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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_MOUSE             Reviewed;        8799 AA.
Q6ZWR6; Q8K3T7; Q9ERT7; Q9ERT8;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 2.
12-SEP-2018, entry version 121.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
6808-8799 (ISOFORM 4), INTERACTION WITH MUSK, AND SUBCELLULAR
LOCATION.
PubMed=10878022; DOI=10.1074/jbc.M004775200;
Apel E.D., Lewis R.M., Grady R.M., Sanes J.R.;
"Syne-1, a dystrophin- and Klarsicht-related protein associated with
synaptic nuclei at the neuromuscular junction.";
J. Biol. Chem. 275:31986-31995(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY,
ACTIN-BINDING, AND SUBCELLULAR LOCATION.
STRAIN=BALB/cJ; TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=12958361; DOI=10.1126/science.1088176;
Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.;
"Nuclear membrane proteins with potential disease links found by
subtractive proteomics.";
Science 301:1380-1382(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8308, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
FUNCTION.
PubMed=19596800; DOI=10.1242/jcs.043794;
Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A.,
Gull K., Johnson C.A.;
"Nesprin-2 interacts with meckelin and mediates ciliogenesis via
remodelling of the actin cytoskeleton.";
J. Cell Sci. 122:2716-2726(2009).
[8]
FUNCTION, AND SUBUNIT.
PubMed=19874786; DOI=10.1016/j.neuron.2009.08.018;
Zhang X., Lei K., Yuan X., Wu X., Zhuang Y., Xu T., Xu R., Han M.;
"SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the
nucleus during neurogenesis and neuronal migration in mice.";
Neuron 64:173-187(2009).
[9]
SUBCELLULAR LOCATION.
PubMed=19509342; DOI=10.1073/pnas.0812037106;
Lei K., Zhang X., Ding X., Guo X., Chen M., Zhu B., Xu T., Zhuang Y.,
Xu R., Han M.;
"SUN1 and SUN2 play critical but partially redundant roles in
anchoring nuclei in skeletal muscle cells in mice.";
Proc. Natl. Acad. Sci. U.S.A. 106:10207-10212(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732; THR-2268; SER-5655;
THR-8278; SER-8284 AND THR-8363, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-377 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-8225 (ISOFORM 4), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
SELF-ASSOCIATION, INTERACTION WITH SYNE3, AND TISSUE SPECIFICITY.
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).
[12]
INTERACTION WITH SPAG4.
PubMed=26621829; DOI=10.1242/bio.015768;
Pasch E., Link J., Beck C., Scheuerle S., Alsheimer M.;
"The LINC complex component Sun4 plays a crucial role in sperm head
formation and fertility.";
Biol. Open 4:1792-1802(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.
During interkinetic nuclear migration (INM) at G2 phase and
nuclear migration in neural progenitors its LINC complex
association with SUN1/2 and probably association with cytoplasmic
dynein-dynactin motor complexes functions to pull the nucleus
toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in
cerebellum, midbrain, brain stem, and other brain regions except
cerebral cortex and hippocampus. 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:Q8NF91,
ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786}.
-!- 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
SUN3; proposed to form a spermatogenesis-specific LINC complex
with SUN3 during sperm head formation. May interact with MUSK.
Interacts with SPAG4/SUN4. Interacts with EMD and LMNA in vitro.
Interacts with F-actin via its N-terminal domain. Interacts with
DCTN1 and DYNC1I1/2; suggesting the association with the dynein-
dynactin motor complex. {ECO:0000250|UniProtKB:Q8NF91,
ECO:0000269|PubMed:10878022, ECO:0000269|PubMed:19874786,
ECO:0000269|PubMed:22518138, ECO:0000269|PubMed:26621829}.
-!- INTERACTION:
Q6ZMZ3-1:SYNE3 (xeno); NbExp=2; IntAct=EBI-10760805, EBI-10760907;
-!- 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 {ECO:0000250}.
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 (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Nesprin-1 Giant, Enaptin;
IsoId=Q6ZWR6-1; Sequence=Displayed;
Name=2;
IsoId=Q6ZWR6-2; Sequence=VSP_038791, VSP_038796, VSP_038797,
VSP_038798;
Note=Contains a phosphoserine at position 377.
{ECO:0000244|PubMed:21183079};
Name=3; Synonyms=Syne-1A;
IsoId=Q6ZWR6-3; Sequence=VSP_038791, VSP_038796, VSP_038797;
Note=Contains a phosphoserine at position 377.
