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Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome-associated polypeptide) (hCAP)

 SMC3_HUMAN              Reviewed;        1217 AA.
Q9UQE7; A8K156; O60464; Q5T482;
25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
25-OCT-2017, entry version 176.
RecName: Full=Structural maintenance of chromosomes protein 3;
Short=SMC protein 3;
Short=SMC-3;
AltName: Full=Basement membrane-associated chondroitin proteoglycan;
Short=Bamacan;
AltName: Full=Chondroitin sulfate proteoglycan 6;
AltName: Full=Chromosome-associated polypeptide;
Short=hCAP;
Name=SMC3; Synonyms=BAM, BMH, CSPG6, SMC3L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH KIFAP3, AND
IDENTIFICATION IN A COMPLEX WITH KIFAP3 AND KIF3B.
TISSUE=B-cell;
PubMed=9506951; DOI=10.1074/jbc.273.12.6591;
Shimizu K., Shirataki H., Honda T., Minami S., Takai Y.;
"Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated
protein, with a human chromosome-associated polypeptide.";
J. Biol. Chem. 273:6591-6594(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1217.
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 827-1217.
TISSUE=Neuron;
Stanchi F., Bertocco E., Simionati B., Zimbello R., Lanfranchi G.,
Valle G.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[7]
CHARACTERIZATION, FUNCTION, AND IDENTIFICATION IN A COHESIN COMPLEX
WITH SMC1A; STAG1 OR STAG2.
PubMed=11076961; DOI=10.1083/jcb.151.4.749;
Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.;
"Characterization of vertebrate cohesin complexes and their regulation
in prophase.";
J. Cell Biol. 151:749-762(2000).
[8]
INTERACTION WITH NUMA1.
PubMed=11590136; DOI=10.1074/jbc.M103364200;
Gregson H.C., Schmiesing J.A., Kim J.-S., Kobayashi T., Zhou S.,
Yokomori K.;
"A potential role for human cohesin in mitotic spindle aster
assembly.";
J. Biol. Chem. 276:47575-47582(2001).
[9]
INTERACTION WITH KIAA1328.
PubMed=15656913; DOI=10.1186/1471-2121-6-3;
Patel C.A., Ghiselli G.;
"Hinderin, a five-domains protein including coiled-coil motifs that
binds to SMC3.";
BMC Cell Biol. 6:3-3(2005).
[10]
IDENTIFICATION IN A COMPLEX WITH CDCA5; SMC1A; RAD21; PDS5A AND PDS5B.
PubMed=15837422; DOI=10.1016/j.molcel.2005.03.017;
Rankin S., Ayad N.G., Kirschner M.W.;
"Sororin, a substrate of the anaphase-promoting complex, is required
for sister chromatid cohesion in vertebrates.";
Mol. Cell 18:185-200(2005).
[11]
ERRATUM.
Rankin S., Ayad N.G., Kirschner M.W.;
Mol. Cell 18:609-609(2005).
[12]
INTERACTION WITH DDX11.
PubMed=17105772; DOI=10.1242/jcs.03262;
Parish J.L., Rosa J., Wang X., Lahti J.M., Doxsey S.J., Androphy E.J.;
"The DNA helicase ChlR1 is required for sister chromatid cohesion in
mammalian cells.";
J. Cell Sci. 119:4857-4865(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787; SER-1065 AND
SER-1067, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[15]
ACETYLATION AT LYS-105 AND LYS-106, AND MUTAGENESIS OF LYS-105 AND
LYS-106.
PubMed=18614053; DOI=10.1016/j.molcel.2008.06.006;
Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X.,
Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.;
"Acetylation of Smc3 by Eco1 is required for S phase sister chromatid
cohesion in both human and yeast.";
Mol. Cell 31:143-151(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1065 AND SER-1067, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
FUNCTION, ACETYLATION AT LYS-105 AND LYS-106, INTERACTION WITH PDS5A
AND WAPL, AND MUTAGENESIS OF LYS-105 AND LYS-106.
PubMed=19907496; DOI=10.1038/nature08550;
Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.;
"Cohesin acetylation speeds the replication fork.";
Nature 462:231-234(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105; LYS-106; LYS-140 AND
LYS-1190, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-783; SER-787; SER-1067
AND SER-1083, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067 AND SER-1083, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
ACETYLATION, AND DEACETYLATION BY HDAC8.
