Q6ZWR6 (SYNE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nesprin-1 Alternative name(s): Enaptin Myocyte nuclear envelope protein 1 Short name=Myne-1 Nuclear envelope spectrin repeat protein 1 Synaptic nuclear envelope protein 1 Short name=Syne-1 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 8799 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. May be involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm By similarity. Required for centrosome migration to the apical cell surface during early ciliogenesis. Ref.8 |
| Subunit structure | Dimer. Component of LINC complexes composed of SUN domain-containing proteins (SUN1 or SUN2) coupled to KASH domain-containing proteins (SYNE1, SYNE2 or SYNE3) also called nesprins. May interact with MUSK. Interacts with EMD and LMNA in vitro By similarity. Interacts with F-actin via its N-terminal domain. Interacts with SYNE3. Ref.1 Ref.10 |
| Subcellular location | Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Potential. Nucleus. Nucleus envelope. Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere By similarity. 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. Ref.1 Ref.2 Ref.5 Ref.9 |
| Tissue specificity | Expressed in C2F3 and CH310T1/2 cells, brain and skeletal muscle (at protein level). Ref.2 Ref.10 |
| 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 By similarity. |
| Sequence similarities | Belongs to the nesprin family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 9 HAT repeats. Contains 1 KASH domain. Contains 44 spectrin repeats. Contains 11 TPR repeats. |
| Sequence caution | The sequence AAG24393.1 differs from that shown. Reason: Frameshift at positions 6810, 7656 and 7658. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton Membrane Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat TPR repeat Transmembrane Transmembrane helix |
| Ligand | Actin-binding |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | establishment of nucleus localization Inferred from mutant phenotype PubMed 17267447. Source: MGI |
| Cellular_component | cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW nuclear envelopeInferred from direct assay Ref.1. Source: MGI nuclear outer membraneInferred from electronic annotation. Source: UniProtKB-SubCell sarcomereInferred from sequence alignment PubMed 12408964. Source: MGI |
| Molecular_function | protein homodimerization activity Inferred from direct assay Ref.10. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q6ZWR6-1) Also known as: Nesprin-1 Giant; Enaptin; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q6ZWR6-2) The sequence of this isoform differs from the canonical sequence as follows: 1-7828: Missing. 7829-7878: IAVAQENKIQ...WQHLLDLMAA → MVVAEDLHGPRMAEDSSVDADLPDCDCDVS 8218-8219: Missing. 8328-8328: S → SDVVIPENPEAYVKLTENAIRNTS | ||||||
| Isoform 3 (identifier: Q6ZWR6-3) Also known as: Syne-1A; The sequence of this isoform differs from the canonical sequence as follows: 1-7828: Missing. 7829-7878: IAVAQENKIQ...WQHLLDLMAA → MVVAEDLHGPRMAEDSSVDADLPDCDCDVS 8218-8219: Missing. | ||||||
| Isoform 4 (identifier: Q6ZWR6-4) Also known as: Syne-1B; The sequence of this isoform differs from the canonical sequence as follows: 8218-8219: Missing. | ||||||
| Note: Incomplete sequence. | ||||||
