Full text data of NCAPG
NCAPG
(CAPG, NYMEL3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Condensin complex subunit 3 (Chromosome-associated protein G; Condensin subunit CAP-G; hCAP-G; Melanoma antigen NY-MEL-3; Non-SMC condensin I complex subunit G; XCAP-G homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Condensin complex subunit 3 (Chromosome-associated protein G; Condensin subunit CAP-G; hCAP-G; Melanoma antigen NY-MEL-3; Non-SMC condensin I complex subunit G; XCAP-G homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BPX3
ID CND3_HUMAN Reviewed; 1015 AA.
AC Q9BPX3; Q3MJE0; Q96SV9; Q9BUR3; Q9BVY1; Q9H914; Q9H9Z6; Q9HBI9;
read moreDT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Condensin complex subunit 3;
DE AltName: Full=Chromosome-associated protein G;
DE AltName: Full=Condensin subunit CAP-G;
DE Short=hCAP-G;
DE AltName: Full=Melanoma antigen NY-MEL-3;
DE AltName: Full=Non-SMC condensin I complex subunit G;
DE AltName: Full=XCAP-G homolog;
GN Name=NCAPG; Synonyms=CAPG, NYMEL3;
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 [MRNA], TISSUE SPECIFICITY, AND VARIANT ILE-581.
RC TISSUE=Melanocyte;
RX PubMed=10910072;
RA Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A.,
RA Old L.J., Chen Y.-T.;
RT "Serological cloning of a melanocyte rab guanosine 5'-triphosphate-
RT binding protein and a chromosome condensation protein from a melanoma
RT complementary DNA library.";
RL Cancer Res. 60:3584-3591(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A CONDENSIN COMPLEX WITH
RP SMC2; SMC4; NCAPD2 AND NCAPH, 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythroleukemia;
RA Minami T., Doi T., Tachibana K., Okada Y.;
RT "Differentiation responsive gene.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-973; SER-975
RP AND SER-1002, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674 AND
RP SER-1015, AND MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674; THR-931
RP AND SER-1015, 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 [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.,
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP MASS SPECTROMETRY.
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 [15]
RP VARIANT [LARGE SCALE ANALYSIS] THR-265.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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 Q15021:NCAPD2; NbExp=2; IntAct=EBI-970214, EBI-1044041;
CC Q15003:NCAPH; NbExp=2; IntAct=EBI-970214, EBI-1046410;
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: Highly expressed in testis.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that
CC of NCAPD2 and NCAPH subunits, activates the condensin complex and
CC is required for chromosome condensation (By similarity).
CC -!- MISCELLANEOUS: Overexpressed in some cancer lines and some tumor
CC cells.
CC -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC -!- SIMILARITY: Contains 10 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00827.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14429.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55165.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF235023; AAG30732.1; -; mRNA.
DR EMBL; AF331796; AAG49627.1; -; mRNA.
DR EMBL; AB013299; BAB21557.1; -; mRNA.
DR EMBL; AK022512; BAB14069.1; -; mRNA.
DR EMBL; AK023147; BAB14429.1; ALT_INIT; mRNA.
DR EMBL; AK027511; BAB55165.1; ALT_INIT; mRNA.
DR EMBL; BC000827; AAH00827.1; ALT_INIT; mRNA.
DR EMBL; BC101476; AAI01477.1; -; mRNA.
DR RefSeq; NP_071741.2; NM_022346.4.
DR UniGene; Hs.567567; -.
DR ProteinModelPortal; Q9BPX3; -.
DR IntAct; Q9BPX3; 8.
DR MINT; MINT-3060256; -.
DR STRING; 9606.ENSP00000251496; -.
DR PhosphoSite; Q9BPX3; -.
DR DMDM; 30172941; -.
DR PaxDb; Q9BPX3; -.
DR PeptideAtlas; Q9BPX3; -.
DR PRIDE; Q9BPX3; -.
DR Ensembl; ENST00000251496; ENSP00000251496; ENSG00000109805.
DR GeneID; 64151; -.
DR KEGG; hsa:64151; -.
DR UCSC; uc003gpp.4; human.
DR CTD; 64151; -.
DR GeneCards; GC04P017812; -.
DR HGNC; HGNC:24304; NCAPG.
DR HPA; HPA039613; -.
DR HPA; HPA040103; -.
DR MIM; 606280; gene.
DR neXtProt; NX_Q9BPX3; -.
