SUN1_HUMAN
ID SUN1_HUMAN Reviewed; 785 AA.
AC O94901; A5PL20; B3KMV7; B4DZF7; B7WNY4; B7WP53; E9PDU4; E9PF23; F8WD13;
AC Q96CZ7; Q9HA14; Q9UH98;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=SUN domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Protein unc-84 homolog A;
DE AltName: Full=Sad1/unc-84 protein-like 1;
GN Name=SUN1 {ECO:0000312|HGNC:HGNC:18587}; Synonyms=KIAA0810, UNC84A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-118.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5; 6 AND 7), AND
RP VARIANT TYR-118.
RC TISSUE=Mammary gland, Substantia nigra, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Cerebellum;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-118.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 362-785.
RX PubMed=10375507; DOI=10.1242/dev.126.14.3171;
RA Malone C.J., Fixsen W.D., Horvitz H.R., Han M.;
RT "UNC-84 localizes to the nuclear envelope and is required for nuclear
RT migration and anchoring during C. elegans development.";
RL Development 126:3171-3181(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12958361; DOI=10.1126/science.1088176;
RA Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.;
RT "Nuclear membrane proteins with potential disease links found by
RT subtractive proteomics.";
RL Science 301:1380-1382(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH MPS3.
RX PubMed=18039933; DOI=10.1083/jcb.200706040;
RA Bupp J.M., Martin A.E., Stensrud E.S., Jaspersen S.L.;
RT "Telomere anchoring at the nuclear periphery requires the budding yeast
RT Sad1-UNC-84 domain protein Mps3.";
RL J. Cell Biol. 179:845-854(2007).
RN [10]
RP SUBCELLULAR LOCATION, SUBUNIT, AND ASSOCIATION WITH THE CENTROSOME.
RX PubMed=17132086; DOI=10.1089/dna.2006.25.554;
RA Wang Q., Du X., Cai Z., Greene M.I.;
RT "Characterization of the structures involved in localization of the SUN
RT proteins to the nuclear envelope and the centrosome.";
RL DNA Cell Biol. 25:554-562(2006).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16445915; DOI=10.1016/j.febslet.2006.01.039;
RA Hasan S., Guttinger S., Muhlhausser P., Anderegg F., Burgler S., Kutay U.;
RT "Nuclear envelope localization of human UNC84A does not require nuclear
RT lamins.";
RL FEBS Lett. 580:1263-1268(2006).
RN [12]
RP INTERACTION WITH NAT10.
RX PubMed=17631499; DOI=10.1074/jbc.m703098200;
RA Chi Y.-H., Haller K., Peloponese J.-M. Jr., Jeang K.-T.;
RT "Histone acetyltransferase hALP and nuclear membrane protein hsSUN1
RT function in de-condensation of mitotic chromosomes.";
RL J. Biol. Chem. 282:27447-27458(2007).
RN [13]
RP SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, AND INTERACTION WITH SUN2.
RX PubMed=18845190; DOI=10.1016/j.bbamcr.2008.09.001;
RA Lu W., Gotzmann J., Sironi L., Jaeger V.M., Schneider M., Luke Y.,
RA Uhlen M., Szigyarto C.A., Brachner A., Ellenberg J., Foisner R.,
RA Noegel A.A., Karakesisoglou I.;
RT "Sun1 forms immobile macromolecular assemblies at the nuclear envelope.";
RL Biochim. Biophys. Acta 1783:2415-2426(2008).
RN [14]
RP INTERACTION WITH SYNE1; SYNE2 AND SYNE3, AND FUNCTION OF THE LINC
RP COMPLEXES.
RX PubMed=18396275; DOI=10.1016/j.yexcr.2008.02.022;
RA Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.;
RT "Structural requirements for the assembly of LINC complexes and their
RT function in cellular mechanical stiffness.";
RL Exp. Cell Res. 314:1892-1905(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP SUBCELLULAR LOCATION, INTERACTION WITH EMD; LMNA AND SYNE2, DOMAIN, AND
RP ASSOCIATION WITH THE NUCLEOSKELETON.
RX PubMed=19933576; DOI=10.1074/jbc.m109.071910;
RA Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M.,
RA Shackleton S.;
RT "Mammalian SUN protein interaction networks at the inner nuclear membrane
RT and their role in laminopathy disease processes.";
RL J. Biol. Chem. 285:3487-3498(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-138,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 (ISOFORM 8), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-138 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-195, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP FUNCTION.