| Isoform 5 (identifier: Q6ZWR6-5) Also known as: Enaptin-165; The sequence of this isoform differs from the canonical sequence as follows: 103-103: K → KSMYRGSP 297-313: Missing. 1435-1441: DIKTMEM → EYVLHHF 1442-8799: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 8799 | 8799 | Nesprin-1 | PRO_0000392209 | |||||
Regions | |||||||||
| Topological domain | 1 – 8748 | 8748 | Cytoplasmic Potential | ||||||
| Transmembrane | 8749 – 8769 | 21 | Helical; Anchor for type IV membrane protein; Potential | ||||||
| Topological domain | 8770 – 8799 | 30 | Perinuclear space Potential | ||||||
| Domain | 1 – 289 | 289 | Actin-binding | ||||||
| Domain | 27 – 134 | 108 | CH 1 | ||||||
| Domain | 178 – 283 | 106 | CH 2 | ||||||
| Repeat | 592 – 624 | 33 | HAT 1 | ||||||
| Repeat | 915 – 949 | 35 | TPR 1 | ||||||
| Repeat | 1015 – 1048 | 34 | TPR 2 | ||||||
| Repeat | 1103 – 1135 | 33 | HAT 2 | ||||||
| Repeat | 1127 – 1229 | 103 | Spectrin 1 | ||||||
| Repeat | 1423 – 1455 | 33 | HAT 3 | ||||||
| Repeat | 1447 – 1546 | 100 | Spectrin 2 | ||||||
| Repeat | 1538 – 1572 | 35 | TPR 3 | ||||||
| Repeat | 1553 – 1649 | 97 | Spectrin 3 | ||||||
| Repeat | 1656 – 1759 | 104 | Spectrin 4 | ||||||
| Repeat | 2087 – 2191 | 105 | Spectrin 5 | ||||||
| Repeat | 2305 – 2402 | 98 | Spectrin 6 | ||||||
| Repeat | 2407 – 2509 | 103 | Spectrin 7 | ||||||
| Repeat | 2516 – 2618 | 103 | Spectrin 8 | ||||||
| Repeat | 2703 – 2742 | 40 | HAT 4 | ||||||
| Repeat | 2841 – 2982 | 142 | Spectrin 9 | ||||||
| Repeat | 2947 – 2980 | 34 | TPR 4 | ||||||
| Repeat | 3065 – 3167 | 103 | Spectrin 10 | ||||||
| Repeat | 3174 – 3274 | 101 | Spectrin 11 | ||||||
| Repeat | 3281 – 3383 | 103 | Spectrin 12 | ||||||
| Repeat | 3390 – 3486 | 97 | Spectrin 13 | ||||||
| Repeat | 3479 – 3512 | 34 | TPR 5 | ||||||
| Repeat | 3490 – 3593 | 104 | Spectrin 14 | ||||||
| Repeat | 3817 – 3916 | 100 | Spectrin 15 | ||||||
| Repeat | 3923 – 4030 | 108 | Spectrin 16 | ||||||
| Repeat | 4138 – 4236 | 99 | Spectrin 17 | ||||||
| Repeat | 4345 – 4447 | 103 | Spectrin 18 | ||||||
| Repeat | 4454 – 4556 | 103 | Spectrin 19 | ||||||
| Repeat | 4563 – 4665 | 103 | Spectrin 20 | ||||||
| Repeat | 4580 – 4613 | 34 | TPR 6 | ||||||
| Repeat | 4672 – 4772 | 101 | Spectrin 21 | ||||||
| Repeat | 4885 – 4987 | 103 | Spectrin 22 | ||||||
| Repeat | 4994 – 5095 | 102 | Spectrin 23 | ||||||
| Repeat | 5078 – 5110 | 33 | HAT 5 | ||||||
| Repeat | 5102 – 5205 | 104 | Spectrin 24 | ||||||
| Repeat | 5212 – 5317 | 106 | Spectrin 25 | ||||||
| Repeat | 5426 – 5521 | 96 | Spectrin 26 | ||||||
| Repeat | 5514 – 5547 | 34 | TPR 7 | ||||||
| Repeat | 5528 – 5626 | 99 | Spectrin 27 | ||||||
| Repeat | 5736 – 5769 | 34 | TPR 8 | ||||||
| Repeat | 5747 – 5867 | 121 | Spectrin 28 | ||||||
| Repeat | 5961 – 5994 | 34 | TPR 9 | ||||||
| Repeat | 5975 – 6078 | 104 | Spectrin 29 | ||||||
| Repeat | 6702 – 6794 | 93 | Spectrin 30 | ||||||
| Repeat | 6777 – 6809 | 33 | HAT 6 | ||||||
| Repeat | 6801 – 6906 | 106 | Spectrin 31 | ||||||
| Repeat | 6917 – 7021 | 105 | Spectrin 32 | ||||||
| Repeat | 7004 – 7036 | 33 | HAT 7 | ||||||
| Repeat | 7028 – 7129 | 102 | Spectrin 33 | ||||||
| Repeat | 7136 – 7238 | 103 | Spectrin 34 | ||||||
| Repeat | 7214 – 7253 | 40 | HAT 8 | ||||||
| Repeat | 7358 – 7455 | 98 | Spectrin 35 | ||||||
| Repeat | 7462 – 7562 | 101 | Spectrin 36 | ||||||
| Repeat | 7569 – 7672 | 104 | Spectrin 37 | ||||||
| Repeat | 7679 – 7779 | 101 | Spectrin 38 | ||||||
| Repeat | 7786 – 7884 | 99 | Spectrin 39 | ||||||
| Repeat | 7891 – 7998 | 108 | Spectrin 40 | ||||||
| Repeat | 7978 – 8010 | 33 | HAT 9 | ||||||
| Repeat | 8005 – 8107 | 103 | Spectrin 41 | ||||||
| Repeat | 8025 – 8058 | 34 | TPR 10 | ||||||
| Repeat | 8114 – 8214 | 101 | Spectrin 42 | ||||||
| Repeat | 8131 – 8165 | 35 | TPR 11 | ||||||
| Repeat | 8445 – 8548 | 104 | Spectrin 43 | ||||||
| Repeat | 8555 – 8659 | 105 | Spectrin 44 | ||||||
| Domain | 8740 – 8799 | 60 | KASH | ||||||
| Compositional bias | 8665 – 8731 | 67 | Ser-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 8227 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 8278 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 8281 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 8284 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 8308 | 1 | Phosphoserine Ref.6 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 7828 | 7828 | Missing in isoform 2 and isoform 3. | VSP_038791 | |||||
| Alternative sequence | 103 | 1 | K → KSMYRGSP in isoform 5. | VSP_038792 | |||||
| Alternative sequence | 297 – 313 | 17 | Missing in isoform 5. | VSP_038793 | |||||
| Alternative sequence | 1435 – 1441 | 7 | DIKTMEM → EYVLHHF in isoform 5. | VSP_038794 | |||||
| Alternative sequence | 1442 – 8799 | 7358 | Missing in isoform 5. | VSP_038795 | |||||
| Alternative sequence | 7829 – 7878 | 50 | IAVAQ…DLMAA → MVVAEDLHGPRMAEDSSVDA DLPDCDCDVS in isoform 2 and isoform 3. | VSP_038796 | |||||
| Alternative sequence | 8218 – 8219 | 2 | Missing in isoform 2, isoform 3 and isoform 4. | VSP_038797 | |||||
| Alternative sequence | 8328 | 1 | S → SDVVIPENPEAYVKLTENAI RNTS in isoform 2. | VSP_038798 | |||||
Experimental info | |||||||||
| Sequence conflict | 1086 | 1 | G → W in AAN03487. Ref.2 | ||||||
| Sequence conflict | 1150 | 1 | I → T in AAN03487. Ref.2 | ||||||
| Sequence conflict | 7187 | 1 | E → G in AAG24393. Ref.1 | ||||||
| Sequence conflict | 7876 | 1 | M → I in AAG24393. Ref.1 | ||||||
| Sequence conflict | 8266 | 1 | P → L in AAG24392. Ref.1 | ||||||
| Sequence conflict | 8266 | 1 | P → L in AAG24393. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction." Apel E.D., Lewis R.M., Grady R.M., Sanes J.R. J. Biol. Chem. 275:31986-31995(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 6808-8799 (ISOFORM 4), INTERACTION WITH MUSK, SUBCELLULAR LOCATION. |
| [2] | "Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton." Padmakumar V.C., Abraham S., Braune S., Noegel A.A., Tunggal B., Karakesisoglou I., Korenbaum E. Exp. Cell Res. 295:330-339(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, ACTIN-BINDING, SUBCELLULAR LOCATION. Strain: BALB/c. Tissue: Brain. |
| [3] | "The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Vagina. |
| [4] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [5] | "Nuclear membrane proteins with potential disease links found by subtractive proteomics." Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L. Science 301:1380-1382(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. |
| [6] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8308, MASS SPECTROMETRY. Tissue: Brain. |
| [7] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8227, MASS SPECTROMETRY. Tissue: Melanoma. |
| [8] | "Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton." Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A., Gull K., Johnson C.A. J. Cell Sci. 122:2716-2726(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [9] | "SUN1 and SUN2 play critical but partially redundant roles in anchoring nuclei in skeletal muscle cells in mice." Lei K., Zhang X., Ding X., Guo X., Chen M., Zhu B., Xu T., Zhuang Y., Xu R., Han M. Proc. Natl. Acad. Sci. U.S.A. 106:10207-10212(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [10] | "Cytoskeletal interactions at the nuclear envelope mediated by nesprins." Taranum S., Sur I., Muller R., Lu W., Rashmi R.N., Munck M., Neumann S., Karakesisoglou I., Noegel A.A. Int. J. Cell Biol. 2012:736524-736524(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION, INTERACTION WITH SYNE3, TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF281869 mRNA. Translation: AAG24392.1. AF281870 mRNA. Translation: AAG24393.1. Frameshift. AF535143 mRNA. Translation: AAN03487.1. AK036828 mRNA. Translation: BAC29595.1. AC156392 Genomic DNA. No translation available. AC156393 Genomic DNA. No translation available. AC157020 Genomic DNA. No translation available. AC159748 Genomic DNA. No translation available. AC161829 Genomic DNA. No translation available. AC162381 Genomic DNA. No translation available. AC162385 Genomic DNA. No translation available. |
| IPI | IPI00403993. IPI00461474. IPI00473373. IPI00816892. IPI00890038. |
| RefSeq | NP_001073154.1. NM_001079686.1. |
| UniGene | Mm.331626. |
3D structure databases | |
| ProteinModelPortal | Q6ZWR6. |
| SMR | Q6ZWR6. Positions 23-283. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000051825. |
PTM databases | |
| PhosphoSite | Q6ZWR6. |
Proteomic databases | |
| PaxDb | Q6ZWR6. |
| PRIDE | Q6ZWR6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000041639; ENSMUSP00000039440; ENSMUSG00000096054. ENSMUST00000095899; ENSMUSP00000093587; ENSMUSG00000019769. |
| GeneID | 64009. |
| KEGG | mmu:64009. |
| UCSC | uc007egn.1. mouse. uc007egt.1. mouse. |
Organism-specific databases | |
| CTD | 23345. |
| MGI | MGI:1927152. Syne1. |
Phylogenomic databases | |
| eggNOG | COG5069. |
| GeneTree | ENSGT00690000102001. |
| HOGENOM | HOG000120125. |
| HOVERGEN | HBG106534. |
| InParanoid | Q9ERT7. |
| OMA | DIQSIEL. |
| OrthoDB | EOG4ZKJK9. |
Enzyme and pathway databases | |
| Reactome | REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_75800. Meiotic Synapsis (mouse). |
Gene expression databases | |
| ArrayExpress | Q6ZWR6. |
| Bgee | Q6ZWR6. |
| Genevestigator | Q6ZWR6. |
Family and domain databases | |
| Gene3D | 1.10.418.10. 2 hits. |
| InterPro | IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR012315. KASH. IPR018159. Spectrin/alpha-actinin. IPR002017. Spectrin_repeat. [Graphical view] |
| Pfam | PF00307. CH. 2 hits. PF10541. KASH. 1 hit. PF00435. Spectrin. 10 hits. [Graphical view] |
| SMART | SM00033. CH. 2 hits. SM00150. SPEC. 42 hits. [Graphical view] |
| SUPFAM | SSF47576. Calponin-homology. 1 hit. |
| PROSITE | PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. PS51049. KASH. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | SYNE1. mouse. |
| NextBio | 319851. |
| SOURCE | Search... |
Entry information
| Entry name | SYNE1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q6ZWR6 Secondary accession number(s): Q8K3T7, Q9ERT7, Q9ERT8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
