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Protein

Nesprin-3

Gene

Syne3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nesprin-3
Alternative name(s):
Nuclear envelope spectrin repeat protein 3
Gene namesi
Name:Syne3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2442408. Syne3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 925925CytoplasmicPROSITE-ProRule annotationAdd
BLAST
Transmembranei926 – 94621Helical; Anchor for type IV membrane proteinPROSITE-ProRule annotationAdd
BLAST
Topological domaini947 – 97529Perinuclear spacePROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • LINC complex Source: MGI
  • membrane Source: MGI
  • nuclear envelope Source: UniProtKB
  • nuclear outer membrane Source: UniProtKB
  • rough endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 975975Nesprin-3PRO_0000281121Add
BLAST

Proteomic databases

EPDiQ4FZC9.
MaxQBiQ4FZC9.
PaxDbiQ4FZC9.
PRIDEiQ4FZC9.

PTM databases

iPTMnetiQ4FZC9.
PhosphoSiteiQ4FZC9.
SwissPalmiQ4FZC9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ4FZC9.
CleanExiMM_4831426I19RIK.
GenevisibleiQ4FZC9. MM.

Interactioni

Subunit structurei

Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN domain-containing proteins interact with A-type lamins of the nuclear lamina, while at the other end of the complex, nesprins interact with unique cytoskeletal components. Interacts with PLEC (via actin-binding domain). Interacts with DST. Interacts with SYNE1. Interacts (via KASH domain) with TOR1A (ATP-bound); the interaction is required for SYNE3 nuclear envelope localization.4 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093090.

Structurei

3D structure databases

ProteinModelPortaliQ4FZC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati220 – 325106Spectrin 1Add
BLAST
Repeati647 – 74094Spectrin 2Add
BLAST
Domaini917 – 97559KASHPROSITE-ProRule annotationAdd
BLAST

Domaini

The KASH domain is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains.By similarity

Sequence similaritiesi

Belongs to the nesprin family.Curated
Contains 1 KASH domain.PROSITE-ProRule annotation
Contains 2 spectrin repeats.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KD4G. Eukaryota.
ENOG4111CQ9. LUCA.
GeneTreeiENSGT00440000039367.
HOGENOMiHOG000154475.
HOVERGENiHBG094014.
InParanoidiQ4FZC9.
OMAiIKAQWEE.
OrthoDBiEOG7XM2X7.
PhylomeDBiQ4FZC9.
TreeFamiTF331132.

Family and domain databases

InterProiIPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF10541. KASH. 1 hit.
PF00435. Spectrin. 2 hits.
[Graphical view]
SMARTiSM01249. KASH. 1 hit.
SM00150. SPEC. 3 hits.
[Graphical view]
PROSITEiPS51049. KASH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q4FZC9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTQQPQEDFE RSVEDAQAWM KVIQEQLQVN DNTKGPRAAL EARLRETEKI
60 70 80 90 100
CQLESEGMVK VELVLRAAEA LLATCQEGQK PEILARLRDI KSQWEETVTY
110 120 130 140 150
MTHCHSRIEW VWLHWSEYLL AQDEFYRWFQ KMVVALEPPV ELQLGLKEKQ
160 170 180 190 200
WQLSHAQVLL HNVDNQAVLL DRLLEEAGSL FSRIGDPSVD EDAQKRMKAE
210 220 230 240 250
YDAVKARAQR RVDLLAQVAQ DHEQYREDVN EFQLWLKAVV EKVHSCLGRN
260 270 280 290 300
CKLATELRLS TLQDIAKDFP RGEESLKRLE EQAVGVIQNT SPLGAEKISG
310 320 330 340 350
ELEEMRGVLE KLRVLWKEEE GRLRGLLQSR GDCEQQIQQL EAELGDFKKS
360 370 380 390 400
LQRLAQEGLE PTVKTATEDE LVAQWRLFSG TRAALASEEP RVDRLQTQLK
410 420 430 440 450
KLVTFPDLQS LSDSVVATIQ EYQSMKGKNT RLHNATRAEL WQRFQRPLND
460 470 480 490 500
LQLWKALAQR LLDITASLPD LASIHTFLPQ IEAALTESSR LKEQLAMLQL
510 520 530 540 550
KTDLLGSIFG QERAATLLEQ VTSSVRDRDL LHNSLLQRKS KLQSLLVQHK
560 570 580 590 600
DFGVAFDPLN RKLLDLQARI QAEKGLPRDL PGKQVQLLRL QGLQEEGLDL
610 620 630 640 650
GTQIEAVRPL AHGNSKHQQK VDQISCDQQA LQRSLEDLVD RCQQNVREHC
660 670 680 690 700
TFSHRLSELQ LWITMATQTL ESHQGDVRLW DAESQEAGLE TLLSEIPEKE
710 720 730 740 750
VQVSLLQALG QLVMKKSSPE GATMVQEELR KLMESWQALR LLEENMLSLM
760 770 780 790 800
RNQQLQRTEV DTGKKQVFTN NIPKAGFLIN PQDPIPRRQH GANPLEGHDL
810 820 830 840 850
PEDHPQLLRD FEQWLQAENS KLRRIITMRV ATAKDLRTRE VKLQELEARI
860 870 880 890 900
PEGQHLFENL LRLRPARDPS NELEDLRYRW MLYKSKLKDS GHLLTESSPG
910 920 930 940 950
ELTAFQKSRR QKRWSPCSLL QKACRVALPL QLLLLLFLLL LFLLPAGEEE
960 970
RSCALANNFA RSFALMLRYN GPPPT
Length:975
Mass (Da):112,035
Last modified:August 30, 2005 - v1
Checksum:i26D80A295CE0CF8B
GO
Isoform 2 (identifier: Q4FZC9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     88-105: RDIKSQWEETVTYMTHCH → MTTRRGPERPWRQGFERQ