PubMed=22885700; DOI=10.1038/nature11316;
Deardorff M.A., Bando M., Nakato R., Watrin E., Itoh T., Minamino M.,
Saitoh K., Komata M., Katou Y., Clark D., Cole K.E., De Baere E.,
Decroos C., Di Donato N., Ernst S., Francey L.J., Gyftodimou Y.,
Hirashima K., Hullings M., Ishikawa Y., Jaulin C., Kaur M., Kiyono T.,
Lombardi P.M., Magnaghi-Jaulin L., Mortier G.R., Nozaki N.,
Petersen M.B., Seimiya H., Siu V.M., Suzuki Y., Takagaki K.,
Wilde J.J., Willems P.J., Prigent C., Gillessen-Kaesbach G.,
Christianson D.W., Kaiser F.J., Jackson L.G., Hirota T., Krantz I.D.,
Shirahige K.;
"HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin
acetylation cycle.";
Nature 489:313-317(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886 AND SER-1067, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1065 AND SER-1067, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
VARIANT CDLS3 GLU-491 DEL.
PubMed=17273969; DOI=10.1086/511888;
Deardorff M.A., Kaur M., Yaeger D., Rampuria A., Korolev S., Pie J.,
Gil-Rodriguez C., Arnedo M., Loeys B., Kline A.D., Wilson M.,
Lillquist K., Siu V., Ramos F.J., Musio A., Jackson L.S., Dorsett D.,
Krantz I.D.;
"Mutations in cohesin complex members SMC3 and SMC1A cause a mild
variant of Cornelia de Lange syndrome with predominant mental
retardation.";
Am. J. Hum. Genet. 80:485-494(2007).
[28]
CHARACTERIZATION OF VARIANT CDLS3 GLU-491 DEL, AND GENOMIC INSTABILITY
OF CDLS CELL LINES TO IONIZING RADIATION.
PubMed=18996922; DOI=10.1093/hmg/ddn369;
Revenkova E., Focarelli M.L., Susani L., Paulis M., Bassi M.T.,
Mannini L., Frattini A., Delia D., Krantz I., Vezzoni P.,
Jessberger R., Musio A.;
"Cornelia de Lange syndrome mutations in SMC1A or SMC3 affect binding
to DNA.";
Hum. Mol. Genet. 18:418-427(2009).
-!- FUNCTION: Central component of cohesin, a complex required for
chromosome cohesion during the cell cycle. The cohesin complex may
form a large proteinaceous ring within which sister chromatids can
be trapped. At anaphase, the complex is cleaved and dissociates
from chromatin, allowing sister chromatids to segregate. Cohesion
is coupled to DNA replication and is involved in DNA repair. The
cohesin complex plays also an important role in spindle pole
assembly during mitosis and in chromosomes movement.
{ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:19907496}.
-!- SUBUNIT: Interacts with MXI1, MXD3 and MXD4. Interacts with SYCP2.
Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and
PDS5B/APRIN (By similarity). Forms a heterodimer with SMC1A or
SMC1B in cohesin complexes. Cohesin complexes are composed of the
SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their
hinge domain, RAD21 which link them, and one STAG protein (STAG1,
STAG2 or STAG3), which interacts with RAD21. Also found in
meiosis-specific cohesin complexes. Interacts with NUMA1, and
forms a ternary complex with KIF3B and KIFAP3, suggesting a
function in tethering the chromosomes to the spindle pole and in
chromosome movement. Interacts with PDS5A and WAPL; regulated by
SMC3 acetylation. Interacts with RPGR (By similarity). Interacts
(via central hinge region) with KIAA1328 (via N- and C-terminal
domains) (PubMed:15656913). Interacts with DDX11
(PubMed:17105772). {ECO:0000250, ECO:0000269|PubMed:15656913,
ECO:0000269|PubMed:17105772}.
-!- INTERACTION:
Q9BTE3:MCMBP; NbExp=6; IntAct=EBI-80718, EBI-749378;
Q29RF7:PDS5A; NbExp=4; IntAct=EBI-80718, EBI-1175454;
Q9NTI5:PDS5B; NbExp=7; IntAct=EBI-80718, EBI-1175604;
O60216:RAD21; NbExp=15; IntAct=EBI-80718, EBI-80739;
P32908:SMC1 (xeno); NbExp=4; IntAct=EBI-80718, EBI-17402;
Q8WVM7:STAG1; NbExp=12; IntAct=EBI-80718, EBI-1175097;
Q8N3U4:STAG2; NbExp=13; IntAct=EBI-80718, EBI-1057252;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
Note=Associates with chromatin. Before prophase it is scattered
along chromosome arms. During prophase, most of cohesin complexes
dissociate from chromatin probably because of phosphorylation by
PLK, except at centromeres, where cohesin complexes remain. At
anaphase, the RAD21 subunit of the cohesin complex is cleaved,
leading to the dissociation of the complex from chromosomes,
allowing chromosome separation. The phosphorylated form at Ser-
1083 is preferentially associated with unsynapsed chromosomal
regions (By similarity). {ECO:0000250}.