DR PharmGKB; PA162397165; -.
DR eggNOG; COG5218; -.
DR HOVERGEN; HBG039407; -.
DR InParanoid; Q9BPX3; -.
DR KO; K06678; -.
DR OMA; EACCYEP; -.
DR OrthoDB; EOG7CVPWZ; -.
DR PhylomeDB; Q9BPX3; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR GeneWiki; NCAPG; -.
DR GenomeRNAi; 64151; -.
DR NextBio; 66065; -.
DR PRO; PR:Q9BPX3; -.
DR ArrayExpress; Q9BPX3; -.
DR Bgee; Q9BPX3; -.
DR CleanEx; HS_CAPG; -.
DR CleanEx; HS_NCAPG; -.
DR Genevestigator; Q9BPX3; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
KW DNA condensation; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 1015 Condensin complex subunit 3.
FT /FTId=PRO_0000095041.
FT REPEAT 94 131 HEAT 1.
FT REPEAT 138 173 HEAT 2.
FT REPEAT 174 212 HEAT 3.
FT REPEAT 238 275 HEAT 4.
FT REPEAT 276 313 HEAT 5.
FT REPEAT 399 436 HEAT 6.
FT REPEAT 439 478 HEAT 7.
FT REPEAT 617 654 HEAT 8.
FT REPEAT 687 724 HEAT 9.
FT REPEAT 865 907 HEAT 10.
FT COMPBIAS 88 91 Poly-Glu.
FT COMPBIAS 912 917 Poly-Thr.
FT MOD_RES 390 390 Phosphoserine.
FT MOD_RES 674 674 Phosphoserine.
FT MOD_RES 931 931 Phosphothreonine.
FT MOD_RES 973 973 Phosphoserine.
FT MOD_RES 975 975 Phosphoserine.
FT MOD_RES 1002 1002 Phosphoserine.
FT MOD_RES 1015 1015 Phosphoserine.
FT VARIANT 64 64 A -> P (in dbSNP:rs35722563).
FT /FTId=VAR_053041.
FT VARIANT 265 265 M -> T (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036125.
FT VARIANT 581 581 M -> I (in dbSNP:rs3795243).
FT /FTId=VAR_053042.
FT CONFLICT 115 115 R -> G (in Ref. 4; BAB14069).
FT CONFLICT 276 276 F -> V (in Ref. 1; AAG30732).
FT CONFLICT 519 519 S -> P (in Ref. 4; BAB55165).
FT CONFLICT 676 676 D -> V (in Ref. 4; BAB14069).
FT CONFLICT 681 681 K -> R (in Ref. 4; BAB14069).
FT CONFLICT 704 704 V -> A (in Ref. 4; BAB14069).
FT CONFLICT 836 836 N -> D (in Ref. 4; BAB55165).
FT CONFLICT 1010 1010 L -> F (in Ref. 1; AAG30732).
SQ SEQUENCE 1015 AA; 114334 MW; D9ACC205C48F3AF5 CRC64;
MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH YLKYVMVVYK
REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF TFLLKSHEAN SNAVRFRVCL
LINKLLGSMP ENAQIDDDVF DKINKAMLIR LKDKIPNVRI QAVLALSRLQ DPKDDECPVV
NAYATLIEND SNPEVRRAVL SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA
MSIAQRVMLL QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV
LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG DEGEEFLEQI
LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF IGQQLILIIK SLDTSEEGGR
KKLLAVLQEI LILPTIPISL VSFLVERLLH IIIDDNKRTQ IVTEIISEIR APIVTVGVNN
DPADVRKKEL KMAEIKVKLI EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE
QLEIKEVHIE KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV
RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM TFGIEPFKTK
KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL DSEVSELRTG AAEGLAKLMF
SGLLVSSRIL SRLILLWYNP VTEEDVQLRH CLGVFFPVFA YASRTNQECF EEAFLPTLQT
LANAPASSPL AEIDITNVAE LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT
SPCSPEIRVY TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE
FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN RGQRKVTVSA
RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE KSKLNLAQFL NEDLS
//
ID CND3_HUMAN Reviewed; 1015 AA.