Note: No experimental confirmation available.
Show »
Length:888
Mass (Da):102,197
Checksum:iB7A7F195E6A61587
GO

Sequence cautioni

The sequence BAC26351.1 differs from that shown. Reason: Frameshift at position 776. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787Missing in isoform 2. 1 PublicationVSP_023979Add
BLAST
Alternative sequencei88 – 10518RDIKS…MTHCH → MTTRRGPERPWRQGFERQ in isoform 2. 1 PublicationVSP_023980Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029216 mRNA. Translation: BAC26351.1. Frameshift.
AK030542 mRNA. Translation: BAC27012.1.
BC099694 mRNA. Translation: AAH99694.1.
CCDSiCCDS36542.1. [Q4FZC9-1]
CCDS36543.1. [Q4FZC9-2]
RefSeqiNP_001036164.1. NM_001042699.2. [Q4FZC9-1]
NP_766088.2. NM_172500.3. [Q4FZC9-2]
XP_006515715.2. XM_006515652.2. [Q4FZC9-1]
XP_006515716.1. XM_006515653.1. [Q4FZC9-1]
XP_006515717.1. XM_006515654.2. [Q4FZC9-1]
UniGeneiMm.212688.

Genome annotation databases

EnsembliENSMUST00000067005; ENSMUSP00000065771; ENSMUSG00000054150. [Q4FZC9-2]
ENSMUST00000095439; ENSMUSP00000093090; ENSMUSG00000054150. [Q4FZC9-1]
ENSMUST00000109927; ENSMUSP00000105553; ENSMUSG00000054150. [Q4FZC9-2]
GeneIDi212073.
KEGGimmu:212073.
UCSCiuc007oxr.2. mouse. [Q4FZC9-1]
uc007oxs.2. mouse. [Q4FZC9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029216 mRNA. Translation: BAC26351.1. Frameshift.
AK030542 mRNA. Translation: BAC27012.1.
BC099694 mRNA. Translation: AAH99694.1.
CCDSiCCDS36542.1. [Q4FZC9-1]
CCDS36543.1. [Q4FZC9-2]
RefSeqiNP_001036164.1. NM_001042699.2. [Q4FZC9-1]
NP_766088.2. NM_172500.3. [Q4FZC9-2]
XP_006515715.2. XM_006515652.2. [Q4FZC9-1]
XP_006515716.1. XM_006515653.1. [Q4FZC9-1]
XP_006515717.1. XM_006515654.2. [Q4FZC9-1]
UniGeneiMm.212688.

3D structure databases

ProteinModelPortaliQ4FZC9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093090.

PTM databases

iPTMnetiQ4FZC9.
PhosphoSiteiQ4FZC9.
SwissPalmiQ4FZC9.

Proteomic databases

EPDiQ4FZC9.
MaxQBiQ4FZC9.
PaxDbiQ4FZC9.
PRIDEiQ4FZC9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067005; ENSMUSP00000065771; ENSMUSG00000054150. [Q4FZC9-2]
ENSMUST00000095439; ENSMUSP00000093090; ENSMUSG00000054150. [Q4FZC9-1]
ENSMUST00000109927; ENSMUSP00000105553; ENSMUSG00000054150. [Q4FZC9-2]
GeneIDi212073.
KEGGimmu:212073.
UCSCiuc007oxr.2. mouse. [Q4FZC9-1]
uc007oxs.2. mouse. [Q4FZC9-2]

Organism-specific databases

CTDi161176.
MGIiMGI:2442408. Syne3.

Phylogenomic databases

eggNOGiENOG410KD4G. Eukaryota.
ENOG4111CQ9. LUCA.
GeneTreeiENSGT00440000039367.
HOGENOMiHOG000154475.
HOVERGENiHBG094014.
InParanoidiQ4FZC9.
OMAiIKAQWEE.
OrthoDBiEOG7XM2X7.
PhylomeDBiQ4FZC9.
TreeFamiTF331132.

Miscellaneous databases

PROiQ4FZC9.
SOURCEiSearch...

Gene expression databases

BgeeiQ4FZC9.
CleanExiMM_4831426I19RIK.
GenevisibleiQ4FZC9. MM.

Family and domain databases

InterProiIPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF10541. KASH. 1 hit.
PF00435. Spectrin. 2 hits.
[Graphical view]
SMARTiSM01249. KASH. 1 hit.
SM00150. SPEC. 3 hits.
[Graphical view]
PROSITEiPS51049. KASH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 691-975 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Head and Pituitary.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  3. "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin."
    Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N., Janssen H., van den Bout I., Raymond K., Sonnenberg A.
    J. Cell Biol. 171:799-810(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEC, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  4. "Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness."
    Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.
    Exp. Cell Res. 314:1892-1905(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope protein in sensory neurons."
    Young K.G., Kothary R.
    Exp. Cell Res. 314:2750-2761(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DST.
  6. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
    Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
    J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A, SUBCELLULAR LOCATION.
  7. Cited for: INTERACTION WITH SYNE1.

Entry informationi

Entry nameiSYNE3_MOUSE
AccessioniPrimary (citable) accession number: Q4FZC9
Secondary accession number(s): Q8BMM1, Q8C117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: August 30, 2005
Last modified: June 8, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.