-!- DOMAIN: The flexible hinge domain, which separates the large
intramolecular coiled coil regions, allows the heterotypic
interaction with the corresponding domain of SMC1A or SMC1B,
forming a V-shaped heterodimer. The two heads of the heterodimer
are then connected by different ends of the cleavable RAD21
protein, forming a ring structure (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-1083 in a SPO11-dependent manner.
{ECO:0000250}.
-!- PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for
genome stability and S phase sister chromatid cohesion. Regulated
by DSCC1, it is required for processive DNA synthesis, coupling
sister chromatid cohesion establishment during S phase to DNA
replication. Deacetylation by HDAC8, regulates release of the
cohesin complex from chromatin. {ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:22885700}.
-!- DISEASE: Cornelia de Lange syndrome 3 (CDLS3) [MIM:610759]: A form
of Cornelia de Lange syndrome, a clinically heterogeneous
developmental disorder associated with malformations affecting
multiple systems. Characterized by facial dysmorphisms, abnormal
hands and feet, growth delay, cognitive retardation, hirsutism,
gastroesophageal dysfunction and cardiac, ophthalmologic and
genitourinary anomalies. Cornelia de Lange syndrome type 3 is a
mild form with absence of major structural anomalies. The
phenotype in some instances approaches that of apparently non-
syndromic mental retardation. {ECO:0000269|PubMed:17273969,
ECO:0000269|PubMed:18996922}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Mutated Cornelia de Lange cell lines display
genomic instability and sensitivity to ionizing radiation and
interstrand cross-linking agents.
-!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
{ECO:0000305}.
-!- CAUTION: Was originally isolated as a proteoglycan protein
(explaining its name). Although not excluded, such secreted
function is not clear. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD32447.1; Type=Frameshift; Positions=457, 488, 523; Evidence={ECO:0000305};
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EMBL; AF020043; AAC14893.1; -; mRNA.
EMBL; AK289771; BAF82460.1; -; mRNA.
EMBL; AL359260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49557.1; -; Genomic_DNA.
EMBL; AF067163; AAD32447.1; ALT_FRAME; mRNA.
EMBL; AJ005015; CAA06289.1; -; mRNA.
CCDS; CCDS31285.1; -.
RefSeq; NP_005436.1; NM_005445.3.
UniGene; Hs.24485; -.
ProteinModelPortal; Q9UQE7; -.
SMR; Q9UQE7; -.
BioGrid; 114574; 141.
CORUM; Q9UQE7; -.
DIP; DIP-29200N; -.
IntAct; Q9UQE7; 74.
MINT; MINT-3083875; -.
STRING; 9606.ENSP00000354720; -.
iPTMnet; Q9UQE7; -.
PhosphoSitePlus; Q9UQE7; -.
SwissPalm; Q9UQE7; -.
BioMuta; SMC3; -.
DMDM; 29337005; -.
EPD; Q9UQE7; -.
MaxQB; Q9UQE7; -.
PaxDb; Q9UQE7; -.
PeptideAtlas; Q9UQE7; -.
PRIDE; Q9UQE7; -.
Ensembl; ENST00000361804; ENSP00000354720; ENSG00000108055.
GeneID; 9126; -.
KEGG; hsa:9126; -.
UCSC; uc001kze.4; human.
CTD; 9126; -.
DisGeNET; 9126; -.
EuPathDB; HostDB:ENSG00000108055.9; -.
GeneCards; SMC3; -.
GeneReviews; SMC3; -.
HGNC; HGNC:2468; SMC3.
HPA; HPA037411; -.
HPA; HPA043206; -.
MalaCards; SMC3; -.
MIM; 606062; gene.
MIM; 610759; phenotype.
neXtProt; NX_Q9UQE7; -.
OpenTargets; ENSG00000108055; -.
