CND2_HUMAN
ID CND2_HUMAN Reviewed; 741 AA.
AC Q15003; B4E189; Q8TB87;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Condensin complex subunit 2;
DE AltName: Full=Barren homolog protein 1;
DE AltName: Full=Chromosome-associated protein H;
DE Short=hCAP-H;
DE AltName: Full=Non-SMC condensin I complex subunit H;
DE AltName: Full=XCAP-H homolog;
GN Name=NCAPH {ECO:0000303|PubMed:27737959, ECO:0000312|HGNC:HGNC:1112};
GN Synonyms=BRRN, BRRN1, CAPH, KIAA0074;
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].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-539.
RC TISSUE=Placenta;
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 SUBCELLULAR LOCATION DURING THE CELL CYCLE, AND TISSUE SPECIFICITY.
RX PubMed=11694586; DOI=10.1091/mbc.12.11.3527;
RA Cabello O.A., Eliseeva E., He W.G., Youssoufian H., Plon S.E.,
RA Brinkley B.R., Belmont J.W.;
RT "Cell cycle-dependent expression and nucleolar localization of hCAP-H.";
RL Mol. Biol. Cell 12:3527-3537(2001).
RN [6]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND NCAPG,
RP AND FUNCTION OF THE 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 IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81; SER-87;
RP SER-92; SER-201; SER-432 AND THR-605, AND IDENTIFICATION BY MASS
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-25; THR-49; SER-78;
RP SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598, AND
RP 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 [13]
RP IDENTIFICATION BY MASS 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 [14]
RP IDENTIFICATION BY 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-70; SER-78; SER-81;
RP SER-87; SER-89; SER-92; SER-201; SER-233; SER-496 AND THR-605, AND
RP IDENTIFICATION BY 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP INVOLVEMENT IN MCPH23, VARIANT MCPH23 LEU-243, CHARACTERIZATION OF VARIANT
RP MCPH23 LEU-243, 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).
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 (PubMed:11136719). Early in
CC neurogenesis, may play an essential role to ensure accurate mitotic
CC chromosome condensation in neuron stem cells, ultimately affecting
CC neuron pool and cortex size (PubMed:27737959).
CC {ECO:0000269|PubMed:11136719, 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.
CC {ECO:0000269|PubMed:11136719}.
CC -!- INTERACTION:
CC Q15003; O00571: DDX3X; NbExp=2; IntAct=EBI-1046410, EBI-353779;
CC Q15003; Q15021: NCAPD2; NbExp=7; IntAct=EBI-1046410, EBI-1044041;
CC Q15003; Q9BPX3: NCAPG; NbExp=8; IntAct=EBI-1046410, EBI-970214;
CC Q15003; O95347: SMC2; NbExp=5; IntAct=EBI-1046410, EBI-355822;
CC Q15003; Q9NTJ3: SMC4; NbExp=3; IntAct=EBI-1046410, EBI-356173;
CC Q15003; P04910: hta2; Xeno; NbExp=2; IntAct=EBI-1046410, EBI-15929287;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11694586}. Cytoplasm
CC {ECO:0000269|PubMed:11694586}. Chromosome
CC {ECO:0000269|PubMed:11694586}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15003-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15003-2; Sequence=VSP_055179;
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in
CC proliferating cells. {ECO:0000269|PubMed:11694586}.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC NCAPD2 and NCAPG subunits, activates the condensin complex and is
CC required for chromosome condensation (By similarity). {ECO:0000250}.
CC -!- DISEASE: Microcephaly 23, primary, autosomal recessive (MCPH23)
CC [MIM:617985]: 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.
CC {ECO:0000269|PubMed:27737959}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07556.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D38553; BAA07556.1; ALT_INIT; mRNA.
DR EMBL; AK303725; BAG64701.1; -; mRNA.
DR EMBL; AC021188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024211; AAH24211.1; -; mRNA.
DR CCDS; CCDS2021.1; -. [Q15003-1]
DR CCDS; CCDS62960.1; -. [Q15003-2]
DR RefSeq; NP_001268639.1; NM_001281710.1.
DR RefSeq; NP_001268640.1; NM_001281711.1.
DR RefSeq; NP_001268641.1; NM_001281712.1. [Q15003-2]
DR RefSeq; NP_056156.2; NM_015341.4. [Q15003-1]
DR PDB; 6IGX; X-ray; 3.00 A; A/C=470-526.
DR PDBsum; 6IGX; -.
DR AlphaFoldDB; Q15003; -.
DR SMR; Q15003; -.
DR BioGRID; 116970; 97.
DR ComplexPortal; CPX-979; Condensin I complex.
DR CORUM; Q15003; -.
DR DIP; DIP-43899N; -.
DR IntAct; Q15003; 43.
DR MINT; Q15003; -.
DR STRING; 9606.ENSP00000240423; -.
DR GlyGen; Q15003; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15003; -.
DR MetOSite; Q15003; -.
DR PhosphoSitePlus; Q15003; -.
DR BioMuta; NCAPH; -.
DR DMDM; 116241306; -.
DR EPD; Q15003; -.
DR jPOST; Q15003; -.
DR MassIVE; Q15003; -.
DR MaxQB; Q15003; -.
DR PaxDb; Q15003; -.
DR PeptideAtlas; Q15003; -.