RX PubMed=27956467; DOI=10.1083/jcb.201604112;
RA Lawrence K.S., Tapley E.C., Cruz V.E., Li Q., Aung K., Hart K.C.,
RA Schwartz T.U., Starr D.A., Engebrecht J.;
RT "LINC complexes promote homologous recombination in part through inhibition
RT of nonhomologous end joining.";
RL J. Cell Biol. 215:801-821(2016).
RN [22]
RP INTERACTION WITH TMEM258.
RX PubMed=28716842; DOI=10.1083/jcb.201606043;
RA Ding Z.Y., Wang Y.H., Huang Y.C., Lee M.C., Tseng M.J., Chi Y.H.,
RA Huang M.L.;
RT "Outer nuclear membrane protein Kuduk modulates the LINC complex and
RT nuclear envelope architecture.";
RL J. Cell Biol. 216:2827-2841(2017).
RN [23]
RP VARIANTS VAL-203 AND VAL-587.
RX PubMed=24375709; DOI=10.1002/humu.22504;
RA Li P., Meinke P., Huong Le T.T., Wehnert M., Noegel A.A.;
RT "Contribution of SUN1 mutations to the pathomechanism in muscular
RT dystrophies.";
RL Hum. Mutat. 35:452-461(2014).
CC -!- FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and
CC Cytoskeleton) complex involved in the connection between the nuclear
CC lamina and the cytoskeleton (PubMed:18039933, PubMed:18396275). The
CC nucleocytoplasmic interactions established by the LINC complex play an
CC important role in the transmission of mechanical forces across the
CC nuclear envelope and in nuclear movement and positioning (By
CC similarity). Required for interkinetic nuclear migration (INM) and
CC essential for nucleokinesis and centrosome-nucleus coupling during
CC radial neuronal migration in the cerebral cortex and during glial
CC migration (By similarity). Involved in telomere attachment to nuclear
CC envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC
CC complex in which SUN1 and SUN2 seem to act at least partial redundantly
CC (By similarity). Required for gametogenesis and involved in selective
CC gene expression of coding and non-coding RNAs needed for gametogenesis
CC (By similarity). Helps to define the distribution of nuclear pore
CC complexes (NPCs) (By similarity). Required for efficient localization
CC of SYNE4 in the nuclear envelope (By similarity). May be involved in
CC nuclear remodeling during sperm head formation in spermatogenesis (By
CC similarity). May play a role in DNA repair by suppressing non-
CC homologous end joining repair to facilitate the repair of DNA cross-
CC links (PubMed:24375709). {ECO:0000250|UniProtKB:Q9D666,
CC ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18396275,
CC ECO:0000269|PubMed:24375709}.
CC -!- SUBUNIT: Core component of the LINC complex which is composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC containing proteins seem to bind each other promiscuously; however,
CC differentially expression of LINC complex constituents is giving rise
CC to specific assemblies. At least SUN1/2-containing core LINC complexes
CC are proposed to be hexameric composed of three protomers of each KASH
CC and SUN domain-containing protein. Interacts with KASH5 (via the last
CC 22 amino acids); this interaction mediates KASH5 telomere localization
CC by forming a SUN1:KASH5 LINC complex. May interact with SYNE3.
CC Interacts with SYNE2 and SYNE1; probably forming respective LINC
CC complexes. Interacts with A-type lamin with a strong preference for
CC unprocessed A-type lamin compared with the mature protein. Interaction
CC with lamins B1 and C is hardly detectable. Interacts with NAT10.
CC Interacts with EMD and TSNAX. Associates with the nuclear pore complex
CC (NPC). Interacts with CCDC79/TERB1; promoting the accumulation of the
CC LINC complex complexes at the telomere-nuclear envelope attachment
CC sites. Interacts (via KASH domain) with TMEM258 (PubMed:28716842).
CC {ECO:0000250|UniProtKB:Q9D666, ECO:0000269|PubMed:17132086,
CC ECO:0000269|PubMed:17631499, ECO:0000269|PubMed:18039933,
CC ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:18845190,
CC ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:28716842}.
CC -!- INTERACTION:
CC O94901; Q8NF91-1: SYNE1; NbExp=2; IntAct=EBI-2796904, EBI-6170938;
CC O94901; Q8WXH0-1: SYNE2; NbExp=2; IntAct=EBI-2796904, EBI-6170976;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915,
CC ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190,
CC ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915,
CC ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190,
CC ECO:0000269|PubMed:19933576}. Note=At oocyte MI stage localized around
CC the spindle, at MII stage localized to the spindle poles.