Orphanet; 199; Cornelia de Lange syndrome.
PharmGKB; PA26966; -.
eggNOG; KOG0964; Eukaryota.
eggNOG; COG1196; LUCA.
GeneTree; ENSGT00580000081628; -.
HOGENOM; HOG000166512; -.
HOVERGEN; HBG039849; -.
InParanoid; Q9UQE7; -.
KO; K06669; -.
OMA; SEMQKTE; -.
OrthoDB; EOG091G011B; -.
PhylomeDB; Q9UQE7; -.
TreeFam; TF105602; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
Reactome; R-HSA-2470946; Cohesin Loading onto Chromatin.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
SIGNOR; Q9UQE7; -.
ChiTaRS; SMC3; human.
GeneWiki; SMC3; -.
GenomeRNAi; 9126; -.
PRO; PR:Q9UQE7; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000108055; -.
CleanEx; HS_SMC3; -.
Genevisible; Q9UQE7; HS.
GO; GO:0005604; C:basement membrane; TAS:CAFA.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; TAS:Reactome.
GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
GO; GO:0008278; C:cohesin complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0000800; C:lateral element; IEA:Ensembl.
GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0034991; C:nuclear meiotic cohesin complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
GO; GO:0036033; F:mediator complex binding; IEA:Ensembl.
GO; GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0051702; P:interaction with symbiont; IDA:CAFA.
GO; GO:0051321; P:meiotic cell cycle; IDA:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:BHF-UCL.
GO; GO:0044791; P:positive regulation by host of viral release from host cell; IDA:CAFA.
GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; IMP:BHF-UCL.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003395; RecF/RecN/SMC_N.
InterPro; IPR024704; SMC.
InterPro; IPR010935; SMC_hinge.
InterPro; IPR036277; SMC_hinge_sf.
Pfam; PF06470; SMC_hinge; 1.
Pfam; PF02463; SMC_N; 1.
PIRSF; PIRSF005719; SMC; 1.
SMART; SM00968; SMC_hinge; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF75553; SSF75553; 2.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell cycle; Cell division; Centromere;
Chromosome; Coiled coil; Complete proteome; Disease mutation;
DNA damage; DNA repair; Meiosis; Mental retardation; Mitosis;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 1217 Structural maintenance of chromosomes
protein 3.
/FTId=PRO_0000119001.
NP_BIND 32 39 ATP. {ECO:0000255}.
REGION 505 667 Flexible hinge.
COILED 179 350 {ECO:0000255}.
COILED 393 503 {ECO:0000255}.
COILED 669 916 {ECO:0000255}.
COILED 958 989 {ECO:0000255}.
COMPBIAS 1115 1150 Ala/Asp-rich (DA-box).
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496}.
MOD_RES 106 106 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496}.
MOD_RES 140 140 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 783 783 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1013 1013 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CW03}.
MOD_RES 1065 1065 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 1067 1067 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1074 1074 Phosphoserine.
{ECO:0000250|UniProtKB:P97690}.
MOD_RES 1083 1083 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1190 1190 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 491 491 Missing (in CDLS3; affects the affinity
of SMC hinge dimers for DNA; mutated
hinge dimers bind DNA with higher
affinity than wild-type proteins).
{ECO:0000269|PubMed:17273969,
ECO:0000269|PubMed:18996922}.
/FTId=VAR_032845.
MUTAGEN 105 105 K->A: 20% loss of sister chromatid
cohesion; when associated with A-106.
{ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496}.
MUTAGEN 105 105 K->R: Stabilizes interaction with PDS5A
and WAPL; when associated with R-106.
{ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496}.
MUTAGEN 106 106 K->A: 20% loss of sister chromatid
cohesion; when associated with A-105.
{ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496}.
MUTAGEN 106 106 K->R: Stabilizes interaction with PDS5A
and WAPL; when associated with R-105.
{ECO:0000269|PubMed:18614053,
ECO:0000269|PubMed:19907496}.
CONFLICT 462 462 K -> T (in Ref. 5; AAD32447).
{ECO:0000305}.
CONFLICT 509 509 I -> V (in Ref. 5; AAD32447).
{ECO:0000305}.
CONFLICT 526 526 Q -> P (in Ref. 5; AAD32447).
{ECO:0000305}.
SEQUENCE 1217 AA; 141542 MW; 21EF9A08A5D8096A CRC64;
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV
ITAEMAKDFV EDDTTHG


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