DR PRIDE; Q15003; -.
DR ProteomicsDB; 5736; -.
DR ProteomicsDB; 60354; -. [Q15003-1]
DR Antibodypedia; 1231; 352 antibodies from 38 providers.
DR DNASU; 23397; -.
DR Ensembl; ENST00000240423.9; ENSP00000240423.4; ENSG00000121152.10. [Q15003-1]
DR Ensembl; ENST00000427946.5; ENSP00000400774.1; ENSG00000121152.10. [Q15003-2]
DR GeneID; 23397; -.
DR KEGG; hsa:23397; -.
DR MANE-Select; ENST00000240423.9; ENSP00000240423.4; NM_015341.5; NP_056156.2.
DR UCSC; uc002svz.3; human. [Q15003-1]
DR CTD; 23397; -.
DR DisGeNET; 23397; -.
DR GeneCards; NCAPH; -.
DR HGNC; HGNC:1112; NCAPH.
DR HPA; ENSG00000121152; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MalaCards; NCAPH; -.
DR MIM; 602332; gene.
DR MIM; 617985; phenotype.
DR neXtProt; NX_Q15003; -.
DR OpenTargets; ENSG00000121152; -.
DR PharmGKB; PA162397273; -.
DR VEuPathDB; HostDB:ENSG00000121152; -.
DR eggNOG; KOG2328; Eukaryota.
DR GeneTree; ENSGT00390000004149; -.
DR InParanoid; Q15003; -.
DR OMA; KPKAKMG; -.
DR OrthoDB; 702078at2759; -.
DR PhylomeDB; Q15003; -.
DR TreeFam; TF105678; -.
DR PathwayCommons; Q15003; -.
DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR SignaLink; Q15003; -.
DR SIGNOR; Q15003; -.
DR BioGRID-ORCS; 23397; 680 hits in 1085 CRISPR screens.
DR ChiTaRS; NCAPH; human.
DR GeneWiki; NCAPH; -.
DR GenomeRNAi; 23397; -.
DR Pharos; Q15003; Tbio.
DR PRO; PR:Q15003; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15003; protein.
DR Bgee; ENSG00000121152; Expressed in ventricular zone and 101 other tissues.
DR ExpressionAtlas; Q15003; baseline and differential.
DR Genevisible; Q15003; HS.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0000796; C:condensin complex; IDA: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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051309; P:female meiosis chromosome separation; IEA:Ensembl.
DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IEA:Ensembl.
DR InterPro; IPR022816; Condensin_barren_su2.
DR PANTHER; PTHR13108; PTHR13108; 1.
DR Pfam; PF05786; Cnd2; 1.
DR PIRSF; PIRSF017126; Condensin_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Chromosome; Cytoplasm; Disease variant; DNA condensation; Isopeptide bond;
KW Mitosis; Nucleus; Phosphoprotein; Primary microcephaly; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..741
FT /note="Condensin complex subunit 2"
FT /id="PRO_0000095038"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C156"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 605
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 637
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055179"
FT VARIANT 243
FT /note="P -> L (in MCPH23; impairs mitotic chromosome
FT compaction; dbSNP:rs1553446603)"
FT /evidence="ECO:0000269|PubMed:27737959"
FT /id="VAR_080954"
FT VARIANT 539
FT /note="V -> A (in dbSNP:rs2305935)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027882"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:6IGX"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:6IGX"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:6IGX"
SQ SEQUENCE 741 AA; 82563 MW; B5B34A36CAE0C28E CRC64;
MGPPGPALPA TMNNSSSETR GHPHSASSPS ERVFPMPLPR KAPLNIPGTP VLEDFPQNDD
EKERLQRRRS RVFDLQFSTD SPRLLASPSS RSIDISATIP KFTNTQITEH YSTCIKLSTE
NKITTKNAFG LHLIDFMSEI LKQKDTEPTN FKVAAGTLDA STKIYAVRVD AVHADVYRVL
GGLGKDAPSL EEVEGHVADG SATEMGTTKK AVKPKKKHLH RTIEQNINNL NVSEADRKCE
IDPMFQKTAA SFDECSTAGV FLSTLHCQDY RSELLFPSDV QTLSTGEPLE LPELGCVEMT
DLKAPLQQCA EDRQICPSLA GFQFTQWDSE THNESVSALV DKFKKNDQVF DINAEVDESD
CGDFPDGSLG DDFDANDEPD HTAVGDHEEF RSWKEPCQVQ SCQEEMISLG DGDIRTMCPL
LSMKPGEYSY FSPRTMSMWA GPDHWRFRPR RKQDAPSQSE NKKKSTKKDF EIDFEDDIDF
DVYFRKTKAA TILTKSTLEN QNWRATTLPT DFNYNVDTLV QLHLKPGTRL LKMAQGHRVE
TEHYEEIEDY DYNNPNDTSN FCPGLQAADS DDEDLDDLFV GPVGNSDLSP YPCHPPKTAQ
QNGDTPEAQG LDITTYGESN LVAEPQKVNK IEIHYAKTAK KMDMKKLKQS MWSLLTALSG
KEADAEANHR EAGKEAALAE VADEKMLSGL TKDLQRSLPP VMAQNLSIPL AFACLLHLAN
EKNLKLEGTE DLSDVLVRQG D