CC {ECO:0000250|UniProtKB:Q9D666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=O94901-8; Sequence=Displayed;
CC Name=2;
CC IsoId=O94901-2; Sequence=VSP_061224, VSP_061225;
CC Name=3;
CC IsoId=O94901-3; Sequence=VSP_061223, VSP_061226;
CC Name=4;
CC IsoId=O94901-4; Sequence=VSP_061218, VSP_061219;
CC Name=5;
CC IsoId=O94901-5; Sequence=VSP_061216, VSP_061221;
CC Name=6;
CC IsoId=O94901-6; Sequence=VSP_061220;
CC Name=7;
CC IsoId=O94901-7; Sequence=VSP_061217, VSP_061224, VSP_061225;
CC Name=8;
CC IsoId=O94901-9; Sequence=VSP_061222;
CC -!- DOMAIN: The coiled coil domains differentially mediate trimerization
CC required for binding to nesprins and are proposed to dynamically
CC regulate the oligomeric state by locking the SUN domain in an inactive
CC confirmation. The coiled coil domains are proposed to be involved in
CC load-bearing and force transmission from the cytoskeleton.
CC {ECO:0000250|UniProtKB:Q8BJS4, ECO:0000250|UniProtKB:Q9UH99}.
CC -!- DOMAIN: The SUN domain may play a role in nuclear anchoring and/or
CC migration. {ECO:0000269|PubMed:19933576}.
CC -!- PTM: The disulfide bond with KASH domain-containing nesprins is
CC required for stability of the respective LINC complexes under tensile
CC forces. {ECO:0000250|UniProtKB:Q9UH99}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34530.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA34530.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AB018353; BAA34530.1; ALT_SEQ; mRNA.
DR EMBL; AK022469; BAB14046.1; -; mRNA.
DR EMBL; AK022816; BAG51119.1; -; mRNA.
DR EMBL; AK302896; BAG64069.1; -; mRNA.
DR EMBL; AK309120; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX538211; CAD98070.1; -; mRNA.
DR EMBL; AC073957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013613; AAH13613.1; -; mRNA.
DR EMBL; BC142707; AAI42708.1; -; mRNA.
DR EMBL; AF202724; AAF15888.1; -; mRNA.
DR CCDS; CCDS43533.1; -. [O94901-5]
DR CCDS; CCDS47525.1; -. [O94901-8]
DR CCDS; CCDS55078.1; -. [O94901-7]
DR CCDS; CCDS55079.1; -. [O94901-2]
DR RefSeq; NP_001124437.1; NM_001130965.2. [O94901-8]
DR RefSeq; NP_001165415.1; NM_001171944.1. [O94901-6]
DR RefSeq; NP_001165416.1; NM_001171945.1. [O94901-7]
DR RefSeq; NP_001165417.1; NM_001171946.1. [O94901-2]
DR RefSeq; NP_079430.3; NM_025154.5. [O94901-5]
DR PDB; 6R15; X-ray; 1.82 A; A=589-785.
DR PDB; 6R16; X-ray; 2.75 A; A/B/C/D/E/F=589-785.
DR PDB; 6R2I; X-ray; 1.54 A; A=589-785.
DR PDB; 7E34; X-ray; 3.19 A; C=126-171.
DR PDBsum; 6R15; -.
DR PDBsum; 6R16; -.
DR PDBsum; 6R2I; -.
DR PDBsum; 7E34; -.
DR AlphaFoldDB; O94901; -.
DR SASBDB; O94901; -.
DR SMR; O94901; -.
DR BioGRID; 116935; 189.
DR IntAct; O94901; 27.
DR MINT; O94901; -.
DR STRING; 9606.ENSP00000384015; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyConnect; 1776; 4 N-Linked glycans (2 sites).
DR GlyGen; O94901; 4 sites, 4 N-linked glycans (2 sites), 1 O-linked glycan (2 sites).
DR iPTMnet; O94901; -.
DR MetOSite; O94901; -.
DR PhosphoSitePlus; O94901; -.
DR SwissPalm; O94901; -.
DR BioMuta; SUN1; -.
DR CPTAC; CPTAC-1297; -.
DR CPTAC; CPTAC-1509; -.
DR EPD; O94901; -.
DR jPOST; O94901; -.
DR MassIVE; O94901; -.
DR MaxQB; O94901; -.
DR PaxDb; O94901; -.
DR PeptideAtlas; O94901; -.
DR PRIDE; O94901; -.
DR ProteomicsDB; 19748; -.
DR ProteomicsDB; 20009; -.
DR ProteomicsDB; 31341; -.
DR ProteomicsDB; 50533; -. [O94901-2]
DR ProteomicsDB; 50534; -. [O94901-3]
DR ProteomicsDB; 50535; -. [O94901-4]
DR ProteomicsDB; 50536; -. [O94901-5]
DR Antibodypedia; 1893; 106 antibodies from 25 providers.