{ECO:0000244|PubMed:21183079};
Name=4; Synonyms=Syne-1B;
IsoId=Q6ZWR6-4; Sequence=VSP_038797;
Note=Incomplete sequence. Contains a phosphoserine at position
8225. {ECO:0000244|PubMed:21183079};
Name=5; Synonyms=Enaptin-165;
IsoId=Q6ZWR6-5; Sequence=VSP_038792, VSP_038793, VSP_038794,
VSP_038795;
-!- TISSUE SPECIFICITY: Expressed in C2F3 and CH310T1/2 cells, brain
and skeletal muscle (at protein level).
{ECO:0000269|PubMed:15093733, 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:0000250}.
-!- PTM: The disulfid bond with SUN1 or SUN2 is required for stability
of the respective LINC complex under tensile forces.
{ECO:0000250|UniProtKB:Q8WXH0}.
-!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG24393.1; Type=Frameshift; Positions=6810, 7656, 7658; Evidence={ECO:0000305};
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EMBL; AF281869; AAG24392.1; -; mRNA.
EMBL; AF281870; AAG24393.1; ALT_FRAME; mRNA.
EMBL; AF535143; AAN03487.1; -; mRNA.
EMBL; AK036828; BAC29595.1; -; mRNA.
EMBL; AC156392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC156393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC157020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC159748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC161829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC162381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC162385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS56679.1; -. [Q6ZWR6-3]
CCDS; CCDS56680.1; -. [Q6ZWR6-5]
RefSeq; NP_001073154.1; NM_001079686.1.
UniGene; Mm.331626; -.
ProteinModelPortal; Q6ZWR6; -.
SMR; Q6ZWR6; -.
BioGrid; 211015; 6.
DIP; DIP-60966N; -.
IntAct; Q6ZWR6; 8.
STRING; 10090.ENSMUSP00000039440; -.
CarbonylDB; Q6ZWR6; -.
iPTMnet; Q6ZWR6; -.
PhosphoSitePlus; Q6ZWR6; -.
PaxDb; Q6ZWR6; -.
PeptideAtlas; Q6ZWR6; -.
PRIDE; Q6ZWR6; -.
Ensembl; ENSMUST00000041639; ENSMUSP00000039440; ENSMUSG00000096054. [Q6ZWR6-5]
Ensembl; ENSMUST00000095899; ENSMUSP00000093587; ENSMUSG00000096054. [Q6ZWR6-3]
GeneID; 64009; -.
KEGG; mmu:64009; -.
UCSC; uc007egn.1; mouse. [Q6ZWR6-5]
UCSC; uc007egt.2; mouse. [Q6ZWR6-2]
CTD; 23345; -.
MGI; MGI:1927152; Syne1.
eggNOG; KOG0516; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00900000140842; -.
HOGENOM; HOG000120125; -.
HOVERGEN; HBG106534; -.
InParanoid; Q6ZWR6; -.
KO; K19326; -.
OMA; IETCDEI; -.
OrthoDB; EOG091G00NK; -.
PhylomeDB; Q6ZWR6; -.
TreeFam; TF317709; -.
TreeFam; TF337116; -.
ChiTaRS; Syne1; mouse.
PRO; PR:Q6ZWR6; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000096054; Expressed in 265 organ(s), highest expression level in cerebellum lobe.
ExpressionAtlas; Q6ZWR6; baseline and differential.
Genevisible; Q6ZWR6; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0044327; C:dendritic spine head; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0000932; C:P-body; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
GO; GO:0030017; C:sarcomere; ISO:MGI.
GO; GO:0005819; C:spindle; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005521; F:lamin binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
GO; GO:0090286; P:cytoskeletal anchoring at nuclear membrane; ISO:MGI.
GO; GO:0007030; P:Golgi organization; ISO:MGI.
GO; GO:0042692; P:muscle cell differentiation; ISO:MGI.
GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; ISO:MGI.
GO; GO:0061886; P:negative regulation of mini excitatory postsynaptic potential; ISO:MGI.
GO; GO:0090292; P:nuclear matrix anchoring at nuclear membrane; ISO:MGI.
GO; GO:0007097; P:nuclear migration; IMP:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:MGI.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
GO; GO:1903353; P:regulation of nucleus organization; ISO:MGI.
GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
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; 11.
SMART; SM00033; CH; 2.
SMART; SM01249; KASH; 1.
SMART; SM00150; SPEC; 42.
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;
Actin-binding; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Differentiation; Disulfide bond; Membrane;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Spermatogenesis;
Transmembrane; Transmembrane helix.
CHAIN 1 8799 Nesprin-1.
/FTId=PRO_0000392209.
