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Structural maintenance of chromosomes protein 2 (SMC protein 2) (SMC-2) (Chromosome-associated protein E) (FGF-inducible protein 16) (XCAP-E homolog)

 SMC2_MOUSE              Reviewed;        1191 AA.
Q8CG48; Q52KE9; Q61076; Q9CS17; Q9CSD8;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 129.
RecName: Full=Structural maintenance of chromosomes protein 2;
Short=SMC protein 2;
Short=SMC-2;
AltName: Full=Chromosome-associated protein E;
AltName: Full=FGF-inducible protein 16;
AltName: Full=XCAP-E homolog;
Name=Smc2; Synonyms=Cape, Fin16, Smc2l1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=14660695; DOI=10.1093/molbev/msh023;
Cobbe N., Heck M.M.S.;
"The evolution of SMC proteins: phylogenetic analysis and structural
implications.";
Mol. Biol. Evol. 21:332-347(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 562-570, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 801-1191.
PubMed=8649829;
Guthridge M.A., Seldin M., Basilico C.;
"Induction of expression of growth-related genes by FGF-4 in mouse
fibroblasts.";
Oncogene 12:1267-1278(1996).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1160, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Central component of the condensin complex, a complex
required for conversion of interphase chromatin into mitotic-like
condense chromosomes. The condensin complex probably introduces
positive supercoils into relaxed DNA in the presence of type I
topoisomerases and converts nicked DNA into positive knotted forms
in the presence of type II topoisomerases (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin
complex, which contains the SMC2 and SMC4 heterodimer, and three
non SMC subunits that probably regulate the complex: BRRN1/CAPH,
CNAP1/CAPD2 and CAPG (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q8BH43:Wasf2; NbExp=4; IntAct=EBI-643436, EBI-643162;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells,
the majority of the condensin complex is found in the cytoplasm,
while a minority of the complex is associated with chromatin. A
subpopulation of the complex however remains associated with
chromosome foci in interphase cells. During mitosis, most of the
condensin complex is associated with the chromatin. At the onset
of prophase, the regulatory subunits of the complex are
phosphorylated by CDC2, leading to condensin's association with
chromosome arms and to chromosome condensation. Dissociation from
chromosomes is observed in late telophase (By similarity).
{ECO:0000250}.
-!- DOMAIN: The hinge domain, which separates the large intramolecular
coiled coil regions, allows the heterodimerization with SMC4,
forming a V-shaped heterodimer. {ECO:0000250}.
-!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB08867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ534939; CAD59182.1; -; mRNA.
EMBL; AK013109; BAB28654.1; -; mRNA.
EMBL; AK019977; BAB31946.1; -; mRNA.
EMBL; AL732619; CAM14006.1; -; Genomic_DNA.
EMBL; CH466565; EDL02299.1; -; Genomic_DNA.
EMBL; BC094380; AAH94380.1; -; mRNA.
EMBL; U42385; AAB08867.1; ALT_INIT; mRNA.
CCDS; CCDS18180.1; -.
RefSeq; NP_001288341.1; NM_001301412.1.
RefSeq; NP_032043.3; NM_008017.4.
UniGene; Mm.2999; -.
PDB; 3L51; X-ray; 1.51 A; A=506-666.
PDBsum; 3L51; -.
ProteinModelPortal; Q8CG48; -.
SMR; Q8CG48; -.
BioGrid; 199677; 3.
CORUM; Q8CG48; -.
IntAct; Q8CG48; 2.
MINT; MINT-1748639; -.
STRING; 10090.ENSMUSP00000099979; -.
iPTMnet; Q8CG48; -.
PhosphoSitePlus; Q8CG48; -.
SwissPalm; Q8CG48; -.
EPD; Q8CG48; -.
MaxQB; Q8CG48; -.
PaxDb; Q8CG48; -.
PeptideAtlas; Q8CG48; -.
PRIDE; Q8CG48; -.
Ensembl; ENSMUST00000102915; ENSMUSP00000099979; ENSMUSG00000028312.
Ensembl; ENSMUST00000117280; ENSMUSP00000113940; ENSMUSG00000028312.
GeneID; 14211; -.
KEGG; mmu:14211; -.
UCSC; uc008swk.2; mouse.
CTD; 10592; -.
MGI; MGI:106067; Smc2.
eggNOG; KOG0933; Eukaryota.
eggNOG; COG1196; LUCA.
GeneTree; ENSGT00550000074857; -.
HOVERGEN; HBG106605; -.
InParanoid; Q8CG48; -.
KO; K06674; -.
OMA; HNKIAME; -.
OrthoDB; EOG091G03K8; -.
TreeFam; TF101157; -.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
EvolutionaryTrace; Q8CG48; -.
PRO; PR:Q8CG48; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028312; -.
CleanEx; MM_SMC2; -.
ExpressionAtlas; Q8CG48; baseline and differential.
