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Protein

SUN domain-containing protein 1

Gene

Sun1

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. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. Helps to define the distribution of nuclear pore complexes (NPCs). Required for efficient localization of SYNE4 in the nuclear envelope.6 Publications

GO - Molecular functioni

  • lamin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
SUN domain-containing protein 1
Alternative name(s):
Protein unc-84 homolog A
Sad1/unc-84 protein-like 1
Gene namesi
Name:Sun1
Synonyms:Unc84a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1924303. Sun1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 415415NuclearAdd
BLAST
Transmembranei416 – 43621HelicalAdd
BLAST
Topological domaini437 – 913477Perinuclear spaceAdd
BLAST

GO - Cellular componenti

  • acrosomal membrane Source: MGI
  • cytoplasm Source: MGI
  • integral component of membrane Source: MGI
  • integral component of nuclear inner membrane Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • LINC complex Source: MGI
  • nuclear envelope Source: MGI
  • nuclear membrane Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant mice are viable, but display hearing loss at all frequencies.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 913913SUN domain-containing protein 1PRO_0000218912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei139 – 1391PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D666.
MaxQBiQ9D666.
PaxDbiQ9D666.
PRIDEiQ9D666.

PTM databases

iPTMnetiQ9D666.
PhosphoSiteiQ9D666.

Expressioni

Tissue specificityi

Widely expressed. Expressed in cochlear outer hair cells (at protein level).4 Publications

Gene expression databases

BgeeiQ9D666.
CleanExiMM_UNC84A.
ExpressionAtlasiQ9D666. baseline and differential.
GenevisibleiQ9D666. MM.

Interactioni

Subunit structurei

Dimers and tetramers. 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 SYNE2. Interact with SYNE1 and SYNE3 (By similarity). Interacts with A-type lamin with a strong preference for unprocessed A-type lamin compared with the mature protein. Interaction with lamins B1 and C is hardly detectable. Interacts with NAT10 (By similarity). Interacts with EMD and TSNAX. Associates with the nuclear pore complex (NPC). Interacts with CCDC155 (via the last 22 amino acids); this interaction mediates CCDC155 telomere localization (By similarity). Interacts with CCDC79/TERB1; promoting the accumulation of the LINC complex complexes at the telomere-nuclear envelope attachment sites.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EMDP504024EBI-6752574,EBI-489887From a different organism.
SYNE2Q8WXH0-42EBI-6752574,EBI-6838657From a different organism.

GO - Molecular functioni

  • lamin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi218484. 5 interactions.
DIPiDIP-60732N.
IntActiQ9D666. 5 interactions.
MINTiMINT-4139090.
STRINGi10090.ENSMUSP00000056655.

Structurei

3D structure databases

ProteinModelPortaliQ9D666.
SMRiQ9D666. Positions 718-911.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini751 – 912162SUNPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 139139LMNA-bindingBy similarityAdd
BLAST
Regioni209 – 399191SYNE2-bindingBy similarityAdd
BLAST
Regioni310 – 39990EMD-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili491 – 53343Sequence analysisAdd
BLAST
Coiled coili563 – 63876Sequence analysisAdd
BLAST

Domaini

The SUN domain may play a role in the nuclear anchoring and/or migration.

Sequence similaritiesi

Contains 1 SUN domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2687. Eukaryota.
ENOG410YM6S. LUCA.
GeneTreeiENSGT00390000011587.
HOVERGENiHBG104132.
InParanoidiQ9D666.
KOiK19347.
OMAiMKLNYES.
OrthoDBiEOG7J446H.
PhylomeDBiQ9D666.
TreeFamiTF323915.