TOPO_DOM 1 8748 Cytoplasmic. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
TRANSMEM 8749 8769 Helical; Anchor for type IV membrane
protein. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
TOPO_DOM 8770 8799 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 1333 Spectrin 10.
REPEAT 1334 1442 Spectrin 11.
REPEAT 1443 1548 Spectrin 12.
REPEAT 1549 1651 Spectrin 13.
REPEAT 1652 1761 Spectrin 14.
REPEAT 1762 1877 Spectrin 15.
REPEAT 1878 1974 Spectrin 16.
REPEAT 1975 2079 Spectrin 17.
REPEAT 2080 2193 Spectrin 18.
REPEAT 2194 2301 Spectrin 19.
REPEAT 2302 2399 Spectrin 20.
REPEAT 2400 2511 Spectrin 21.
REPEAT 2512 2617 Spectrin 22.
REPEAT 2618 2729 Spectrin 23.
REPEAT 2730 2836 Spectrin 24.
REPEAT 2837 2960 Spectrin 25.
REPEAT 2961 3060 Spectrin 26.
REPEAT 3061 3169 Spectrin 27.
REPEAT 3170 3273 Spectrin 28.
REPEAT 3274 3385 Spectrin 29.
REPEAT 3386 3488 Spectrin 30.
REPEAT 3489 3591 Spectrin 31.
REPEAT 3592 3718 Spectrin 32.
REPEAT 3719 3812 Spectrin 33.
REPEAT 3813 3918 Spectrin 34.
REPEAT 3919 4026 Spectrin 35.
REPEAT 4027 4137 Spectrin 36.
REPEAT 4138 4233 Spectrin 37.
REPEAT 4234 4337 Spectrin 38.
REPEAT 4338 4449 Spectrin 39.
REPEAT 4450 4558 Spectrin 40.
REPEAT 4559 4667 Spectrin 41.
REPEAT 4668 4774 Spectrin 42.
REPEAT 4775 4880 Spectrin 43.
REPEAT 4881 4989 Spectrin 44.
REPEAT 4990 5097 Spectrin 45.
REPEAT 5098 5207 Spectrin 46.
REPEAT 5208 5316 Spectrin 47.
REPEAT 5317 5422 Spectrin 48.
REPEAT 5423 5520 Spectrin 49.
REPEAT 5521 5628 Spectrin 50.
REPEAT 5629 5745 Spectrin 51.
REPEAT 5746 5851 Spectrin 52.
REPEAT 5971 6080 Spectrin 53.
REPEAT 6081 6187 Spectrin 54.
REPEAT 6377 6488 Spectrin 55.
REPEAT 6489 6584 Spectrin 56.
REPEAT 6585 6694 Spectrin 57.
REPEAT 6695 6798 Spectrin 58.
REPEAT 6799 6905 Spectrin 59.
REPEAT 6906 7023 Spectrin 60.
REPEAT 7024 7131 Spectrin 61.
REPEAT 7132 7240 Spectrin 62.
REPEAT 7241 7353 Spectrin 63.
REPEAT 7354 7457 Spectrin 64.
REPEAT 7458 7561 Spectrin 65.
REPEAT 7562 7674 Spectrin 66.
REPEAT 7675 7786 Spectrin 67.
REPEAT 7787 7886 Spectrin 68.
REPEAT 7887 8000 Spectrin 69.
REPEAT 8001 8109 Spectrin 70.
REPEAT 8110 8221 Spectrin 71.
REPEAT 8332 8440 Spectrin 72.
REPEAT 8441 8550 Spectrin 73.
REPEAT 8551 8668 Spectrin 74.
DOMAIN 8740 8799 KASH. {ECO:0000255|PROSITE-
ProRule:PRU00385}.
REGION 1 289 Actin-binding.
COILED 314 8666 {ECO:0000255}.
COMPBIAS 8665 8731 Ser-rich.
MOD_RES 732 732 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2268 2268 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 5655 5655 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 8227 8227 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NF91}.
MOD_RES 8278 8278 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 8281 8281 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NF91}.
MOD_RES 8284 8284 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 8308 8308 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 8363 8363 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
DISULFID 8776 8776 Interchain (with C-577 in SUN2);
alternate.
{ECO:0000250|UniProtKB:Q8WXH0}.
DISULFID 8776 8776 Interchain (with C-759 in SUN1);
alternate.
{ECO:0000250|UniProtKB:Q8WXH0}.
VAR_SEQ 1 7828 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10878022,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_038791.
VAR_SEQ 103 103 K -> KSMYRGSP (in isoform 5).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_038792.
