LOCUS       NP_878918               6907 aa            linear   PRI 30-APR-2025
DEFINITION  nesprin-2 isoform 5 [Homo sapiens].
ACCESSION   NP_878918
VERSION     NP_878918.2
DBSOURCE    REFSEQ: accession NM_182914.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 6907)
  AUTHORS   Li Mow Chee,F., Beernaert,B., Griffith,B.G.C., Loftus,A.E.P.,
            Kumar,Y., Wills,J.C., Lee,M., Valli,J., Wheeler,A.P.,
            Armstrong,J.D., Parsons,M., Leigh,I.M., Proby,C.M., von
            Kriegsheim,A., Bickmore,W.A., Frame,M.C. and Byron,A.
  TITLE     Mena regulates nesprin-2 to control actin-nuclear lamina
            associations, trans-nuclear membrane signalling and gene expression
  JOURNAL   Nat Commun 14 (1), 1602 (2023)
   PUBMED   36959177
  REMARK    GeneRIF: Mena regulates nesprin-2 to control actin-nuclear lamina
            associations, trans-nuclear membrane signalling and gene
            expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 6907)
  AUTHORS   Yi,J., Zhao,X., Noell,C.R., Helmer,P., Solmaz,S.R. and Vallee,R.B.
  TITLE     Role of Nesprin-2 and RanBP2 in BICD2-associated brain
            developmental disorders
  JOURNAL   PLoS Genet 19 (3), e1010642 (2023)
   PUBMED   36930595
  REMARK    GeneRIF: Role of Nesprin-2 and RanBP2 in BICD2-associated brain
            developmental disorders.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 6907)
  AUTHORS   Xu,Q., Miao,Y., Ren,J., Sun,Y., Li,C., Cai,X. and Wang,Z.
  TITLE     Silencing of Nesprin-2 inhibits the differentiation of
            myofibroblasts from fibroblasts induced by mechanical stretch
  JOURNAL   Int Wound J 19 (5), 978-986 (2022)
   PUBMED   34558192
  REMARK    GeneRIF: Silencing of Nesprin-2 inhibits the differentiation of
            myofibroblasts from fibroblasts induced by mechanical stretch.
REFERENCE   4  (residues 1 to 6907)
  AUTHORS   Wallis,S.S., Ventimiglia,L.N., Otigbah,E., Infante,E.,
            Cuesta-Geijo,M.A., Kidiyoor,G.R., Carbajal,M.A., Fleck,R.A.,
            Foiani,M., Garcia-Manyes,S., Martin-Serrano,J. and Agromayor,M.
  TITLE     The ESCRT machinery counteracts Nesprin-2G-mediated mechanical
            forces during nuclear envelope repair
  JOURNAL   Dev Cell 56 (23), 3192-3202 (2021)
   PUBMED   34818527
REFERENCE   5  (residues 1 to 6907)
  AUTHORS   Hieda,M., Matsumoto,T., Isobe,M., Kurono,S., Yuka,K., Kametaka,S.,
            Wang,J.Y., Chi,Y.H., Kameda,K., Kimura,H., Matsuura,N. and
            Matsuura,S.
  TITLE     The SUN2-nesprin-2 LINC complex and KIF20A function in the Golgi
            dispersal
  JOURNAL   Sci Rep 11 (1), 5358 (2021)
   PUBMED   33686165
  REMARK    GeneRIF: The SUN2-nesprin-2 LINC complex and KIF20A function in the
            Golgi dispersal.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 6907)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   7  (residues 1 to 6907)
  AUTHORS   Zhang,Q., Ragnauth,C., Greener,M.J., Shanahan,C.M. and Roberts,R.G.
  TITLE     The nesprins are giant actin-binding proteins, orthologous to
            Drosophila melanogaster muscle protein MSP-300
  JOURNAL   Genomics 80 (5), 473-481 (2002)
   PUBMED   12408964
REFERENCE   8  (residues 1 to 6907)
  AUTHORS   Zhen,Y.Y., Libotte,T., Munck,M., Noegel,A.A. and Korenbaum,E.
