ID CND1_HUMAN Reviewed; 1401 AA. AC Q15021; D3DUR4; Q8N6U3; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 3. DT 27-MAR-2024, entry version 209. 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=hCAP-D2; DE AltName: Full=Non-SMC condensin I complex subunit D2; DE AltName: Full=XCAP-D2 homolog; GN Name=NCAPD2 {ECO:0000303|PubMed:27737959, GN ECO:0000312|HGNC:HGNC:24305}; Synonyms=CAPD2, CNAP1, KIAA0159; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-83. RC TISSUE=Bone marrow; RX PubMed=8590280; DOI=10.1093/dnares/2.4.167; RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. IV. The RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:167-174(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-83. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-83 AND SER-1321. RC TISSUE=Mammary gland; 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 [5] RP PROTEIN SEQUENCE OF 359-365; 537-560; 698-709 AND 1324-1331, IDENTIFICATION RP IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4, AND SUBCELLULAR LOCATION. RX PubMed=10958694; DOI=10.1128/mcb.20.18.6996-7006.2000; RA Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.; RT "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of RT Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the RT early stage of mitotic chromosome condensation."; RL Mol. Cell. Biol. 20:6996-7006(2000). RN [6] RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPH AND NCAPG, AND RP FUNCTION OF THE CONDENSIN COMPLEX. RX PubMed=11136719; DOI=10.1074/jbc.c000873200; RA Kimura K., Cuvier O., Hirano T.; RT "Chromosome condensation by a human condensin complex in Xenopus egg RT extracts."; RL J. Biol. Chem. 276:5417-5420(2001). RN [7] RP INTERACTION WITH HISTONE H1 AND HISTONE H3, AND MUTAGENESIS OF RP 1343-ARG--ARG-1348 AND 1358-LYS--LYS-1360. RX PubMed=12138188; DOI=10.1128/mcb.22.16.5769-5781.2002; RA Ball A.R. Jr., Schmiesing J.A., Zhou C., Gregson H.C., Okada Y., Doi T., RA Yokomori K.; RT "Identification of a chromosome-targeting domain in the human condensin RT subunit CNAP1/hCAP-D2/Eg7."; RL Mol. Cell. Biol. 22:5769-5781(2002). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1330; THR-1331; RP SER-1333; THR-1339; SER-1366; SER-1367; SER-1370 AND SER-1371, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333 AND THR-1339, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-1333 AND THR-1339, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1310; SER-1315; RP SER-1330; THR-1331; SER-1333; THR-1339 AND SER-1395, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP VARIANT [LARGE SCALE ANALYSIS] GLU-83, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP INVOLVEMENT IN MCPH21, AND FUNCTION. RX PubMed=27737959; DOI=10.1101/gad.286351.116; RG Deciphering Developmental Disorders Study; RA Martin C.A., Murray J.E., Carroll P., Leitch A., Mackenzie K.J., RA Halachev M., Fetit A.E., Keith C., Bicknell L.S., Fluteau A., Gautier P., RA Hall E.A., Joss S., Soares G., Silva J., Bober M.B., Duker A., Wise C.A., RA Quigley A.J., Phadke S.R., Wood A.J., Vagnarelli P., Jackson A.P.; RT "Mutations in genes encoding condensin complex proteins cause microcephaly RT through decatenation failure at mitosis."; RL Genes Dev. 30:2158-2172(2016). RN [22] RP VARIANT MCPH21 SER-8. RX PubMed=28097321; DOI=10.1001/jamapsychiatry.2016.3798; RA Reuter M.S., Tawamie H., Buchert R., Hosny Gebril O., Froukh T., Thiel C., RA Uebe S., Ekici A.B., Krumbiegel M., Zweier C., Hoyer J., Eberlein K., RA Bauer J., Scheller U., Strom T.M., Hoffjan S., Abdelraouf E.R., RA Meguid N.A., Abboud A., Al Khateeb M.A., Fakher M., Hamdan S., Ismael A., RA Muhammad S., Abdallah E., Sticht H., Wieczorek D., Reis A., Abou Jamra R.; RT "Diagnostic yield and novel candidate genes by exome sequencing in 152 RT consanguineous families with neurodevelopmental disorders."; RL JAMA Psychiatry 74:293-299(2017). 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 (PubMed:11136719). May promote CC the resolution of double-strand DNA catenanes (intertwines) between CC sister chromatids. Condensin-mediated compaction likely increases CC tension in catenated sister chromatids, providing directionality for CC type II topoisomerase-mediated strand exchanges toward chromatid CC decatenation. Required for decatenation of non-centromeric ultrafine CC DNA bridges during anaphase. Early in neurogenesis, may play an CC essential role to ensure accurate mitotic chromosome condensation in CC neuron stem cells, ultimately affecting neuron pool and cortex size CC (PubMed:27737959). {ECO:0000269|PubMed:11136719, CC ECO:0000269|PubMed:27737959}. 