SMC6_HUMAN
ID SMC6_HUMAN Reviewed; 1091 AA.
AC Q96SB8; A8K8Q6; D6W518; Q05BV4; Q9H0X3; Q9H6M0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Structural maintenance of chromosomes protein 6;
DE Short=SMC protein 6;
DE Short=SMC-6;
DE Short=hSMC6;
GN Name=SMC6; Synonyms=SMC6L1;
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 [MRNA] (ISOFORM 1), INTERACTION WITH SMC5, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND VARIANTS GLY-464 AND
RP THR-691.
RX PubMed=11408570; DOI=10.1091/mbc.12.6.1583;
RA Taylor E.M., Moghraby J.S., Lees J.H., Smit B., Moens P.B., Lehmann A.R.;
RT "Characterization of a novel human SMC heterodimer homologous to the
RT Schizosaccharomyces pombe Rad18/Spr18 complex.";
RL Mol. Biol. Cell 12:1583-1594(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 467-1091, AND VARIANT THR-691.
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-717 (ISOFORM 2), AND VARIANTS GLY-464 AND THR-691.
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 [8]
RP INTERACTION WITH NSMCE1.
RX PubMed=14701739; DOI=10.1128/mcb.24.2.662-674.2004;
RA Harvey S.H., Sheedy D.M., Cuddihy A.R., O'Connell M.J.;
RT "Coordination of DNA damage responses via the Smc5/Smc6 complex.";
RL Mol. Cell. Biol. 24:662-674(2004).
RN [9]
RP INTERACTION WITH NSMCE2, AND SUMOYLATION.
RX PubMed=16055714; DOI=10.1128/mcb.25.16.7021-7032.2005;
RA Potts P.R., Yu H.;
RT "Human MMS21/NSE2 is a SUMO ligase required for DNA repair.";
RL Mol. Cell. Biol. 25:7021-7032(2005).
RN [10]
RP FUNCTION.
RX PubMed=16810316; DOI=10.1038/sj.emboj.7601218;
RA Potts P.R., Porteus M.H., Yu H.;
RT "Human SMC5/6 complex promotes sister chromatid homologous recombination by
RT recruiting the SMC1/3 cohesin complex to double-strand breaks.";
RL EMBO J. 25:3377-3388(2006).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17589526; DOI=10.1038/nsmb1259;
RA Potts P.R., Yu H.;
RT "The SMC5/6 complex maintains telomere length in ALT cancer cells through
RT SUMOylation of telomere-binding proteins.";
RL Nat. Struct. Mol. Biol. 14:581-590(2007).
RN [12]
RP INTERACTION WITH NSMCE1; NSMCE2; EID3; NSMCE4A AND NSMCE3, IDENTIFICATION
RP IN THE SMC5-SMC6 COMPLEX, SUMOYLATION, AND UBIQUITINATION.
RX PubMed=18086888; DOI=10.1128/mcb.00767-07;
RA Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.;
RT "Identification of the proteins, including MAGEG1, that make up the human
RT SMC5-6 protein complex.";
RL Mol. Cell. Biol. 28:1197-1206(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268 AND LYS-773, AND
RP IDENTIFICATION BY MASS 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 [17]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-292.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [18]
RP INTERACTION WITH RAD18; SLF1 AND SLF2, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25931565; DOI=10.1126/science.1253671;
RA Raeschle M., Smeenk G., Hansen R.K., Temu T., Oka Y., Hein M.Y.,
RA Nagaraj N., Long D.T., Walter J.C., Hofmann K., Storchova Z., Cox J.,
RA Bekker-Jensen S., Mailand N., Mann M.;
RT "DNA repair. Proteomics reveals dynamic assembly of repair complexes during
RT bypass of DNA cross-links.";
RL Science 348:1253671-1253671(2015).
RN [19]
RP FUNCTION, INDUCTION (MICROBIAL INFECTION), AND DEGRADATION (MICROBIAL
RP INFECTION).
RX PubMed=26983541; DOI=10.1038/nature17170;
RA Decorsiere A., Mueller H., van Breugel P.C., Abdul F., Gerossier L.,
RA Beran R.K., Livingston C.M., Niu C., Fletcher S.P., Hantz O., Strubin M.;
RT "Hepatitis B virus X protein identifies the Smc5/6 complex as a host
RT restriction factor.";
RL Nature 531:386-389(2016).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved
CC in DNA double-strand breaks by homologous recombination. The complex
CC may promote sister chromatid homologous recombination by recruiting the
CC SMC1-SMC3 cohesin complex to double-strand breaks. The complex is
CC required for telomere maintenance via recombination in ALT (alternative
CC lengthening of telomeres) cell lines and mediates sumoylation of
CC shelterin complex (telosome) components which is proposed to lead to
CC shelterin complex disassembly in ALT-associated PML bodies (APBs).
CC Required for recruitment of telomeres to PML nuclear bodies. SMC5-SMC6
CC complex may prevent transcription of episomal DNA, such as circular
CC viral DNA genome (PubMed:26983541). {ECO:0000269|PubMed:16810316,
CC ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:26983541}.
CC -!- SUBUNIT: Forms a heterodimer with SMC5 (PubMed:11408570). Component of
CC the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2,
CC NSMCE1, NSMCE4A or EID3 and NSMCE3 (PubMed:18086888). Interacts with
CC NSMCE1 (PubMed:14701739). Interacts with NSMCE2 (PubMed:16055714).
CC Interacts with SLF1 (PubMed:25931565). Interacts with SLF2
CC (PubMed:25931565). Interacts with RAD18 (PubMed:25931565).
CC {ECO:0000269|PubMed:11408570, ECO:0000269|PubMed:14701739,
CC ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:18086888,
CC ECO:0000269|PubMed:25931565}.
CC -!- SUBUNIT: (Microbial infection) SMC5-SMC6 complex interacts with
CC Hepatitis B X protein. {ECO:0000269|PubMed:26983541}.
CC -!- INTERACTION:
CC Q96SB8; Q8WV22: NSMCE1; NbExp=9; IntAct=EBI-605415, EBI-2557372;
CC Q96SB8; Q96MF7: NSMCE2; NbExp=3; IntAct=EBI-605415, EBI-2557388;
CC Q96SB8; Q96MG7: NSMCE3; NbExp=5; IntAct=EBI-605415, EBI-2557356;
CC Q96SB8; Q8IX21: SLF2; NbExp=5; IntAct=EBI-605415, EBI-2682240;
CC Q96SB8; Q8IY18: SMC5; NbExp=5; IntAct=EBI-605415, EBI-605405;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11408570,
CC ECO:0000269|PubMed:25931565}. Nucleus speckle
CC {ECO:0000269|PubMed:11408570}. Chromosome
CC {ECO:0000250|UniProtKB:Q924W5}. Nucleus, PML body
CC {ECO:0000269|PubMed:17589526}. Chromosome, telomere
CC {ECO:0000269|PubMed:17589526}. Note=Colocalizes with SMC5 on the X-Y
CC chromosome pair within the sex vesicle during late pachytene/diplotene
CC (By similarity). Localizes to PML nuclear bodies in ALT cell lines
CC (PubMed:17589526). Associates with chromatin (PubMed:25931565).
CC Accumulates with RAD18 and the SLF1-SLF2 complex at replication-coupled
CC DNA interstrand repair and DNA double-strand breaks (DSBs) sites on
CC chromatin in a ubiquitin-dependent manner (PubMed:25931565). Localizes
CC in interchromatin granule clusters (PubMed:11408570).
CC {ECO:0000250|UniProtKB:Q924W5, ECO:0000269|PubMed:11408570,
CC ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:25931565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96SB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96SB8-2; Sequence=VSP_022253;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11408570). Strongly
CC expressed in testis (PubMed:11408570). {ECO:0000269|PubMed:11408570}.
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC5, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11408570}.
CC -!- PTM: Sumoylated by NSMCE2/MMS21. {ECO:0000269|PubMed:16055714,
CC ECO:0000269|PubMed:18086888}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:18086888}.
CC -!- PTM: (Microbial infection) SMC5-SMC6 complex is degraded by the
CC activity of Hepatitis B X protein. {ECO:0000269|PubMed:26983541}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32675.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB15236.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ310551; CAC39248.1; -; mRNA.
DR EMBL; AL136544; CAB66479.1; -; mRNA.
DR EMBL; AK025769; BAB15236.1; ALT_FRAME; mRNA.
DR EMBL; AK292421; BAF85110.1; -; mRNA.
DR EMBL; AL832979; CAH56327.1; -; mRNA.
DR EMBL; AC097377; AAX88851.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00866.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00867.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00868.1; -; Genomic_DNA.
DR EMBL; BC032675; AAH32675.1; ALT_SEQ; mRNA.
DR EMBL; BC039828; AAH39828.1; -; mRNA.
DR CCDS; CCDS1690.1; -. [Q96SB8-1]
DR RefSeq; NP_001135758.1; NM_001142286.1. [Q96SB8-1]
DR RefSeq; NP_078900.1; NM_024624.5. [Q96SB8-1]
DR RefSeq; XP_016860404.1; XM_017004915.1. [Q96SB8-1]
DR AlphaFoldDB; Q96SB8; -.
DR SMR; Q96SB8; -.
DR BioGRID; 122802; 77.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR DIP; DIP-34562N; -.
DR IntAct; Q96SB8; 63.
DR MINT; Q96SB8; -.
DR STRING; 9606.ENSP00000404092; -.
DR CarbonylDB; Q96SB8; -.
DR iPTMnet; Q96SB8; -.
DR PhosphoSitePlus; Q96SB8; -.
DR BioMuta; SMC6; -.
DR DMDM; 122070455; -.
DR EPD; Q96SB8; -.
DR jPOST; Q96SB8; -.
DR MassIVE; Q96SB8; -.
DR MaxQB; Q96SB8; -.
DR PaxDb; Q96SB8; -.
DR PeptideAtlas; Q96SB8; -.
DR PRIDE; Q96SB8; -.
DR ProteomicsDB; 78100; -. [Q96SB8-1]
DR ProteomicsDB; 78101; -. [Q96SB8-2]
DR Antibodypedia; 27034; 171 antibodies from 27 providers.
DR DNASU; 79677; -.
DR Ensembl; ENST00000351948.8; ENSP00000323439.4; ENSG00000163029.16. [Q96SB8-1]
DR Ensembl; ENST00000402989.5; ENSP00000384539.1; ENSG00000163029.16. [Q96SB8-1]
DR Ensembl; ENST00000448223.7; ENSP00000404092.2; ENSG00000163029.16. [Q96SB8-1]
DR GeneID; 79677; -.
DR KEGG; hsa:79677; -.
DR MANE-Select; ENST00000448223.7; ENSP00000404092.2; NM_001142286.2; NP_001135758.1.
DR UCSC; uc002rcn.4; human. [Q96SB8-1]
DR CTD; 79677; -.
DR DisGeNET; 79677; -.
DR GeneCards; SMC6; -.
DR HGNC; HGNC:20466; SMC6.
DR HPA; ENSG00000163029; Low tissue specificity.
DR MIM; 609387; gene.
DR neXtProt; NX_Q96SB8; -.
DR OpenTargets; ENSG00000163029; -.
DR PharmGKB; PA134892702; -.
DR VEuPathDB; HostDB:ENSG00000163029; -.
DR eggNOG; KOG0250; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_009063_0_1_1; -.
DR InParanoid; Q96SB8; -.
DR OMA; MCHDHFY; -.
DR OrthoDB; 263113at2759; -.
DR PhylomeDB; Q96SB8; -.
DR TreeFam; TF314520; -.
DR PathwayCommons; Q96SB8; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR SignaLink; Q96SB8; -.
DR SIGNOR; Q96SB8; -.
DR BioGRID-ORCS; 79677; 594 hits in 1096 CRISPR screens.
DR GeneWiki; SMC6; -.
DR GenomeRNAi; 79677; -.
DR Pharos; Q96SB8; Tbio.
DR PRO; PR:Q96SB8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96SB8; protein.
DR Bgee; ENSG00000163029; Expressed in sperm and 180 other tissues.
DR ExpressionAtlas; Q96SB8; baseline and differential.
DR Genevisible; Q96SB8; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0035061; C:interchromatin granule; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0000803; C:sex chromosome; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; Coiled coil; DNA damage;
KW DNA recombination; DNA repair; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT CHAIN 1..1091
FT /note="Structural maintenance of chromosomes protein 6"
FT /id="PRO_0000270956"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..659
FT /note="Flexible hinge"
FT REGION 806..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..451
FT /evidence="ECO:0000255"
FT COILED 660..914
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 773
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 80
FT /note="S -> SWSAVVRSRLNATSASQVQAILLFQPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022253"
FT VARIANT 292
FT /note="A -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035875"
FT VARIANT 464
FT /note="R -> G (in dbSNP:rs35195207)"
FT /evidence="ECO:0000269|PubMed:11408570,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_052441"
FT VARIANT 691
FT /note="A -> T (in dbSNP:rs1065381)"
FT /evidence="ECO:0000269|PubMed:11408570,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_029826"
FT VARIANT 928
FT /note="K -> Q (in dbSNP:rs35257753)"
FT /id="VAR_052442"
FT VARIANT 1046
FT /note="I -> M (in dbSNP:rs10221907)"
FT /id="VAR_029827"
FT CONFLICT 483
FT /note="N -> Y (in Ref. 3; BAB15236)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="D -> N (in Ref. 3; BAB15236)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="V -> A (in Ref. 3; BAB15236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 126326 MW; 03C6F478E34285E6 CRC64;
MAKRKEENFS SPKNAKRPRQ EELEDFDKDG DEDECKGTTL TAAEVGIIES IHLKNFMCHS
MLGPFKFGSN VNFVVGNNGS GKSAVLTALI VGLGGRAVAT NRGSSLKGFV KDGQNSADIS
ITLRNRGDDA FKASVYGNSI LIQQHISIDG SRSYKLKSAT GSVVSTRKEE LIAILDHFNI
QVDNPVSVLT QEMSKQFLQS KNEGDKYKFF MKATQLEQMK EDYSYIMETK ERTKEQIHQG
EERLTELKRQ CVEKEERFQS IAGLSTMKTN LESLKHEMAW AVVNEIEKQL NAIRDNIKIG
EDRAARLDRK MEEQQVRLNE AEQKYKDIQD KLEKISEETN ARAPECMALK ADVVAKKRAY
NEAEVLYNRS LNEYKALKKD DEQLCKRIEE LKKSTDQSLE PERLERQKKI SWLKERVKAF
QNQENSVNQE IEQFQQAIEK DKEEHGKIKR EELDVKHALS YNQRQLKELK DSKTDRLKRF
GPNVPALLEA IDDAYRQGHF TYKPVGPLGA CIHLRDPELA LAIESCLKGL LQAYCCHNHA
DERVLQALMK RFYLPGTSRP PIIVSEFRNE IYDVRHRAAY HPDFPTVLTA LEIDNAVVAN
SLIDMRGIET VLLIKNNSVA RAVMQSQKPP KNCREAFTAD GDQVFAGRYY SSENTRPKFL
SRDVDSEISD LENEVENKTA QILNLQQHLS ALEKDIKHNE ELLKRCQLHY KELKMKIRKN
ISEIRELENI EEHQSVDIAT LEDEAQENKS KMKMVEEHME QQKENMEHLK SLKIEAENKY
DAIKFKINQL SELADPLKDE LNLADSEVDN QKRGKRHYEE KQKEHLDTLN KKKRELDMKE
KELEEKMSQA RQICPERIEV EKSASILDKE INRLRQKIQA EHASHGDREE IMRQYQEARE
TYLDLDSKVR TLKKFIKLLG EIMEHRFKTY QQFRRCLTLR CKLYFDNLLS QRAYCGKMNF
DHKNETLSIS VQPGEGNKAA FNDMRALSGG ERSFSTVCFI LSLWSIAESP FRCLDEFDVY
MDMVNRRIAM DLILKMADSQ RFRQFILLTP QSMSSLPSSK LIRILRMSDP ERGQTTLPFR
PVTQEEDDDQ R