DR DNASU; 23353; -.
DR Ensembl; ENST00000389574.7; ENSP00000374225.3; ENSG00000164828.18. [O94901-5]
DR Ensembl; ENST00000401592.6; ENSP00000384015.1; ENSG00000164828.18. [O94901-8]
DR Ensembl; ENST00000403868.5; ENSP00000383947.1; ENSG00000164828.18. [O94901-2]
DR Ensembl; ENST00000425407.6; ENSP00000392309.2; ENSG00000164828.18. [O94901-5]
DR Ensembl; ENST00000457378.6; ENSP00000395952.2; ENSG00000164828.18. [O94901-7]
DR GeneID; 23353; -.
DR KEGG; hsa:23353; -.
DR MANE-Select; ENST00000401592.6; ENSP00000384015.1; NM_001130965.3; NP_001124437.1.
DR UCSC; uc003sjf.4; human. [O94901-8]
DR CTD; 23353; -.
DR DisGeNET; 23353; -.
DR GeneCards; SUN1; -.
DR HGNC; HGNC:18587; SUN1.
DR HPA; ENSG00000164828; Low tissue specificity.
DR MIM; 607723; gene.
DR neXtProt; NX_O94901; -.
DR OpenTargets; ENSG00000164828; -.
DR PharmGKB; PA165618311; -.
DR VEuPathDB; HostDB:ENSG00000164828; -.
DR eggNOG; KOG2687; Eukaryota.
DR GeneTree; ENSGT00940000155830; -.
DR HOGENOM; CLU_012938_0_0_1; -.
DR InParanoid; O94901; -.
DR OrthoDB; 1000585at2759; -.
DR PhylomeDB; O94901; -.
DR TreeFam; TF323915; -.
DR PathwayCommons; O94901; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR SignaLink; O94901; -.
DR SIGNOR; O94901; -.
DR BioGRID-ORCS; 23353; 13 hits in 1085 CRISPR screens.
DR ChiTaRS; SUN1; human.
DR GeneWiki; UNC84A; -.
DR GenomeRNAi; 23353; -.
DR Pharos; O94901; Tbio.
DR PRO; PR:O94901; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O94901; protein.
DR Bgee; ENSG00000164828; Expressed in secondary oocyte and 203 other tissues.
DR ExpressionAtlas; O94901; baseline and differential.
DR Genevisible; O94901; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0140444; F:cytoskeleton-nuclear membrane anchor activity; IDA:GO_Central.
DR GO; GO:0005521; F:lamin binding; IEA:Ensembl.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IEA:Ensembl.
DR GO; GO:0006998; P:nuclear envelope organization; IGI:MGI.
DR GO; GO:0090292; P:nuclear matrix anchoring at nuclear membrane; IDA:UniProtKB.
DR GO; GO:0021817; P:nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR018539; SUN1.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR032680; SUN1_N.
DR InterPro; IPR040994; Sun_CC2.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 2.
DR PANTHER; PTHR12911:SF23; PTHR12911:SF23; 2.
DR Pfam; PF18580; HTH_SUN2; 1.
DR Pfam; PF09387; MRP; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Differentiation;
KW Disulfide bond; Isopeptide bond; Meiosis; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal-anchor; Spermatogenesis;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..785
FT /note="SUN domain-containing protein 1"
FT /id="PRO_0000218911"
FT TOPO_DOM 1..288
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:18845190"
FT TRANSMEM 289..308
FT /note="Helical"
FT TOPO_DOM 309..785
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:18845190"
FT DOMAIN 622..784
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 1..138
FT /note="LMNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9D666"
FT REGION 574..785
FT /note="Sufficient for interaction with SYNE1 and SYNE2"
FT /evidence="ECO:0000250|UniProtKB:Q9UH99"
FT COILED 428..495
FT /evidence="ECO:0000255"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 630
FT /note="Interchain (with KASH domain-containing nesprins)"
FT /evidence="ECO:0000250|UniProtKB:Q9UH99"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_061216"
FT VAR_SEQ 1
FT /note="M -> MGRISPGSPGLPRTVWFEVVNM (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_061217"
FT VAR_SEQ 109
FT /note="R -> V (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_061218"
FT VAR_SEQ 110..785
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_061219"
FT VAR_SEQ 152..254
FT /note="LDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPA
FT APGPVSRVYSRDRNQKCYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGK -> K
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_061220"
FT VAR_SEQ 220..253