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. {ECO:0000269|PubMed:10958694, CC ECO:0000269|PubMed:11136719, ECO:0000269|PubMed:12138188}. CC -!- INTERACTION: CC Q15021; Q9BPX3: NCAPG; NbExp=2; IntAct=EBI-1044041, EBI-970214; CC Q15021; Q15003: NCAPH; NbExp=7; IntAct=EBI-1044041, EBI-1046410; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm CC {ECO:0000269|PubMed:10958694}. Chromosome CC {ECO:0000269|PubMed:10958694}. 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, 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. 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 CC region. 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 -!- DISEASE: Microcephaly 21, primary, autosomal recessive (MCPH21) CC [MIM:617983]: A form of microcephaly, a disease defined as a head CC circumference more than 3 standard deviations below the age, sex and CC ethnically matched mean. Brain weight is markedly reduced and the CC cerebral cortex is disproportionately small. MCPH21 features include CC mild intellectual disability, intrauterine growth retardation, short CC stature, and microcephaly. {ECO:0000269|PubMed:27737959, CC ECO:0000269|PubMed:28097321}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA09930.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63880; BAA09930.2; ALT_INIT; mRNA. DR EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471116; EAW88788.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88789.1; -; Genomic_DNA. DR EMBL; BC028182; AAH28182.1; -; mRNA. DR CCDS; CCDS8548.1; -. DR RefSeq; NP_055680.3; NM_014865.3. DR AlphaFoldDB; Q15021; -. DR EMDB; EMD-10827; -. DR SMR; Q15021; -. DR BioGRID; 115246; 246. DR ComplexPortal; CPX-979; Condensin I complex. DR CORUM; Q15021; -. DR IntAct; Q15021; 47. DR MINT; Q15021; -. DR STRING; 9606.ENSP00000325017; -. DR GlyGen; Q15021; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q15021; -. DR MetOSite; Q15021; -. DR PhosphoSitePlus; Q15021; -. DR SwissPalm; Q15021; -. DR BioMuta; NCAPD2; -. DR DMDM; 259016362; -. DR EPD; Q15021; -. DR jPOST; Q15021; -. DR MassIVE; Q15021; -. DR MaxQB; Q15021; -. DR PaxDb; 9606-ENSP00000325017; -. DR PeptideAtlas; Q15021; -. DR ProteomicsDB; 60373; -. DR Pumba; Q15021; -. DR Antibodypedia; 22418; 161 antibodies from 28 providers. DR DNASU; 9918; -. DR Ensembl; ENST00000315579.10; ENSP00000325017.5; ENSG00000010292.13. DR GeneID; 9918; -. DR KEGG; hsa:9918; -. DR MANE-Select; ENST00000315579.10; ENSP00000325017.5; NM_014865.4; NP_055680.3. DR UCSC; uc001qoo.3; human. DR AGR; HGNC:24305; -. DR CTD; 9918; -. DR DisGeNET; 9918; -. DR GeneCards; NCAPD2; -. DR HGNC; HGNC:24305; NCAPD2. DR HPA; ENSG00000010292; Tissue enhanced (lymphoid). DR MalaCards; NCAPD2; -. DR MIM; 615638; gene. DR MIM; 617983; phenotype. DR neXtProt; NX_Q15021; -. DR OpenTargets; ENSG00000010292; -. DR PharmGKB; PA162397021; -. DR VEuPathDB; HostDB:ENSG00000010292; -. DR eggNOG; KOG0414; Eukaryota. DR GeneTree; ENSGT00940000153566; -. DR HOGENOM; CLU_001867_3_1_1; -. DR InParanoid; Q15021; -. DR OMA; CPLEKLW; -. DR OrthoDB; 5480287at2759; -. DR PhylomeDB; Q15021; -. DR TreeFam; TF105712; -. DR PathwayCommons; Q15021; -. DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes. DR SignaLink; Q15021; -. DR SIGNOR; Q15021; -. DR BioGRID-ORCS; 9918; 646 hits in 1163 CRISPR screens. DR ChiTaRS; NCAPD2; human. DR GeneWiki; NCAPD2; -. DR GenomeRNAi; 9918; -. DR Pharos; Q15021; Tbio. DR PRO; PR:Q15021; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q15021; Protein. DR Bgee; ENSG00000010292; Expressed in ventricular zone and 136 other cell types or tissues. DR ExpressionAtlas; Q15021; baseline and differential. 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; ISO:ComplexPortal. DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:1905821; P:positive regulation of chromosome condensation; IDA:ComplexPortal. DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISO:ComplexPortal. DR GO; GO:1905820; P:positive regulation of chromosome separation; ISO:ComplexPortal. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; CONDENSIN; 1. DR PANTHER; PTHR14222:SF2; CONDENSIN COMPLEX SUBUNIT 1; 1. DR Pfam; PF12717; Cnd1; 1. DR Pfam; PF12922; Cnd1_N; 1. DR PIRSF; PIRSF017127; Condensin_D2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q15021; HS. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Chromosome; Cytoplasm; KW Direct protein sequencing; Disease variant; DNA condensation; Mitosis; KW Nucleus; Phosphoprotein; Primary microcephaly; Reference proteome. FT CHAIN 1..1401 FT /note="Condensin complex subunit 1" FT /id="PRO_0000095035" FT REGION 1..603 FT /note="Interactions with SMC2 and SMC4" FT REGION 576..611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 956..978 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1303..1401 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1342..1362 FT /note="Bipartite nuclear localization signal" FT COMPBIAS 578..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 956..975 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1313..1339 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 585 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1331 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1339 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1366 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1367 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1371 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1376 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 1384 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000250" FT MOD_RES 1389 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000250" FT MOD_RES 1395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 8 FT /note="F -> S (in MCPH21; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28097321" FT /id="VAR_080953" FT VARIANT 83 FT /note="Q -> E (in dbSNP:rs714774)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8590280, ECO:0000269|Ref.3, FT ECO:0007744|PubMed:21269460" FT /id="VAR_024421" FT VARIANT 580 FT /note="K -> R (in dbSNP:rs17725914)" FT /id="VAR_057511" FT VARIANT 797 FT /note="V -> M (in dbSNP:rs10849482)" FT /id="VAR_024422" FT VARIANT 1321 FT /note="T -> S (in dbSNP:rs2240871)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_058713" FT MUTAGEN 1343..1348 FT /note="RRTTRR->AATTAA: Abolishes localization to the FT nucleus, while it only reduces chromosome binding." FT /evidence="ECO:0000269|PubMed:12138188" FT MUTAGEN 1358..1360 FT /note="KKK->AAA: Abolishes localization to the nucleus, FT while it only reduces chromosome binding." FT /evidence="ECO:0000269|PubMed:12138188" FT CONFLICT 1062 FT /note="M -> I (in Ref. 1; BAA09930)" FT /evidence="ECO:0000305" FT CONFLICT 1218 FT /note="R -> L (in Ref. 1; BAA09930)" FT /evidence="ECO:0000305" SQ SEQUENCE 1401 AA; 157182 MW; 35E31642B94B513D CRC64; MAPQMYEFHL PLSPEELLKS GGVNQYVVQE VLSIKHLPPQ LRAFQAAFRA QGPLAMLQHF DTIYSILHHF RSIDPGLKED TLQFLIKVVS RHSQELPAIL DDTTLSGSDR NAHLNALKMN CYALIRLLES FETMASQTNL VDLDLGGKGK KARTKAAHGF DWEEERQPIL QLLTQLLQLD IRHLWNHSII EEEFVSLVTG CCYRLLENPT INHQKNRPTR EAITHLLGVA LTRYNHMLSA TVKIIQMLQH FEHLAPVLVA AVSLWATDYG MKSIVGEIVR EIGQKCPQEL SRDPSGTKGF AAFLTELAER VPAILMSSMC ILLDHLDGEN YMMRNAVLAA MAEMVLQVLS GDQLEAAARD TRDQFLDTLQ AHGHDVNSFV RSRVLQLFTR IVQQKALPLT RFQAVVALAV GRLADKSVLV CKNAIQLLAS FLANNPFSCK LSDADLAGPL QKETQKLQEM RAQRRTAAAS AVLDPEEEWE AMLPELKSTL QQLLQLPQGE EEIPEQIANT ETTEDVKGRI YQLLAKASYK KAIILTREAT GHFQESEPFS HIDPEESEET RLLNILGLIF KGPAASTQEK NPRESTGNMV TGQTVCKNKP NMSDPEESRG NDELVKQEML VQYLQDAYSF SRKITEAIGI ISKMMYENTT TVVQEVIEFF VMVFQFGVPQ ALFGVRRMLP LIWSKEPGVR EAVLNAYRQL YLNPKGDSAR AKAQALIQNL SLLLVDASVG TIQCLEEILC EFVQKDELKP AVTQLLWERA TEKVACCPLE RCSSVMLLGM MARGKPEIVG SNLDTLVSIG LDEKFPQDYR LAQQVCHAIA NISDRRKPSL GKRHPPFRLP QEHRLFERLR ETVTKGFVHP DPLWIPFKEV AVTLIYQLAE GPEVICAQIL QGCAKQALEK LEEKRTSQED PKESPAMLPT FLLMNLLSLA GDVALQQLVH LEQAVSGELC RRRVLREEQE HKTKDPKEKN TSSETTMEEE LGLVGATADD TEAELIRGIC EMELLDGKQT LAAFVPLLLK VCNNPGLYSN PDLSAAASLA LGKFCMISAT FCDSQLRLLF TMLEKSPLPI VRSNLMVATG DLAIRFPNLV DPWTPHLYAR LRDPAQQVRK TAGLVMTHLI LKDMVKVKGQ VSEMAVLLID PEPQIAALAK NFFNELSHKG NAIYNLLPDI ISRLSDPELG VEEEPFHTIM KQLLSYITKD KQTESLVEKL CQRFRTSRTE RQQRDLAYCV SQLPLTERGL RKMLDNFDCF GDKLSDESIF SAFLSVVGKL RRGAKPEGKA IIDEFEQKLR ACHTRGLDGI KELEIGQAGS QRAPSAKKPS TGSRYQPLAS TASDNDFVTP EPRRTTRRHP NTQQRASKKK PKVVFSSDES SEEDLSAEMT EDETPKKTTP ILRASARRHR S //