Family and domain databases

InterProiIPR032680. SUN1_N.
IPR012919. SUN_dom.
[Graphical view]
PfamiPF09387. MRP. 1 hit.
PF07738. Sad1_UNC. 1 hit.
[Graphical view]
PROSITEiPS51469. SUN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D666-1) [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
MDFSRLHTYT PPQCVPENTG YTYALSSSYS SDALDFETEH KLEPVFDSPR
60 70 80 90 100
MSRRSLRLVT TASYSSGDSQ AIDSHISTSR ATPAKGRETR TVKQRRSASK
110 120 130 140 150
PAFSINHLSG KGLSSSTSHD SSCSLRSATV LRHPVLDESL IREQTKVDHF
160 170 180 190 200
WGLDDDGDLK GGNKAATQGN GELAAEVASS NGYTCRDCRM LSARTDALTA
210 220 230 240 250
HSAIHGTTSR VYSRDRTLKP RGVSFYLDRT LWLAKSTSSS FASFIVQLFQ
260 270 280 290 300
VVLMKLNFET YKLKGYESRA YESQSYETKS HESEAHLGHC GRMTAGELSR
310 320 330 340 350
VDGESLCDDC KGKKHLEIHT ATHSQLPQPH RVAGAMGRLC IYTGDLLVQA
360 370 380 390 400
LRRTRAAGWS VAEAVWSVLW LAVSAPGKAA SGTFWWLGSG WYQFVTLISW
410 420 430 440 450
LNVFLLTRCL RNICKVFVLL LPLLLLLGAG VSLWGQGNFF SLLPVLNWTA
460 470 480 490 500
MQPTQRVDDS KGMHRPGPLP PSPPPKVDHK ASQWPQESDM GQKVASLSAQ
510 520 530 540 550
CHNHDERLAE LTVLLQKLQI RVDQVDDGRE GLSLWVKNVV GQHLQEMGTI
560 570 580 590 600
EPPDAKTDFM TFHHDHEVRL SNLEDVLRKL TEKSEAIQKE LEETKLKAGS
610 620 630 640 650
RDEEQPLLDR VQHLELELNL LKSQLSDWQH LKTSCEQAGA RIQETVQLMF
660 670 680 690 700
SEDQQGGSLE WLLEKLSSRF VSKDELQVLL HDLELKLLQN ITHHITVTGQ
710 720 730 740 750
APTSEAIVSA VNQAGISGIT EAQAHIIVNN ALKLYSQDKT GMVDFALESG
760 770 780 790 800
GGSILSTRCS ETYETKTALL SLFGVPLWYF SQSPRVVIQP DIYPGNCWAF
810 820 830 840 850
KGSQGYLVVR LSMKIYPTTF TMEHIPKTLS PTGNISSAPK DFAVYGLETE
860 870 880 890 900
YQEEGQPLGR FTYDQEGDSL QMFHTLERPD QAFQIVELRV LSNWGHPEYT
910
CLYRFRVHGE PIQ
Length:913
Mass (Da):101,976
Last modified:February 2, 2004 - v2
Checksum:iB9872C8F2E044964
GO
Isoform 2 (identifier: Q9D666-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     222-344: Missing.

Note: No experimental confirmation available.
Show »
Length:790
Mass (Da):88,203
Checksum:i127979E6640F2CD4
GO
Isoform 3 (identifier: Q9D666-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-344: Missing.

Note: No experimental confirmation available.
Show »
Length:876
Mass (Da):97,924
Checksum:i09357E280A0B8392
GO
Isoform 4 (identifier: Q9D666-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-285: RGVSFYLDRTLWLAKSTSSSFASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEA → P

Show »
Length:849
Mass (Da):94,507
Checksum:i7810982DFA292D25
GO

Sequence cautioni

The sequence AAH30330.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61L → V in AAT90501 (PubMed:17132086).Curated
Sequence conflicti108 – 1081L → P in BAE39733 (PubMed:16141072).Curated
Sequence conflicti439 – 4391F → L in AAT90501 (PubMed:17132086).Curated
Sequence conflicti479 – 4791H → N in BAE35723 (PubMed:16141072).Curated
Sequence conflicti505 – 5051D → G in BAE39733 (PubMed:16141072).Curated
Sequence conflicti593 – 5931E → A in BAE39733 (PubMed:16141072).Curated
Sequence conflicti704 – 7041S → F in BAE39733 (PubMed:16141072).Curated
Sequence conflicti856 – 8572QP → AA in AAK13526 (PubMed:12036294).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei221 – 28565RGVSF…HESEA → P in isoform 4. 1 PublicationVSP_039552Add
BLAST
Alternative sequencei222 – 344123Missing in isoform 2. 1 PublicationVSP_009346Add
BLAST
Alternative sequencei308 – 34437Missing in isoform 3. 1 PublicationVSP_009347Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY682989 mRNA. Translation: AAT90501.1.
AK014585 mRNA. Translation: BAB29445.1.
AK036187 mRNA. Translation: BAC29339.1.
AK160281 mRNA. Translation: BAE35723.1.
AK167686 mRNA. Translation: BAE39733.1.
BC030330 mRNA. Translation: AAH30330.1. Different initiation.
BC047928 mRNA. Translation: AAH47928.1.
BC048156 mRNA. Translation: AAH48156.1.
AF343752 mRNA. Translation: AAK13526.1.
CCDSiCCDS19804.1. [Q9D666-1]
CCDS57395.1. [Q9D666-3]
CCDS57396.1. [Q9D666-4]
CCDS57397.1. [Q9D666-2]
RefSeqiNP_001243044.1. NM_001256115.1. [Q9D666-3]
NP_001243045.1. NM_001256116.1. [Q9D666-4]
NP_001243046.1. NM_001256117.1. [Q9D666-2]
NP_001243047.1. NM_001256118.1.
NP_077771.1. NM_024451.2. [Q9D666-1]
XP_006504823.1. XM_006504760.1. [Q9D666-1]
XP_006504824.1. XM_006504761.2. [Q9D666-1]
XP_011239291.1. XM_011240989.1. [Q9D666-1]
UniGeneiMm.210845.

