CND2_YEAST
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 03-AUG-2022, entry version 170.
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 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 AlphaFoldDB; P38170; -.
DR SMR; P38170; -.
DR BioGRID; 32608; 448.
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; P38170; -.
DR PRIDE; P38170; -.
DR EnsemblFungi; YBL097W_mRNA; YBL097W; YBL097W.
DR GeneID; 852180; -.
DR KEGG; sce:YBL097W; -.
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 BioCyc; YEAST:G3O-28983-MON; -.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
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; IC: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; PTHR13108; 1.
DR Pfam; PF05786; Cnd2; 2.
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 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"
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