  TITLE     NUANCE, a giant protein connecting the nucleus and actin
            cytoskeleton
  JOURNAL   J Cell Sci 115 (Pt 15), 3207-3222 (2002)
   PUBMED   12118075
REFERENCE   9  (residues 1 to 6907)
  AUTHORS   Zhang,Q., Skepper,J.N., Yang,F., Davies,J.D., Hegyi,L.,
            Roberts,R.G., Weissberg,P.L., Ellis,J.A. and Shanahan,C.M.
  TITLE     Nesprins: a novel family of spectrin-repeat-containing proteins
            that localize to the nuclear membrane in multiple tissues
  JOURNAL   J Cell Sci 114 (Pt 24), 4485-4498 (2001)
   PUBMED   11792814
REFERENCE   10 (residues 1 to 6907)
  AUTHORS   Apel,E.D., Lewis,R.M., Grady,R.M. and Sanes,J.R.
  TITLE     Syne-1, a dystrophin- and Klarsicht-related protein associated with
            synaptic nuclei at the neuromuscular junction
  JOURNAL   J Biol Chem 275 (41), 31986-31995 (2000)
   PUBMED   10878022
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162832.6, AL359235.3 and
            AL355094.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 7, 2006 this sequence version replaced NP_878918.1.
            
            Summary: The protein encoded by this gene is a nuclear outer
            membrane protein that binds cytoplasmic F-actin. This binding
            tethers the nucleus to the cytoskeleton and aids in the maintenance
            of the structural integrity of the nucleus. Several transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (5) represents the longest
            transcript and encodes the longest isoform (5).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000555002.6/ ENSP00000450831.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..6907
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..6907
                     /product="nesprin-2 isoform 5"
                     /note="nesprin 2; synaptic nuclei expressed gene 2;
                     polytrophin; synaptic nuclear envelope protein 2; nuclear
                     envelope spectrin repeat protein 2; nucleus and actin
                     connecting element protein; spectrin repeat containing,
                     nuclear envelope 2; KASH domain-containing protein 2;
                     nesprin-2 spectrin repeats 3-54"
                     /calculated_mol_wt=798735
     Region          1..286
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          28..138
                     /region_name="CH_SYNE2_rpt1"
                     /note="first calponin homology (CH) domain found in
                     synaptic nuclear envelope protein 2; cd21242"
                     /db_xref="CDD:409091"
     Site            order(33,37,89,91..92,95..96,98,107..115,120,122..123,
                     125..126,129..130,133)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409091"
     Region          178..286
                     /region_name="CH_SYNE2_rpt2"
                     /note="second calponin homology (CH) domain found in
                     synaptic nuclear envelope protein 2 (SYNE-2) and similar
                     proteins; cd21244"
                     /db_xref="CDD:409093"
     Site            order(183,187,237,239..240,243..244,246,255..263,270,
                     272..273,275..276,279..280,283)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409093"
     Region          297..378
                     /region_name="Spectrin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          379..472
                     /region_name="Spectrin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          473..575
                     /region_name="Spectrin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          576..680
                     /region_name="Spectrin 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          735..838
                     /region_name="Spectrin 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          839..932
                     /region_name="Spectrin 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            841
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          933..1034
                     /region_name="Spectrin 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            955
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1042..1084
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1121..1212
                     /region_name="Spectrin 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1263..1323
