Full text data of NCAPH
NCAPH
(BRRN, BRRN1, CAPH, KIAA0074)
[Confidence: low (only semi-automatic identification from reviews)]
Condensin complex subunit 2 (Barren homolog protein 1; Chromosome-associated protein H; hCAP-H; Non-SMC condensin I complex subunit H; XCAP-H homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Condensin complex subunit 2 (Barren homolog protein 1; Chromosome-associated protein H; hCAP-H; Non-SMC condensin I complex subunit H; XCAP-H homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15003
ID CND2_HUMAN Reviewed; 741 AA.
AC Q15003; Q8TB87;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 118.
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; Synonyms=BRRN, BRRN1, CAPH, KIAA0074;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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-
RT H.";
RL Mol. Biol. Cell 12:3527-3537(2001).
RN [4]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND
RP NCAPG, 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 [5]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81;
RP SER-87; SER-92; SER-201; SER-432 AND THR-605, AND MASS SPECTROMETRY.
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 [7]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-25; THR-49;
RP SER-78; SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598,
RP AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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
CC in the presence of type II topoisomerases.
CC -!- SUBUNIT: Component of the condensin complex, which contains the
CC SMC2 and SMC4 heterodimer, and three non SMC subunits that
CC probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and
CC NCAPG.
CC -!- INTERACTION:
CC O00571:DDX3X; NbExp=2; IntAct=EBI-1046410, EBI-353779;
CC Q15021:NCAPD2; NbExp=4; IntAct=EBI-1046410, EBI-1044041;
CC Q9BPX3:NCAPG; NbExp=2; IntAct=EBI-1046410, EBI-970214;
CC O95347:SMC2; NbExp=2; IntAct=EBI-1046410, EBI-355822;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found
CC in the cytoplasm, while a minority of the complex is associated
CC with chromatin. A subpopulation of the complex however remains
CC associated with chromosome foci in interphase cells. During
CC mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of
CC the complex are phosphorylated by CDK1, leading to condensin's
CC association with chromosome arms and to chromosome condensation.
CC Dissociation from chromosomes is observed in late telophase.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in
CC proliferating cells.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that
CC of NCAPD2 and NCAPG subunits, activates the condensin complex and
CC is required for chromosome condensation (By similarity).
CC -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07556.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D38553; BAA07556.1; ALT_INIT; mRNA.
DR EMBL; BC024211; AAH24211.1; -; mRNA.
DR RefSeq; NP_001268639.1; NM_001281710.1.
DR RefSeq; NP_001268640.1; NM_001281711.1.
DR RefSeq; NP_056156.2; NM_015341.4.
DR UniGene; Hs.308045; -.
DR ProteinModelPortal; Q15003; -.
DR DIP; DIP-43899N; -.
DR IntAct; Q15003; 7.
DR MINT; MINT-5004625; -.
DR STRING; 9606.ENSP00000240423; -.
DR PhosphoSite; Q15003; -.
DR DMDM; 116241306; -.
DR PaxDb; Q15003; -.
DR PeptideAtlas; Q15003; -.
DR PRIDE; Q15003; -.
DR DNASU; 23397; -.
DR Ensembl; ENST00000240423; ENSP00000240423; ENSG00000121152.
DR GeneID; 23397; -.
DR KEGG; hsa:23397; -.
DR UCSC; uc002svz.1; human.
DR CTD; 23397; -.
DR GeneCards; GC02P097001; -.
DR HGNC; HGNC:1112; NCAPH.
DR HPA; HPA002647; -.
DR HPA; HPA003008; -.
DR MIM; 602332; gene.
DR neXtProt; NX_Q15003; -.
DR PharmGKB; PA162397273; -.
DR eggNOG; COG5229; -.
DR HOGENOM; HOG000231887; -.
DR HOVERGEN; HBG036823; -.
DR InParanoid; Q15003; -.
DR KO; K06676; -.
DR OMA; SERVFPM; -.
DR OrthoDB; EOG7JMGDB; -.
DR PhylomeDB; Q15003; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR GeneWiki; NCAPH; -.
DR GenomeRNAi; 23397; -.
DR NextBio; 45541; -.
DR PMAP-CutDB; Q15003; -.
