAR_056226.
VARIANT 5426 5426 T -> M (in dbSNP:rs2306914).
/FTId=VAR_056227.
VARIANT 5507 5507 L -> R (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036253.
VARIANT 6566 6566 M -> I (in dbSNP:rs35654757).
/FTId=VAR_056228.
VARIANT 6664 6664 T -> I (in dbSNP:rs35079654).
/FTId=VAR_056229.
VARIANT 6951 6951 Q -> H (in dbSNP:rs3945783).
/FTId=VAR_056230.
VARIANT 7302 7302 F -> V (in dbSNP:rs2147377).
{ECO:0000269|PubMed:11792814,
ECO:0000269|PubMed:12408964,
ECO:0000269|PubMed:9872452,
ECO:0000269|Ref.6}.
/FTId=VAR_056231.
VARIANT 7506 7506 S -> G (in dbSNP:rs35763277).
/FTId=VAR_056232.
VARIANT 8095 8095 R -> H (in EDMD4; dbSNP:rs119103246).
{ECO:0000269|PubMed:17761684}.
/FTId=VAR_062974.
VARIANT 8161 8161 N -> H (in dbSNP:rs36215251).
/FTId=VAR_056233.
VARIANT 8168 8168 A -> S (in dbSNP:rs17082236).
/FTId=VAR_056234.
VARIANT 8323 8323 G -> A (in dbSNP:rs2252755).
{ECO:0000269|PubMed:11792814,
ECO:0000269|PubMed:11801724,
ECO:0000269|PubMed:12408964,
ECO:0000269|PubMed:9872452,
ECO:0000269|Ref.6}.
/FTId=VAR_015548.
VARIANT 8387 8387 V -> L (in EDMD4; dbSNP:rs119103247).
{ECO:0000269|PubMed:17761684}.
/FTId=VAR_062975.
VARIANT 8461 8461 E -> K (in EDMD4; dbSNP:rs119103248).
{ECO:0000269|PubMed:17761684}.
/FTId=VAR_062976.
VARIANT 8468 8468 R -> H (in a colorectal cancer sample;
somatic mutation; dbSNP:rs143049227).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036254.
VARIANT 8687 8687 T -> I (in dbSNP:rs35591210).
/FTId=VAR_056235.
VARIANT 8741 8741 L -> M (in dbSNP:rs2295190).
/FTId=VAR_056236.
MUTAGEN 8758 8763 Missing: Abolishes the nuclear envelope
targeting, induces a cytoplasmic
localization.
{ECO:0000269|PubMed:11792814}.
CONFLICT 98 98 F -> L (in Ref. 2; AAN60442).
{ECO:0000305}.
CONFLICT 494 494 S -> P (in Ref. 9; AAM95335).
{ECO:0000305}.
CONFLICT 1440 1440 T -> P (in Ref. 12; CAD28486).
{ECO:0000305}.
CONFLICT 3096 3096 N -> D (in Ref. 10; BAB71097).
{ECO:0000305}.
CONFLICT 5526 5526 A -> T (in Ref. 1; AAL33798).
{ECO:0000305}.
CONFLICT 5564 5564 E -> K (in Ref. 1; AAL33798).
{ECO:0000305}.
CONFLICT 5735 5735 E -> A (in Ref. 5; AAN03486).
{ECO:0000305}.
CONFLICT 6549 6549 K -> E (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
CONFLICT 6626 6626 L -> P (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
CONFLICT 6645 6645 E -> V (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
CONFLICT 6923 6923 I -> T (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
CONFLICT 6929 6929 V -> A (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
CONFLICT 7075 7075 E -> D (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
CONFLICT 7091 7091 N -> T (in Ref. 1; AAL33798, 2; AAN60442
and 6; AAO27774). {ECO:0000305}.
HELIX 8780 8782 {ECO:0000244|PDB:4DXR}.
STRAND 8783 8785 {ECO:0000244|PDB:4DXR}.
STRAND 8787 8793 {ECO:0000244|PDB:4DXR}.
