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Protein

Condensin-2 complex subunit D3

Gene

NCAPD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis.1 Publication

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • methylated histone binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2299718. Condensation of Prophase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Condensin-2 complex subunit D3
Alternative name(s):
Non-SMC condensin II complex subunit D3
Short name:
hCAP-D3
Gene namesi
Name:NCAPD3
Synonyms:CAPD3, KIAA0056
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28952. NCAPD3.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome, centromeric region Source: GO_Central
  • membrane Source: UniProtKB
  • nuclear condensin complex Source: UniProtKB
  • nuclear pericentric heterochromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162397090.

Polymorphism and mutation databases

BioMutaiNCAPD3.
DMDMi82654946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14981498Condensin-2 complex subunit D3PRO_0000050716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei567 – 5671PhosphoserineCombined sources
Modified residuei1329 – 13291PhosphoserineCombined sources
Modified residuei1331 – 13311PhosphothreonineCombined sources
Modified residuei1348 – 13481PhosphoserineCombined sources
Modified residuei1357 – 13571PhosphoserineCombined sources
Modified residuei1379 – 13791PhosphothreonineCombined sources
Modified residuei1382 – 13821PhosphoserineCombined sources
Modified residuei1384 – 13841PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP42695.
MaxQBiP42695.
PaxDbiP42695.
PRIDEiP42695.

PTM databases

iPTMnetiP42695.
PhosphoSiteiP42695.

Expressioni

Gene expression databases

BgeeiP42695.
CleanExiHS_NCAPD3.
ExpressionAtlasiP42695. baseline and differential.
GenevisibleiP42695. HS.

Organism-specific databases

HPAiCAB022623.
CAB034091.

Interactioni

Subunit structurei

Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and 3 non SMC subunits that probably regulate the complex: NCAPH2, NCAPD3 and NCAPG2. Interacts with BRD4 (isoform B), leading to insulate chromatin from DNA damage response pathway.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPH2Q6IBW43EBI-722805,EBI-2548296

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116902. 54 interactions.
DIPiDIP-43903N.
IntActiP42695. 19 interactions.
MINTiMINT-1423980.
STRINGi9606.ENSP00000433681.

Structurei

3D structure databases

ProteinModelPortaliP42695.
SMRiP42695. Positions 448-474, 542-646, 981-1006.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati441 – 47535HEAT 1Add
BLAST
Repeati537 – 57236HEAT 2Add
BLAST
Repeati579 – 61032HEAT 3Add
BLAST
Repeati973 – 100937HEAT 4Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1219 – 127557Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 4 HEAT repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0413. Eukaryota.
ENOG410XSGK. LUCA.
GeneTreeiENSGT00390000011258.
HOGENOMiHOG000111840.
HOVERGENiHBG061537.
InParanoidiP42695.
KOiK11491.
OMAiRAHAIIT.
PhylomeDBiP42695.
TreeFamiTF101162.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026971. CND1/NCAPD3.
IPR032682. Cnd1_C.
IPR012371. NCAPD3.
[Graphical view]
PANTHERiPTHR14222. PTHR14222. 2 hits.
PfamiPF12717. Cnd1. 1 hit.
[Graphical view]
PIRSFiPIRSF036508. Condns_HCP-6. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

P42695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVALRGLGSG LQPWCPLDLR LEWVDTVWEL DFTETEPLDP SIEAEIIETG
60 70 80 90 100
LAAFTKLYES LLPFATGEHG SMESIWTFFI ENNVSHSTLV ALFYHFVQIV
110 120 130 140 150
HKKNVSVQYR EYGLHAAGLY FLLLEVPGSV ANQVFHPVMF DKCIQTLKKS
160 170 180 190 200
WPQESNLNRK RKKEQPKSSQ ANPGRHRKRG KPPRREDIEM DEIIEEQEDE
210 220 230 240 250
NICFSARDLS QIRNAIFHLL KNFLRLLPKF SLKEKPQCVQ NCIEVFVSLT
260 270 280 290 300
NFEPVLHECH VTQARALNQA KYIPELAYYG LYLLCSPIHG EGDKVISCVF
310 320 330 340 350
HQMLSVILML EVGEGSHRAP LAVTSQVINC RNQAVQFISA LVDELKESIF
360 370 380 390 400
PVVRILLQHI CAKVVDKSEY RTFAAQSLVQ LLSKLPCGEY AMFIAWLYKY
410 420 430 440 450
SRSSKIPHRV FTLDVVLALL ELPEREVDNT LSLEHQKFLK HKFLVQEIMF
460 470 480 490 500
DRCLDKAPTV RSKALSSFAH CLELTVTSAS ESILELLINS PTFSVIESHP
510 520 530 540 550
GTLLRNSSAF SYQRQTSNRS EPSGEINIDS SGETVGSGER CVMAMLRRRI
560 570 580 590 600
RDEKTNVRKS ALQVLVSILK HCDVSGMKED LWILQDQCRD PAVSVRKQAL
610 620 630 640 650
QSLTELLMAQ PRCVQIQKAW LRGVVPVVMD CESTVQEKAL EFLDQLLLQN
660 670 680 690 700
IRHHSHFHSG DDSQVLAWAL LTLLTTESQE LSRYLNKAFH IWSKKEKFSP
710 720 730 740 750
TFINNVISHT GTEHSAPAWM LLSKIAGSSP RLDYSRIIQS WEKISSQQNP
760 770 780 790 800
NSNTLGHILC VIGHIAKHLP KSTRDKVTDA VKCKLNGFQW SLEVISSAVD
810 820 830 840 850
ALQRLCRASA ETPAEEQELL TQVCGDVLST CEHRLSNIVL KENGTGNMDE
860 870 880 890 900
DLLVKYIFTL GDIAQLCPAR VEKRIFLLIQ SVLASSADAD HSPSSQGSSE
910 920 930 940 950
APASQPPPQV RGSVMPSVIR AHAIITLGKL CLQHEDLAKK SIPALVRELE
960 970 980 990 1000
VCEDVAVRNN VIIVMCDLCI RYTIMVDKYI PNISMCLKDS DPFIRKQTLI
1010 1020 1030 1040 1050
LLTNLLQEEF VKWKGSLFFR FVSTLIDSHP DIASFGEFCL AHLLLKRNPV
1060 1070 1080 1090 1100
MFFQHFIECI FHFNNYEKHE KYNKFPQSER EKRLFSLKGK SNKERRMKIY
1110 1120 1130 1140 1150
KFLLEHFTDE QRFNITSKIC LSILACFADG ILPLDLDASE LLSDTFEVLS
1160 1170 1180 1190 1200
SKEIKLLAMR SKPDKDLLME EDDMALANVV MQEAQKKLIS QVQKRNFIEN
1210 1220 1230 1240 1250
IIPIIISLKT VLEKNKIPAL RELMHYLREV MQDYRDELKD FFAVDKQLAS
1260 1270 1280 1290 1300
ELEYDMKKYQ EQLVQEQELA KHADVAGTAG GAEVAPVAQV ALCLETVPVP
1310 1320 1330 1340 1350
AGQENPAMSP AVSQPCTPRA SAGHVAVSSP TPETGPLQRL LPKARPMSLS
1360 1370 1380 1390 1400
TIAILNSVKK AVESKSRHRS RSLGVLPFTL NSGSPEKTCS QVSSYSLEQE
1410 1420 1430 1440 1450
SNGEIEHVTK RAISTPEKSI SDVTFGAGVS YIGTPRTPSS AKEKIEGRSQ
1460 1470 1480 1490
GNDILCLSLP DKPPPQPQQW NVRSPARNKD TPACSRRSLR KTPLKTAN
Length:1,498
Mass (Da):168,891
Last modified:November 22, 2005 - v2
Checksum:i038033DA393E4310
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti622 – 6221R → Q.
Corresponds to variant rs12292394 [ dbSNP | Ensembl ].
VAR_053043
Natural varianti907 – 9071P → T.
Corresponds to variant rs34739733 [ dbSNP | Ensembl ].
VAR_053044
Natural varianti1034 – 10341S → R.
Corresponds to variant rs7927108 [ dbSNP | Ensembl ].
VAR_053045

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29954 mRNA. Translation: BAA06224.1.
AP001775 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67824.1.
BC098398 mRNA. Translation: AAH98398.1.
AF070553 mRNA. Translation: AAC28639.1.
CCDSiCCDS31723.1.
RefSeqiNP_056076.1. NM_015261.2.
XP_011541020.1. XM_011542718.1.
UniGeneiHs.438550.

Genome annotation databases

EnsembliENST00000534548; ENSP00000433681; ENSG00000151503.
GeneIDi23310.
KEGGihsa:23310.
UCSCiuc001qhd.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29954 mRNA. Translation: BAA06224.1.
AP001775 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67824.1.
BC098398 mRNA. Translation: AAH98398.1.
AF070553 mRNA. Translation: AAC28639.1.
CCDSiCCDS31723.1.
RefSeqiNP_056076.1. NM_015261.2.
XP_011541020.1. XM_011542718.1.
UniGeneiHs.438550.

3D structure databases

ProteinModelPortaliP42695.
SMRiP42695. Positions 448-474, 542-646, 981-1006.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116902. 54 interactions.
DIPiDIP-43903N.
IntActiP42695. 19 interactions.
MINTiMINT-1423980.
STRINGi9606.ENSP00000433681.

PTM databases

iPTMnetiP42695.
PhosphoSiteiP42695.

Polymorphism and mutation databases

BioMutaiNCAPD3.
DMDMi82654946.

Proteomic databases

EPDiP42695.
MaxQBiP42695.
PaxDbiP42695.
PRIDEiP42695.

Protocols and materials databases

DNASUi23310.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000534548; ENSP00000433681; ENSG00000151503.
GeneIDi23310.
KEGGihsa:23310.
UCSCiuc001qhd.2. human.

Organism-specific databases

CTDi23310.
GeneCardsiNCAPD3.
HGNCiHGNC:28952. NCAPD3.
HPAiCAB022623.
CAB034091.
MIMi609276. gene.
neXtProtiNX_P42695.
PharmGKBiPA162397090.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0413. Eukaryota.
ENOG410XSGK. LUCA.
GeneTreeiENSGT00390000011258.
HOGENOMiHOG000111840.
HOVERGENiHBG061537.
InParanoidiP42695.
KOiK11491.
OMAiRAHAIIT.
PhylomeDBiP42695.
TreeFamiTF101162.

Enzyme and pathway databases

ReactomeiR-HSA-2299718. Condensation of Prophase Chromosomes.

Miscellaneous databases

ChiTaRSiNCAPD3. human.
GeneWikiiNCAPD3.
GenomeRNAii23310.
NextBioi45178.
PROiP42695.
SOURCEiSearch...

Gene expression databases

BgeeiP42695.
CleanExiHS_NCAPD3.
ExpressionAtlasiP42695. baseline and differential.
GenevisibleiP42695. HS.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026971. CND1/NCAPD3.
IPR032682. Cnd1_C.
IPR012371. NCAPD3.
[Graphical view]
PANTHERiPTHR14222. PTHR14222. 2 hits.
PfamiPF12717. Cnd1. 1 hit.
[Graphical view]
PIRSFiPIRSF036508. Condns_HCP-6. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1162-1498.
    Tissue: Brain.
  6. "Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells."
    Ono T., Losada A., Hirano M., Myers M.P., Neuwald A.F., Hirano T.
    Cell 115:109-121(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1329; THR-1331; SER-1348; SER-1357 AND SER-1384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; THR-1379; SER-1382 AND SER-1384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INTERACTION WITH BRD4.

Entry informationi

Entry nameiCNDD3_HUMAN
AccessioniPrimary (citable) accession number: P42695
Secondary accession number(s): A6NFS2, Q4KMQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 22, 2005
Last modified: May 11, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.