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Protein

Nesprin-1

Gene

Syne1

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

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  1. actin binding Source: MGI
  2. actin filament binding Source: UniProtKB
  3. lamin binding Source: MGI
  4. poly(A) RNA binding Source: MGI
  5. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. cytoskeletal anchoring at nuclear membrane Source: MGI
  2. establishment of nucleus localization Source: MGI
  3. Golgi organization Source: MGI
  4. muscle cell differentiation Source: MGI
  5. nuclear matrix anchoring at nuclear membrane Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_287050. Meiotic synapsis.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Syne1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1927152. Syne1.

Subcellular locationi

  1. Nucleus outer membrane Curated; Single-pass type IV membrane protein Curated; Cytoplasmic side Curated
  2. Nucleus
  3. Nucleus envelope
  4. Cytoplasmcytoskeleton
  5. Cytoplasmmyofibrilsarcomere By similarity

  6. 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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 87488748CytoplasmicPROSITE-ProRule annotationAdd
BLAST
Transmembranei8749 – 876921Helical; Anchor for type IV membrane proteinPROSITE-ProRule annotationAdd
BLAST
Topological domaini8770 – 879930Perinuclear spacePROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoskeleton Source: UniProtKB-SubCell
  3. Golgi apparatus Source: MGI
  4. integral component of membrane Source: MGI
  5. LINC complex Source: MGI
  6. nuclear envelope Source: UniProtKB
  7. nuclear membrane Source: MGI
  8. nuclear outer membrane Source: UniProtKB-SubCell
  9. nucleoplasm Source: MGI
  10. nucleus Source: MGI
  11. postsynaptic membrane Source: MGI
  12. sarcomere Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 87998799Nesprin-1PRO_0000392209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8227 – 82271PhosphoserineBy similarity
Modified residuei8278 – 82781PhosphothreonineBy similarity
Modified residuei8281 – 82811PhosphoserineBy similarity
Modified residuei8284 – 82841PhosphoserineBy similarity
Modified residuei8308 – 83081Phosphoserine1 Publication
Modified residuei8363 – 83631PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6ZWR6.
PaxDbiQ6ZWR6.
PRIDEiQ6ZWR6.

PTM databases

PhosphoSiteiQ6ZWR6.

Expressioni

Tissue specificityi

Expressed in C2F3 and CH310T1/2 cells, brain and skeletal muscle (at protein level).2 Publications

Gene expression databases

BgeeiQ6ZWR6.
ExpressionAtlasiQ6ZWR6. baseline and differential.
GenevestigatoriQ6ZWR6.

Interactioni

Subunit structurei

Dimer. 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 SYNE3. May interact with MUSK. Interacts with EMD and LMNA in vitro (By similarity). Interacts with F-actin via its N-terminal domain.By similarity2 Publications

