CND1_YEAST
ID CND1_YEAST Reviewed; 1176 AA.
AC Q06156; D6VYR9;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Condensin complex subunit 1;
DE AltName: Full=XCAP-D2 homolog;
GN Name=YCS4; Synonyms=LOC7; OrderedLocusNames=YLR272C; ORFNames=L8479.14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
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 [3]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; BRN1 AND YCG1.
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11854418; DOI=10.1091/mbc.01-05-0264;
RA Bhalla N., Biggins S., Murray A.W.;
RT "Mutation of YCS4, a budding yeast condensin subunit, affects mitotic and
RT nonmitotic chromosome behavior.";
RL Mol. Biol. Cell 13:632-645(2002).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION BY
RP 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:11854418}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11854418}. Chromosome
CC {ECO:0000269|PubMed:11854418}. Note=Nuclear throughout the cell cycle.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, condensin associates with
CC chromosome arms and to chromosome condensation. At anaphase, it is
CC enriched at rDNA. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- MISCELLANEOUS: Present with 2540 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000305}.
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DR EMBL; U17244; AAB67384.1; -; Genomic_DNA.
DR EMBL; U17245; AAB67369.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09585.1; -; Genomic_DNA.
DR PIR; S51408; S51408.
DR RefSeq; NP_013374.1; NM_001182159.1.
DR PDB; 6YVU; EM; 7.50 A; D=1-1176.
DR PDB; 6YVV; EM; 7.50 A; D=1-1176.
DR PDB; 7Q2X; EM; 3.00 A; D=1-1176.
DR PDB; 7Q2Y; EM; -; D=1-1176.
DR PDBsum; 6YVU; -.
DR PDBsum; 6YVV; -.
DR PDBsum; 7Q2X; -.
DR PDBsum; 7Q2Y; -.
DR AlphaFoldDB; Q06156; -.
DR SMR; Q06156; -.
DR BioGRID; 31539; 239.
DR ComplexPortal; CPX-1869; Nuclear condensin complex.
DR IntAct; Q06156; 9.
DR MINT; Q06156; -.
DR STRING; 4932.YLR272C; -.
DR CarbonylDB; Q06156; -.
DR iPTMnet; Q06156; -.
DR MaxQB; Q06156; -.
DR PaxDb; Q06156; -.
DR PRIDE; Q06156; -.
DR EnsemblFungi; YLR272C_mRNA; YLR272C; YLR272C.
DR GeneID; 850977; -.
DR KEGG; sce:YLR272C; -.
DR SGD; S000004262; YCS4.
DR VEuPathDB; FungiDB:YLR272C; -.
DR eggNOG; KOG0414; Eukaryota.
DR GeneTree; ENSGT00940000153566; -.
DR HOGENOM; CLU_001867_1_0_1; -.
DR InParanoid; Q06156; -.
DR OMA; RNCVLQI; -.
DR BioCyc; YEAST:G3O-32371-MON; -.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q06156; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06156; protein.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IC:ComplexPortal.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:SGD.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:SGD.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:SGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:1903342; P:negative regulation of meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
DR GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR007673; Condensin_cplx_su1.
DR InterPro; IPR024324; Condensin_cplx_su1_N.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR PANTHER; PTHR14222:SF2; PTHR14222:SF2; 1.
DR Pfam; PF12717; Cnd1; 2.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; DNA condensation;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1176
FT /note="Condensin complex subunit 1"
FT /id="PRO_0000095046"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1176 AA; 132967 MW; 0C1BEFEF6D057D18 CRC64;
MSGFSLSEYL TKFQTTDRES YPRLQDPSRE LNVIIDQLAV SPEQIDASPD SLEALIDLCH
DFPHLTPKLQ TQLSYLISSS LSNLSKDIKA NLSSNVNFTE IGGLIPQWKR HLEEYGYLIQ
VLLTFLQDEL HKVSSQSTNL NRSAKNSKND SANVELFKRD CNQMENLLES ITKLLEINLS
KIFQTTPEKD LFIGLFTRPL FVLLEIEPVT KVSSLKMFIQ RILAMCVKNH GQSSSIQSSL
MTNLTYFLHL SVFNAELLKL LNDEYNYPQL TEDILKEIST RVFNAKDTTG PKAISNFLIK
LSELSPGIML RQMNLVITLL NNSSITLRCS VVEACGNIVA ELAQDPQTME HYKQQIAVLI
ELLEERFQDS NPYVRTKAIQ GCSKICDLSS KFNKSKAKFT SLAVRSLQDR SSLVRRNSVK
LLSKLLLKHP FKAIHGSQLR LSEWEEYLKG SESQLNSTLK KVESQETLND TIERSLIEEE
VEQDEGQCRT ELEGSFNKSA ELSRIENEVE NINATNTSVL MKLKLMIVYY KDAISFIKEI
HKSIELISNL LFSKNRNEVL ESMDFLVLAD AFDIELSEFG IKKMLHLVWM KGTNDEGTSI
SVHLIECYKQ LFLTAPDSCN MQEKAAHIAK NLINLSIGAS IADLASLEQL LGMMYEQKLI
DQHVINILWA IYNSASKASM QKEQNVNNRD SEKGFSKEQI HGSIIILGML SLADNEIALK
GLESLLNIGL GAVGLKDLTL CRYSCLALER MVPKRSTIIT KAINQELEDV AVKKLYAIII
NYTKDNEYYP MCEQALSALF TISSKPDILA TDLIREKTMM TFGKPEEEDS ILSLEQSSRV
VSLSQLLFIV GQVAIKTLVY LEKCEAEFKK RKIEAETRNG KVKNQGADVT NTTQDNGGDK
ELEMIGGTNE DDFTDAIQFV KENELLFGEK SILGKFCPIV EEIVSNSSRF SDPMLQRTAT
LCLEKLMCLS SKYCEKSLPL LITVMEKSPD PTIRSNAVLG LGDMAVCFNN LVDENTDYLY
RRLHDENLMV QRTCLMTVTF LILAGQVKVK GQLGEMAKCL DNPDQGISDM CRLFFTELAS
KDNAIYNGFI DIFSNLSSDD LLGKESFKKI IKFLLTFIDK ERHQKQLNEK LVGRLRKCET
QKQWDDIAFV LNNLPYKNED VTALLEQGFK VVSAKE