DR PRO; PR:Q15003; -.
DR ArrayExpress; Q15003; -.
DR Bgee; Q15003; -.
DR CleanEx; HS_NCAPH; -.
DR Genevestigator; Q15003; -.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR InterPro; IPR022816; Condensin_barren_su2.
DR Pfam; PF05786; Cnd2; 1.
DR PIRSF; PIRSF017126; Condensin_H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Chromosome; Complete proteome;
KW Cytoplasm; DNA condensation; Mitosis; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 741 Condensin complex subunit 2.
FT /FTId=PRO_0000095038.
FT MOD_RES 15 15 Phosphoserine.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 49 49 Phosphothreonine.
FT MOD_RES 70 70 Phosphoserine.
FT MOD_RES 78 78 Phosphoserine.
FT MOD_RES 81 81 Phosphoserine.
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 92 92 Phosphoserine.
FT MOD_RES 96 96 Phosphoserine.
FT MOD_RES 201 201 Phosphoserine.
FT MOD_RES 432 432 Phosphoserine.
FT MOD_RES 598 598 Phosphothreonine.
FT MOD_RES 605 605 Phosphothreonine.
FT MOD_RES 637 637 N6-acetyllysine.
FT VARIANT 539 539 V -> A (in dbSNP:rs2305935).
FT /FTId=VAR_027882.
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
//
ID CND2_HUMAN Reviewed; 741 AA.
AC Q15003; Q8TB87;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 118.
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; Synonyms=BRRN, BRRN1, CAPH, KIAA0074;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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-
RT H.";
RL Mol. Biol. Cell 12:3527-3537(2001).
RN [4]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND
RP NCAPG, 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 [5]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81;
RP SER-87; SER-92; SER-201; SER-432 AND THR-605, AND MASS SPECTROMETRY.
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 [7]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-25; THR-49;
RP SER-78; SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598,
RP AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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
CC in the presence of type II topoisomerases.
CC -!- SUBUNIT: Component of the condensin complex, which contains the
CC SMC2 and SMC4 heterodimer, and three non SMC subunits that
CC probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and
CC NCAPG.
CC -!- INTERACTION:
CC O00571:DDX3X; NbExp=2; IntAct=EBI-1046410, EBI-353779;
CC Q15021:NCAPD2; NbExp=4; IntAct=EBI-1046410, EBI-1044041;
CC Q9BPX3:NCAPG; NbExp=2; IntAct=EBI-1046410, EBI-970214;
CC O95347:SMC2; NbExp=2; IntAct=EBI-1046410, EBI-355822;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found
CC in the cytoplasm, while a minority of the complex is associated
CC with chromatin. A subpopulation of the complex however remains
CC associated with chromosome foci in interphase cells. During
CC mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of
CC the complex are phosphorylated by CDK1, leading to condensin's
CC association with chromosome arms and to chromosome condensation.
CC Dissociation from chromosomes is observed in late telophase.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in
CC proliferating cells.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that
CC of NCAPD2 and NCAPG subunits, activates the condensin complex and
CC is required for chromosome condensation (By similarity).
CC -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07556.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D38553; BAA07556.1; ALT_INIT; mRNA.
DR EMBL; BC024211; AAH24211.1; -; mRNA.
DR RefSeq; NP_001268639.1; NM_001281710.1.
DR RefSeq; NP_001268640.1; NM_001281711.1.
DR RefSeq; NP_056156.2; NM_015341.4.
DR UniGene; Hs.308045; -.
DR ProteinModelPortal; Q15003; -.
DR DIP; DIP-43899N; -.
DR IntAct; Q15003; 7.
DR MINT; MINT-5004625; -.
DR STRING; 9606.ENSP00000240423; -.
DR PhosphoSite; Q15003; -.
DR DMDM; 116241306; -.
DR PaxDb; Q15003; -.
DR PeptideAtlas; Q15003; -.
DR PRIDE; Q15003; -.
DR DNASU; 23397; -.
DR Ensembl; ENST00000240423; ENSP00000240423; ENSG00000121152.
DR GeneID; 23397; -.
DR KEGG; hsa:23397; -.
DR UCSC; uc002svz.1; human.