SEQUENCE 8797 AA; 1011086 MW; 02A53B8AFBF34A17 CRC64;
MATSRGASRC PRDIANVMQR LQDEQEIVQK RTFTKWINSH LAKRKPPMVV DDLFEDMKDG
VKLLALLEVL SGQKLPCEQG RRMKRIHAVA NIGTALKFLE GRKIKLVNIN STDIADGRPS
IVLGLMWTII LYFQIEELTS NLPQLQSLSS SASSVDSIVS SETPSPPSKR KVTTKIQGNA
KKALLKWVQY TAGKQTGIEV KDFGKSWRSG VAFHSVIHAI RPELVDLETV KGRSNRENLE
DAFTIAETEL GIPRLLDPED VDVDKPDEKS IMTYVAQFLK HYPDIHNAST DGQEDDEILP
GFPSFANSVQ NFKREDRVIF KEMKVWIEQF ERDLTRAQMV ESNLQDKYQS FKHFRVQYEM
KRKQIEHLIQ PLHRDGKLSL DQALVKQSWD RVTSRLFDWH IQLDKSLPAP LGTIGAWLYR
AEVALREEIT VQQVHEETAN TIQRKLEQHK DLLQNTDAHK RAFHEIYRTR SVNGIPVPPD
QLEDMAERFH FVSSTSELHL MKMEFLELKY RLLSLLVLAE SKLKSWIIKY GRRESVEQLL
QNYVSFIENS KFFEQYEVTY QILKQTAEMY VKADGSVEEA ENVMKFMNET TAQWRNLSVE
VRSVRSMLEE VISNWDRYGN TVASLQAWLE DAEKMLNQSE NAKKDFFRNL PHWIQQHTAM
NDAGNFLIET CDEMVSRDLK QQLLLLNGRW RELFMEVKQY AQADEMDRMK KEYTDCVVTL
SAFATEAHKK LSEPLEVSFM NVKLLIQDLE DIEQRVPVMD AQYKIITKTA HLITKESPQE
EGKEMFATMS KLKEQLTKVK ECYSPLLYES QQLLIPLEEL EKQMTSFYDS LGKINEIITV
LEREAQSSAL FKQKHQELLA CQENCKKTLT LIEKGSQSVQ KFVTLSNVLK HFDQTRLQRQ
IADIHVAFQS MVKKTGDWKK HVETNSRLMK KFEESRAELE KVLRIAQEGL EEKGDPEELL
RRHTEFFSQL DQRVLNAFLK ACDELTDILP EQEQQGLQEA VRKLHKQWKD LQGEAPYHLL
HLKIDVEKNR FLASVEECRT ELDRETKLMP QEGSEKIIKE HRVFFSDKGP HHLCEKRLQL
IEELCVKLPV RDPVRDTPGT CHVTLKELRA AIDSTYRKLM EDPDKWKDYT SRFSEFSSWI
STNETQLKGI KGEAIDTANH GEVKRAVEEI RNGVTKRGET LSWLKSRLKV LTEVSSENEA
QKQGDELAKL SSSFKALVTL LSEVEKMLSN FGDCVQYKEI VKNSLEELIS GSKEVQEQAE
KILDTENLFE AQQLLLHHQQ KTKRISAKKR DVQQQIAQAQ QGEGGLPDRG HEELRKLEST
LDGLERSRER QERRIQVTLR KWERFETNKE TVVRYLFQTG SSHERFLSFS SLESLSSELE
QTKEFSKRTE SIAVQAENLV KEASEIPLGP QNKQLLQQQA KSIKEQVKKL EDTLEEDIKT
MEMVKTKWDH FGSNFETLSV WITEKEKELN ALETSSSAMD MQISQIKVTI QEIESKLSSI
VGLEEEAQSF AQFVTTGESA RIKAKLTQIR RYGEELREHA QCLEGTILGH LSQQQKFEEN
LRKIQQSVSE FEDKLAVPIK ICSSATETYK VLQEHMDLCQ ALESLSSAIT AFSASARKVV
NRDSCVQEAA ALQQQYEDIL RRAKERQTAL ENLLAHWQRL EKELSSFLTW LERGEAKASS
PEMDISADRV KVEGELQLIQ ALQNEVVSQA SFYSKLLQLK ESLFSVASKD DVKMMKLHLE