                     /region_name="Spectrin 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1324..1419
                     /region_name="Spectrin 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <1418..2014
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          1420..1524
                     /region_name="Spectrin 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1525..1636
                     /region_name="Spectrin 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1637..1738
                     /region_name="Spectrin 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1739..1830
                     /region_name="Spectrin 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          1831..1938
                     /region_name="Spectrin 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <1868..2417
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          1939..2036
                     /region_name="Spectrin 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2037..2132
                     /region_name="Spectrin 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2133..2243
                     /region_name="Spectrin 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2244..2360
                     /region_name="Spectrin 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <2338..2712
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          2368..2394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2432..2513
                     /region_name="Spectrin 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2514..2620
                     /region_name="Spectrin 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2621..2717
                     /region_name="Spectrin 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2718..2831
                     /region_name="Spectrin 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            2781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2805..>3389
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:464943"
     Region          2832..2933
                     /region_name="Spectrin 24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          2934..3036
                     /region_name="Spectrin 25"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3037..3142
                     /region_name="Spectrin 26"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3143..3248
                     /region_name="Spectrin 27"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3249..3352
                     /region_name="Spectrin 28"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3353..3465
                     /region_name="Spectrin 29"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3466..3573
                     /region_name="Spectrin 30"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3574..3679
                     /region_name="Spectrin 31"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <3656..>3950
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          3680..3777
                     /region_name="Spectrin 32"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3778..3880
                     /region_name="Spectrin 33"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <3811..4113
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          3881..3986
                     /region_name="Spectrin 34"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          3987..4086
                     /region_name="Spectrin 35"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4073..4162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            4108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4184..4232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4229..4348
                     /region_name="Spectrin 36"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4335..4363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4416..4448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <4496..5321
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          4520..4639
                     /region_name="Spectrin 37"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4640..4727
                     /region_name="Spectrin 38"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4728..4837
