Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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)

 CND1_HUMAN              Reviewed;        1401 AA.
Q15021; D3DUR4; Q8N6U3;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
25-OCT-2017, entry version 170.
RecName: Full=Condensin complex subunit 1;
AltName: Full=Chromosome condensation-related SMC-associated protein 1;
AltName: Full=Chromosome-associated protein D2;
Short=hCAP-D2;
AltName: Full=Non-SMC condensin I complex subunit D2;
AltName: Full=XCAP-D2 homolog;
Name=NCAPD2; Synonyms=CAPD2, CNAP1, KIAA0159;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-83.
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-83.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-83 AND
SER-1321.
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 359-365; 537-560; 698-709 AND 1324-1331,
IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4, AND
SUBCELLULAR LOCATION.
PubMed=10958694; DOI=10.1128/MCB.20.18.6996-7006.2000;
Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.;
"A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a
homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3
during the early stage of mitotic chromosome condensation.";
Mol. Cell. Biol. 20:6996-7006(2000).
[6]
IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPH AND
NCAPG, AND FUNCTION OF THE CONDENSIN COMPLEX.
PubMed=11136719; DOI=10.1074/jbc.C000873200;
Kimura K., Cuvier O., Hirano T.;
"Chromosome condensation by a human condensin complex in Xenopus egg
extracts.";
J. Biol. Chem. 276:5417-5420(2001).
[7]
INTERACTION WITH HISTONE H1 AND HISTONE H3, AND MUTAGENESIS OF
1343-ARG--ARG-1348 AND 1358-LYS--LYS-1360.
PubMed=12138188; DOI=10.1128/MCB.22.16.5769-5781.2002;
Ball A.R. Jr., Schmiesing J.A., Zhou C., Gregson H.C., Okada Y.,
Doi T., Yokomori K.;
"Identification of a chromosome-targeting domain in the human
condensin subunit CNAP1/hCAP-D2/Eg7.";
Mol. Cell. Biol. 22:5769-5781(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1330; THR-1331;
SER-1333; THR-1339; SER-1366; SER-1367; SER-1370 AND SER-1371, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333 AND THR-1339, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-1333 AND
THR-1339, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1310; SER-1315;
SER-1330; THR-1331; SER-1333; THR-1339 AND SER-1395, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
VARIANT [LARGE SCALE ANALYSIS] GLU-83, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Regulatory subunit of the condensin complex, a complex
required for conversion of interphase chromatin into mitotic-like
condense chromosomes. The condensin complex probably introduces
positive supercoils into relaxed DNA in the presence of type I
topoisomerases and converts nicked DNA into positive knotted forms
in the presence of type II topoisomerases. May target the
condensin complex to DNA via its C-terminal domain.
{ECO:0000269|PubMed:11136719}.
-!- SUBUNIT: Component of the condensin complex, which contains the
SMC2 and SMC4 heterodimer, and three non SMC subunits that
probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and
NCAPG. Interacts with histones H1 and H3.
{ECO:0000269|PubMed:10958694, ECO:0000269|PubMed:11136719,
ECO:0000269|PubMed:12138188}.
-!- INTERACTION:
Q15003:NCAPH; NbExp=4; IntAct=EBI-1044041, EBI-1046410;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}.
Cytoplasm {ECO:0000269|PubMed:10958694}. Chromosome
{ECO:0000269|PubMed:10958694}. Note=In interphase cells, the
majority of the condensin complex is found in the cytoplasm, while
a minority of the complex is associated with chromatin. A
subpopulation of the complex however remains associated with
chromosome foci in interphase cells. During mitosis, most of the
condensin complex is associated with the chromatin. At the onset
of prophase, the regulatory subunits of the complex are
phosphorylated by CDK1, leading to condensin's association with
chromosome arms and to chromosome condensation. Dissociation from
chromosomes is observed in late telophase.
-!- DOMAIN: The C-terminal domain interacts with histones H1 and H3,
and may be responsible for condensin complex targeting to mitotic
chromosomes. This domain is independent from the bipartite nuclear
localization signal, although they are contained within the same
region.
-!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that
of NCAPH and NCAPG subunits, activates the condensin complex and
is required for chromosome condensation (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA09930.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D63880; BAA09930.2; ALT_INIT; mRNA.
EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88788.1; -; Genomic_DNA.
EMBL; CH471116; EAW88789.1; -; Genomic_DNA.
