CND1_HUMAN
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 03-AUG-2022, entry version 200.
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, ECO:0000312|HGNC:HGNC:24305};
GN 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};
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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 SMR; Q15021; -.
DR BioGRID; 115246; 162.
DR ComplexPortal; CPX-979; Condensin I complex.
DR CORUM; Q15021; -.
DR IntAct; Q15021; 46.
DR MINT; Q15021; -.
DR STRING; 9606.ENSP00000325017; -.
DR GlyGen; Q15021; 1 site, 1 O-linked glycan (1 site).
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; Q15021; -.
DR PeptideAtlas; Q15021; -.
DR PRIDE; Q15021; -.
DR ProteomicsDB; 60373; -.
DR Antibodypedia; 22418; 141 antibodies from 27 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 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; RNCVLQI; -.
DR OrthoDB; 166920at2759; -.
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; 615 hits in 1085 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 134 other tissues.
DR ExpressionAtlas; Q15021; baseline and differential.
DR Genevisible; Q15021; HS.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
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 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 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; found in two patients from a
FT consanguineous family; unknown pathological 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
