Full text data of NCAPD2
NCAPD2
(CAPD2, CNAP1, KIAA0159)
[Confidence: low (only semi-automatic identification from reviews)]
Condensin complex subunit 1 (Chromosome condensation-related SMC-associated protein 1; Chromosome-associated protein D2; hCAP-D2; Non-SMC condensin I complex subunit D2; XCAP-D2 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Condensin complex subunit 1 (Chromosome condensation-related SMC-associated protein 1; Chromosome-associated protein D2; hCAP-D2; Non-SMC condensin I complex subunit D2; XCAP-D2 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15021
ID CND1_HUMAN Reviewed; 1401 AA.
AC Q15021; D3DUR4; Q8N6U3;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 132.
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; Synonyms=CAPD2, CNAP1, KIAA0159;
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], 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.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP 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
RT project: 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,
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4, AND
RP 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
RT homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3
RT during the 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
RP NCAPG, AND 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.,
RA Doi T., Yokomori K.;
RT "Identification of a chromosome-targeting domain in the human
RT condensin subunit CNAP1/hCAP-D2/Eg7.";
RL Mol. Cell. Biol. 22:5769-5781(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376, AND MASS
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND MASS
RP 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 [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 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 [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.,
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333 AND THR-1339, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-1333 AND
RP THR-1339, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333, AND MASS
RP 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 [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-83, AND MASS SPECTROMETRY.
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).
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. May target the
CC condensin complex to DNA via its C-terminal domain.
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. Interacts with histones H1 and H3.
CC -!- INTERACTION:
CC Q9BPX3:NCAPG; NbExp=2; IntAct=EBI-1044041, EBI-970214;
CC Q15003:NCAPH; NbExp=4; IntAct=EBI-1044041, 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 -!- DOMAIN: The C-terminal domain interacts with histones H1 and H3,
CC and 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
CC of NCAPH and NCAPG subunits, activates the condensin complex and
CC is required for chromosome condensation (By similarity).
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09930.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 RefSeq; NP_055680.3; NM_014865.3.
DR UniGene; Hs.5719; -.
DR ProteinModelPortal; Q15021; -.
DR IntAct; Q15021; 7.
DR MINT; MINT-3030640; -.
DR STRING; 9606.ENSP00000325017; -.
DR PhosphoSite; Q15021; -.
DR DMDM; 259016362; -.
DR PaxDb; Q15021; -.
DR PRIDE; Q15021; -.
DR Ensembl; ENST00000315579; ENSP00000325017; ENSG00000010292.
DR GeneID; 9918; -.
DR KEGG; hsa:9918; -.
DR UCSC; uc001qoo.2; human.
DR CTD; 9918; -.
DR GeneCards; GC12P006602; -.
DR H-InvDB; HIX0201829; -.
DR HGNC; HGNC:24305; NCAPD2.
DR HPA; CAB012423; -.
DR HPA; HPA036947; -.
DR HPA; HPA037363; -.
DR neXtProt; NX_Q15021; -.
DR PharmGKB; PA162397021; -.
DR eggNOG; COG5098; -.
DR HOGENOM; HOG000068001; -.
DR HOVERGEN; HBG038048; -.
DR InParanoid; Q15021; -.
DR KO; K06677; -.
DR OMA; ATEKVAC; -.
DR OrthoDB; EOG7FJGZN; -.
DR PhylomeDB; Q15021; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; NCAPD2; human.
DR GeneWiki; NCAPD2; -.
DR GenomeRNAi; 9918; -.
DR NextBio; 37412; -.
DR PRO; PR:Q15021; -.
DR ArrayExpress; Q15021; -.
DR Bgee; Q15021; -.
DR CleanEx; HS_NCAPD2; -.
DR Genevestigator; Q15021; -.
DR GO; GO:0000797; C:condensin core heterodimer; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IDA: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; IPR026971; CND1/NCAPD3.