QLDERWRDLP QIINKRINFL QSVVAEHQQF DELLLSFSVW IKLFLSELQT TSEISIMDHQ
VALTRHKDHA AEVESKKGEL QSLQGHLAKL GSLGRAEDLH LLQGKAEDCF QLFEEASQVV
ERRQLALSHL AEFLQSHASL SGILRQLRQT VEATNSMNKN ESDLIEKDLN DALQNAKALE
SAAVSLDGIL SKAQYHLKIG SSEQRTSCRA TADQLCGEVE RIQNLLGTKQ SEADALAVLK
KAFQDQKEEL LKSIEDIEER TDKERLKEPT RQALQQRLRV FNQLEDELNS HEHELCWLKD
KAKQIAQKDV AFAPEVDREI NRLEVTWDDT KRLIHENQGQ CCGLIDLMRE YQNLKSAVSK
VLENASSVIV TRTTIKDQED LKWAFSKHET AKNKMNYKQK DLDNFTSKGK HLLSELKKIH
SSDFSLVKTD MESTVDKWLD VSEKLEENMD RLRVSLSIWD DVLSTRDEIE GWSNNCVPQM
AENISNLDNH LRAEELLKEF ESEVKNKALR LEELHSKVND LKELTKNLET PPDLQFIEAD
LMQKLEHAKE ITEVAKGTLK DFTAQSTQVE KFINDITTWF TKVEESLMNC AQNETCEALK
KVKDIQKELQ SQQSNISSTQ ENLNSLCRKY HSAELESLGR AMTGLIKKHE AVSQLCSKTQ
ASLQESLEKH FSESMQEFQE WFLGAKAAAK ESSDRTGDSK VLEAKLHDLQ NILDSVSDGQ
SKLDAVTQEG QTLYAHLSKQ IVSSIQEQIT KANEEFQAFL KQCLKDKQAL QDCASELGSF
EDQHRKLNLW IHEMEERFNT ENLGESKQHI PEKKNEVHKV EMFLGELLAA RESLDKLSQR
GQLLSEEGHG AGQEGRLCSQ LLTSHQNLLR MTKEKLRSCQ VALQEHEALE EALQSMWFWV
KAIQDRLACA ESTLGSKDTL EKRLSQIQDI LLMKGEGEVK LNMAIGKGEQ ALRSSNKEGQ
RVIQTQLETL KEVWADIMSS SVHAQSTLES VISQWNDYVE RKNQLEQWME SVDQKIEHPL
QPQPGLKEKF VLLDHLQSIL SEAEDHTRAL HRLIAKSREL YEKTEDESFK DTAQEELKTQ
FNDIMTVAKE KMRKVEEIVK DHLMYLDAVH EFTDWLHSAK EELHRWSDMS GDSSATQKKL
SKIKELIDSR EIGASRLSRV ESLAPEVKQN TTASGCELMH TEMQALRADW KQWEDSVFQT
QSCLENLVSQ MALSEQEFSG QVAQLEQALE QFSALLKTWA QQLTLLEGKN TDEEIVECWH
KGQEILDALQ KAEPRTEDLK SQLNELCRFS RDLSTYSGKV SGLIKEYNCL CLQASKGCQN
KEQILQQRFR KAFRDFQQWL VNAKITTAKC FDIPQNISEV STSLQKIQEF LSESENGQHK
LNMMLSKGEL LSTLLTKEKA KGIQAKVTAA KEDWKNFHSN LHQKESALEN LKIQMKDFEV
SAEPIQDWLS KTEKMVHESS NRLYDLPAKR REQQKLQSVL EEIHCYEPQL NRLKEKAQQL
WEGQAASKSF RHRVSQLSSQ YLALSNLTKE KVSRLDRIVA EHNQFSLGIK ELQDWMTDAI
HMLDSYCHPT SDKSVLDSRT LKLEALLSVK QEKEIQMKMI VTRGESVLQN TSPEGIPTIQ
QQLQSVKDMW ASLLSAGIRC KSQLEGALSK WTSYQDGVRQ FSGWMDSMEA NLNESERQHA
ELRDKTTMLG KAKLLNEEVL SYSSLLETIE VKGAGMTEHY VTQLELQDLQ ERYRAIQERA
KEAVTKSEKL VRLHQEYQRD LKAFEVWLGQ EQEKLDQYSV LEGDAHTHET TLRDLQELQV