                     /region_name="Spectrin 39"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4838..4943
                     /region_name="Spectrin 40"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4944..5051
                     /region_name="Spectrin 41"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          4945..5169
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          5052..5164
                     /region_name="Spectrin 42"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            5054..5059
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          5063..5276
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          5123..>5875
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          5165..5266
                     /region_name="Spectrin 43"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            5168..5173
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          5178..5384
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Region          5267..5391
                     /region_name="Spectrin 44"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            5275..5280
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          5392..5487
                     /region_name="Spectrin 45"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          5488..5589
                     /region_name="Spectrin 46"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          5590..5704
                     /region_name="Spectrin 47"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          5705..5799
                     /region_name="Spectrin 48"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            5785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          5800..5907
                     /region_name="Spectrin 49"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          5908..6017
                     /region_name="Spectrin 50"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          5919..6133
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          6018..6135
                     /region_name="Spectrin 51"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6020..6025
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6136..6243
                     /region_name="Spectrin 52"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          6137..6350
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            6243..6248
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6244..6355
                     /region_name="Spectrin 53"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZWQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZWQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZWQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZWQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZWQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          6484..6572
                     /region_name="Spectrin 54"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          6573..6688
                     /region_name="Spectrin 55"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          6576..6785
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            6682..6687
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6689..6805
                     /region_name="Spectrin 56"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Site            6857..6877
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     Region          <6876..6907
                     /region_name="KASH"
                     /note="Nuclear envelope localization domain; pfam10541"
                     /db_xref="CDD:463142"
     Region          6894..6907
                     /region_name="Sufficient for interaction with SUN2.
                     /evidence=ECO:0000269|PubMed:22632968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXH0.3)"
     CDS             1..6907
                     /gene="SYNE2"
                     /gene_synonym="EDMD5; KASH2; Nesp2; Nesprin-2; NUA;
                     NUANCE; SYNE-2; TROPH"
                     /coded_by="NM_182914.3:192..20915"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS9761.2"
                     /db_xref="GeneID:23224"
                     /db_xref="HGNC:HGNC:17084"
                     /db_xref="MIM:608442"
ORIGIN      