DR InterPro; IPR007673; Condensin_cplx_su1.
DR InterPro; IPR024324; Condensin_cplx_su1_N.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1401 Condensin complex subunit 1.
FT /FTId=PRO_0000095035.
FT REGION 1 603 Interactions with SMC2 and SMC4.
FT MOTIF 1342 1362 Bipartite nuclear localization signal.
FT MOD_RES 20 20 Phosphoserine.
FT MOD_RES 585 585 Phosphoserine.
FT MOD_RES 1310 1310 Phosphoserine.
FT MOD_RES 1330 1330 Phosphoserine.
FT MOD_RES 1331 1331 Phosphothreonine.
FT MOD_RES 1333 1333 Phosphoserine.
FT MOD_RES 1339 1339 Phosphothreonine.
FT MOD_RES 1366 1366 Phosphoserine.
FT MOD_RES 1367 1367 Phosphoserine.
FT MOD_RES 1370 1370 Phosphoserine.
FT MOD_RES 1371 1371 Phosphoserine.
FT MOD_RES 1376 1376 Phosphoserine.
FT MOD_RES 1384 1384 Phosphothreonine; by CDK1 (By
FT similarity).
FT MOD_RES 1389 1389 Phosphothreonine; by CDK1 (By
FT similarity).
FT VARIANT 83 83 Q -> E (in dbSNP:rs714774).
FT /FTId=VAR_024421.
FT VARIANT 580 580 K -> R (in dbSNP:rs17725914).
FT /FTId=VAR_057511.
FT VARIANT 797 797 V -> M (in dbSNP:rs10849482).
FT /FTId=VAR_024422.
FT VARIANT 1321 1321 T -> S (in dbSNP:rs2240871).
FT /FTId=VAR_058713.
FT MUTAGEN 1343 1348 RRTTRR->AATTAA: Abolishes localization to
FT the nucleus, while it only reduces
FT chromosome binding.
FT MUTAGEN 1358 1360 KKK->AAA: Abolishes localization to the
FT nucleus, while it only reduces chromosome
FT binding.
FT CONFLICT 1062 1062 M -> I (in Ref. 1; BAA09930).
FT CONFLICT 1218 1218 R -> L (in Ref. 1; BAA09930).
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
//
ID CND1_HUMAN Reviewed; 1401 AA.
AC Q15021; D3DUR4; Q8N6U3;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 132.
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; Synonyms=CAPD2, CNAP1, KIAA0159;
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], 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.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP 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
RT project: 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,
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4, AND
RP 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
RT homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3
RT during the 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
RP NCAPG, AND 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.,
RA Doi T., Yokomori K.;
RT "Identification of a chromosome-targeting domain in the human
RT condensin subunit CNAP1/hCAP-D2/Eg7.";
RL Mol. Cell. Biol. 22:5769-5781(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376, AND MASS
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND MASS
RP 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 [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 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 [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.,
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333 AND THR-1339, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-1333 AND
RP THR-1339, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333, AND MASS
RP 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 [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-83, AND MASS SPECTROMETRY.
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).
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. May target the
CC condensin complex to DNA via its C-terminal domain.
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. Interacts with histones H1 and H3.
CC -!- INTERACTION:
CC Q9BPX3:NCAPG; NbExp=2; IntAct=EBI-1044041, EBI-970214;
CC Q15003:NCAPH; NbExp=4; IntAct=EBI-1044041, 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 -!- DOMAIN: The C-terminal domain interacts with histones H1 and H3,
CC and 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
CC of NCAPH and NCAPG subunits, activates the condensin complex and
CC is required for chromosome condensation (By similarity).
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09930.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 RefSeq; NP_055680.3; NM_014865.3.
DR UniGene; Hs.5719; -.
DR ProteinModelPortal; Q15021; -.
DR IntAct; Q15021; 7.
DR MINT; MINT-3030640; -.