VAR_SEQ 297 313 Missing (in isoform 5).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_038793.
VAR_SEQ 1435 1441 DIKTMEM -> EYVLHHF (in isoform 5).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_038794.
VAR_SEQ 1442 8799 Missing (in isoform 5).
{ECO:0000303|PubMed:15093733}.
/FTId=VSP_038795.
VAR_SEQ 7829 7878 IAVAQENKIQLQEMGERLAKASHESKASEIQYKLSRVKDRW
QHLLDLMAA -> MVVAEDLHGPRMAEDSSVDADLPDCDCD
VS (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10878022,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_038796.
VAR_SEQ 8218 8219 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:10878022,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_038797.
VAR_SEQ 8328 8328 S -> SDVVIPENPEAYVKLTENAIRNTS (in isoform
2). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_038798.
CONFLICT 1086 1086 G -> W (in Ref. 2; AAN03487).
{ECO:0000305}.
CONFLICT 1150 1150 I -> T (in Ref. 2; AAN03487).
{ECO:0000305}.
CONFLICT 7187 7187 E -> G (in Ref. 1; AAG24393).
{ECO:0000305}.
CONFLICT 7876 7876 M -> I (in Ref. 1; AAG24393).
{ECO:0000305}.
CONFLICT 8266 8266 P -> L (in Ref. 1; AAG24392/AAG24393).
{ECO:0000305}.
SEQUENCE 8799 AA; 1009926 MW; 2A457DC081969CF0 CRC64;
MATSRASSRS HRDITNVMQR LQDEQEIVQK RTFTKWINSH LAKRKPPMVV DDLFEDMKDG
IKLLALLEVL SGQKLPCEQG HRVKRIHAVA NIGTALKFLE GRKIKLVNIN ATDIADGRPS
IVLGLMWTII LYFQIEELTS NLPQLQSLSS SASSVDSMVS TETASPPSKR KVAAKIQGNA
KKTLLKWVQH TAGKQMGIEV KDFGKSWRTG LAFHSVIHAI QPELVDLEKV KTRSNRENLE
DAFTIAETQL GIPRLLDPED VDVDKPDEKS IMTYVAQFLT QYPDIHGAGC DGQEDDVVFV
GFTNNIALLL GFQRDDRLIL KETKVWIEQF ERDFTRAQMT ESSLQDKYQA FKHFRVQYEM
KRKQVEHIIQ PLQRDGKLTL DQALVKQCWE RVSSRLFDWH IQLDKSLPAP LGTIGAWLYR
AEVALREEIT IQQVHEETAN TIQRKLEQHK DLLQNTDAHK RAFHEIYQTR SVNGIPMPPD
QLEDMAERFH FVSSTSELHL MKMEFLELKY RLLSLLVLAE SKLKSWIIKY GRRESVELLL
QSYISFIENS KFFEQYEVTY QILKQTADIY VKAEGSVEEA ENVMKFMSEA TAQWRNLSVE
VRSVRSMLEE VISNWDRYGD TVASLQAWLE DAEKMLSQSE HAKKDFFRNL PHWIQQHTAM
NDAGNFLIET CDEIVSRDLK QQLLLLNGRW RELFMEVKQY ARADEMDRMK KEYIDVTTTL
FGFATEAHRK LSEPLEVSFI NVKLLIQDLE DLEKRVPVMD AQYKMIAKKA HLFAKESPQE
EANEMLTTMS KLKEQLSKVK ECCSPLLYEA QQLTVPLEEL ETQITSFYDS LGKINEILSV
LEQEAQSSTL FKQKHQELLA SQENCKKSLT LIEKGSQSVQ KLVTSSQARK PWDHTKLQKQ