HCAEGQALLN SVLHTREDVI PSGIPQAEDR ALESLRQDWQ AYQHRLSETR TQFNNVVNKL
RLMEQKFQQV DEWLKTAEEK VSPRTRRQSN RATKEIQLHQ MKKWHEEVTA YRDEVEEVGA
RAQEILDESH VNSRMGCQAT QLTSRYQALL LQVLEQIKFL EEEIQSLEES ESSLSSYSDW
YGSTHKNFKN VATKIDKVDT VMMGKKLKTL EVLLKDMEKG HSLLKSAREK GERAVKYLEE
GEAERLRKEI HDHMEQLKEL TSTVRKEHMT LEKGLHLAKE FSDKCKALTQ WIAEYQEILH
VPEEPKMELY EKKAQLSKYK SLQQTVLSHE PSVKSVREKG EALLELVQDV TLKDKIDQLQ
SDYQDLCSIG KEHVFSLEAK VKDHEDYNSE LQEVEKWLLQ MSGRLVAPDL LETSSLETIT
QQLAHHKAMM EEIAGFEDRL NNLQMKGDTL IGQCADHLQA KLKQNVHAHL QGTKDSYSAI
CSTAQRMYQS LEHELQKHVS RQDTLQQCQA WLSAVQPDLE PSPQPPLSRA EAIKQVKHFR
ALQEQARTYL DLLCSMCDLS NASVKTTAKD IQQTEQTIEQ KLVQAQNLTQ GWEEIKHLKS
ELWIYLQDAD QQLQNMKRRH SELELNIAQN MVSQVKDFVK KLQSKQASVN TIIEKVNKLT
KKEESPEHKE INHLNDQWLD LCRQSNNLCL QREEDLQRTR DYHDCMNVVE VFLEKFTTEW
DNLARSDAES TAVHLEALKK LALALQERKY AIEDLKDQKQ KMIEHLNLDD KELVKEQTSH
LEQRWFQLED LIKRKIQVSV TNLEELNVVQ SRFQELMEWA EEQQPNIAEA LKQSPPPDMA
QNLLMDHLAI CSELEAKQML LKSLIKDADR VMADLGLNER QVIQKALSDA QSHVNCLSDL
VGQRRKYLNK ALSEKTQFLM AVFQATSQIQ QHERKIMFRE HICLLPDDVS KQVKTCKSAQ
ASLKTYQNEV TGLWAQGREL MKEVTEQEKS EVLGKLQELQ SVYDSVLQKC SHRLQELEKN
LVSRKHFKED FDKACHWLKQ ADIVTFPEIN LMNESSELHT QLAKYQNILE QSPEYENLLL
TLQRTGQTIL PSLNEVDHSY LSEKLNALPR QFNVIVALAK DKFYKVQEAI LARKEYASLI
ELTTQSLSEL EAQFLRMSKV PTDLAVEEAL SLQDGCRAIL DEVAGLGEAV DELNQKKEGF
RSTGQPWQPD KMLHLVTLYH RLKRQTEQRV SLLEDTTSAY QEHEKMCQQL ERQLKSVKEE
QSKVNEETLP AEEKLKMYHS LAGSLQDSGI VLKRVTIHLE DLAPHLDPLA YEKARHQIQS
WQGELKLLTS AIGETVTECE SRMVQSIDFQ TEMSRSLDWL RRVKAELSGP VYLDLNLQDI
QEEIRKIQIH QEEVQSSLRI MNALSHKEKE KFTKAKELIS ADLEHSLAEL SELDGDIQEA
LRTRQATLTE IYSQCQRYYQ VFQAANDWLE DAQELLQLAG NGLDVESAEE NLKSHMEFFS
TEDQFHSNLE ELHSLVATLD PLIKPTGKED LEQKVASLEL RSQRMSRDSG AQVDLLQRCT
AQWHDYQKAR EEVIELMNDT EKKLSEFSLL KTSSSHEAEE KLSEHKALVS VVNSFHEKIV
ALEEKASQLE KTGNDASKAT LSRSMTTVWQ RWTRLRAVAQ DQEKILEDAV DEWTGFNNKV
KKATEMIDQL QDKLPGSSAE KASKAELLTL LEYHDTFVLE LEQQQSALGM LRQQTLSMLQ
DGAAPTPGEE PPLMQEITAM QDRCLNMQEK VKTNGKLVKQ ELKDREMVET QINSVKCWVQ
ETKEYLGNPT IEIDAQLEEL QILLTEATNH RQNIEKMAEE QKEKYLGLYT ILPSELSLQL