Protein-protein interaction databases

BioGridi211015. 1 interaction.
DIPiDIP-60966N.
STRINGi10090.ENSMUSP00000051825.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWR6.
SMRiQ6ZWR6. Positions 23-279, 997-1042.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 289289Actin-bindingAdd
BLAST
Domaini27 – 134108CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini178 – 283106CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati314 – 39784Spectrin 1Add
BLAST
Repeati398 – 502105Spectrin 2Add
BLAST
Repeati503 – 609107Spectrin 3Add
BLAST
Repeati610 – 70394Spectrin 4Add
BLAST
Repeati704 – 815112Spectrin 5Add
BLAST
Repeati816 – 923108Spectrin 6Add
BLAST
Repeati924 – 1024101Spectrin 7Add
BLAST
Repeati1025 – 112298Spectrin 8Add
BLAST
Repeati1123 – 1246124Spectrin 9Add
BLAST
Repeati1247 – 133387Spectrin 10Add
BLAST
Repeati1334 – 1442109Spectrin 11Add
BLAST
Repeati1443 – 1548106Spectrin 12Add
BLAST
Repeati1549 – 1651103Spectrin 13Add
BLAST
Repeati1652 – 1761110Spectrin 14Add
BLAST
Repeati1762 – 1877116Spectrin 15Add
BLAST
Repeati1878 – 197497Spectrin 16Add
BLAST
Repeati1975 – 2079105Spectrin 17Add
BLAST
Repeati2080 – 2193114Spectrin 18Add
BLAST
Repeati2194 – 2301108Spectrin 19Add
BLAST
Repeati2302 – 239998Spectrin 20Add
BLAST
Repeati2400 – 2511112Spectrin 21Add
BLAST
Repeati2512 – 2617106Spectrin 22Add
BLAST
Repeati2618 – 2729112Spectrin 23Add
BLAST
Repeati2730 – 2836107Spectrin 24Add
BLAST
Repeati2837 – 2960124Spectrin 25Add
BLAST
Repeati2961 – 3060100Spectrin 26Add
BLAST
Repeati3061 – 3169109Spectrin 27Add
BLAST
Repeati3170 – 3273104Spectrin 28Add
BLAST
Repeati3274 – 3385112Spectrin 29Add
BLAST
Repeati3386 – 3488103Spectrin 30Add
BLAST
Repeati3489 – 3591103Spectrin 31Add
BLAST
Repeati3592 – 3718127Spectrin 32Add
BLAST
Repeati3719 – 381294Spectrin 33Add
BLAST
Repeati3813 – 3918106Spectrin 34Add
BLAST
Repeati3919 – 4026108Spectrin 35Add
BLAST
Repeati4027 – 4137111Spectrin 36Add
BLAST
Repeati4138 – 423396Spectrin 37Add
BLAST
Repeati4234 – 4337104Spectrin 38Add
BLAST
Repeati4338 – 4449112Spectrin 39Add
BLAST
Repeati4450 – 4558109Spectrin 40Add
BLAST
Repeati4559 – 4667109Spectrin 41Add
BLAST
Repeati4668 – 4774107Spectrin 42Add
BLAST
Repeati4775 – 4880106Spectrin 43Add
BLAST
Repeati4881 – 4989109Spectrin 44Add
BLAST
Repeati4990 – 5097108Spectrin 45Add
BLAST
Repeati5098 – 5207110Spectrin 46Add
BLAST
Repeati5208 – 5316109Spectrin 47Add
BLAST
Repeati5317 – 5422106Spectrin 48Add
BLAST
Repeati5423 – 552098Spectrin 49Add
BLAST
Repeati5521 – 5628108Spectrin 50Add
BLAST
Repeati5629 – 5745117Spectrin 51Add
BLAST
Repeati5746 – 5851106Spectrin 52Add
BLAST
Repeati5971 – 6080110Spectrin 53Add
BLAST
Repeati6081 – 6187107Spectrin 54Add
BLAST
Repeati6377 – 6488112Spectrin 55Add
BLAST
Repeati6489 – 658496Spectrin 56Add
BLAST
Repeati6585 – 6694110Spectrin 57Add
BLAST
Repeati6695 – 6798104Spectrin 58Add
BLAST
Repeati6799 – 6905107Spectrin 59Add
BLAST
Repeati6906 – 7023118Spectrin 60Add
BLAST
Repeati7024 – 7131108Spectrin 61Add
BLAST
Repeati7132 – 7240109Spectrin 62Add
BLAST
Repeati7241 – 7353113Spectrin 63Add
BLAST
Repeati7354 – 7457104Spectrin 64Add
BLAST
Repeati7458 – 7561104Spectrin 65Add
BLAST
Repeati7562 – 7674113Spectrin 66Add
BLAST
Repeati7675 – 7786112Spectrin 67Add
BLAST
Repeati7787 – 7886100Spectrin 68Add
BLAST
Repeati7887 – 8000114Spectrin 69Add
BLAST
Repeati8001 – 8109109Spectrin 70Add
BLAST
Repeati8110 – 8221112Spectrin 71Add
BLAST
Repeati8332 – 8440109Spectrin 72Add
BLAST
Repeati8441 – 8550110Spectrin 73Add
BLAST
Repeati8551 – 8668118Spectrin 74Add
BLAST
Domaini8740 – 879960KASHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili314 – 86668353Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8665 – 873167Ser-richAdd
BLAST

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.By similarity

Sequence similaritiesi

Belongs to the nesprin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 1 KASH domain.PROSITE-ProRule annotation
Contains 74 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000120125.
HOVERGENiHBG106534.
InParanoidiQ6ZWR6.
OMAiCATESEC.
OrthoDBiEOG72JWF7.
PhylomeDBiQ6ZWR6.
TreeFamiTF317709.
TF337116.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR030265. SYNE1.
[Graphical view]
PANTHERiPTHR11915:SF267. PTHR11915:SF267. 1 hit.
PfamiPF00307. CH. 2 hits.
PF10541. KASH. 1 hit.
PF00435. Spectrin. 10 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00150. SPEC. 42 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS51049. KASH. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZWR6-1) [UniParc]FASTAAdd to basket

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.