EMBL; BC028182; AAH28182.1; -; mRNA.
CCDS; CCDS8548.1; -.
RefSeq; NP_055680.3; NM_014865.3.
UniGene; Hs.5719; -.
ProteinModelPortal; Q15021; -.
SMR; Q15021; -.
BioGrid; 115246; 54.
CORUM; Q15021; -.
IntAct; Q15021; 15.
MINT; MINT-3030640; -.
STRING; 9606.ENSP00000325017; -.
iPTMnet; Q15021; -.
PhosphoSitePlus; Q15021; -.
BioMuta; NCAPD2; -.
DMDM; 259016362; -.
EPD; Q15021; -.
MaxQB; Q15021; -.
PaxDb; Q15021; -.
PeptideAtlas; Q15021; -.
PRIDE; Q15021; -.
Ensembl; ENST00000315579; ENSP00000325017; ENSG00000010292.
GeneID; 9918; -.
KEGG; hsa:9918; -.
UCSC; uc001qoo.3; human.
CTD; 9918; -.
DisGeNET; 9918; -.
EuPathDB; HostDB:ENSG00000010292.12; -.
GeneCards; NCAPD2; -.
H-InvDB; HIX0201829; -.
HGNC; HGNC:24305; NCAPD2.
HPA; CAB012423; -.
HPA; HPA036947; -.
HPA; HPA037363; -.
MIM; 615638; gene.
neXtProt; NX_Q15021; -.
OpenTargets; ENSG00000010292; -.
PharmGKB; PA162397021; -.
eggNOG; KOG0414; Eukaryota.
eggNOG; COG5098; LUCA.
GeneTree; ENSGT00390000017108; -.
HOGENOM; HOG000068001; -.
HOVERGEN; HBG038048; -.
InParanoid; Q15021; -.
KO; K06677; -.
OMA; HLDGENY; -.
OrthoDB; EOG091G00PU; -.
PhylomeDB; Q15021; -.
TreeFam; TF105712; -.
Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
ChiTaRS; NCAPD2; human.
GeneWiki; NCAPD2; -.
GenomeRNAi; 9918; -.
PRO; PR:Q15021; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000010292; -.
CleanEx; HS_NCAPD2; -.
ExpressionAtlas; Q15021; baseline and differential.
Genevisible; Q15021; HS.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
GO; GO:0000797; C:condensin core heterodimer; NAS:UniProtKB.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000799; C:nuclear condensin complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051304; P:chromosome separation; IBA:GO_Central.
GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR026971; CND1/NCAPD3.
InterPro; IPR032682; Cnd1_C.
InterPro; IPR007673; Condensin_cplx_su1.
InterPro; IPR024324; Condensin_cplx_su1_N.
PANTHER; PTHR14222; PTHR14222; 1.
PANTHER; PTHR14222:SF2; PTHR14222:SF2; 1.
Pfam; PF12717; Cnd1; 1.
Pfam; PF12922; Cnd1_N; 1.
PIRSF; PIRSF017127; Condensin_D2; 1.
SUPFAM; SSF48371; SSF48371; 4.
1: Evidence at protein level;
Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 1401 Condensin complex subunit 1.
/FTId=PRO_0000095035.
REGION 1 603 Interactions with SMC2 and SMC4.
MOTIF 1342 1362 Bipartite nuclear localization signal.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1310 1310 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1315 1315 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1330 1330 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1331 1331 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1333 1333 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1339 1339 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1366 1366 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1367 1367 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1370 1370 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1371 1371 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1376 1376 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1384 1384 Phosphothreonine; by CDK1. {ECO:0000250}.
MOD_RES 1389 1389 Phosphothreonine; by CDK1. {ECO:0000250}.
MOD_RES 1395 1395 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 83 83 Q -> E (in dbSNP:rs714774).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8590280,
ECO:0000269|Ref.3}.
/FTId=VAR_024421.
VARIANT 580 580 K -> R (in dbSNP:rs17725914).
/FTId=VAR_057511.
VARIANT 797 797 V -> M (in dbSNP:rs10849482).
/FTId=VAR_024422.
VARIANT 1321 1321 T -> S (in dbSNP:rs2240871).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058713.
MUTAGEN 1343 1348 RRTTRR->AATTAA: Abolishes localization to
the nucleus, while it only reduces
chromosome binding.
{ECO:0000269|PubMed:12138188}.