AC Q9BPX3; Q3MJE0; Q96SV9; Q9BUR3; Q9BVY1; Q9H914; Q9H9Z6; Q9HBI9;
read moreDT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Condensin complex subunit 3;
DE AltName: Full=Chromosome-associated protein G;
DE AltName: Full=Condensin subunit CAP-G;
DE Short=hCAP-G;
DE AltName: Full=Melanoma antigen NY-MEL-3;
DE AltName: Full=Non-SMC condensin I complex subunit G;
DE AltName: Full=XCAP-G homolog;
GN Name=NCAPG; Synonyms=CAPG, NYMEL3;
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 [MRNA], TISSUE SPECIFICITY, AND VARIANT ILE-581.
RC TISSUE=Melanocyte;
RX PubMed=10910072;
RA Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A.,
RA Old L.J., Chen Y.-T.;
RT "Serological cloning of a melanocyte rab guanosine 5'-triphosphate-
RT binding protein and a chromosome condensation protein from a melanoma
RT complementary DNA library.";
RL Cancer Res. 60:3584-3591(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A CONDENSIN COMPLEX WITH
RP SMC2; SMC4; NCAPD2 AND NCAPH, 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythroleukemia;
RA Minami T., Doi T., Tachibana K., Okada Y.;
RT "Differentiation responsive gene.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-973; SER-975
RP AND SER-1002, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674 AND
RP SER-1015, AND MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674; THR-931
RP AND SER-1015, 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 [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.,
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP MASS SPECTROMETRY.
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 [15]
RP VARIANT [LARGE SCALE ANALYSIS] THR-265.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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 Q15021:NCAPD2; NbExp=2; IntAct=EBI-970214, EBI-1044041;
CC Q15003:NCAPH; NbExp=2; IntAct=EBI-970214, EBI-1046410;
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: Highly expressed in testis.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that
CC of NCAPD2 and NCAPH subunits, activates the condensin complex and
CC is required for chromosome condensation (By similarity).
CC -!- MISCELLANEOUS: Overexpressed in some cancer lines and some tumor
CC cells.
CC -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC -!- SIMILARITY: Contains 10 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00827.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14429.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55165.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF235023; AAG30732.1; -; mRNA.
DR EMBL; AF331796; AAG49627.1; -; mRNA.
DR EMBL; AB013299; BAB21557.1; -; mRNA.
DR EMBL; AK022512; BAB14069.1; -; mRNA.
DR EMBL; AK023147; BAB14429.1; ALT_INIT; mRNA.
DR EMBL; AK027511; BAB55165.1; ALT_INIT; mRNA.
DR EMBL; BC000827; AAH00827.1; ALT_INIT; mRNA.
DR EMBL; BC101476; AAI01477.1; -; mRNA.
DR RefSeq; NP_071741.2; NM_022346.4.
DR UniGene; Hs.567567; -.
DR ProteinModelPortal; Q9BPX3; -.
DR IntAct; Q9BPX3; 8.
DR MINT; MINT-3060256; -.
DR STRING; 9606.ENSP00000251496; -.
DR PhosphoSite; Q9BPX3; -.
DR DMDM; 30172941; -.
DR PaxDb; Q9BPX3; -.
DR PeptideAtlas; Q9BPX3; -.
DR PRIDE; Q9BPX3; -.
DR Ensembl; ENST00000251496; ENSP00000251496; ENSG00000109805.
DR GeneID; 64151; -.
DR KEGG; hsa:64151; -.
DR UCSC; uc003gpp.4; human.
DR CTD; 64151; -.
DR GeneCards; GC04P017812; -.
DR HGNC; HGNC:24304; NCAPG.
DR HPA; HPA039613; -.
DR HPA; HPA040103; -.
DR MIM; 606280; gene.
DR neXtProt; NX_Q9BPX3; -.
DR PharmGKB; PA162397165; -.
DR eggNOG; COG5218; -.
DR HOVERGEN; HBG039407; -.
DR InParanoid; Q9BPX3; -.
DR KO; K06678; -.
DR OMA; EACCYEP; -.
DR OrthoDB; EOG7CVPWZ; -.
DR PhylomeDB; Q9BPX3; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR GeneWiki; NCAPG; -.
DR GenomeRNAi; 64151; -.
DR NextBio; 66065; -.
DR PRO; PR:Q9BPX3; -.
DR ArrayExpress; Q9BPX3; -.
DR Bgee; Q9BPX3; -.
DR CleanEx; HS_CAPG; -.
DR CleanEx; HS_NCAPG; -.
DR Genevestigator; Q9BPX3; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
KW DNA condensation; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 1015 Condensin complex subunit 3.
