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NCAPG

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

NCAPG

Identifiers

Aliases

NCAPG, CAPG, CHCG, NY-MEL-3, YCG1, non-SMC condensin I complex subunit G

External IDs

OMIM:606280;MGI:1930197;HomoloGene:44071;GeneCards:NCAPG;OMA:NCAPG - orthologs

Gene location (Human)

Chr.	Chromosome 4 (human)^[1]

Band	4p15.31	Start	17,810,979bp^[1]
Band	4p15.31	End	17,844,865bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5\|5 B3	Start	45,827,261bp^[2]
Band	5\|5 B3	End	45,857,888bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ventricular zone

embryo

ganglionic eminence

gonad

trabecular bone

sperm

bone marrow

gingival epithelium

testicle

amniotic fluid

Top expressed in

otic placode

secondary oocyte

otic vesicle

primary oocyte

zygote

saccule

spermatocyte

epiblast

spermatid

tail of embryo

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding
Cellular component	condensin complex cytosol membrane condensed chromosome nucleus chromosome condensed chromosome, centromeric region cytoplasm
Biological process	cell division cell cycle mitotic chromosome condensation chromosome condensation
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


64151


54392

Ensembl


ENSG00000109805


ENSMUSG00000015880

UniProt


Q9BPX3


E9PWG6

RefSeq (mRNA)


NM_022346


NM_019438

RefSeq (protein)


NP_071741


NP_062311

Location (UCSC)

Chr 4: 17.81 – 17.84 Mb

Chr 5: 45.83 – 45.86 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Condensin complex subunit 3 also known ascondensin subunit CAP-G (CAP-G) ornon-SMC condensin I complex subunit G (NCAPG) is aprotein that in humans is encoded by theNCAPGgene.^[5]^[6]^[7] CAP-G is a subunit ofcondensin I, a large protein complex involved in chromosome condensation.

Interactions

[edit]

NCAPG has been shown tointeract withDNMT3B.^[8]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000109805 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000015880 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Jäger D, Stockert E, Jäger E, Güre AO, Scanlan MJ, Knuth A, Old LJ, Chen YT (Aug 2000). "Serological cloning of a melanocyte rab guanosine 5'-triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library".Cancer Res.60 (13):3584–91.PMID 10910072.
^Kimura K, Cuvier O, Hirano T (Feb 2001)."Chromosome condensation by a human condensin complex in Xenopus egg extracts".J. Biol. Chem.276 (8):5417–20.doi:10.1074/jbc.C000873200.PMID 11136719.
^"Entrez Gene: NCAPG non-SMC condensin I complex, subunit G".
^Geiman TM, Sankpal UT, Robertson AK, Chen Y, Mazumdar M, Heale JT, Schmiesing JA, Kim W, Yokomori K, Zhao Y, Robertson KD (2004)."Isolation and characterization of a novel DNA methyltransferase complex linking DNMT3B with components of the mitotic chromosome condensation machinery".Nucleic Acids Res.32 (9):2716–29.doi:10.1093/nar/gkh589.PMC 419596.PMID 15148359.

Geiman TM, Sankpal UT, Robertson AK, Chen Y, Mazumdar M, Heale JT, Schmiesing JA, Kim W, Yokomori K, Zhao Y, Robertson KD (2004)."Isolation and characterization of a novel DNA methyltransferase complex linking DNMT3B with components of the mitotic chromosome condensation machinery".Nucleic Acids Res.32 (9):2716–29.doi:10.1093/nar/gkh589.PMC 419596.PMID 15148359.
Xing H, Wilkerson DC, Mayhew CN, