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Protein

Condensin complex subunit 3

Gene

NCAPG

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 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.1 Publication

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic chromosome condensation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000109805-MONOMER.
ReactomeiR-HSA-2514853. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Condensin complex subunit 3
Alternative name(s):
Chromosome-associated protein G
Condensin subunit CAP-G
Short name:
hCAP-G
Melanoma antigen NY-MEL-3
Non-SMC condensin I complex subunit G
XCAP-G homolog
Gene namesi
Name:NCAPG
Synonyms:CAPG, NYMEL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24304. NCAPG.

Subcellular locationi

  • Nucleus
  • Cytoplasm
  • Chromosome

  • 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.

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • centrosome Source: HPA
  • condensin complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi64151.
OpenTargetsiENSG00000109805.
PharmGKBiPA162397165.

Polymorphism and mutation databases

BioMutaiNCAPG.
DMDMi30172941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000950411 – 1015Condensin complex subunit 3Add BLAST1015

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei390PhosphoserineCombined sources1
Modified residuei674PhosphoserineCombined sources1
Modified residuei931PhosphothreonineCombined sources1
Modified residuei973PhosphoserineCombined sources1
Modified residuei975PhosphoserineCombined sources1
Modified residuei1002PhosphoserineCombined sources1
Modified residuei1015PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPH subunits, activates the condensin complex and is required for chromosome condensation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BPX3.
MaxQBiQ9BPX3.
PaxDbiQ9BPX3.
PeptideAtlasiQ9BPX3.
PRIDEiQ9BPX3.

PTM databases

iPTMnetiQ9BPX3.
PhosphoSitePlusiQ9BPX3.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

BgeeiENSG00000109805.
CleanExiHS_CAPG.
HS_NCAPG.
ExpressionAtlasiQ9BPX3. baseline and differential.
GenevisibleiQ9BPX3. HS.

Organism-specific databases

HPAiHPA039613.
HPA040103.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPD2Q150212EBI-970214,EBI-1044041
NCAPHQ150033EBI-970214,EBI-1046410

Protein-protein interaction databases

BioGridi122089. 53 interactors.
DIPiDIP-34891N.
IntActiQ9BPX3. 12 interactors.
MINTiMINT-3060256.
STRINGi9606.ENSP00000251496.

Structurei

3D structure databases

ProteinModelPortaliQ9BPX3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati94 – 131HEAT 1Add BLAST38
Repeati138 – 173HEAT 2Add BLAST36
Repeati174 – 212HEAT 3Add BLAST39
Repeati238 – 275HEAT 4Add BLAST38
Repeati276 – 313HEAT 5Add BLAST38
Repeati399 – 436HEAT 6Add BLAST38
Repeati439 – 478HEAT 7Add BLAST40
Repeati617 – 654HEAT 8Add BLAST38
Repeati687 – 724HEAT 9Add BLAST38
Repeati865 – 907HEAT 10Add BLAST43

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi88 – 91Poly-Glu4
Compositional biasi912 – 917Poly-Thr6

Sequence similaritiesi

Belongs to the CND3 (condensin subunit 3) family.Curated
Contains 10 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2025. Eukaryota.
COG5218. LUCA.
GeneTreeiENSGT00390000001577.
HOVERGENiHBG039407.
InParanoidiQ9BPX3.
KOiK06678.
OMAiKCLHIVQ.
OrthoDBiEOG091G0K3M.
PhylomeDBiQ9BPX3.
TreeFamiTF101160.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027165. CND3.
IPR025977. Cnd3_C.
[Graphical view]
PANTHERiPTHR14418. PTHR14418. 1 hit.
PfamiPF12719. Cnd3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9BPX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH
60 70 80 90 100
YLKYVMVVYK REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF
110 120 130 140 150
TFLLKSHEAN SNAVRFRVCL LINKLLGSMP ENAQIDDDVF DKINKAMLIR
160 170 180 190 200
LKDKIPNVRI QAVLALSRLQ DPKDDECPVV NAYATLIEND SNPEVRRAVL
210 220 230 240 250
SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA MSIAQRVMLL
260 270 280 290 300
QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV
310 320 330 340 350
LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG
360 370 380 390 400
DEGEEFLEQI LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF
410 420 430 440 450
IGQQLILIIK SLDTSEEGGR KKLLAVLQEI LILPTIPISL VSFLVERLLH
460 470 480 490 500
IIIDDNKRTQ IVTEIISEIR APIVTVGVNN DPADVRKKEL KMAEIKVKLI
510 520 530 540 550
EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE QLEIKEVHIE
560 570 580 590 600
KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV
610 620 630 640 650
RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM
660 670 680 690 700
TFGIEPFKTK KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL
710 720 730 740 750
DSEVSELRTG AAEGLAKLMF SGLLVSSRIL SRLILLWYNP VTEEDVQLRH
760 770 780 790 800
CLGVFFPVFA YASRTNQECF EEAFLPTLQT LANAPASSPL AEIDITNVAE
810 820 830 840 850
LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT SPCSPEIRVY
860 870 880 890 900
TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE
910 920 930 940 950
FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN
960 970 980 990 1000
RGQRKVTVSA RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE
1010
KSKLNLAQFL NEDLS
Length:1,015
Mass (Da):114,334
Last modified:June 1, 2001 - v1
Checksum:iD9ACC205C48F3AF5
GO