DR CTD; 23397; -.
DR GeneCards; GC02P097001; -.
DR HGNC; HGNC:1112; NCAPH.
DR HPA; HPA002647; -.
DR HPA; HPA003008; -.
DR MIM; 602332; gene.
DR neXtProt; NX_Q15003; -.
DR PharmGKB; PA162397273; -.
DR eggNOG; COG5229; -.
DR HOGENOM; HOG000231887; -.
DR HOVERGEN; HBG036823; -.
DR InParanoid; Q15003; -.
DR KO; K06676; -.
DR OMA; SERVFPM; -.
DR OrthoDB; EOG7JMGDB; -.
DR PhylomeDB; Q15003; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR GeneWiki; NCAPH; -.
DR GenomeRNAi; 23397; -.
DR NextBio; 45541; -.
DR PMAP-CutDB; Q15003; -.
DR PRO; PR:Q15003; -.
DR ArrayExpress; Q15003; -.
DR Bgee; Q15003; -.
DR CleanEx; HS_NCAPH; -.
DR Genevestigator; Q15003; -.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR InterPro; IPR022816; Condensin_barren_su2.
DR Pfam; PF05786; Cnd2; 1.
DR PIRSF; PIRSF017126; Condensin_H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Chromosome; Complete proteome;
KW Cytoplasm; DNA condensation; Mitosis; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 741 Condensin complex subunit 2.
FT /FTId=PRO_0000095038.
FT MOD_RES 15 15 Phosphoserine.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 49 49 Phosphothreonine.
FT MOD_RES 70 70 Phosphoserine.
FT MOD_RES 78 78 Phosphoserine.
FT MOD_RES 81 81 Phosphoserine.
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 92 92 Phosphoserine.
FT MOD_RES 96 96 Phosphoserine.
FT MOD_RES 201 201 Phosphoserine.
FT MOD_RES 432 432 Phosphoserine.
FT MOD_RES 598 598 Phosphothreonine.
FT MOD_RES 605 605 Phosphothreonine.
FT MOD_RES 637 637 N6-acetyllysine.
FT VARIANT 539 539 V -> A (in dbSNP:rs2305935).
FT /FTId=VAR_027882.
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
//
MIM
602332
*RECORD*
*FIELD* NO
602332
*FIELD* TI
*602332 NON-SMC CONDENSIN I COMPLEX SUBUNIT H; NCAPH
;;CONDENSIN I COMPLEX, NON-SMC SUBUNIT H;;
read moreCHROMOSOME-ASSOCIATED PROTEIN H; CAPH;;
BARREN, DROSOPHILA, HOMOLOG OF, 1; BRRN1
*FIELD* TX
CLONING
Bhat et al. (1996) established that in Drosophila the product of 'barr'
(barren) is necessary for sister chromatid separation and modulates
topoisomerase II (126430) activity. The barr gene is evolutionarily
conserved and sequence similarity searches identified a 2.7-kb human
homolog.
MAPPING
Cabello et al. (1997) reported the genomic localization of this human
member of the barr gene family, symbolized BRRN1 by them. By Southern
analysis of monochromosomal human/rodent hybrid cells, they mapped the
BRRN1 gene to chromosome 2. By fluorescence in situ hybridization, they
localized the assignment to 2q11.2. This assignment was confirmed and
refined by radiation hybrid analysis.
GENE FUNCTION
Aono et al. (2002) reported that Cnd2, the fission yeast homolog of
Drosophila barren and the budding yeast protein Brn1, is required for
both interphase and mitotic condensation. In Cnd2 mutants,
ultraviolet-induced DNA damage was not repaired and cells arrested by
hydroxyurea did not recover. Cds1 (604373) activation was abolished in
the presence of hydroxyurea in Cnd2 mutant cells and in cells where
other condensin subunits had been disrupted. In the absence of
hydroxyurea, a G2 checkpoint delay occurred in Cnd2 mutants in a manner
dependent on Cds1 and Rad3 but not Chk1 (603078), before the mitotic
condensation defect. Furthermore, the Cnd2 mutation was synthetic-lethal
with mutations of excision repair, RecQ helicase (see 600537), and DNA
replication enzymes.
