CND1_MOUSE
ID CND1_MOUSE Reviewed; 1392 AA.
AC Q8K2Z4; Q6ZQI1; Q8R0F2; Q8R3H0; Q922B7; Q923A3; Q9CS25; Q9CT32;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Condensin complex subunit 1;
DE AltName: Full=Chromosome condensation-related SMC-associated protein 1;
DE AltName: Full=Chromosome-associated protein D2;
DE Short=mCAP-D2;
DE AltName: Full=Non-SMC condensin I complex subunit D2;
DE AltName: Full=XCAP-D2 homolog;
GN Name=Ncapd2; Synonyms=Capd2, Cnap1, Kiaa0159;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 577-1392 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320 AND SER-1323, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1323; THR-1329; SER-1358;
RP SER-1361 AND SER-1362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. May target the condensin
CC complex to DNA via its C-terminal domain. May promote the resolution of
CC double-strand DNA catenanes (intertwines) between sister chromatids.
CC Condensin-mediated compaction likely increases tension in catenated
CC sister chromatids, providing directionality for type II topoisomerase-
CC mediated strand exchanges toward chromatid decatenation. Required for
CC decatenation of non-centromeric ultrafine DNA bridges during anaphase.
CC Early in neurogenesis, may play an essential role to ensure accurate
CC mitotic chromosome condensation in neuron stem cells, ultimately
CC affecting neuron pool and cortex size. {ECO:0000250|UniProtKB:Q15021}.
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: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Interacts with
CC histones H1 and H3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC condensin complex is found in the cytoplasm, while a minority of the
CC complex is associated with chromatin. A subpopulation of the complex
CC however remains associated with chromosome foci in interphase cells.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDK1, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2Z4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2Z4-2; Sequence=VSP_007246;
CC -!- DOMAIN: The C-terminal domain interacts with histones H1 and H3, and
CC may be responsible for condensin complex targeting to mitotic
CC chromosomes. This domain is independent from the bipartite nuclear
CC localization signal, although they are contained within the same region
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC NCAPH and NCAPG subunits, activates the condensin complex and is
CC required for chromosome condensation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06673.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=BAC97878.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BC025460; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129068; BAC97878.1; ALT_INIT; mRNA.
DR EMBL; BC006673; AAH06673.1; ALT_SEQ; mRNA.
DR EMBL; BC008592; AAH08592.1; -; mRNA.
DR EMBL; BC025460; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC026982; AAH26982.1; -; mRNA.
DR EMBL; BC029133; AAH29133.1; -; mRNA.
DR EMBL; AK011352; BAB27560.1; -; mRNA.
DR EMBL; AK019259; BAB31633.1; -; mRNA.
DR CCDS; CCDS39636.1; -. [Q8K2Z4-1]
DR RefSeq; NP_666283.1; NM_146171.1.
DR RefSeq; XP_006506594.1; XM_006506531.3.
DR AlphaFoldDB; Q8K2Z4; -.
DR SMR; Q8K2Z4; -.
DR BioGRID; 212791; 15.
DR ComplexPortal; CPX-980; Condensin I complex.
DR IntAct; Q8K2Z4; 1.
DR STRING; 10090.ENSMUSP00000042260; -.
DR iPTMnet; Q8K2Z4; -.
DR PhosphoSitePlus; Q8K2Z4; -.
DR EPD; Q8K2Z4; -.
DR jPOST; Q8K2Z4; -.
DR MaxQB; Q8K2Z4; -.
DR PaxDb; Q8K2Z4; -.
DR PeptideAtlas; Q8K2Z4; -.
DR PRIDE; Q8K2Z4; -.
DR ProteomicsDB; 283537; -. [Q8K2Z4-1]
DR ProteomicsDB; 283538; -. [Q8K2Z4-2]
DR DNASU; 68298; -.
DR GeneID; 68298; -.
DR KEGG; mmu:68298; -.
DR UCSC; uc009dtt.1; mouse. [Q8K2Z4-1]
DR CTD; 9918; -.
DR MGI; MGI:1915548; Ncapd2.
DR eggNOG; KOG0414; Eukaryota.
DR InParanoid; Q8K2Z4; -.
DR OrthoDB; 166920at2759; -.
DR PhylomeDB; Q8K2Z4; -.
DR TreeFam; TF105712; -.
DR Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
DR BioGRID-ORCS; 68298; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Ncapd2; mouse.
DR PRO; PR:Q8K2Z4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K2Z4; protein.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; ISO:MGI.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:ComplexPortal.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IMP:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 1.
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; 1.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW DNA condensation; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1392
FT /note="Condensin complex subunit 1"
FT /id="PRO_0000095036"
FT REGION 1..593
FT /note="Interaction with SMC2 and SMC4"
FT /evidence="ECO:0000250"
FT REGION 569..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1332..1353
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 572..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15021"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15021"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15021"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1329
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15021"
FT MOD_RES 1375
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
FT MOD_RES 1380
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15021"
FT VAR_SEQ 1382..1392
FT /note="IRRASGRRHRS -> TLVEVLVVCGFNMEMAFALRSFS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007246"
FT CONFLICT 574
FT /note="D -> G (in Ref. 2; AAH26982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="I -> V (in Ref. 2; AAH26982 and 3; BAB31633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1392 AA; 155665 MW; 192E117CC7172A87 CRC64;
MSPHNFEFHL PLSPEELLKS GGVNQYVVRE VLPVKHLSSQ LRAFQSAFRA QGPLAILEHF
DTVYSILHHF RSIEPGLKED TLEFLKKVVS RHSQELSSIL DDAALSGSDR SAHLNALKMN
CYALIRLLES FENMTSQTSL IDLDIGGKGK RARAKATLGF DWEEERQPVL QLLTQLLQLD
IRHLWNHSAI EEEFVSLVTG CCYRLLENPT ISHQKNRSTK EAIAHLLGVA LVRYNHMLSA
TVKIIQMLQH FEHLPPVLVT AVSLWATDYG MKSIVGEIVR EIGQKCPQEL SRDTAGAKGF
AAFLTELAER IPAVLMANMC ILLDHLDGEN YMMRNAVLAA IAEMVLQVLN GDQLEESARE
TRDQFLDILQ AHGHDVNSFV RSRVLQLFAR IVQQKALPLT RFQAVVALAV GRLADKSVLV
CKNAIQLLAS FLANNPFSCK LSDIDLAGPL QKEIQKLQEM RAQRRSAAAT AALDPEEEWD
AMLPELKSTL QQLLKLPQEE GDHQIADAET AEEVKGRIRQ LLAKASYKQA IVLTREATSH
FQESEPFSHT EPEENSFLNL LGLIFKGPEA STQDSHGDTD PGLTGSKDSP SVPEPEGSQS
NDELVKQEML VQYLQDAYGF SQKITEAIGI ISKMMYENTT TVVQEVIEFF VMVFQFGVPQ
ALFGVRRMLP LIWSKEPGVR EAVLNAYRQL YLNPKGDSAR AKAQTLIHNL SLLLVDASVG
TIQCLEEILC EFVQKDEVKP AVIQLLWERA TEKVPSSPLE RCSSVMLLGM MARGKPEIVG
SNLDALVRVG LDEKSPQDYR LAQQVCLAIA NISDRRKPSL GERHPPFRLP QEHRLFERLQ
DMVTKGFAHP DPLWIPFKEV AVTLTYQLAE SPDVLCAQML QGCAKQVLEK LEKNATEADP
KETAPRLPTF LLMNLLSLAG DVALQQLVHL EQAVSGELGR RRVLREEQEH RAKEPKEKTA
SSETTMEEEL GLVGGATADD TEAELIRSIC EKELLDGNQV LAAFVPLLLK VCNNPGLYSN
PELCAAASLA LGKFCMISAP FCDSQLRLLF TMLEKSSLPT VRSNLMVATG DLAIRFPNLV
DPWTPHLYAR LRDPAQQVRK TAGLVMTHLI LKDMVKVKGQ VSEMAVLLID PVPQIAALAK
NFFNELSHKG NAIYNLLPDI ISRLSDPEGG VEEEPFHTIM KQLLSYITKD KQTESLVEKL
CQRFRTARTE RQYRDLAYCM SQLPLTERGL QKMLDNFECF GDKLLDESVF SAFLSIVGKL
RRGAKPEGKA IIDEFEQKLR ACHTRGMDGI EEFETGQGGS QRALSAKKPS AVSRLQPLTS
VDSDNDFVTP KPRRTKPGRP QTQQRKKSQR KAKVVFLSDE SSEDELSAEM TEEETPKRTT
PIRRASGRRH RS