FT /note="CYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPG -> W (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_061221"
FT VAR_SEQ 220
FT /note="C -> CGASFYVNRILWLARYTASSFSSFLVQLFQVVLMKLSYESENYKLKT
FT HESKDCESESYKSKSHESKAHASYYGRMNVREVLREDGHLSVNGEALCDDCKGKRHLDA
FT HTAAHSQSPRLPGRAGTLWHIWACAG (in isoform 8)"
FT /id="VSP_061222"
FT VAR_SEQ 221..341
FT /note="YFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVT
FT LISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQR
FT VDDPQDVFKP -> GASFYVNRILWLARYTASSFSSFLVQLFQVVLMKLSYESENYKLK
FT THESKDCESESYKSKSHESKAHASYYGRMNVREVLREDGHLSVNGEALCKYGFVFLWAS
FT VVELVPHAVMLGTSSRE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_061223"
FT VAR_SEQ 221..257
FT /note="YFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAAS -> KSQSFKTQKKV
FT CFPNLIFPFCKSQCLHYLSWRLKIIP (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_061224"
FT VAR_SEQ 258..785
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_061225"
FT VAR_SEQ 342..785
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_061226"
FT VARIANT 118
FT /note="H -> Y (in dbSNP:rs6461378)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9872452"
FT /id="VAR_059828"
FT VARIANT 203
FT /note="A -> V (in dbSNP:rs144929525)"
FT /evidence="ECO:0000269|PubMed:24375709"
FT /id="VAR_071065"
FT VARIANT 587
FT /note="A -> V (in dbSNP:rs114701323)"
FT /evidence="ECO:0000269|PubMed:24375709"
FT /id="VAR_071066"
FT CONFLICT 15
FT /note="V -> A (in Ref. 3; CAD98070)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="S -> G (in Ref. 3; CAD98070)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="A -> V (in Ref. 1; BAA34530)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="A -> P (in Ref. 5; AAH13613)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="Missing (in Ref. 2; BAG64069)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="P -> L (in Ref. 2; BAG51119)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="E -> K (in Ref. 2; BAG64069)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="R -> Q (in Ref. 2; BAG51119)"
FT /evidence="ECO:0000305"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7E34"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7E34"
FT HELIX 592..607
FT /evidence="ECO:0007829|PDB:6R2I"
FT TURN 608..611
FT /evidence="ECO:0007829|PDB:6R2I"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:6R2I"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:6R2I"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 676..694
FT /evidence="ECO:0007829|PDB:6R2I"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 712..720
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 727..733
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 740..745
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 755..762
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:6R2I"
FT STRAND 776..783
FT /evidence="ECO:0007829|PDB:6R2I"
FT REGION O94901-9:209..309
FT /note="SYNE2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9D666"
FT REGION O94901-9:223..309
FT /note="EMD-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9D666"
FT MOD_RES O94901-9:333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 785 AA; 87110 MW; 1099A50C9540ECF5 CRC64;
MDFSRLHMYS PPQCVPENTG YTYALSSSYS SDALDFETEH KLDPVFDSPR MSRRSLRLAT
TACTLGDGEA VGADSGTSSA VSLKNRAART TKQRRSTNKS AFSINHVSRQ VTSSGVSHGG
TVSLQDAVTR RPPVLDESWI REQTTVDHFW GLDDDGDLKG GNKAAIQGNG DVGAAAATAH
NGFSCSNCSM LSERKDVLTA HPAAPGPVSR VYSRDRNQKC YFLLQILRRI GAVGQAVSRT
AWSALWLAVV APGKAASGVF WWLGIGWYQF VTLISWLNVF LLTRCLRNIC KFLVLLIPLF
LLLAGLSLRG QGNFFSFLPV LNWASMHRTQ RVDDPQDVFK PTTSRLKQPL QGDSEAFPWH
WMSGVEQQVA SLSGQCHHHG ENLRELTTLL QKLQARVDQM EGGAAGPSAS VRDAVGQPPR
ETDFMAFHQE HEVRMSHLED ILGKLREKSE AIQKELEQTK QKTISAVGEQ LLPTVEHLQL
ELDQLKSELS SWRHVKTGCE TVDAVQERVD VQVREMVKLL FSEDQQGGSL EQLLQRFSSQ
FVSKGDLQTM LRDLQLQILR NVTHHVSVTK QLPTSEAVVS AVSEAGASGI TEAQARAIVN
SALKLYSQDK TGMVDFALES GGGSILSTRC SETYETKTAL MSLFGIPLWY FSQSPRVVIQ
PDIYPGNCWA FKGSQGYLVV RLSMMIHPAA FTLEHIPKTL SPTGNISSAP KDFAVYGLEN
EYQEEGQLLG QFTYDQDGES LQMFQALKRP DDTAFQIVEL RIFSNWGHPE YTCLYRFRVH
GEPVK