        1 masspelpte deqgswgidd lhislqaeqe dtqkkaftcw insqlarhts psvisdlftd
       61 ikkghvlldl levlsgqqlp rdkgsntfqc riniehaltf lrnrsiklin ihvtdiidgn
      121 psiilgliwt iilhfhiekl aqtlscnynq pslddvsvvd sspassppak kcskvqarwq
      181 msarkalllw aqeqcatyes vnvtdfkssw rngmaflaii halrpdlidm ksvkhrsnkd
      241 nlreafriae qelkiprlle pedvdvvdpd eksimtyvaq flqyskdapg tgeeaqgkvk
      301 damgwltlqk eklqkllkds endtyfkkyn sllsfmesfn eekksfldvl sikrdldeld
      361 kdhlqlreaw dgldhqinaw kiklnyalpp plhqteawlq eveelmdedl sasqdhsqav
      421 tliqekmtlf kslmdrfehh snilltfenk denhlplvpp nkleemkrri nnilekkfil
      481 llefhyykcl vlglvdevks kldiwnikyg sresvellle dwhkfieeke flarldtsfq
      541 kcgeiyknla gecqninkqy mmvksdvcmy rkniynvkst lqkvlacwat yvenlrllra
      601 cfeetkkeei kevpfetlaq wnlehatlne agnflvevsn dvvgssiske lrrlnkrwrk
      661 lvsktqlemn lplmikkqdq ptfdnsgnil skeekatvef stdmsvelpe nynqnikage
      721 khekeneeft gqlkvakdve kligqveiwe aeaksvldqd dvdtsmeesl khliakgsmf
      781 delmarsedm lqmdiqniss qesfqhvltt glqakiqeak ekvqinvvkl iaalknltdv
      841 spdldirlkm eesqkelesy mmraqqllgq respgelisk hkealiisnt kslakylkav
      901 eelknnvted ikmsleeksr dvcakweslh helslyvqql kidiekgkls dnilklekqi
      961 nkekklirrg rtkglikehe acfseegcly qlnhhmevlr elceelpsqk sqqevkrllk
     1021 dyeqkierll kcaseihmtl qptaggtskn egtittsenr ggdphseapf aksdnqpste
     1081 kameptmkfs lasvlrplqe esimekdysa sinslleryd tyrdilehhl qnnkfritsd
     1141 fsseedrsss clqakltdlq viknetdarw kefeiislkl enhvndikkp fvikerdtlk
     1201 ererelqmtl ntrmesleta lrlvlpveka slllcgsdlp lhkmaiqgfh lidadriyqh
     1261 lrniqdsiak qieicnrlee pgnfvlkelh pfdlhamqni ilkyktqfeg mnhrvqrsed
     1321 tlkaledfla slrtaklsae pvtdlsasdt qvaqentltv knkegeihlm kdkakhldkc
     1381 lkmldmsfkd aergddtsce nlldafsikl sethgygvqe efteenklle acifknnell
     1441 kniqdvqsqi skiglkdptv pavkhrkksl irldkvldey eeekrhlqem anslphfkdg
     1501 rektvnqqcq ntvvlwentk alvtecleqc grvlellkqy qnfksilttl iqkeesvisl
     1561 qasymgkenl kkriaeieiv keefnehlev vdkinqvckn lqfylnkmkt feeppfekea
     1621 niivdrwldi nektedyyen lgralalwdk lfnlknvide wtekalqkme lhqlteedre
     1681 rlkeelqvhe qktsefsrrv aeiqfllqss eiplelqvme ssilnkmehv qkcltgesnc
     1741 halsgstael redldqaktq igmtesllka lspsdsleif tkleeiqqqi lqqkhsmill
     1801 enqigcltpe lselkkqyes vsdlfntkks vlqdhfskll ndqcknfndw fsnikvnlke
     1861 cfessetkks veqklqklsd fltlegrnsk ikqvdsvlkh vkkhlpkahv keliswlvgq
     1921 efelekmesi cqarakeled slqqllrlqd dhrnlrkwlt nqeekwkgme epgektelfc
     1981 qalarkreqf esvaqlnnsl keygfteeee iimeatclmd ryqtllrqls eieeedkllp
     2041 tedqsfndla hdvihwikei keslmvlnss egkmpleeri qkikeiillk pegdarieti
     2101 mkqaesseap lvqktltdis nqwdntlhla stylshqekl llegekylqs kedlrlmlie
     2161 lkkkqeagfa lqhglqekka qlkiykkflk kaqdltsllk elksqgnyll ectknpsfse
     2221 epwleikhlh esllqqlqds vqnldghvre hdsyqvcvtd lnttldnfsk efvsfsdkpv
     2281 dqiaveeklq klqelenrls lqdgtlkkil alaksvkqnt ssvgqkiikd dikslqckqk
     2341 dlenrlasak qemecclnsi lkskrstekk gkftlpgrek qatsdvqest qesaavekle
     2401 edweinkdsa vemamskqls lnaqesmknt ederkvnelq nqpleldtml rneqleeiek
     2461 lytqleakka aikpleqtec lnktetgalv lhnigysaqh ldnllqalit lkknkesqyc
     2521 vlrdfqeyla avessmkall tdkeslkvgp ldsvtyldki kkfiasieke kdslgnlkik
     2581 wenlsnhvtd mdkkllesqi kqlehgweqv eqqiqkkysq qvveydeftt lmnkvqdtei
     2641 slqqqqqhlq lrlkspeera gnqsmialtt dlqatkhgfs vlkgqaelqm kriwgekekk
     2701 nledginnlk kqwetleplh leaenqikkc dirnkmketi lwaknllgel npsipllpdd
     2761 ilsqirkckv thdgilarqq sveslaeevk dkvpslttye gsdlnntled lrnqyqmlvl
     2821 kstqrsqqle fkleersnff aiirkfqlmv qesetliipr vetaateael khhhvtleas
     2881 qkelqeidsg isthlqeltn iyeelnvfer lfledqlknl kirtnriqrf iqntcneveh
     2941 kikfcrqfhe ktsalqeead siqrnellln qevnkgvkee iynlkdrlta ikccilqvlk
     3001 lkkvfdyigl nwdfsqldql qtqvfekeke leekikqldt feeehgkyqa llskmraidl
     3061 qikkmtevvl kapdsspesr rlnaqilsqr iekakclcde iikklnenkt fddsfkekei
     3121 lqiklnaeen dklykvlqnm vlelspkeld ekncqdklet slhvlnqiks qlqqpllinl
     3181 eikhiqnekd nceafqeqvw aemcsikavt aiekqreens seasdvetkl refedlqmql
     3241 ntsidlrtnv lndayenltr ykeavtrave sitsleaiii pyrvdvgnpe eslemplrkq
     3301 eelestvahi qdlteklgmi sspeaklqlq ytlqelvskn samkeafkaq eteaerylen
     3361 ykcyrkmeed iytnlskmet vlgqsmsslp lsyrealerl eqskalvsnl istkeelmkl
     3421 rqilrllrlr ctendgicll kivsalwekw lslleaakew emwceelkqe wkfvseeier