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        10         20         30         40         50
MATSRASSRS HRDITNVMQR LQDEQEIVQK RTFTKWINSH LAKRKPPMVV
60 70 80 90 100
DDLFEDMKDG IKLLALLEVL SGQKLPCEQG HRVKRIHAVA NIGTALKFLE
110 120 130 140 150
GRKIKLVNIN ATDIADGRPS IVLGLMWTII LYFQIEELTS NLPQLQSLSS
160 170 180 190 200
SASSVDSMVS TETASPPSKR KVAAKIQGNA KKTLLKWVQH TAGKQMGIEV
210 220 230 240 250
KDFGKSWRTG LAFHSVIHAI QPELVDLEKV KTRSNRENLE DAFTIAETQL
260 270 280 290 300
GIPRLLDPED VDVDKPDEKS IMTYVAQFLT QYPDIHGAGC DGQEDDVVFV
310 320 330 340 350
GFTNNIALLL GFQRDDRLIL KETKVWIEQF ERDFTRAQMT ESSLQDKYQA
360 370 380 390 400
FKHFRVQYEM KRKQVEHIIQ PLQRDGKLTL DQALVKQCWE RVSSRLFDWH
410 420 430 440 450
IQLDKSLPAP LGTIGAWLYR AEVALREEIT IQQVHEETAN TIQRKLEQHK
460 470 480 490 500
DLLQNTDAHK RAFHEIYQTR SVNGIPMPPD QLEDMAERFH FVSSTSELHL
510 520 530 540 550
MKMEFLELKY RLLSLLVLAE SKLKSWIIKY GRRESVELLL QSYISFIENS
560 570 580 590 600
KFFEQYEVTY QILKQTADIY VKAEGSVEEA ENVMKFMSEA TAQWRNLSVE
610 620 630 640 650
VRSVRSMLEE VISNWDRYGD TVASLQAWLE DAEKMLSQSE HAKKDFFRNL
660 670 680 690 700
PHWIQQHTAM NDAGNFLIET CDEIVSRDLK QQLLLLNGRW RELFMEVKQY
710 720 730 740 750
ARADEMDRMK KEYIDVTTTL FGFATEAHRK LSEPLEVSFI NVKLLIQDLE
760 770 780 790 800
DLEKRVPVMD AQYKMIAKKA HLFAKESPQE EANEMLTTMS KLKEQLSKVK
810 820 830 840 850
ECCSPLLYEA QQLTVPLEEL ETQITSFYDS LGKINEILSV LEQEAQSSTL
860 870 880 890 900
FKQKHQELLA SQENCKKSLT LIEKGSQSVQ KLVTSSQARK PWDHTKLQKQ
910 920 930 940 950
IADVHHAFQS MIKKTGDWKK HVEANSRLMK KFEESRAELE KVLRVAQEGL
960 970 980 990 1000
EEKGDPEELL RRHTEFFSQL DQRVLNAFLK ACDELTDILP EQEQQGLQEA
1010 1020 1030 1040 1050
VRKLHKQWKD LQGEAPYHLL HLKIAVEKDR FSAAVEECRA ELEQETKLAP
1060 1070 1080 1090 1100
QEGSEKIIKE HRVFFSDKGP HHLCEKRLQL IEELCGKLPV QDPVRDTCGA
1110 1120 1130 1140 1150
CHTALKELKA SIDNTYTMLV DDPDKWKDYT SRFSEFSSWV SAKKACLKKI
1160 1170 1180 1190 1200
KDEPIDTGNH DEVKHMVDEI RNDITKKGES LSWLKSRLKY LIDISSENEA
1210 1220 1230 1240 1250
QKRGDELAEL SSSFKALVAL LSEVEKLLSN FGECVQYKEI VKSSLEGLIS
1260 1270 1280 1290 1300
GPQESKEEAE MILDSKNLLE AQQLLLHHQQ KTKMISAKKR DLQEQMEQAQ
1310 1320 1330 1340 1350
QGGQAGPGQE ELRKLESTLT GLEQSRERQE RRIQVSLRKW ERFETNKETV
1360 1370 1380 1390 1400
VRYLFQTGSS HERFLSFSSL ESLSSELEQT KEFSKRTESI ATQAENLVKE
1410 1420 1430 1440 1450
AAELPLGPRN KRVLQRQAKS IKEQVTTLED TLEEDIKTME MVKSKWDHFG
1460 1470 1480 1490 1500
SNFETLSIWI LEKENELSSL EASASAADVQ ISQIKVTIQE IESKIDSIVG
1510 1520 1530 1540 1550
LEEEAQSFAQ FVTTGESARI KAKLTQIRRY WEELQEHARG LEGTILGHLS
1560 1570 1580 1590 1600
QQQKFEENLR KIRQSVSEFA ERLADPIKIC SSAAETYKVL QEHMDLCQAV
1610 1620 1630 1640 1650
ESLSSTVTMF SASAQKAVNR ESCTQEAAAL QQQYEEILHK AKEMQTALED
1660 1670 1680 1690 1700
LLARWQRLEK GLSPFLTWLE RCEAIASSPE KDISADRGKV ESELQLIQAL
1710 1720 1730 1740 1750
QNEVVSQASL YSNLLQLKEA LFSVASKEDV AVMKLQLEQL DERWGDLPQI
1760 1770 1780 1790 1800
ISKRMHFLQS VLAEHKQFDE LLFSFSVWIK QFLGELQRTS EINLRDHQVA
1810 1820 1830 1840 1850
LTRHKDHAAE IEKKRGEITH LQGHLSQLRS LGRAQDLHPL QSKVDDCFQL
1860 1870 1880 1890 1900
FEEASQVVER RKLALAQLAE FLQSHACMST LLYQLRQTVE ATKSMSKKQS
1910 1920 1930 1940 1950
DSLKTDLHSA IQDVKTLESS AISLDGTLTK AQCHLKSASP EERTSCRATT
1960 1970 1980 1990 2000
DQLSLEVERI QNLLGTKQSE ADALVALKEA FREQKEELLR SIEDIEERMD
2010 2020 2030 2040 2050
RERLKVPTRQ ALQHRLRVFN QLEDELNSHE HELCWLKDKA KQIAQKDVAF
2060 2070 2080 2090 2100
APEVDREING LEATWDDTRR QIHENQGQCC GLIDLVREYQ SLKSTVCNVL
2110 2120 2130 2140 2150
EDASNVVVMR ATIKDQGDLK WAFSKHETSR NEMNSKQKEL DSFTSKGKHL
2160 2170 2180 2190 2200
LSELKKIHSG DFSLVKTDME STLDKWLDVS ERIEENMDML RVSLSIWDDV
2210 2220 2230 2240 2250
LSRKDEIEGW SNSSLPKLAE NISNLNNSLR AEELLKELES EVKIKALKLE
2260 2270 2280 2290 2300
DLHSKINNLK ELTKNPETPT ELQFIEADLR QKLEHAKEIT EEARGTLKDF
2310 2320 2330 2340 2350
TAQRTQVERF VKDITAWLIN VEESLTRCAQ TETCEGLKKA KDIRKELQSQ
2360 2370 2380 2390 2400
QNSITSTQEE LNSLCRKHHS VELESLGRAM TGLIKKHEAT SQLCSQTQAR
2410 2420 2430 2440 2450
IQDSLEKHFS GSMKEFQEWF LGAKAAARES SNLTGDSQIL EARLHNLQGV
2460 2470 2480 2490 2500
LDSLSDGQSK LDVVTQEGQT LYAHLPKQIV SSIQEQITKA NEEFQAFLKQ
2510 2520 2530 2540 2550
CLKEKQALQD CVSELGSFED QHRKLNLWIH EMEERLKTEN LGESKHHISE
2560 2570 2580 2590 2600
KKNEVRKVEM FLGELLAARE SLDKLSQRGQ LLSEESHSAG KGGCRSTQLL
2610 2620 2630 2640 2650
TSYQSLLRVT KEKLRSCQLA LKEHEALEEA TQSMWARVKD VQDRLACAES
2660 2670 2680 2690 2700
TLGNKETLEG RLSQIQDILL MKGEGEVKLN LAIGKGDQAL RSSNKEGQQA
2710 2720 2730 2740 2750
IQDQLEMLKK AWAEAMNSAV HAQSTLESVI DQWNDYLEKK SQLEQWMESV
2760 2770 2780 2790 2800
DQRLEHPLQL QPGLKEKFSL LDHFQSIVSE AEDHTGALQQ LAAKSRELYQ
2810 2820 2830 2840 2850
KTQDESFKEA GQEELRTQFQ DIMTVAKEKM RTVEDLVKDH LMYLDAVQEF
2860 2870 2880 2890 2900
ADWLHSAKEE LHRWSDTSGD PSATQKKLLK IKELIDSREI GAGRLSRVES
2910 2920 2930 2940 2950
LAPAVKQNTA ASGCELLNSE MQALRADWRQ WEDCLFQTQS SLESLVSEMA
2960 2970 2980 2990 3000
LSEQEFFGQV TQLEQALEQF CTLLKTWAQQ LTLLEGKNSD EEILECWHKG
3010 3020 3030 3040 3050
REILDALQKA EPMTEDLKSQ LNELCRFSRD LSPYSEKVSG LIKEYNCLCL
3060 3070 3080 3090 3100
QASKGCQNKE QILQERFQKA SRGFQQWLVN AKITTAKCFD LPQNLSEVSS
3110 3120 3130 3140 3150
SLQKIQEFLS ESENGQHKLN TMLFKGELLS SLLTEEKAQA VQAKVLTAKE
3160 3170 3180 3190 3200
EWKSFHANLH QKESALENLK IQMKDFEVSA ELVQNWLSKT ERLVQESSNR
3210 3220 3230 3240 3250
LYDLPAKRRE QQKLQSVLEE IQCYEPQLHR LKEKARQLWE GQAASKSFVH
3260 3270 3280 3290 3300
RVSQLSSQYL ALSNVTKEKV SRLDRIIAEH NRFSQGVKEL QDWMSDAVHM
3310 3320 3330 3340 3350
LDSYCLPTSD KSVLDSRMLK LEALLSVRQE KEIQMKMVVT RGEYVLQSTS
3360 3370 3380 3390 3400
LEGSAAVQQQ LQAVKDMWES LLSAAIRCKS QLEGALSKWT SYQDDVRQFS
3410 3420 3430 3440 3450
SWMDSVEVSL TESEKQHTEL REKITALGKA KLLNEEVLSH SSLLETIEVK
3460 3470 3480 3490 3500
RAAMTEHYVT QLELQDLQER HQALKEKAKE AVTKLEKLVR LHQEYQRDLK
3510 3520 3530 3540 3550
AFESWLEQEQ EKLDRCSVHE GDTNAHETML RDLQELQVRC AEGQALLNSV
3560 3570 3580 3590 3600
LHTREDVIPS GLPQAEDRVL ESLRQDWQVY QHRLAEARMQ LNNVVNKLRL
3610 3620 3630 3640 3650
MEQKFQQADE WLKRMEEKIN FRSECQSSRS DKEIQLLQLK KWHEDLSAHR
3660 3670 3680 3690 3700
DEVEEVGTRA QGILDETHIS SRMGCQATQL TSRYQALLLQ VLEQIKFFEE
3710 3720 3730 3740 3750
ELQCLEETES SLSSYSDWYG STHKNFKNVA TKIDKVDESM MGKKLKTLEV
3760 3770 3780 3790 3800
LLKDMEKGHS LLKSAREKGE RAMKFLAEHE AEALRKEIHT YMEQLKNLTS
3810 3820 3830 3840 3850
TVRKECMSLE KGLHLAKEFS DKYKVLAQWM AEYQEILCTP EEPKMELYEK
3860 3870 3880 3890 3900
KAQLSKYKSL QQMVLSHEPS VTSVQEKSEA LLELVQDQSL KDKIQKLQSD
3910 3920 3930 3940 3950
FQDLCSRAKE RVFSLEAKVK DHEDYNTELQ EVEKWLLQMS GRLVAPDLLE
3960 3970 3980 3990 4000
MSSLETITQQ LAHHKAMMEE IAGFEDRLDN LKAKGDTLIG QCPEHLQAKQ
4010 4020 4030 4040 4050
KQTVQAHLQG TKDSYSAICS TAQRVYRSLE YELQKHVSSQ DTLQQCQAWI
4060 4070 4080 4090 4100
SAVQPDLKPS PQPPLSRAEA VKQVKHFRAL QEQARTYLDL LCSMCDLSNS
4110 4120 4130 4140 4150
SVKNTAKDIQ QTEQLIEQRL VQAQNLTQGW EEIKSLKAEL WIYLQDADQQ
4160 4170 4180 4190 4200
LQNMKRRHTE LEINIAQNMV MQVKDFIKQL QCKQVSVSTI VEKVDKLTKN
4210 4220 4230 4240 4250
QESPEHKEIT HLNDQWQDLC LQSDKLCAQR EQDLQRTSSY HDHMRVVEAF
4260 4270 4280 4290 4300
LEKFTTEWDS LARSNAESTA IHLEALKKLA LALQEEMYAI DDLKDCKQKL
4310 4320 4330 4340 4350
IEQLGLDDRE LVREQTSHLE QRWFQLQDLV KRKIQVSVTN LEELNVIQSR
4360 4370 4380 4390 4400
FQELMEWAEE QQPNIVEALK QSPPPGMAQH LLMDHLAICS ELEAKQVLLK
4410 4420 4430 4440 4450
SLMKDADRVM ADLGLNERKV IQKALSEAQK HVSCLSDLVG QRRKYLNKAL
4460 4470 4480 4490 4500
SEKTQFLMAV FQATSQIQQH ERKIVFREYI CLLPDDVSKQ VKTCKTAQAS
4510 4520 4530 4540 4550
LKTYQNEVTG LCAQGRELMK GITKQEQEEV LGKLQELQTV YDTVLQKCSH
4560 4570 4580 4590 4600
RLQELEKSLV SRKHFKEDFD KACHWLKQAD IVTFPEINLM NEKTELHAQL
4610 4620 4630 4640 4650
DKYQSILEQS PEYENLLLTL QTTGQAMLPS LNEVDHSYLS EKLSALPQQF
4660 4670 4680 4690 4700
NVIVALAKDK FYKTQEAILA RKEYTSLIEL TTQSLGDLED QFLKMRKMPS
4710 4720 4730 4740 4750
DLIVEESVSL QQSCSALLGE VVALGEAVNE LNQKKESFRS TGQPWQPEKM
4760 4770 4780 4790 4800
LQLATLYHRL KRQAEQRVSF LEDTTSVYKE HAQMCRQLES QLEVVKREQA
4810 4820 4830 4840 4850
KVNEETLPAE EKLKVYHSLA GSLQDSGILL KRVATHLEDL SPHLDPTAYE
4860 4870 4880 4890 4900
KAKSQVQSWQ EELKQMTSDV GELVTECESR MVQSIDFQTE MSRSLDWLRR
4910 4920 4930 4940 4950
VKAELSGPVC LDLSLQDIQE EIRKIQIHQE EVLSSLRIMS ALSHKEQEKF
4960 4970 4980 4990 5000
TKAKELISAD LEHTLAELQE LDGDVQEALR TRQATLTEIY SRCQRYYQVF
5010 5020 5030 5040 5050
QAANDWLDDA QEMLQLAGNG LDVESAEENL RSHMEFFKTE GQFHSNMEEL
5060 5070 5080 5090 5100
RGLVARLDPL IKATGKEELA QKMASLEKRS QGIIQESHTQ RDLLQRCMVQ
5110 5120 5130 5140 5150
WQEYQKAREG VIELMNDAEK KLSEFAVLKT SSIHEAEEKL SKHKALVSVV
5160 5170 5180 5190 5200
DSFHEKIVAL EEKASQLEQT GNDTSKATLS RSMTTVWQRW TRLRAVAQDQ
5210 5220 5230 5240 5250
EKILEDAVDE WKRLSAKVKE TTEVINQLQG RLPGSSTEKA SKAELMTLLE
5260 5270 5280 5290 5300
SHDTYLMDLE SQQLTLGVLQ QRALSMLQDR AFPGTEEEVP ILRAITALQD
5310 5320 5330 5340 5350
QCLNMQEKVK NHGKLVKQEL QEREAVETRI NSVKSWVQET KDYLGNPTIE
5360 5370 5380 5390 5400
IDTQLEELKR LLAEATSHQE SIEKIAEEQK NKYLGLYTVL PSEISLQLAE
5410 5420 5430 5440 5450
VALDLKIHDQ IQEKVQEIEE GKAMSQEFSC KIQKVTKDLT TILTKLKAKT
5460 5470 5480 5490 5500
DDLVHAKAEH KMLGEELDGC NSKLMELDAA IQTFSERHSQ LGQPLAKKIG
5510 5520 5530 5540 5550
KLTELHQQTI RQAENRLSKL NQALSHMEEY NEMLETVRKW IEKAKVLVHG
5560 5570 5580 5590 5600
NIAWNSASQL QEQYILHQTL LEESGEIDSD LEAMAEKVQH LANVYCTGKL
5610 5620 5630 5640 5650
SQQVTQFGRE MEELRQAIRV RLRNLQDAAK DMKKFEGELR NLQVALEQAQ
5660 5670 5680 5690 5700
TILTSPEVGR RSLKEQLCHR QHLLSEMESL KPKMQAVQLC QSALRIPEDV
5710 5720 5730 5740 5750
VASLPLCHAA LRLQEEASQL QHTAIQQCNI MQAKKHSLIF PPKEAVVQYE
5760 5770 5780 5790 5800
QYKQEMKHLQ QLIEEAHREI EDKPVATSNI QELQAQISLH EELAQKIKGY
5810 5820 5830 5840 5850
QEQIDSLNSK CKMLTMKAKH ATMLLTVTEV EGLAEGTEDL DRELHPTPSA
5860 5870 5880 5890 5900
HPSVVMMTAG RCHTLLSPVT EESGEEGTNS EISSPPACRS PSPVANTEAA
5910 5920 5930 5940 5950
VNQDIAYYQA LSAEGLQTDA ARIPPSAAVS QELYEPGLEP SATAKLGDLQ
5960 5970 5980 5990 6000
RSWETLKNVI SEKQRTLYEV LERQQKYQDS LQSISTKMEA MEMKLGESLE
6010 6020 6030 6040 6050
PSRSPESQMA EHQALMDEVQ MLQDEINGLQ VSLAEELVAE SQESDPAEQL
6060 6070 6080 6090 6100
ALQSTLTVLA ERMSTIRMKA AGKRQLLEEK LSDQLEEQRQ EQALQRYRCE
6110 6120 6130 6140 6150
ADELDHWLLN TKATLDVALG TSQEPMDMDA QLVDCQNMLV EIEQKVVALS
6160 6170 6180 6190 6200
QLSVHNENLL LEGKAHTKEE AEQLAVKLRL LKGSLGELQR ALHDRQLDMQ
6210 6220 6230 6240 6250
GVTQEKEEND VDFTDTQSPG VQEWLAQART TRTHQRQSSL QQQKEFEQEL
6260 6270 6280 6290 6300
AEQKSLLRSV ASRGEEILTQ HSTAEGSGGL GEKPDVLSQE LGIAEDQMRV
6310 6320 6330 6340 6350
KWESLHQEFS AKQKLLQNIL EQEQEQVLYS SPNRLLSGVL PFRGEAQTQD
6360 6370 6380 6390 6400
KTSVTSLLDG LSQAFGEASS QSGGTDRQSI HLEQKLYDGV SATSTWLNDV
6410 6420 6430 6440 6450
EERLFVATAP LPEETEACLF NQEALAKDIK EMSEEMDKNK NLFSQAFPED
6460 6470 6480 6490 6500
SDNRDVIEDT LGCLLGRLSL LDSVVDQRCH QMKERLQQIL RFQNDLKVLF
6510 6520 6530 6540 6550
TSLADSKYII LQKLANVFEQ PIVEQMQAIQ QAEEGLRDLE GGISELKRWA
6560 6570 6580 6590 6600
DKLQVEQSAV QELSKLQDMY DELLMTVSSR RSSLHQNLAL KSQYDKALQD
6610 6620 6630 6640 6650
LVDLLDTGQE KMTGDQKIIV CSKEEIQQLL GKHKEYFQGL ESHMILTEIL
6660 6670 6680 6690 6700
FRKIVGFAAV KETQFHTDCM AQASAVLKQA HKRGVELEYI LEMWSHLDEN
6710 6720 6730 6740 6750
RQELSRQLEV IENSIPSVGL VEESEDRLVE RTNLYQHLKS SLNEYQPKLY
6760 6770 6780 6790 6800
QALDDGKRLL MSVSCSELES QLNQLGEHWL SNTNKVSKEL HRLETILKHW
6810 6820 6830 6840 6850
TRYQSEAAAL NHWLQCAKDR LAFWTQQSVT VPQELEMVRD HLSAFLEFSK
6860 6870 6880 6890 6900
EVDAKSALKS SVTSTGNQLL RLKKVDTAAL RAELSRMDSQ WTDLLTGIPV
6910 6920 6930 6940 6950
VQEKLHQLQM DKLPSRHAIS EVMSWISLME SVILKDEEDI RNAIGYKAIH
6960 6970 6980 6990 7000
EYLQKYKGFK IDLNCKQLTA DFVNQSVLQI SSQDVESKRS DKTDFAEQLG
7010 7020 7030 7040 7050
AMNKSWQLLQ GRVGEKIQML EGLLESWSEY ENSVQSLKAW FANQERKLKE
7060 7070 7080 7090 7100
QHLLGDRNSV ENALKDCQEL EDLIKAKEKE VEKIEQNGLA LIQNKREEVS
7110 7120 7130 7140 7150
