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 27-MAR-2024, entry version 200. 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; Q8N6L0: KASH5; NbExp=5; IntAct=EBI-2796904, EBI-749265; CC O94901; O94901: SUN1; NbExp=3; IntAct=EBI-2796904, EBI-2796904; CC O94901; Q8NF91: SYNE1; NbExp=6; IntAct=EBI-2796904, EBI-928867; 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 O94901; Q8N205: SYNE4; NbExp=7; IntAct=EBI-2796904, EBI-7131783; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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 PDB; 7Z8Y; X-ray; 2.29 A; A/B/C=589-785. DR PDB; 8AU0; X-ray; 2.07 A; A/B/C=362-401. DR PDB; 8B46; X-ray; 1.67 A; A/B/C=589-785. DR PDB; 8B5X; X-ray; 1.98 A; A/B/C=589-785. DR PDBsum; 6R15; -. DR PDBsum; 6R16; -. DR PDBsum; 6R2I; -. DR PDBsum; 7E34; -. DR PDBsum; 7Z8Y; -. DR PDBsum; 8AU0; -. DR PDBsum; 8B46; -. DR PDBsum; 8B5X; -. DR AlphaFoldDB; O94901; -. DR SASBDB; O94901; -. DR SMR; O94901; -. DR BioGRID; 116935; 200. DR ComplexPortal; CPX-2537; LINC complex, SUN1-KASH5 variant. DR ComplexPortal; CPX-7668; LINC complex, SUN1-SYNE1 variant. DR ComplexPortal; CPX-7670; LINC complex, SUN1-SYNE2 variant. DR ComplexPortal; CPX-7673; LINC complex, SUN1-SYNE3 variant. DR ComplexPortal; CPX-7675; LINC complex, SUN1-SYNE4 variant. DR IntAct; O94901; 30. 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 GlyCosmos; O94901; 4 sites, 5 glycans. DR GlyGen; O94901; 3 sites, 1 O-linked glycan (1 site). 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; 9606-ENSP00000384015; -. DR PeptideAtlas; 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 Pumba; O94901; -. DR Antibodypedia; 1893; 125 antibodies from 26 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 AGR; HGNC:18587; -. 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; 39017at2759; -. 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 1161 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 205 other cell types or tissues. DR ExpressionAtlas; O94901; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; 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:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell. 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:0042802; F:identical protein binding; IPI:IntAct. 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: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:0001503; P:ossification; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR CDD; cd21439; SUN1_cc1; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR InterPro; IPR045119; SUN1-5. DR InterPro; IPR032680; SUN1_N. DR InterPro; IPR040994; Sun_CC2. DR InterPro; IPR012919; SUN_dom. DR PANTHER; PTHR12911; SAD1/UNC-84-LIKE PROTEIN-RELATED; 1. DR PANTHER; PTHR12911:SF23; SUN DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF18580; HTH_SUN2; 1. DR Pfam; PF09387; MRP; 1. DR Pfam; PF07738; Sad1_UNC; 1. DR PROSITE; PS51469; SUN; 1. DR Genevisible; O94901; HS. 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 //