     3481 eaiildnlqe elpeisktke aatteelsel ldclcqygen vekqqllltl llqrirsiqn
     3541 vpessgavet vpafqeitsm kercnkllqk vqknkelvqt eiqerhsftk eiialknffq
     3601 qtttsfqnma fqdhpekseq feelqsilkk gkltfenime klrikysemy tivpaeiesq
     3661 veecrkaled idekisnevl ksspsyamrr kieeinnglh nvekmlqqks kniekaqeiq
     3721 kkmwdeldlw hsklneldse vqdiveqdpg qaqewmdnlm ipfqqyqqvs qraecrtsql
     3781 nkatvkmeey sdllksteaw ientshllan padydslrtl shhastvqma ledseqkhnl
     3841 lhsifmdled lsiifetdel tqsiqelsnq vtalqqkime slpqiqrmad dvvaiesevk
     3901 smekrvskik tillskeifd fspeehlkhg evilenirpm kktiaeivsy qvelrlpqtg
     3961 mkplpvfqrt nqllqdikll envtqeqnel lkvvikqtne wdeeienlkq ilnnysaqfs
     4021 lehmspdqad klpqlqgeie rmekqilsln qrkedllvdl katvlnlhqh lkqeqegver
     4081 drlpavtsee ggvaerdase rklnrrgsms ylaaveeeve essvksdngd ekaepspqsw
     4141 sslwkhdkdm eedrassssg tivqeaygki stsdnsmaqi ltpdslnteq gpecslrpnq
     4201 teegttppie adtldssdaq ggleprvekt rpeptevlha cktqvaelel wlqqanvave
     4261 petlnadmqq vleqqlvgcq amlteiehkv aflletckdq glgdngatqh eaealslklk
     4321 tvkcnlekvq mmlqekhsed qhptilkkss epehqealqp vnlselesiv terpqfsrqk
     4381 dfqqqqvlel kpmeqkdfik fiefnakkmw pqycqhdndt tqessasnqa sspendvpds
     4441 ilspqgqngd kwqylhhels skiklplpql vepqvstnmg ilpsvtmynf ryptteelkt
     4501 yttqledlrq easnlqtqen mteeayinld kklfelfltl sqclssveem lemprlyred
     4561 gsgqqvhyet lalelkklyl alsdkkgdll kamtwpgent nlllecfdnl qvclehtqaa
     4621 avcrskslka gldynrsyqn eikrlyhqli ksktslqqsl neisgqsvae qlqkadaytv
     4681 elenaesrva klrdegerlh lpyallqevy kledvldsmw gmlrarytel sspfvtesqq
     4741 dallqgmvel vkigkeklah ghlkqtkskv alqaqienhk vffqklvadm lliqaysaki
     4801 lpsllqnret fwaeqvtevk ileeksrqcg mklqsllqkw eefdenyasl ekdleilist
     4861 lpsvslveet eerlverisf yqqikrnigg kharlyqtln egkqlvasvs cpelegqiak
     4921 leeqwlslnk kidhelhrlq allkhllsyn rdsdqltkwl essqhtlnyw keqslnvsqd
     4981 ldtirsninn ffefskevde ksslktavis ignqllhlke tdtatlrasl aqfeqkwtml
     5041 itqlpdiqek lhqlqmeklp srkaitemis wmnnvehqts dedsvhspss asqvkhllqk
     5101 hkefrmemdy kqwivdfvnq sllqlstcdv eskryertef aehlgemnrq whrvhgmlnr
     5161 kiqhleqlle sitesenkiq ilnnwleaqe erlktlqkpe svisvqklll dcqdienqla
     5221 ikskaldelk qsyltlesga vplledtasr idelfqkrss vltqvnqlkt smqsvlqewk
     5281 iydqlydevn mmtirfwycm ehskpvvlsl etlrcqvenl qslqdeaess egsweklqev
     5341 igklkglcps vaeiieekcq nthkrwtqvn qaiadqlqka qsllqlwkay snahgeaaar
     5401 lkqqeakfqq lanismsgnn laeilppalq dikelqhdvq ktkeaflqns svldrlpqpa
     5461 essthmllpg plhslqraay lekmllvkan efefvlsqfk dfgvrleslk glimheeenl
     5521 drlhqqeken pdsflnhvla ltaqspdieh lnevslklpl sdvavktlqn mnrqwirata
     5581 talercselq giglnekfly ccekwiqlle kieealkvdv anslpelleq qktykmleae
     5641 vsinqtiads yvtqslqlld tteienrpef itefskltdr wqnavqgvrq rkgdvdglvr
     5701 qwqdfttsve nlfrfltdts hllsavkgqe rfslyqtrsl ihelknkeih fqrrrttcal
     5761 tleageklll ttdlktkesv grrisqlqds wkdmepqlae mikqfqstve twdqcekkik
     5821 elksrlqvlk aqsedplpel hedlhnekel ikeleqslas wtqnlkelqt mkadltrhvl
     5881 vedvmvlkeq iehlhrqwed lclrvairkq eiedrlntwv vfneknkelc awlvqmenkv
     5941 lqtadisiee mieklqkdcm eeinlfsenk lqlkqmgdql ikasnksraa eiddklnkin
     6001 drwqhlfdvi gsrvkklket fafiqqldkn msnlrtwlar ieselskpvv ydvcddqeiq
     6061 krlaeqqdlq rdieqhsagv esvfnicdvl lhdsdacane tecdsiqqtt rsldrrwrni
     6121 camsmerrmk ieetwrlwqk flddysrfed wlksaertaa cpnssevlyt sakeelkrfe
     6181 afqrqiherl tqlelinkqy rrlarenrtd tasrlkqmvh egnqrwdnlq rrvtavlrrl
     6241 rhftnqreef egtresilvw ltemdlqltn vehfsesdad dkmrqlngfq qeitlntnki
     6301 dqlivfgeql iqksepldav liedeleelh rycqevfgrv srfhrrltsc tpgledekea
     6361 senetdmedp reiqtdswrk rgeseepssp qslchlvapg hersgcetpv svdsiplewd
     6421 htgdvggsss heedeegpyy salsdveipe npeaylkmtt ktlkassgks isdghswhvp
     6481 dspscpehhy kqmegdrnvp pvppasstpy kppygklllp pgtdggkegp rvlngnpqqe
     6541 dgglagiteq qsgafdrwem iqaqelhnkl kikqnlqqln sdisaittwl kkteaeleml
     6601 kmakppsdiq eielrvkrlq eilkafdtyk alvvsvnvss keflqtespe stelqsrlrq
     6661 lsllweaaqg avdswrgglr qslmqcqdfh qlsqnlllwl asaknrrqka hvtdpkadpr
     6721 allecrrelm qlekelverq pqvdmlqeis nsllikghge dcieaeekvh viekklkqlr
     6781 eqvsqdlmal qgtqnpaspl psfdevdsgd qppatsvpap rakfravrtt egeeetesrv
     6841 pgstrpqrsf lsrvvraalp lqllllllll lacllpssee dysctqannf arsfypmlry
     6901 tngpppt
//