AEVALDLKIR DQIQDKIKEV EQSKATSQEL SRQIQKLAKD LTTILTKLKA KTDNVVQAKT
DQKVLGEELD GCNSKLMELD AAVQKFLEQN GQLGKPLAKK IGKLTELHQQ TIRQAENRLS
KLNQAASHLE EYNEMLELIL KWIEKAKVLA HGTIAWNSAS QLREQYILHQ TLLEESKEID
SELEAMTEKL QYLTSVYCTE KMSQQVAELG RETEELRQMI KIRLQNLQDA AKDMKKFEAE
LKKLQAALEQ AQATLTSPEV GRLSLKEQLS HRQHLLSEME SLKPKVQAVQ LCQSALRIPE
DVVASLPLCH AALRLQEEAS RLQHTAIQQC NIMQEAVVQY EQYEQEMKHL QQLIEGAHRE
IEDKPVATSN IQELQAQISR HEELAQKIKG YQEQIASLNS KCKMLTMKAK HATMLLTVTE
VEGLAEGTED LDGELLPTPS AHPSVVMMTA GRCHTLLSPV TEESGEEGTN SEISSPPACR
SPSPVANTDA SVNQDIAYYQ ALSAERLQTD AAKIHPSTSA SQEFYEPGLE PSATAKLGDL
QRSWETLKNV ISEKQRTLYE ALERQQKYQD SLQSISTKME AIELKLSESP EPGRSPESQM
AEHQALMDEI LMLQDEINEL QSSLAEELVS ESCEADPAEQ LALQSTLTVL AERMSTIRMK
ASGKRQLLEE KLNDQLEEQR QEQALQRYRC EADELDSWLL STKATLDTAL SPPKEPMDME
AQLMDCQNML VEIEQKVVAL SELSVHNENL LLEGKAHTKD EAEQLAGKLR RLKGSLLELQ
RALHDKQLNM QGTAQEKEES DVDLTATQSP GVQEWLAQAR TTWTQQRQSS LQQQKELEQE
LAEQKSLLRS VASRGEEILI QHSAAETSGD AGEKPDVLSQ ELGMEGEKSS AEDQMRMKWE
SLHQEFSTKQ KLLQNVLEQE QEQVLYSRPN RLLSGVPLYK GDVPTQDKSA VTSLLDGLNQ
AFEEVSSQSG GAKRQSIHLE QKLYDGVSAT STWLDDVEER LFVATALLPE ETETCLFNQE
ILAKDIKEMS EEMDKNKNLF SQAFPENGDN RDVIEDTLGC LLGRLSLLDS VVNQRCHQMK
ERLQQILNFQ NDLKVLFTSL ADNKYIILQK LANVFEQPVA EQIEAIQQAE DGLKEFDAGI
IELKRRGDKL QVEQPSMQEL SKLQDMYDEL MMIIGSRRSG LNQNLTLKSQ YERALQDLAD
LLETGQEKMA GDQKIIVSSK EEIQQLLDKH KEYFQGLESH MILTETLFRK IISFAVQKET
QFHTELMAQA SAVLKRAHKR GVELEYILET WSHLDEDQQE LSRQLEVVES SIPSVGLVEE
NEDRLIDRIT LYQHLKSSLN EYQPKLYQVL DDGKRLLISI SCSDLESQLN QLGECWLSNT
NKMSKELHRL ETILKHWTRY QSESADLIHW LQSAKDRLEF WTQQSVTVPQ ELEMVRDHLN
AFLEFSKEVD AQSSLKSSVL STGNQLLRLK KVDTATLRSE LSRIDSQWTD LLTNIPAVQE
KLHQLQMDKL PSRHAISEVM SWISLMENVI QKDEDNIKNS IGYKAIHEYL QKYKGFKIDI
NCKQLTVDFV NQSVLQISSQ DVESKRSDKT DFAEQLGAMN KSWQILQGLV TEKIQLLEGL
LESWSEYENN VQCLKTWFET QEKRLKQQHR IGDQASVQNA LKDCQDLEDL IKAKEKEVEK
IEQNGLALIQ NKKEDVSSIV MSTLRELGQT WANLDHMVGQ LKILLKSVLD QWSSHKVAFD
KINSYLMEAR YSLSRFRLLT GSLEAVQVQV DNLQNLQDDL EKQERSLQKF GSITNQLLKE