DR STRING; 9606.ENSP00000325017; -.
DR PhosphoSite; Q15021; -.
DR DMDM; 259016362; -.
DR PaxDb; Q15021; -.
DR PRIDE; Q15021; -.
DR Ensembl; ENST00000315579; ENSP00000325017; ENSG00000010292.
DR GeneID; 9918; -.
DR KEGG; hsa:9918; -.
DR UCSC; uc001qoo.2; human.
DR CTD; 9918; -.
DR GeneCards; GC12P006602; -.
DR H-InvDB; HIX0201829; -.
DR HGNC; HGNC:24305; NCAPD2.
DR HPA; CAB012423; -.
DR HPA; HPA036947; -.
DR HPA; HPA037363; -.
DR neXtProt; NX_Q15021; -.
DR PharmGKB; PA162397021; -.
DR eggNOG; COG5098; -.
DR HOGENOM; HOG000068001; -.
DR HOVERGEN; HBG038048; -.
DR InParanoid; Q15021; -.
DR KO; K06677; -.
DR OMA; ATEKVAC; -.
DR OrthoDB; EOG7FJGZN; -.
DR PhylomeDB; Q15021; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; NCAPD2; human.
DR GeneWiki; NCAPD2; -.
DR GenomeRNAi; 9918; -.
DR NextBio; 37412; -.
DR PRO; PR:Q15021; -.
DR ArrayExpress; Q15021; -.
DR Bgee; Q15021; -.
DR CleanEx; HS_NCAPD2; -.
DR Genevestigator; Q15021; -.
DR GO; GO:0000797; C:condensin core heterodimer; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IDA: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; IPR026971; CND1/NCAPD3.
DR InterPro; IPR007673; Condensin_cplx_su1.
DR InterPro; IPR024324; Condensin_cplx_su1_N.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1401 Condensin complex subunit 1.
FT /FTId=PRO_0000095035.
FT REGION 1 603 Interactions with SMC2 and SMC4.
FT MOTIF 1342 1362 Bipartite nuclear localization signal.
FT MOD_RES 20 20 Phosphoserine.
FT MOD_RES 585 585 Phosphoserine.
FT MOD_RES 1310 1310 Phosphoserine.
FT MOD_RES 1330 1330 Phosphoserine.
FT MOD_RES 1331 1331 Phosphothreonine.
FT MOD_RES 1333 1333 Phosphoserine.
FT MOD_RES 1339 1339 Phosphothreonine.
FT MOD_RES 1366 1366 Phosphoserine.
FT MOD_RES 1367 1367 Phosphoserine.
FT MOD_RES 1370 1370 Phosphoserine.
FT MOD_RES 1371 1371 Phosphoserine.
FT MOD_RES 1376 1376 Phosphoserine.
FT MOD_RES 1384 1384 Phosphothreonine; by CDK1 (By
FT similarity).
FT MOD_RES 1389 1389 Phosphothreonine; by CDK1 (By
FT similarity).
FT VARIANT 83 83 Q -> E (in dbSNP:rs714774).
FT /FTId=VAR_024421.
FT VARIANT 580 580 K -> R (in dbSNP:rs17725914).
FT /FTId=VAR_057511.
FT VARIANT 797 797 V -> M (in dbSNP:rs10849482).
FT /FTId=VAR_024422.
FT VARIANT 1321 1321 T -> S (in dbSNP:rs2240871).
FT /FTId=VAR_058713.
FT MUTAGEN 1343 1348 RRTTRR->AATTAA: Abolishes localization to
FT the nucleus, while it only reduces
FT chromosome binding.
FT MUTAGEN 1358 1360 KKK->AAA: Abolishes localization to the
FT nucleus, while it only reduces chromosome
FT binding.
FT CONFLICT 1062 1062 M -> I (in Ref. 1; BAA09930).
FT CONFLICT 1218 1218 R -> L (in Ref. 1; BAA09930).
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
//