Genome annotation databases

EnsembliENSMUST00000058716; ENSMUSP00000056655; ENSMUSG00000036817. [Q9D666-1]
ENSMUST00000078690; ENSMUSP00000077756; ENSMUSG00000036817. [Q9D666-4]
ENSMUST00000110883; ENSMUSP00000106507; ENSMUSG00000036817. [Q9D666-2]
ENSMUST00000110884; ENSMUSP00000106508; ENSMUSG00000036817. [Q9D666-3]
GeneIDi77053.
KEGGimmu:77053.
UCSCiuc009agb.2. mouse. [Q9D666-1]
uc009agc.2. mouse. [Q9D666-3]
uc009agd.2. mouse. [Q9D666-2]
uc009age.2. mouse. [Q9D666-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY682989 mRNA. Translation: AAT90501.1.
AK014585 mRNA. Translation: BAB29445.1.
AK036187 mRNA. Translation: BAC29339.1.
AK160281 mRNA. Translation: BAE35723.1.
AK167686 mRNA. Translation: BAE39733.1.
BC030330 mRNA. Translation: AAH30330.1. Different initiation.
BC047928 mRNA. Translation: AAH47928.1.
BC048156 mRNA. Translation: AAH48156.1.
AF343752 mRNA. Translation: AAK13526.1.
CCDSiCCDS19804.1. [Q9D666-1]
CCDS57395.1. [Q9D666-3]
CCDS57396.1. [Q9D666-4]
CCDS57397.1. [Q9D666-2]
RefSeqiNP_001243044.1. NM_001256115.1. [Q9D666-3]
NP_001243045.1. NM_001256116.1. [Q9D666-4]
NP_001243046.1. NM_001256117.1. [Q9D666-2]
NP_001243047.1. NM_001256118.1.
NP_077771.1. NM_024451.2. [Q9D666-1]
XP_006504823.1. XM_006504760.1. [Q9D666-1]
XP_006504824.1. XM_006504761.2. [Q9D666-1]
XP_011239291.1. XM_011240989.1. [Q9D666-1]
UniGeneiMm.210845.

3D structure databases

ProteinModelPortaliQ9D666.
SMRiQ9D666. Positions 718-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218484. 5 interactions.
DIPiDIP-60732N.
IntActiQ9D666. 5 interactions.
MINTiMINT-4139090.
STRINGi10090.ENSMUSP00000056655.

PTM databases

iPTMnetiQ9D666.
PhosphoSiteiQ9D666.

Proteomic databases

EPDiQ9D666.
MaxQBiQ9D666.
PaxDbiQ9D666.
PRIDEiQ9D666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058716; ENSMUSP00000056655; ENSMUSG00000036817. [Q9D666-1]
ENSMUST00000078690; ENSMUSP00000077756; ENSMUSG00000036817. [Q9D666-4]
ENSMUST00000110883; ENSMUSP00000106507; ENSMUSG00000036817. [Q9D666-2]
ENSMUST00000110884; ENSMUSP00000106508; ENSMUSG00000036817. [Q9D666-3]
GeneIDi77053.
KEGGimmu:77053.
UCSCiuc009agb.2. mouse. [Q9D666-1]
uc009agc.2. mouse. [Q9D666-3]
uc009agd.2. mouse. [Q9D666-2]
uc009age.2. mouse. [Q9D666-4]

Organism-specific databases

CTDi23353.
MGIiMGI:1924303. Sun1.