FT /FTId=PRO_0000095041.
FT REPEAT 94 131 HEAT 1.
FT REPEAT 138 173 HEAT 2.
FT REPEAT 174 212 HEAT 3.
FT REPEAT 238 275 HEAT 4.
FT REPEAT 276 313 HEAT 5.
FT REPEAT 399 436 HEAT 6.
FT REPEAT 439 478 HEAT 7.
FT REPEAT 617 654 HEAT 8.
FT REPEAT 687 724 HEAT 9.
FT REPEAT 865 907 HEAT 10.
FT COMPBIAS 88 91 Poly-Glu.
FT COMPBIAS 912 917 Poly-Thr.
FT MOD_RES 390 390 Phosphoserine.
FT MOD_RES 674 674 Phosphoserine.
FT MOD_RES 931 931 Phosphothreonine.
FT MOD_RES 973 973 Phosphoserine.
FT MOD_RES 975 975 Phosphoserine.
FT MOD_RES 1002 1002 Phosphoserine.
FT MOD_RES 1015 1015 Phosphoserine.
FT VARIANT 64 64 A -> P (in dbSNP:rs35722563).
FT /FTId=VAR_053041.
FT VARIANT 265 265 M -> T (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036125.
FT VARIANT 581 581 M -> I (in dbSNP:rs3795243).
FT /FTId=VAR_053042.
FT CONFLICT 115 115 R -> G (in Ref. 4; BAB14069).
FT CONFLICT 276 276 F -> V (in Ref. 1; AAG30732).
FT CONFLICT 519 519 S -> P (in Ref. 4; BAB55165).
FT CONFLICT 676 676 D -> V (in Ref. 4; BAB14069).
FT CONFLICT 681 681 K -> R (in Ref. 4; BAB14069).
FT CONFLICT 704 704 V -> A (in Ref. 4; BAB14069).
FT CONFLICT 836 836 N -> D (in Ref. 4; BAB55165).
FT CONFLICT 1010 1010 L -> F (in Ref. 1; AAG30732).
SQ SEQUENCE 1015 AA; 114334 MW; D9ACC205C48F3AF5 CRC64;
MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH YLKYVMVVYK
REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF TFLLKSHEAN SNAVRFRVCL
LINKLLGSMP ENAQIDDDVF DKINKAMLIR LKDKIPNVRI QAVLALSRLQ DPKDDECPVV
NAYATLIEND SNPEVRRAVL SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA
MSIAQRVMLL QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV
LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG DEGEEFLEQI
LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF IGQQLILIIK SLDTSEEGGR
KKLLAVLQEI LILPTIPISL VSFLVERLLH IIIDDNKRTQ IVTEIISEIR APIVTVGVNN
DPADVRKKEL KMAEIKVKLI EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE
QLEIKEVHIE KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV
RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM TFGIEPFKTK
KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL DSEVSELRTG AAEGLAKLMF
SGLLVSSRIL SRLILLWYNP VTEEDVQLRH CLGVFFPVFA YASRTNQECF EEAFLPTLQT
LANAPASSPL AEIDITNVAE LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT
SPCSPEIRVY TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE
FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN RGQRKVTVSA
RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE KSKLNLAQFL NEDLS
//
MIM
606280
*RECORD*
*FIELD* NO
606280
*FIELD* TI
*606280 NON-SMC CONDENSIN I COMPLEX SUBUNIT G; NCAPG
;;CONDENSIN I COMPLEX, NON-SMC SUBUNIT G;;
read moreCHROMOSOME-ASSOCIATED PROTEIN G; CAPG
*FIELD* TX
Members of the structural maintenance of chromosomes (SMC) family of
proteins (e.g., CAPC; 605575) are critical for mitotic chromosome
condensation in frogs and for DNA repair in mammals.
CLONING
Jager et al. (2000) screened a melanoma cDNA library by SEREX (serologic
analysis of cDNA expression libraries) and isolated a novel cDNA, called
NY-MEL-3, encoding a deduced 1,015-amino acid mitotic protein highly
homologous to the Xenopus chromosome condensation protein XCAP-G and
designated human CAPG. RT-PCR and Northern blot analyses showed highest
expression of CAPG in the testis among normal tissues and variable
expression in tumor cells, reflecting the proliferative activity in
these cells.
GENE FUNCTION
In contrast to most genomic DNA in mitotic cells, the promoter regions
of some genes, such as the stress-inducible hsp70i gene that codes for a
heat-shock protein, remain uncompacted, a phenomenon known as
bookmarking. Xing et al. (2005) showed that hsp70i (see 140550)
bookmarking is mediated by a transcription factor called HSF2 (140581),
which binds this promoter in mitotic cells, recruits protein phosphatase
2A (see 605997), and interacts with the CAPG subunit of the condensin
enzyme to promote efficient dephosphorylation and inactivation of
condensin complexes in the vicinity, thereby preventing compaction at
this site.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CAPG
gene to chromosome 4 (TMAP stSG54871).
*FIELD* RF
1. Jager, D.; Stockert, E.; Jager, E.; Gure, A. O.; Scanlan, M. J.;
Knuth, A.; Old, L. J.; Chen, Y.-T.: Serological cloning of a melanocyte
rab guanosine 5-prime-triphosphate-binding protein and a chromosome
condensation protein from a melanoma complementary DNA library. Cancer
Res. 60: 3584-3591, 2000.
2. Xing, H.; Wilkerson, D. C.; Mayhew, C. N.; Lubert, E. J.; Skaggs,
H. S.; Goodson, M. L.; Hong, Y.; Park-Sarge, O.-K.; Sarge, K. D.:
Mechanism of hsp70i gene bookmarking. Science 307: 421-423, 2005.
*FIELD* CN
Ada Hamosh - updated: 2/22/2005
*FIELD* CD
Victor A. McKusick: 9/25/2001
*FIELD* ED
mgross: 07/20/2007
alopez: 2/22/2005
carol: 9/27/2001
*RECORD*
*FIELD* NO
606280
*FIELD* TI
*606280 NON-SMC CONDENSIN I COMPLEX SUBUNIT G; NCAPG
;;CONDENSIN I COMPLEX, NON-SMC SUBUNIT G;;
read moreCHROMOSOME-ASSOCIATED PROTEIN G; CAPG
*FIELD* TX
Members of the structural maintenance of chromosomes (SMC) family of
proteins (e.g., CAPC; 605575) are critical for mitotic chromosome
condensation in frogs and for DNA repair in mammals.
CLONING
Jager et al. (2000) screened a melanoma cDNA library by SEREX (serologic
analysis of cDNA expression libraries) and isolated a novel cDNA, called
NY-MEL-3, encoding a deduced 1,015-amino acid mitotic protein highly
homologous to the Xenopus chromosome condensation protein XCAP-G and
designated human CAPG. RT-PCR and Northern blot analyses showed highest
expression of CAPG in the testis among normal tissues and variable
expression in tumor cells, reflecting the proliferative activity in
these cells.
GENE FUNCTION
In contrast to most genomic DNA in mitotic cells, the promoter regions
of some genes, such as the stress-inducible hsp70i gene that codes for a
heat-shock protein, remain uncompacted, a phenomenon known as
bookmarking. Xing et al. (2005) showed that hsp70i (see 140550)
bookmarking is mediated by a transcription factor called HSF2 (140581),
which binds this promoter in mitotic cells, recruits protein phosphatase
2A (see 605997), and interacts with the CAPG subunit of the condensin
enzyme to promote efficient dephosphorylation and inactivation of
condensin complexes in the vicinity, thereby preventing compaction at
this site.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CAPG
gene to chromosome 4 (TMAP stSG54871).
*FIELD* RF
1. Jager, D.; Stockert, E.; Jager, E.; Gure, A. O.; Scanlan, M. J.;
Knuth, A.; Old, L. J.; Chen, Y.-T.: Serological cloning of a melanocyte
rab guanosine 5-prime-triphosphate-binding protein and a chromosome
condensation protein from a melanoma complementary DNA library. Cancer
Res. 60: 3584-3591, 2000.
2. Xing, H.; Wilkerson, D. C.; Mayhew, C. N.; Lubert, E. J.; Skaggs,
H. S.; Goodson, M. L.; Hong, Y.; Park-Sarge, O.-K.; Sarge, K. D.:
Mechanism of hsp70i gene bookmarking. Science 307: 421-423, 2005.
*FIELD* CN
Ada Hamosh - updated: 2/22/2005
*FIELD* CD
Victor A. McKusick: 9/25/2001
*FIELD* ED
mgross: 07/20/2007
alopez: 2/22/2005
carol: 9/27/2001