GSVMSTLQEL RQTWISLDRT VEQLKIQLTS ALGQWSNHKA ACDEINGHLM
7160 7170 7180 7190 7200
EARYSLSRFR LLTGSSEAVQ VQVDNLQNLH DELEKQEGGL QKFGSITNQL
7210 7220 7230 7240 7250
LKECHPPVAE TLSSTLQEVN MRWNNLLEEI AEQLHSSKAL LQLWQRYKDY
7260 7270 7280 7290 7300
SKQCASAIQR QEEQTSVLLK AATNKDIADD EVTKWIQDCN DLLKGLETVK
7310 7320 7330 7340 7350
DSLFILRELG EQLGQQVDVS AAAAIQCEQL CFSQRLGALE QALCKQQAVL
7360 7370 7380 7390 7400
QAGVVDYETF AKSLEALEVW MVEAEGILQG QDPTHSSDLS TIQERMEELK
7410 7420 7430 7440 7450
GQMLKFSSLA PDLDRLNELG YRLPLNDKEI KRMQNLNRHW SLTSSQTTER
7460 7470 7480 7490 7500
FSKLQSFLLQ HQTFLEKCET WMEFLVQTEH KLAVEISGNY QHLLEQQRAH
7510 7520 7530 7540 7550
ELFQAEMFSR QQILHSIIVD GQNLLEQGQV DDREEFSLKL TLLSNQWQGV
7560 7570 7580 7590 7600
IRRAQQRRGI IDSQIRQWQR YREMAEKLRK WLAEVSHLPL SGLGNIPVPL
7610 7620 7630 7640 7650
QQVRMLFDEV QFKEKVFLRQ QGSYILTVEA GKQLLLSADS GAEAALQAEL
7660 7670 7680 7690 7700
TDIQEKWKAA SMHLEEQKKK LAFLLKDWEK CERGIANSLE KLRMFKKRLS
7710 7720 7730 7740 7750
QPLPDHHEEL HAEQMRCKEL ENAVGRWTDD LTELMLVRDA LAVYLSAEDI
7760 7770 7780 7790 7800
SMLKERVELL QRQWEELCHQ VSLRRQQVSE RLNEWAVFSE KNKELCEWLT
7810 7820 7830 7840 7850
QMESKVSQNG DILIEEMIEK LKKDYQEEIA VAQENKIQLQ EMGERLAKAS
7860 7870 7880 7890 7900
HESKASEIQY KLSRVKDRWQ HLLDLMAARV KKLKETLVAV QQLDKNMGSL
7910 7920 7930 7940 7950
RTWLAHMESE LAKPIVYDSC NSEEIQRKLN EQQELQRDIE KHSTGVASVL
7960 7970 7980 7990 8000
NLCEVLLHDC DACATDAECD SIQQATRNLD RRWRNICAMS MERRLKIEET
8010 8020 8030 8040 8050
WRLWQKFLDD YSRFEDWLEV SERTAAFPSS SGVLYTVAKE ELKKFEAFQR
8060 8070 8080 8090 8100
QVHESLTQLE LINKQYRRLA RENRTDSACS LRQMVHGGNQ RWDDLQKRVT
8110 8120 8130 8140 8150
SILRRLKHFI SQREEFETAR DSILVWLTEM DLQLTNIEHF SECDVQAKIK
8160 8170 8180 8190 8200
QLKAFQQEIS LNHNKIEQII AQGEQLIEKS EPLDAAVIEE ELDELRRYCQ
8210 8220 8230 8240 8250
EVFGRVERYH KKLIRLPVRL PDDHDLSDRE LDLEDSTALS DLRWQDPSAD
8260 8270 8280 8290 8300
GMPSPQPSSN PSLSLPQPLR SERSGRDTPA SVDSIPLEWD HDYDLSRDLE
8310 8320 8330 8340 8350
SASRTLPSED EEGEEDKEFY LRGAVGLSGD PSSLESQMRQ LDKALDDSRF
8360 8370 8380 8390 8400
QIQQTANILR SKTPTGPDLD TSYKGYMKLL GECSGSIDSV RRLEHKLAEE
8410 8420 8430 8440 8450
ESFPGFVNLN STETQTAGVI DRWELLQAQA MSKELRMKQN LQKWQQFNSD
8460 8470 8480 8490 8500
LNNIWAWLGE TEEELDRLQH LALSTDIHTI ESHIKKLKEL QKAVDHRKAI
8510 8520 8530 8540 8550
ILSINLCSSE FTQADSKESH DLQDRLSQMN GRWDRVCSLL EDWRGLLQDA
8560 8570 8580 8590 8600
LMQCQEFHEM SHALLLMLEN IDRRKNEIVP IDSTLDPETL QDHHKQLMQI
8610 8620 8630 8640 8650
KQELLKSQLR VASLQDMSRQ LLVNAEGSDC LEAKEKVHVI GNRLKLLLKE
8660 8670 8680 8690 8700
VSHHIKDLEK LLDMSSSQQD LSSWSSADEL DTSGSVSPTS GRSTPNRQKS
8710 8720 8730 8740 8750
PRGKCSLSQP GPSVSSPKSR STRDGSDSSR SDPRPERVGR AFLFRILRAA
8760 8770 8780 8790
LPFQLLLLLL IGLTCLVPMS EKDYSCALSN NFARSFHPML RYTNGPPPL
Length:8,799
Mass (Da):1,009,926
Last modified:March 23, 2010 - v2
Checksum:i2A457DC081969CF0
GO
Isoform 2 (identifier: Q6ZWR6-2) [UniParc]FASTAAdd to basket

