ID   CND2_YEAST              Reviewed;         754 AA.
AC   P38170; D6VPQ8; Q6Q5G8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Condensin complex subunit 2;
DE   AltName: Full=Barren homolog;
DE   AltName: Full=CAPH homolog;
GN   Name=BRN1; OrderedLocusNames=YBL097W; ORFNames=YBL0830;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / FY1678;
RX   PubMed=7502586; DOI=10.1002/yea.320111112;
RA   Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT   "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT   cerevisiae chromosome II.";
RL   Yeast 11:1103-1112(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 517.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-754.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; YCG1 AND YCS4.
RX   PubMed=10811823; DOI=10.1083/jcb.149.4.811;
RA   Freeman L., Aragon-Alcaide L., Strunnikov A.V.;
RT   "The condensin complex governs chromosome condensation and mitotic
RT   transmission of rDNA.";
RL   J. Cell Biol. 149:811-824(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=10749930; DOI=10.1091/mbc.11.4.1293;
RA   Lavoie B.D., Tuffo K.M., Oh S., Koshland D., Holm C.;
RT   "Mitotic chromosome condensation requires Brn1p, the yeast homologue of
RT   Barren.";
RL   Mol. Biol. Cell 11:1293-1304(2000).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMC2.
RX   PubMed=10749931; DOI=10.1091/mbc.11.4.1305;
RA   Ouspenski I.I., Cabello O.A., Brinkley B.R.;
RT   "Chromosome condensation factor Brn1p is required for chromatid separation
RT   in mitosis.";
RL   Mol. Biol. Cell 11:1305-1313(2000).
RN   [8]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-548, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Regulatory subunit of the condensin complex, a complex
CC       required for conversion of interphase chromatin into mitotic-like
CC       condense chromosomes. The condensin complex probably introduces
CC       positive supercoils into relaxed DNA in the presence of type I
CC       topoisomerases and converts nicked DNA into positive knotted forms in
CC       the presence of type II topoisomerases. The condensin complex probably
CC       also plays a role during interphase. {ECO:0000269|PubMed:10749930,
CC       ECO:0000269|PubMed:10749931}.
CC   -!- SUBUNIT: Component of the condensin complex, which contains the SMC2
CC       and SMC4 heterodimer, and three non SMC subunits that probably regulate
CC       the complex: BRN1, YCS4 and YCG1/YCS5. {ECO:0000269|PubMed:10811823}.
CC   -!- INTERACTION:
CC       P38170; P38989: SMC2; NbExp=2; IntAct=EBI-4792, EBI-17412;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10749931}. Cytoplasm
CC       {ECO:0000269|PubMed:10749931}. Chromosome
CC       {ECO:0000269|PubMed:10749931}. Note=In interphase cells, the majority
CC       of the condensin complex is found in the cytoplasm, while a minority of
CC       the complex is associated with chromatin. A subpopulation of the
CC       complex however remains associated with chromosome foci in interphase
CC       cells. During mitosis, most of the condensin complex is associated with
CC       the chromatin. At the onset of prophase, condensin associates with
CC       chromosome arms and to chromosome condensation. Dissociation from
CC       chromosomes is observed in late telophase.
CC   -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA56003.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA84919.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X79489; CAA56003.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z35858; CAA84919.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY558077; AAS56403.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07028.2; -; Genomic_DNA.
DR   PIR; S45403; S45403.
DR   RefSeq; NP_009455.3; NM_001178337.2.
DR   PDB; 5OQN; X-ray; 3.15 A; B=384-529.
DR   PDB; 5OQO; X-ray; 3.25 A; B=384-529.
DR   PDB; 5OQP; X-ray; 2.98 A; B=384-529.
DR   PDB; 5OQQ; X-ray; 2.79 A; C/D=384-529.
DR   PDB; 6YVD; EM; 7.60 A; B=1-754.
DR   PDB; 6YVU; EM; 7.50 A; C=1-754.
DR   PDB; 6YVV; EM; 7.50 A; C=1-754.
DR   PDB; 7Q2X; EM; 3.00 A; C=1-754.
DR   PDB; 7Q2Y; EM; -; C=1-754.
DR   PDB; 7Q2Z; EM; 3.20 A; C=1-754.
DR   PDB; 7QEN; EM; 3.46 A; C=1-754.
DR   PDB; 7QFW; EM; 3.86 A; B=1-754.
DR   PDBsum; 5OQN; -.
DR   PDBsum; 5OQO; -.
DR   PDBsum; 5OQP; -.
DR   PDBsum; 5OQQ; -.
DR   PDBsum; 6YVD; -.
DR   PDBsum; 6YVU; -.
DR   PDBsum; 6YVV; -.
DR   PDBsum; 7Q2X; -.
DR   PDBsum; 7Q2Y; -.
DR   PDBsum; 7Q2Z; -.
DR   PDBsum; 7QEN; -.
DR   PDBsum; 7QFW; -.
DR   AlphaFoldDB; P38170; -.
DR   EMDB; EMD-10944; -.
DR   EMDB; EMD-10951; -.
DR   EMDB; EMD-10952; -.
DR   EMDB; EMD-13783; -.
DR   EMDB; EMD-13784; -.
DR   EMDB; EMD-13786; -.
DR   EMDB; EMD-13934; -.
DR   EMDB; EMD-13950; -.
DR   SMR; P38170; -.
DR   BioGRID; 32608; 449.