MUTAGEN 1358 1360 KKK->AAA: Abolishes localization to the
nucleus, while it only reduces chromosome
binding. {ECO:0000269|PubMed:12138188}.
CONFLICT 1062 1062 M -> I (in Ref. 1; BAA09930).
{ECO:0000305}.
CONFLICT 1218 1218 R -> L (in Ref. 1; BAA09930).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
EIAAB08146 CAPG,Chromosome-associated protein G,Condensin complex subunit 3,Condensin subunit CAP-G,hCAP-G,Homo sapiens,Human,Melanoma antigen NY-MEL-3,NCAPG,Non-SMC condensin I complex subunit G,NYMEL3,XCAP-G h
EIAAB08142 CAPD2,Chromosome condensation-related SMC-associated protein 1,Chromosome-associated protein D2,CNAP1,Condensin complex subunit 1,hCAP-D2,Homo sapiens,Human,KIAA0159,NCAPD2,Non-SMC condensin I complex
EIAAB08144 Barren homolog protein 1,BRRN,BRRN1,CAPH,Chromosome-associated protein H,Condensin complex subunit 2,hCAP-H,Homo sapiens,Human,KIAA0074,NCAPH,Non-SMC condensin I complex subunit H,XCAP-H homolog
EIAAB08143 Capd2,Chromosome condensation-related SMC-associated protein 1,Chromosome-associated protein D2,Cnap1,Condensin complex subunit 1,Kiaa0159,mCAP-D2,Mouse,Mus musculus,Ncapd2,Non-SMC condensin I complex
EIAAB08145 Barren homolog protein 1,Brrn,Brrn1,Caph,Chromosome-associated protein H,Condensin complex subunit 2,mCAP-H,Mouse,Mus musculus,Ncaph,Non-SMC condensin I complex subunit H,XCAP-H homolog
EIAAB08152 CAPH2,Chromosome-associated protein H2,Condensin-2 complex subunit H2,hCAP-H2,Homo sapiens,Human,Kleisin-beta,NCAPH2,Non-SMC condensin II complex subunit H2
EIAAB08149 CAP-G2,Chromosome-associated protein G2,Condensin-2 complex subunit G2,hCAP-G2,Homo sapiens,Human,Leucine zipper protein 5,LUZP5,NCAPG2,Non-SMC condensin II complex subunit G2
EIAAB08150 CAP-G2,Chromosome-associated protein G2,Condensin-2 complex subunit G2,Leucine zipper protein 5,Luzp5,More than blood protein,Mouse,Mtb,Mus musculus,Ncapg2,Non-SMC condensin II complex subunit G2
EIAAB08147 CAPD3,Condensin-2 complex subunit D3,hCAP-D3,Homo sapiens,Human,KIAA0056,NCAPD3,Non-SMC condensin II complex subunit D3
30-174 NCAPD2 is the regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces p 0.05 mg
EIAAB08154 Condensin-2 complex subunit H2,D15Ertd785e,Kleisin-beta,Mouse,Mus musculus,Ncaph2,Non-SMC condensin II complex subunit H2
EIAAB08148 Condensin-2 complex subunit D3,Kiaa0056,Mouse,Mus musculus,Ncapd3,Non-SMC condensin II complex subunit D3
EIAAB08153 Bos taurus,Bovine,Condensin-2 complex subunit H2,NCAPH2,Non-SMC condensin II complex subunit H2
EIAAB08151 Condensin-2 complex subunit H2,Ncaph2,Non-SMC condensin II complex subunit H2,Rat,Rattus norvegicus
26-111 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
30-178 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.1 mg
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.05 mg
EIAAB38768 CAPC,Chromosome-associated polypeptide C,hCAP-C,Homo sapiens,Human,SMC protein 4,SMC4,SMC-4,SMC4L1,Structural maintenance of chromosomes protein 4,XCAP-C homolog
CNDH2_RAT Rat ELISA Kit FOR Condensin-2 complex subunit H2 96T
E6910h Human Non SMC Condensin II Complex Subunit D2 ELIS 96T
NCAPH2 NCAPG2 Gene non-SMC condensin II complex, subunit G2
201-20-3654 NCAPD2{non-SMC condensin I complex, subunit D2}rabbit.pAb 0.2ml
NCAPG NCAPD2 Gene non-SMC condensin I complex, subunit D2


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur