Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nesprin-4

Gene

Syne4

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

Functioni

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 (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology, by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus.By similarity1 Publication

GO - Biological processi

  • establishment of epithelial cell apical/basal polarity Source: UniProtKB

Names & Taxonomyi

Protein namesi
Recommended name:
Nesprin-4
Alternative name(s):
KASH domain-containing protein 4
Short name:
KASH4
Nuclear envelope spectrin repeat protein 4
Gene namesi
Name:Syne4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2141950 Syne4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 339CytoplasmicPROSITE-ProRule annotationAdd BLAST339
Transmembranei340 – 360Helical; Anchor for type IV membrane proteinPROSITE-ProRule annotationAdd BLAST21
Topological domaini361 – 388Perinuclear spacePROSITE-ProRule annotationAdd BLAST28

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are born at the expected Mendelian rate and look overtly normal. In the cochlea, outer hair cells form, but appear to degenerate as hearing matures. Inner hair cells remain intact. Hearing loss is already detected at P15 and progresses at all frequencies by P60.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003062651 – 388Nesprin-4Add BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi365Interchain (with C-577 in SUN2); alternateBy similarity
Disulfide bondi365Interchain (with C-759 in SUN1)By similarity

Post-translational modificationi

The disulfid bond with SUN1 or SUN2 is required for stability of the respective LINC complex under tensile forces.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ8CII8
PRIDEiQ8CII8

PTM databases

iPTMnetiQ8CII8
PhosphoSitePlusiQ8CII8

Expressioni

Tissue specificityi

Expressed in secretory epithelial cells, such as those found in exocrine pancreas, bulbourethral gland, mammary gland and salivary gland (at protein level). Also expressed in the cochlea, where it is restricted primarily to the 3 rows of outer hair cells and 1 row of inner hair cells (at protein level). Not detected in other cells of the cochlea, including Deiter's cells and pillar cells, nor in liver and kidney (at protein level).2 Publications

Developmental stagei

In the cochlea, low expression at P0 and P15, then rises significantly by P30 and remains steady. In the HC11 cell line model, up-regulated during differentiation of mammary cells into milk-secreting cells (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000019737
CleanExiMM_AI428936
ExpressionAtlasiQ8CII8 baseline and differential
GenevisibleiQ8CII8 MM

Interactioni

Subunit structurei

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. Probably part of a SUN1-containing LINC complex. Interacts with kinesins KIF5B and KLC1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KIF5BP331762EBI-15752280,EBI-355878From Homo sapiens.

Protein-protein interaction databases

DIPiDIP-48702N
IntActiQ8CII8, 6 interactors
STRINGi10090.ENSMUSP00000055874

Structurei

3D structure databases

ProteinModelPortaliQ8CII8
SMRiQ8CII8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini331 – 388KASHPROSITE-ProRule annotationAdd BLAST58

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the nesprin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIPP Eukaryota
ENOG4111B09 LUCA
GeneTreeiENSGT00510000049061
HOGENOMiHOG000111992
HOVERGENiHBG107763
InParanoidiQ8CII8
OMAiSHRKHLA
OrthoDBiEOG091G0CR5
PhylomeDBiQ8CII8

Family and domain databases

InterProiView protein in InterPro
IPR012315 KASH
IPR030268 SYNE4
PANTHERiPTHR21640:SF1 PTHR21640:SF1, 1 hit
PfamiView protein in Pfam
PF10541 KASH, 1 hit
SMARTiView protein in SMART
SM01249 KASH, 1 hit
PROSITEiView protein in PROSITE
PS51049 KASH, 1 hit

Sequencei

Sequence statusi: Complete.

Q8CII8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVPPLGRE FPPEPVNCPL AAPRELDVVG GTICPAPEEE TSRPEQVQAS
60 70 80 90 100
LGLPEHCMGE LKSTESATSP SRLPLASSHE HQDGGKPCEH SDSGLEVLEA
110 120 130 140 150
EQDSLHLCLL RLNFRLQDLE RGLGSWTLAH NRIVQMQALQ AELRGAAERV
160 170 180 190 200
DALLAFGEGL AERSEPRAWA SLEQVLRALG THRDTIFQRL WQLQAQLISY
210 220 230 240 250
SLVLEKANLL DQDLEVEGDS DGPAAGGVWG PWAPSTFPTP AELEWDPAGD
260 270 280 290 300
VGGLGPSGQK ISRIPGAPCE LCGYRGPQSS GQGLEDLLSL GLGHRKHLAA
310 320 330 340 350
HHRRRLRKPQ DRKRQVSPSL PDAMLEVDRG VPAPASKRPL TLFFLLLFLL
360 370 380
LVGATLLLPL SGVSCCSHAR LARTPYLVLS YVNGLPPI
Length:388
Mass (Da):42,024
Last modified:March 1, 2003 - v1
Checksum:iD407808F62CB5498
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56H → Q in AAH04761 (PubMed:15489334).Curated1
Sequence conflicti56H → Q in AAH56649 (PubMed:15489334).Curated1
Sequence conflicti239T → I in AAH56649 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC004761 mRNA Translation: AAH04761.2
BC023803 mRNA Translation: AAH23803.1
BC056649 mRNA Translation: AAH56649.1
CCDSiCCDS21086.1
RefSeqiNP_705805.1, NM_153577.2
UniGeneiMm.227325

Genome annotation databases

EnsembliENSMUST00000054594; ENSMUSP00000055874; ENSMUSG00000019737
GeneIDi233066
KEGGimmu:233066
UCSCiuc009gec.1 mouse

Similar proteinsi

Entry informationi

Entry nameiSYNE4_MOUSE
AccessioniPrimary (citable) accession number: Q8CII8
Secondary accession number(s): Q6PH99, Q99J42
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2003
Last modified: March 28, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health