CHPPVTETLT NTLKEVNMRW NNLLEEIAEQ LQSSKALLQL WQRYKDYSKQ CASTVQQQED
RTNELLKAAT NKDIADDEVA TWIQDCNDLL KGLGTVKDSL FFLHELGEQL KQQVDASAAS
AIQSDQLSLS QHLCALEQAL CKQQTSLQAG VLDYETFAKS LEALEAWIVE AEEILQGQDP
SHSSDLSTIQ ERMEELKGQM LKFSSMAPDL DRLNELGYRL PLNDKEIKRM QNLNRHWSLI
SSQTTERFSK LQSFLLQHQT FLEKCETWME FLVQTEQKLA VEISGNYQHL LEQQRAHELF
QAEMFSRQQI LHSIIIDGQR LLEQGQVDDR DEFNLKLTLL SNQWQGVIRR AQQRRGIIDS
QIRQWQRYRE MAEKLRKWLV EVSYLPMSGL GSVPIPLQQA RTLFDEVQFK EKVFLRQQGS
YILTVEAGKQ LLLSADSGAE AALQAELAEI QEKWKSASMR LEEQKKKLAF LLKDWEKCEK
GIADSLEKLR TFKKKLSQSL PDHHEELHAE QMRCKELENA VGSWTDDLTQ LSLLKDTLSA
YISADDISIL NERVELLQRQ WEELCHQLSL RRQQIGERLN EWAVFSEKNK ELCEWLTQME
SKVSQNGDIL IEEMIEKLKK DYQEEIAIAQ ENKIQLQQMG ERLAKASHES KASEIEYKLG
KVNDRWQHLL DLIAARVKKL KETLVAVQQL DKNMSSLRTW LAHIESELAK PIVYDSCNSE
EIQRKLNEQQ ELQRDIEKHS TGVASVLNLC EVLLHDCDAC ATDAECDSIQ QATRNLDRRW
RNICAMSMER RLKIEETWRL WQKFLDDYSR FEDWLKSSER TAAFPSSSGV IYTVAKEELK
KFEAFQRQVH ECLTQLELIN KQYRRLAREN RTDSACSLKQ MVHEGNQRWD NLQKRVTSIL
RRLKHFIGQR EEFETARDSI LVWLTEMDLQ LTNIEHFSEC DVQAKIKQLK AFQQEISLNH
NKIEQIIAQG EQLIEKSEPL DAAIIEEELD ELRRYCQEVF GRVERYHKKL IRLPLPDDEH
DLSDRELELE DSAALSDLHW HDRSADSLLS PQPSSNLSLS LAQPLRSERS GRDTPASVDS
IPLEWDHDYD LSRDLESAMS RALPSEDEEG QDDKDFYLRG AVGLSGDHSA LESQIRQLGK
ALDDSRFQIQ QTENIIRSKT PTGPELDTSY KGYMKLLGEC SSSIDSVKRL EHKLKEEEES
LPGFVNLHST ETQTAGVIDR WELLQAQALS KELRMKQNLQ KWQQFNSDLN SIWAWLGDTE
EELEQLQRLE LSTDIQTIEL QIKKLKELQK AVDHRKAIIL SINLCSPEFT QADSKESRDL
QDRLSQMNGR WDRVCSLLEE WRGLLQDALM QCQGFHEMSH GLLLMLENID RRKNEIVPID
SNLDAEILQD HHKQLMQIKH ELLESQLRVA SLQDMSCQLL VNAEGTDCLE AKEKVHVIGN
RLKLLLKEVS RHIKELEKLL DVSSSQQDLS SWSSADELDT SGSVSPTSGR STPNRQKTPR
GKCSLSQPGP SVSSPHSRST KGGSDSSLSE PGPGRSGRGF LFRVLRAALP LQLLLLLLIG
LACLVPMSEE DYSCALSNNF ARSFHPMLRY TNGPPPL


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
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GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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