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

Show »
Length:972
Mass (Da):111,334
Checksum:i6ED3F1A381AACC9A
GO
Isoform 3 (identifier: Q6ZWR6-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:949
Mass (Da):108,779
Checksum:i40ABE338F614825E
GO
Isoform 4 (identifier: Q6ZWR6-4) [UniParc]FASTAAdd to basket

Also known as: Syne-1B

The sequence of this isoform differs from the canonical sequence as follows:
     8218-8219: Missing.

Note: Incomplete sequence.

Show »
Length:8,797
Mass (Da):1,009,670
Checksum:i08970A024A161721
GO
Isoform 5 (identifier: Q6ZWR6-5) [UniParc]FASTAAdd to basket

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.

Show »
Length:1,431
Mass (Da):165,244
Checksum:i0D4C7DA8ADAE612F
GO

Sequence cautioni

The sequence AAG24393.1 differs from that shown. Reason: Frameshift at positions 6810, 7656 and 7658. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1086 – 10861G → W in AAN03487 (PubMed:15093733).Curated
Sequence conflicti1150 – 11501I → T in AAN03487 (PubMed:15093733).Curated
Sequence conflicti7187 – 71871E → G in AAG24393 (PubMed:10878022).Curated
Sequence conflicti7876 – 78761M → I in AAG24393 (PubMed:10878022).Curated
Sequence conflicti8266 – 82661P → L in AAG24392 (PubMed:10878022).Curated
Sequence conflicti8266 – 82661P → L in AAG24393 (PubMed:10878022).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 78287828Missing in isoform 2 and isoform 3. 2 PublicationsVSP_038791Add
BLAST
Alternative sequencei103 – 1031K → KSMYRGSP in isoform 5. 1 PublicationVSP_038792
Alternative sequencei297 – 31317Missing in isoform 5. 1 PublicationVSP_038793Add
BLAST
Alternative sequencei1435 – 14417DIKTMEM → EYVLHHF in isoform 5. 1 PublicationVSP_038794
Alternative sequencei1442 – 87997358Missing in isoform 5. 1 PublicationVSP_038795Add
BLAST
Alternative sequencei7829 – 787850IAVAQ…DLMAA → MVVAEDLHGPRMAEDSSVDA DLPDCDCDVS in isoform 2 and isoform 3. 2 PublicationsVSP_038796Add
BLAST
Alternative sequencei8218 – 82192Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_038797
Alternative sequencei8328 – 83281S → SDVVIPENPEAYVKLTENAI RNTS in isoform 2. 1 PublicationVSP_038798

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS56679.1. [Q6ZWR6-3]
CCDS56680.1. [Q6ZWR6-5]
RefSeqiNP_001073154.1. NM_001079686.1.
UniGeneiMm.331626.

Genome annotation databases

EnsembliENSMUST00000041639; ENSMUSP00000039440; ENSMUSG00000096054. [Q6ZWR6-5]
ENSMUST00000095899; ENSMUSP00000093587; ENSMUSG00000096054. [Q6ZWR6-3]
GeneIDi64009.
KEGGimmu:64009.
UCSCiuc007egn.1. mouse. [Q6ZWR6-5]
uc007egt.2. mouse. [Q6ZWR6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS56679.1. [Q6ZWR6-3]
CCDS56680.1. [Q6ZWR6-5]
RefSeqiNP_001073154.1. NM_001079686.1.
UniGeneiMm.331626.

3D structure databases

ProteinModelPortaliQ6ZWR6.
SMRiQ6ZWR6. Positions 23-279, 997-1042.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211015. 1 interaction.
DIPiDIP-60966N.
STRINGi10090.ENSMUSP00000051825.

PTM databases

PhosphoSiteiQ6ZWR6.

Proteomic databases

MaxQBiQ6ZWR6.
PaxDbiQ6ZWR6.
PRIDEiQ6ZWR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041639; ENSMUSP00000039440; ENSMUSG00000096054. [Q6ZWR6-5]
ENSMUST00000095899; ENSMUSP00000093587; ENSMUSG00000096054. [Q6ZWR6-3]
GeneIDi64009.
KEGGimmu:64009.
UCSCiuc007egn.1. mouse. [Q6ZWR6-5]
uc007egt.2. mouse. [Q6ZWR6-2]

Organism-specific databases

CTDi23345.
MGIiMGI:1927152. Syne1.

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000120125.
HOVERGENiHBG106534.
InParanoidiQ6ZWR6.
OMAiCATESEC.
OrthoDBiEOG72JWF7.
PhylomeDBiQ6ZWR6.
TreeFamiTF317709.
TF337116.

Enzyme and pathway databases

ReactomeiREACT_287050. Meiotic synapsis.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

ChiTaRSiSyne1. mouse.
NextBioi319851.
PROiQ6ZWR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWR6.
ExpressionAtlasiQ6ZWR6. baseline and differential.
GenevestigatoriQ6ZWR6.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR030265. SYNE1.
[Graphical view]
PANTHERiPTHR11915:SF267. PTHR11915:SF267. 1 hit.
PfamiPF00307. CH. 2 hits.
PF10541. KASH. 1 hit.
PF00435. Spectrin. 10 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00150. SPEC. 42 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS51049. KASH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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).
    Strain: C57BL/6J.
    Tissue: Vagina.
  4. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "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.
  8. "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.
  9. Cited for: SELF-ASSOCIATION, INTERACTION WITH SYNE3, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSYNE1_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWR6
Secondary accession number(s): Q8K3T7, Q9ERT7, Q9ERT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: April 1, 2015
This is version 91 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

External Data

Dasty 3

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 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.