*FIELD* RF
1. Aono, N.; Sutani, T.; Tomonaga, T.; Mochida, S.; Yanagida, M.:
Cnd2 has dual roles in mitotic condensation and interphase. Nature 417:
197-202, 2002.
2. Bhat, M. A.; Philp, A. V.; Glover, D. M.; Bellen, H. J.: Chromatid
segregation at anaphase requires the barren product, a novel chromosome-associated
protein that interacts with topoisomerase II. Cell 87: 1103-1114,
1996.
3. Cabello, O. A.; Baldini, A.; Bhat, M.; Bellen, H.; Belmont, J.
W.: Localization of BRRN1, the human homologue of Drosophila barr,
to 2q11.2. Genomics 46: 311-313, 1997.
*FIELD* CN
Ada Hamosh - updated: 5/28/2002
*FIELD* CD
Victor A. McKusick: 2/9/1998
*FIELD* ED
mgross: 07/20/2007
alopez: 5/31/2002
terry: 5/28/2002
dholmes: 3/10/1998
mark: 2/19/1998
mark: 2/18/1998
mark: 2/9/1998
*RECORD*
*FIELD* NO
602332
*FIELD* TI
*602332 NON-SMC CONDENSIN I COMPLEX SUBUNIT H; NCAPH
;;CONDENSIN I COMPLEX, NON-SMC SUBUNIT H;;
read moreCHROMOSOME-ASSOCIATED PROTEIN H; CAPH;;
BARREN, DROSOPHILA, HOMOLOG OF, 1; BRRN1
*FIELD* TX
CLONING
Bhat et al. (1996) established that in Drosophila the product of 'barr'
(barren) is necessary for sister chromatid separation and modulates
topoisomerase II (126430) activity. The barr gene is evolutionarily
conserved and sequence similarity searches identified a 2.7-kb human
homolog.
MAPPING
Cabello et al. (1997) reported the genomic localization of this human
member of the barr gene family, symbolized BRRN1 by them. By Southern
analysis of monochromosomal human/rodent hybrid cells, they mapped the
BRRN1 gene to chromosome 2. By fluorescence in situ hybridization, they
localized the assignment to 2q11.2. This assignment was confirmed and
refined by radiation hybrid analysis.
GENE FUNCTION
Aono et al. (2002) reported that Cnd2, the fission yeast homolog of
Drosophila barren and the budding yeast protein Brn1, is required for
both interphase and mitotic condensation. In Cnd2 mutants,
ultraviolet-induced DNA damage was not repaired and cells arrested by
hydroxyurea did not recover. Cds1 (604373) activation was abolished in
the presence of hydroxyurea in Cnd2 mutant cells and in cells where
other condensin subunits had been disrupted. In the absence of
hydroxyurea, a G2 checkpoint delay occurred in Cnd2 mutants in a manner
dependent on Cds1 and Rad3 but not Chk1 (603078), before the mitotic
condensation defect. Furthermore, the Cnd2 mutation was synthetic-lethal
with mutations of excision repair, RecQ helicase (see 600537), and DNA
replication enzymes.
*FIELD* RF
1. Aono, N.; Sutani, T.; Tomonaga, T.; Mochida, S.; Yanagida, M.:
Cnd2 has dual roles in mitotic condensation and interphase. Nature 417:
197-202, 2002.
2. Bhat, M. A.; Philp, A. V.; Glover, D. M.; Bellen, H. J.: Chromatid
segregation at anaphase requires the barren product, a novel chromosome-associated
protein that interacts with topoisomerase II. Cell 87: 1103-1114,
1996.
3. Cabello, O. A.; Baldini, A.; Bhat, M.; Bellen, H.; Belmont, J.
W.: Localization of BRRN1, the human homologue of Drosophila barr,
to 2q11.2. Genomics 46: 311-313, 1997.
*FIELD* CN
Ada Hamosh - updated: 5/28/2002
*FIELD* CD
Victor A. McKusick: 2/9/1998
*FIELD* ED
mgross: 07/20/2007
alopez: 5/31/2002
terry: 5/28/2002
dholmes: 3/10/1998
mark: 2/19/1998
mark: 2/18/1998
mark: 2/9/1998