Phylogenomic databases

eggNOGiKOG2687. Eukaryota.
ENOG410YM6S. LUCA.
GeneTreeiENSGT00390000011587.
HOVERGENiHBG104132.
InParanoidiQ9D666.
KOiK19347.
OMAiMKLNYES.
OrthoDBiEOG7J446H.
PhylomeDBiQ9D666.
TreeFamiTF323915.

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.

Miscellaneous databases

NextBioi346388.
PROiQ9D666.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D666.
CleanExiMM_UNC84A.
ExpressionAtlasiQ9D666. baseline and differential.
GenevisibleiQ9D666. MM.

Family and domain databases

InterProiIPR032680. SUN1_N.
IPR012919. SUN_dom.
[Graphical view]
PfamiPF09387. MRP. 1 hit.
PF07738. Sad1_UNC. 1 hit.
[Graphical view]
PROSITEiPS51469. SUN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the structures involved in localization of the SUN proteins to the nuclear envelope and the centrosome."
    Wang Q., Du X., Cai Z., Greene M.I.
    DNA Cell Biol. 25:554-562(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBUNIT, SUBCELLULAR LOCATION, ASSOCIATION WITH THE CENTROSOME, TISSUE SPECIFICITY.
  2. "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] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo, Placenta and Skin.
  3. "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).
    Strain: C57BL/6J, FVB/N and FVB/N-3.
    Tissue: Brain and Mammary tumor.
  4. "Identification and characterization of cDNAs encoding four novel proteins that interact with translin associated factor-X."
    Bray J.D., Chennathukuzhi V.M., Hecht N.B.
    Genomics 79:799-808(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 605-913, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TSNAX.
    Tissue: Testis.
  5. "Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane."
    Dreger M., Bengtsson L., Schoeneberg T., Otto H., Hucho F.
    Proc. Natl. Acad. Sci. U.S.A. 98:11943-11948(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  6. "Coupling of the nucleus and cytoplasm: role of the LINC complex."
    Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B., Stahl P.D., Hodzic D.
    J. Cell Biol. 172:41-53(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE LINC COMPLEX, INTERACTION WITH LAMINS AND SYNE2, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
  7. "SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton."
    Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M., Fry A.M., Trembath R.C., Shackleton S.
    Mol. Cell. Biol. 26:3738-3751(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH LMNA; SYNE1 AND SYNE2.
  8. "SUN1 is required for telomere attachment to nuclear envelope and gametogenesis in mice."
    Ding X., Xu R., Yu J., Xu T., Zhuang Y., Han M.
    Dev. Cell 12:863-872(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Functional association of Sun1 with nuclear pore complexes."
    Liu Q., Pante N., Misteli T., Elsagga M., Crisp M., Hodzic D., Burke B., Roux K.J.
    J. Cell Biol. 178:785-798(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH THE NUCLEAR PORE COMPLEX.
  10. Cited for: SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
  11. "Requirement for Sun1 in the expression of meiotic reproductive genes and piRNA."
    Chi Y.H., Cheng L.I., Myers T., Ward J.M., Williams E., Su Q., Faucette L., Wang J.Y., Jeang K.T.
    Development 136:965-973(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH TELOMERES.
  13. "Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins."
    Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G., Worman H.J.
    J. Cell Sci. 122:4099-4108(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LMNA AND SYN2.
  14. "SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus during neurogenesis and neuronal migration in mice."
    Zhang X., Lei K., Yuan X., Wu X., Zhuang Y., Xu T., Xu R., Han M.
    Neuron 64:173-187(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNE2.
  15. "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: FUNCTION.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  17. "Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes."
    Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S.
    J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMD.
  18. "A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis."
    Morimoto A., Shibuya H., Zhu X., Kim J., Ishiguro K., Han M., Watanabe Y.
    J. Cell Biol. 198:165-172(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC155.
  19. Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  20. "The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis."
    Shibuya H., Ishiguro K.I., Watanabe Y.
    Nat. Cell Biol. 16:145-156(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC79.

Entry informationi

Entry nameiSUN1_MOUSE
AccessioniPrimary (citable) accession number: Q9D666
Secondary accession number(s): Q3TIW3
, Q3TV96, Q6B4H0, Q80SU8, Q8BZ99, Q99P23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: February 2, 2004
Last modified: May 11, 2016
This is version 133 of the entry and version 2 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.