Sequence cautioni

The sequence AAH00827 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14429 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB55165 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115R → G in BAB14069 (PubMed:14702039).Curated1
Sequence conflicti276F → V in AAG30732 (PubMed:10910072).Curated1
Sequence conflicti519S → P in BAB55165 (PubMed:14702039).Curated1
Sequence conflicti676D → V in BAB14069 (PubMed:14702039).Curated1
Sequence conflicti681K → R in BAB14069 (PubMed:14702039).Curated1
Sequence conflicti704V → A in BAB14069 (PubMed:14702039).Curated1
Sequence conflicti836N → D in BAB55165 (PubMed:14702039).Curated1
Sequence conflicti1010L → F in AAG30732 (PubMed:10910072).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05304164A → P.Corresponds to variant rs35722563dbSNPEnsembl.1
Natural variantiVAR_036125265M → T in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_053042581M → I.1 PublicationCorresponds to variant rs3795243dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235023 mRNA. Translation: AAG30732.1.
AF331796 mRNA. Translation: AAG49627.1.
AB013299 mRNA. Translation: BAB21557.1.
AK022512 mRNA. Translation: BAB14069.1.
AK023147 mRNA. Translation: BAB14429.1. Different initiation.
AK027511 mRNA. Translation: BAB55165.1. Different initiation.
BC000827 mRNA. Translation: AAH00827.1. Different initiation.
BC101476 mRNA. Translation: AAI01477.1.
CCDSiCCDS3424.1.
RefSeqiNP_071741.2. NM_022346.4.
UniGeneiHs.567567.

Genome annotation databases

EnsembliENST00000251496; ENSP00000251496; ENSG00000109805.
GeneIDi64151.
KEGGihsa:64151.
UCSCiuc003gpp.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235023 mRNA. Translation: AAG30732.1.
AF331796 mRNA. Translation: AAG49627.1.
AB013299 mRNA. Translation: BAB21557.1.
AK022512 mRNA. Translation: BAB14069.1.
AK023147 mRNA. Translation: BAB14429.1. Different initiation.
AK027511 mRNA. Translation: BAB55165.1. Different initiation.
BC000827 mRNA. Translation: AAH00827.1. Different initiation.
BC101476 mRNA. Translation: AAI01477.1.
CCDSiCCDS3424.1.
RefSeqiNP_071741.2. NM_022346.4.
UniGeneiHs.567567.

3D structure databases

ProteinModelPortaliQ9BPX3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122089. 53 interactors.
DIPiDIP-34891N.
IntActiQ9BPX3. 12 interactors.
MINTiMINT-3060256.
STRINGi9606.ENSP00000251496.

PTM databases

iPTMnetiQ9BPX3.
PhosphoSitePlusiQ9BPX3.

Polymorphism and mutation databases

BioMutaiNCAPG.
DMDMi30172941.

Proteomic databases

EPDiQ9BPX3.
MaxQBiQ9BPX3.
PaxDbiQ9BPX3.
PeptideAtlasiQ9BPX3.
PRIDEiQ9BPX3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251496; ENSP00000251496; ENSG00000109805.
GeneIDi64151.
KEGGihsa:64151.
UCSCiuc003gpp.5. human.

Organism-specific databases

CTDi64151.
DisGeNETi64151.
GeneCardsiNCAPG.
HGNCiHGNC:24304. NCAPG.
HPAiHPA039613.
HPA040103.
MIMi606280. gene.
neXtProtiNX_Q9BPX3.
OpenTargetsiENSG00000109805.
PharmGKBiPA162397165.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2025. Eukaryota.
COG5218. LUCA.
GeneTreeiENSGT00390000001577.
HOVERGENiHBG039407.
InParanoidiQ9BPX3.
KOiK06678.
OMAiKCLHIVQ.
OrthoDBiEOG091G0K3M.
PhylomeDBiQ9BPX3.
TreeFamiTF101160.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000109805-MONOMER.
ReactomeiR-HSA-2514853. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

ChiTaRSiNCAPG. human.
GeneWikiiNCAPG.
GenomeRNAii64151.
PROiQ9BPX3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109805.
CleanExiHS_CAPG.
HS_NCAPG.
ExpressionAtlasiQ9BPX3. baseline and differential.
GenevisibleiQ9BPX3. HS.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027165. CND3.
IPR025977. Cnd3_C.
[Graphical view]
PANTHERiPTHR14418. PTHR14418. 1 hit.
PfamiPF12719. Cnd3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCND3_HUMAN
AccessioniPrimary (citable) accession number: Q9BPX3
Secondary accession number(s): Q3MJE0
, Q96SV9, Q9BUR3, Q9BVY1, Q9H914, Q9H9Z6, Q9HBI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 145 of the entry and version 1 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

Miscellaneous

Overexpressed in some cancer lines and some tumor cells.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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.