IADVHHAFQS MIKKTGDWKK HVEANSRLMK KFEESRAELE KVLRVAQEGL EEKGDPEELL
RRHTEFFSQL DQRVLNAFLK ACDELTDILP EQEQQGLQEA VRKLHKQWKD LQGEAPYHLL
HLKIAVEKDR FSAAVEECRA ELEQETKLAP QEGSEKIIKE HRVFFSDKGP HHLCEKRLQL
IEELCGKLPV QDPVRDTCGA CHTALKELKA SIDNTYTMLV DDPDKWKDYT SRFSEFSSWV
SAKKACLKKI KDEPIDTGNH DEVKHMVDEI RNDITKKGES LSWLKSRLKY LIDISSENEA
QKRGDELAEL SSSFKALVAL LSEVEKLLSN FGECVQYKEI VKSSLEGLIS GPQESKEEAE
MILDSKNLLE AQQLLLHHQQ KTKMISAKKR DLQEQMEQAQ QGGQAGPGQE ELRKLESTLT
GLEQSRERQE RRIQVSLRKW ERFETNKETV VRYLFQTGSS HERFLSFSSL ESLSSELEQT
KEFSKRTESI ATQAENLVKE AAELPLGPRN KRVLQRQAKS IKEQVTTLED TLEEDIKTME
MVKSKWDHFG SNFETLSIWI LEKENELSSL EASASAADVQ ISQIKVTIQE IESKIDSIVG
LEEEAQSFAQ FVTTGESARI KAKLTQIRRY WEELQEHARG LEGTILGHLS QQQKFEENLR
KIRQSVSEFA ERLADPIKIC SSAAETYKVL QEHMDLCQAV ESLSSTVTMF SASAQKAVNR
ESCTQEAAAL QQQYEEILHK AKEMQTALED LLARWQRLEK GLSPFLTWLE RCEAIASSPE
KDISADRGKV ESELQLIQAL QNEVVSQASL YSNLLQLKEA LFSVASKEDV AVMKLQLEQL
DERWGDLPQI ISKRMHFLQS VLAEHKQFDE LLFSFSVWIK QFLGELQRTS EINLRDHQVA
LTRHKDHAAE IEKKRGEITH LQGHLSQLRS LGRAQDLHPL QSKVDDCFQL FEEASQVVER
RKLALAQLAE FLQSHACMST LLYQLRQTVE ATKSMSKKQS DSLKTDLHSA IQDVKTLESS
AISLDGTLTK AQCHLKSASP EERTSCRATT DQLSLEVERI QNLLGTKQSE ADALVALKEA
FREQKEELLR SIEDIEERMD RERLKVPTRQ ALQHRLRVFN QLEDELNSHE HELCWLKDKA
KQIAQKDVAF APEVDREING LEATWDDTRR QIHENQGQCC GLIDLVREYQ SLKSTVCNVL
EDASNVVVMR ATIKDQGDLK WAFSKHETSR NEMNSKQKEL DSFTSKGKHL LSELKKIHSG
DFSLVKTDME STLDKWLDVS ERIEENMDML RVSLSIWDDV LSRKDEIEGW SNSSLPKLAE
NISNLNNSLR AEELLKELES EVKIKALKLE DLHSKINNLK ELTKNPETPT ELQFIEADLR
QKLEHAKEIT EEARGTLKDF TAQRTQVERF VKDITAWLIN VEESLTRCAQ TETCEGLKKA
KDIRKELQSQ QNSITSTQEE LNSLCRKHHS VELESLGRAM TGLIKKHEAT SQLCSQTQAR
IQDSLEKHFS GSMKEFQEWF LGAKAAARES SNLTGDSQIL EARLHNLQGV LDSLSDGQSK
LDVVTQEGQT LYAHLPKQIV SSIQEQITKA NEEFQAFLKQ CLKEKQALQD CVSELGSFED
QHRKLNLWIH EMEERLKTEN LGESKHHISE KKNEVRKVEM FLGELLAARE SLDKLSQRGQ
LLSEESHSAG KGGCRSTQLL TSYQSLLRVT KEKLRSCQLA LKEHEALEEA TQSMWARVKD
VQDRLACAES TLGNKETLEG RLSQIQDILL MKGEGEVKLN LAIGKGDQAL RSSNKEGQQA
IQDQLEMLKK AWAEAMNSAV HAQSTLESVI DQWNDYLEKK SQLEQWMESV DQRLEHPLQL
QPGLKEKFSL LDHFQSIVSE AEDHTGALQQ LAAKSRELYQ KTQDESFKEA GQEELRTQFQ
DIMTVAKEKM RTVEDLVKDH LMYLDAVQEF ADWLHSAKEE LHRWSDTSGD PSATQKKLLK