DR   ComplexPortal; CPX-1869; Nuclear condensin complex.
DR   DIP; DIP-4662N; -.
DR   IntAct; P38170; 11.
DR   MINT; P38170; -.
DR   STRING; 4932.YBL097W; -.
DR   CarbonylDB; P38170; -.
DR   iPTMnet; P38170; -.
DR   MaxQB; P38170; -.
DR   PaxDb; 4932-YBL097W; -.
DR   PeptideAtlas; P38170; -.
DR   EnsemblFungi; YBL097W_mRNA; YBL097W; YBL097W.
DR   GeneID; 852180; -.
DR   KEGG; sce:YBL097W; -.
DR   AGR; SGD:S000000193; -.
DR   SGD; S000000193; BRN1.
DR   VEuPathDB; FungiDB:YBL097W; -.
DR   eggNOG; KOG2328; Eukaryota.
DR   GeneTree; ENSGT00390000004149; -.
DR   HOGENOM; CLU_010510_0_1_1; -.
DR   InParanoid; P38170; -.
DR   OMA; GREHWKV; -.
DR   OrthoDB; 153509at2759; -.
DR   BioCyc; YEAST:G3O-28983-MONOMER; -.
DR   Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR   BioGRID-ORCS; 852180; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P38170; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38170; Protein.
DR   GO; GO:0000796; C:condensin complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003682; F:chromatin binding; IGI:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; NAS:ComplexPortal.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR   GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
DR   InterPro; IPR022816; Condensin_barren_su2.
DR   PANTHER; PTHR13108; CONDENSIN COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR13108:SF9; CONDENSIN COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF05786; Cnd2; 1.
DR   PIRSF; PIRSF017126; Condensin_H; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW   DNA condensation; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..754
FT                   /note="Condensin complex subunit 2"
FT                   /id="PRO_0000095047"
FT   REGION          104..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        517
FT                   /note="G -> A (in Ref. 1; CAA56003 and 2; CAA84919)"
FT                   /evidence="ECO:0000305"
FT   HELIX           23..39
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:7QEN"
FT   HELIX           72..103
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           186..197
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           276..287
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          290..293
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           301..310
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           314..322
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           385..398
FT                   /evidence="ECO:0007829|PDB:5OQQ"
FT   HELIX           399..401
FT                   /evidence="ECO:0007829|PDB:5OQP"
FT   HELIX           405..408
FT                   /evidence="ECO:0007829|PDB:5OQO"
FT   STRAND          463..465
FT                   /evidence="ECO:0007829|PDB:5OQP"
FT   HELIX           469..474
FT                   /evidence="ECO:0007829|PDB:5OQQ"
FT   HELIX           487..490
FT                   /evidence="ECO:0007829|PDB:5OQQ"
FT   TURN            493..496
FT                   /evidence="ECO:0007829|PDB:5OQQ"
FT   HELIX           506..510
FT                   /evidence="ECO:0007829|PDB:5OQQ"
FT   STRAND          518..520
FT                   /evidence="ECO:0007829|PDB:5OQP"
FT   HELIX           647..668
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           692..700
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           705..710
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   HELIX           713..726
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          730..733
FT                   /evidence="ECO:0007829|PDB:7Q2X"
FT   STRAND          735..738
FT                   /evidence="ECO:0007829|PDB:7QEN"
FT   STRAND          740..743
FT                   /evidence="ECO:0007829|PDB:7Q2X"
SQ   SEQUENCE   754 AA;  86216 MW;  7B30373738D4AE7A CRC64;
     MTTQLRYENN DDDERVEYNL FTNRSTMMAN FEEWIKMATD NKINSRNSWN FALIDYFYDL
     DVLKDGENNI NFQKASATLD GCIKIYSSRV DSVTTETGKL LSGLAQRKTN GASNGDDSNG
     GNGEGLGGDS DEANIEIDPL TGMPISNDPD VNNTRRRVYN RVLETTLVEF ETIKMKELDQ
     ELIIDPLFKK ALVDFDEGGA KSLLLNTLNI DNTARVIFDA SIKDTQNVGQ GKLQRKEEEL
     IERDSLVDDE NEPSQSLIST RNDSTVNDSV ISAPSMEDEI LSLGMDFIKF DQIAVCEISG
     SIEQLRNVVE DINQAKDFIE NVNNRFDNFL TEEELQAAVP DNAEDDSDGF DMGMQQELCY
     PDENHDNTSH DEQDDDNVNS TTGSIFEKDL MAYFDENLNR NWRGREHWKV RNFKKANLVN
     KESDLLEETR TTIGDTTDKN TTDDKSMDTK KKHKQKKVLE IDFFKTDDSF EDKVFASKGR
     TKIDMPIKNR KNDTHYLLPD DFHFSTDRIT RLFIKPGQKM SLFSHRKHTR GDVSSGLFEK
     STVSANHSNN DIPTIADEHF WADNYERKEQ EEKEKEQSKE VGDVVGGALD NPFEDDMDGV
     DFNQAFEGTD DNEEASVKLD LQDDEDHKFP IRENKVTYSR VSKKVDVRRL KKNVWRSINN
     LIQEHDSRKN REQSSNDSET HTEDESTKEL KFSDIIQGIS KMYSDDTLKD ISTSFCFICL
     LHLANEHGLQ ITHTENYNDL IVNYEDLATT QAAS
//