Genevisible; Q8CG48; MM.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0000796; C:condensin complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051383; P:kinetochore organization; IMP:MGI.
GO; GO:0010032; P:meiotic chromosome condensation; IMP:MGI.
GO; GO:0045132; P:meiotic chromosome segregation; IMP:MGI.
GO; GO:0007076; P:mitotic chromosome condensation; ISO:MGI.
CDD; cd03273; ABC_SMC2_euk; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003395; RecF/RecN/SMC_N.
InterPro; IPR024704; SMC.
InterPro; IPR027120; Smc2_ABC.
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; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Chromosome; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA condensation; Mitosis;
Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 1191 Structural maintenance of chromosomes
protein 2.
/FTId=PRO_0000118996.
NP_BIND 32 39 ATP. {ECO:0000255}.
REGION 508 671 Flexible hinge.
COILED 173 507 {ECO:0000255}.
COILED 672 936 {ECO:0000255}.
COILED 963 1031 {ECO:0000255}.
COMPBIAS 1085 1120 Ala/Asp-rich (DA-box).
MOD_RES 114 114 N6-acetyllysine.
{ECO:0000250|UniProtKB:O95347}.
MOD_RES 222 222 N6-acetyllysine.
{ECO:0000250|UniProtKB:O95347}.
MOD_RES 677 677 N6-acetyllysine.
{ECO:0000250|UniProtKB:O95347}.
MOD_RES 1158 1158 N6-acetyllysine.
{ECO:0000250|UniProtKB:O95347}.
MOD_RES 1160 1160 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CONFLICT 62 62 L -> F (in Ref. 1; CAD59182).
{ECO:0000305}.
HELIX 519 521 {ECO:0000244|PDB:3L51}.
STRAND 522 525 {ECO:0000244|PDB:3L51}.
HELIX 526 528 {ECO:0000244|PDB:3L51}.
STRAND 531 533 {ECO:0000244|PDB:3L51}.
HELIX 535 537 {ECO:0000244|PDB:3L51}.
HELIX 538 545 {ECO:0000244|PDB:3L51}.
HELIX 546 550 {ECO:0000244|PDB:3L51}.
STRAND 552 555 {ECO:0000244|PDB:3L51}.
HELIX 557 566 {ECO:0000244|PDB:3L51}.
STRAND 573 577 {ECO:0000244|PDB:3L51}.
TURN 578 580 {ECO:0000244|PDB:3L51}.
HELIX 588 598 {ECO:0000244|PDB:3L51}.
STRAND 602 605 {ECO:0000244|PDB:3L51}.
HELIX 606 609 {ECO:0000244|PDB:3L51}.
HELIX 614 616 {ECO:0000244|PDB:3L51}.
HELIX 617 624 {ECO:0000244|PDB:3L51}.
STRAND 628 632 {ECO:0000244|PDB:3L51}.
HELIX 633 641 {ECO:0000244|PDB:3L51}.
TURN 643 645 {ECO:0000244|PDB:3L51}.
STRAND 649 651 {ECO:0000244|PDB:3L51}.
SEQUENCE 1191 AA; 134239 MW; 56CC351A7855D0BB CRC64;
MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS
NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEAHDE ITVTRQVVIG GRNKYLINGV
NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA
AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL
RAEDTKERSA GELKEMQDKI VNLQEVLSEN EKKIKALNCE IEELERRKDK ETGGKLKSLE
DACAEAQRVN TKSQSAFDLK KKNLASEETK RKELQNSMAE DSKALAAKEK EVKKITDGLH
GLQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMIACKNDIS KAQTEAKQAQ
MKLKHAQQEL KSKQAEVKKM DSGYKKDQDA FEAVKKAKEK LETEMKKLNY EENKEEKLLE
KHRQLSRDIN NLKGKHEALL AKFPNLQFAY KDPEKNWNRN SVKGLVASLI NVKDNSTATA
LEVVAGERLY NVVVDTEVTA KKLLEKGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
DNVHVALSLV DYKPELQKGM EFVFGTTFVC NNMDNAKKVA FDKRIMTRTV TLGGDVFDPH
GTLSGGARSQ AASILTKFQE VKDVQDELRT KENELRALEE ELAGLKNVAE KYRQLKQQWE
MKTEEGDLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK STKEIQKKAE EKYEALENKM
KNAEAEREKE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHASNEQQL
DAVNEAIKAY EGQIEKMAAE VAKNKESVNK AQDELMKQKQ IITAQDNIIK DKCAEVAKHN
LQNNESQLKI KELDHSISKH KREADDAAAK VSKMLSDYDW INAEKHLFGQ PNSAYDFKTN
NPKEAGQRLQ KLQEVKEKLG RNVNLRAMNV LTEAEERYND LMKKKRIVEN DKSKILATIE
DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE
NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF
IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQSQAGKIP KEAKSRGKEP N


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