IKELIDSREI GAGRLSRVES LAPAVKQNTA ASGCELLNSE MQALRADWRQ WEDCLFQTQS
SLESLVSEMA LSEQEFFGQV TQLEQALEQF CTLLKTWAQQ LTLLEGKNSD EEILECWHKG
REILDALQKA EPMTEDLKSQ LNELCRFSRD LSPYSEKVSG LIKEYNCLCL QASKGCQNKE
QILQERFQKA SRGFQQWLVN AKITTAKCFD LPQNLSEVSS SLQKIQEFLS ESENGQHKLN
TMLFKGELLS SLLTEEKAQA VQAKVLTAKE EWKSFHANLH QKESALENLK IQMKDFEVSA
ELVQNWLSKT ERLVQESSNR LYDLPAKRRE QQKLQSVLEE IQCYEPQLHR LKEKARQLWE
GQAASKSFVH RVSQLSSQYL ALSNVTKEKV SRLDRIIAEH NRFSQGVKEL QDWMSDAVHM
LDSYCLPTSD KSVLDSRMLK LEALLSVRQE KEIQMKMVVT RGEYVLQSTS LEGSAAVQQQ
LQAVKDMWES LLSAAIRCKS QLEGALSKWT SYQDDVRQFS SWMDSVEVSL TESEKQHTEL
REKITALGKA KLLNEEVLSH SSLLETIEVK RAAMTEHYVT QLELQDLQER HQALKEKAKE
AVTKLEKLVR LHQEYQRDLK AFESWLEQEQ EKLDRCSVHE GDTNAHETML RDLQELQVRC
AEGQALLNSV LHTREDVIPS GLPQAEDRVL ESLRQDWQVY QHRLAEARMQ LNNVVNKLRL
MEQKFQQADE WLKRMEEKIN FRSECQSSRS DKEIQLLQLK KWHEDLSAHR DEVEEVGTRA
QGILDETHIS SRMGCQATQL TSRYQALLLQ VLEQIKFFEE ELQCLEETES SLSSYSDWYG
STHKNFKNVA TKIDKVDESM MGKKLKTLEV LLKDMEKGHS LLKSAREKGE RAMKFLAEHE
AEALRKEIHT YMEQLKNLTS TVRKECMSLE KGLHLAKEFS DKYKVLAQWM AEYQEILCTP
EEPKMELYEK KAQLSKYKSL QQMVLSHEPS VTSVQEKSEA LLELVQDQSL KDKIQKLQSD
FQDLCSRAKE RVFSLEAKVK DHEDYNTELQ EVEKWLLQMS GRLVAPDLLE MSSLETITQQ
LAHHKAMMEE IAGFEDRLDN LKAKGDTLIG QCPEHLQAKQ KQTVQAHLQG TKDSYSAICS
TAQRVYRSLE YELQKHVSSQ DTLQQCQAWI SAVQPDLKPS PQPPLSRAEA VKQVKHFRAL
QEQARTYLDL LCSMCDLSNS SVKNTAKDIQ QTEQLIEQRL VQAQNLTQGW EEIKSLKAEL
WIYLQDADQQ LQNMKRRHTE LEINIAQNMV MQVKDFIKQL QCKQVSVSTI VEKVDKLTKN
QESPEHKEIT HLNDQWQDLC LQSDKLCAQR EQDLQRTSSY HDHMRVVEAF LEKFTTEWDS
LARSNAESTA IHLEALKKLA LALQEEMYAI DDLKDCKQKL IEQLGLDDRE LVREQTSHLE
QRWFQLQDLV KRKIQVSVTN LEELNVIQSR FQELMEWAEE QQPNIVEALK QSPPPGMAQH
LLMDHLAICS ELEAKQVLLK SLMKDADRVM ADLGLNERKV IQKALSEAQK HVSCLSDLVG
QRRKYLNKAL SEKTQFLMAV FQATSQIQQH ERKIVFREYI CLLPDDVSKQ VKTCKTAQAS
LKTYQNEVTG LCAQGRELMK GITKQEQEEV LGKLQELQTV YDTVLQKCSH RLQELEKSLV
SRKHFKEDFD KACHWLKQAD IVTFPEINLM NEKTELHAQL DKYQSILEQS PEYENLLLTL
QTTGQAMLPS LNEVDHSYLS EKLSALPQQF NVIVALAKDK FYKTQEAILA RKEYTSLIEL
TTQSLGDLED QFLKMRKMPS DLIVEESVSL QQSCSALLGE VVALGEAVNE LNQKKESFRS
TGQPWQPEKM LQLATLYHRL KRQAEQRVSF LEDTTSVYKE HAQMCRQLES QLEVVKREQA
KVNEETLPAE EKLKVYHSLA GSLQDSGILL KRVATHLEDL SPHLDPTAYE KAKSQVQSWQ
EELKQMTSDV GELVTECESR MVQSIDFQTE MSRSLDWLRR VKAELSGPVC LDLSLQDIQE
EIRKIQIHQE EVLSSLRIMS ALSHKEQEKF TKAKELISAD LEHTLAELQE LDGDVQEALR
TRQATLTEIY SRCQRYYQVF QAANDWLDDA QEMLQLAGNG LDVESAEENL RSHMEFFKTE
GQFHSNMEEL RGLVARLDPL IKATGKEELA QKMASLEKRS QGIIQESHTQ RDLLQRCMVQ
WQEYQKAREG VIELMNDAEK KLSEFAVLKT SSIHEAEEKL SKHKALVSVV DSFHEKIVAL
EEKASQLEQT GNDTSKATLS RSMTTVWQRW TRLRAVAQDQ EKILEDAVDE WKRLSAKVKE
TTEVINQLQG RLPGSSTEKA SKAELMTLLE SHDTYLMDLE SQQLTLGVLQ QRALSMLQDR
AFPGTEEEVP ILRAITALQD QCLNMQEKVK NHGKLVKQEL QEREAVETRI NSVKSWVQET
KDYLGNPTIE IDTQLEELKR LLAEATSHQE SIEKIAEEQK NKYLGLYTVL PSEISLQLAE
VALDLKIHDQ IQEKVQEIEE GKAMSQEFSC KIQKVTKDLT TILTKLKAKT DDLVHAKAEH
KMLGEELDGC NSKLMELDAA IQTFSERHSQ LGQPLAKKIG KLTELHQQTI RQAENRLSKL
NQALSHMEEY NEMLETVRKW IEKAKVLVHG NIAWNSASQL QEQYILHQTL LEESGEIDSD
LEAMAEKVQH LANVYCTGKL SQQVTQFGRE MEELRQAIRV RLRNLQDAAK DMKKFEGELR
NLQVALEQAQ TILTSPEVGR RSLKEQLCHR QHLLSEMESL KPKMQAVQLC QSALRIPEDV
VASLPLCHAA LRLQEEASQL QHTAIQQCNI MQAKKHSLIF PPKEAVVQYE QYKQEMKHLQ
QLIEEAHREI EDKPVATSNI QELQAQISLH EELAQKIKGY QEQIDSLNSK CKMLTMKAKH
ATMLLTVTEV EGLAEGTEDL DRELHPTPSA HPSVVMMTAG RCHTLLSPVT EESGEEGTNS
EISSPPACRS PSPVANTEAA VNQDIAYYQA LSAEGLQTDA ARIPPSAAVS QELYEPGLEP
SATAKLGDLQ RSWETLKNVI SEKQRTLYEV LERQQKYQDS LQSISTKMEA MEMKLGESLE
PSRSPESQMA EHQALMDEVQ MLQDEINGLQ VSLAEELVAE SQESDPAEQL ALQSTLTVLA
ERMSTIRMKA AGKRQLLEEK LSDQLEEQRQ EQALQRYRCE ADELDHWLLN TKATLDVALG
TSQEPMDMDA QLVDCQNMLV EIEQKVVALS QLSVHNENLL LEGKAHTKEE AEQLAVKLRL
LKGSLGELQR ALHDRQLDMQ GVTQEKEEND VDFTDTQSPG VQEWLAQART TRTHQRQSSL
QQQKEFEQEL AEQKSLLRSV ASRGEEILTQ HSTAEGSGGL GEKPDVLSQE LGIAEDQMRV
KWESLHQEFS AKQKLLQNIL EQEQEQVLYS SPNRLLSGVL PFRGEAQTQD KTSVTSLLDG
LSQAFGEASS QSGGTDRQSI HLEQKLYDGV SATSTWLNDV EERLFVATAP LPEETEACLF
NQEALAKDIK EMSEEMDKNK NLFSQAFPED SDNRDVIEDT LGCLLGRLSL LDSVVDQRCH
QMKERLQQIL RFQNDLKVLF TSLADSKYII LQKLANVFEQ PIVEQMQAIQ QAEEGLRDLE
GGISELKRWA DKLQVEQSAV QELSKLQDMY DELLMTVSSR RSSLHQNLAL KSQYDKALQD
LVDLLDTGQE KMTGDQKIIV CSKEEIQQLL GKHKEYFQGL ESHMILTEIL FRKIVGFAAV
KETQFHTDCM AQASAVLKQA HKRGVELEYI LEMWSHLDEN RQELSRQLEV IENSIPSVGL
VEESEDRLVE RTNLYQHLKS SLNEYQPKLY QALDDGKRLL MSVSCSELES QLNQLGEHWL
SNTNKVSKEL HRLETILKHW TRYQSEAAAL NHWLQCAKDR LAFWTQQSVT VPQELEMVRD
HLSAFLEFSK EVDAKSALKS SVTSTGNQLL RLKKVDTAAL RAELSRMDSQ WTDLLTGIPV
VQEKLHQLQM DKLPSRHAIS EVMSWISLME SVILKDEEDI RNAIGYKAIH EYLQKYKGFK
IDLNCKQLTA DFVNQSVLQI SSQDVESKRS DKTDFAEQLG AMNKSWQLLQ GRVGEKIQML
EGLLESWSEY ENSVQSLKAW FANQERKLKE QHLLGDRNSV ENALKDCQEL EDLIKAKEKE
VEKIEQNGLA LIQNKREEVS GSVMSTLQEL RQTWISLDRT VEQLKIQLTS ALGQWSNHKA
ACDEINGHLM EARYSLSRFR LLTGSSEAVQ VQVDNLQNLH DELEKQEGGL QKFGSITNQL
LKECHPPVAE TLSSTLQEVN MRWNNLLEEI AEQLHSSKAL LQLWQRYKDY SKQCASAIQR
QEEQTSVLLK AATNKDIADD EVTKWIQDCN DLLKGLETVK DSLFILRELG EQLGQQVDVS
AAAAIQCEQL CFSQRLGALE QALCKQQAVL QAGVVDYETF AKSLEALEVW MVEAEGILQG
QDPTHSSDLS TIQERMEELK GQMLKFSSLA PDLDRLNELG YRLPLNDKEI KRMQNLNRHW
SLTSSQTTER FSKLQSFLLQ HQTFLEKCET WMEFLVQTEH KLAVEISGNY QHLLEQQRAH
ELFQAEMFSR QQILHSIIVD GQNLLEQGQV DDREEFSLKL TLLSNQWQGV IRRAQQRRGI
IDSQIRQWQR YREMAEKLRK WLAEVSHLPL SGLGNIPVPL QQVRMLFDEV QFKEKVFLRQ
QGSYILTVEA GKQLLLSADS GAEAALQAEL TDIQEKWKAA SMHLEEQKKK LAFLLKDWEK
CERGIANSLE KLRMFKKRLS QPLPDHHEEL HAEQMRCKEL ENAVGRWTDD LTELMLVRDA
LAVYLSAEDI SMLKERVELL QRQWEELCHQ VSLRRQQVSE RLNEWAVFSE KNKELCEWLT
QMESKVSQNG DILIEEMIEK LKKDYQEEIA VAQENKIQLQ EMGERLAKAS HESKASEIQY
KLSRVKDRWQ HLLDLMAARV KKLKETLVAV QQLDKNMGSL RTWLAHMESE LAKPIVYDSC
NSEEIQRKLN EQQELQRDIE KHSTGVASVL NLCEVLLHDC DACATDAECD SIQQATRNLD
RRWRNICAMS MERRLKIEET WRLWQKFLDD YSRFEDWLEV SERTAAFPSS SGVLYTVAKE
ELKKFEAFQR QVHESLTQLE LINKQYRRLA RENRTDSACS LRQMVHGGNQ RWDDLQKRVT
SILRRLKHFI SQREEFETAR DSILVWLTEM DLQLTNIEHF SECDVQAKIK QLKAFQQEIS
LNHNKIEQII AQGEQLIEKS EPLDAAVIEE ELDELRRYCQ EVFGRVERYH KKLIRLPVRL
PDDHDLSDRE LDLEDSTALS DLRWQDPSAD GMPSPQPSSN PSLSLPQPLR SERSGRDTPA
SVDSIPLEWD HDYDLSRDLE SASRTLPSED EEGEEDKEFY LRGAVGLSGD PSSLESQMRQ
LDKALDDSRF QIQQTANILR SKTPTGPDLD TSYKGYMKLL GECSGSIDSV RRLEHKLAEE
ESFPGFVNLN STETQTAGVI DRWELLQAQA MSKELRMKQN LQKWQQFNSD LNNIWAWLGE
TEEELDRLQH LALSTDIHTI ESHIKKLKEL QKAVDHRKAI ILSINLCSSE FTQADSKESH
DLQDRLSQMN GRWDRVCSLL EDWRGLLQDA LMQCQEFHEM SHALLLMLEN IDRRKNEIVP
IDSTLDPETL QDHHKQLMQI KQELLKSQLR VASLQDMSRQ LLVNAEGSDC LEAKEKVHVI
GNRLKLLLKE VSHHIKDLEK LLDMSSSQQD LSSWSSADEL DTSGSVSPTS GRSTPNRQKS
PRGKCSLSQP GPSVSSPKSR STRDGSDSSR SDPRPERVGR AFLFRILRAA LPFQLLLLLL
IGLTCLVPMS EKDYSCALSN NFARSFHPML RYTNGPPPL


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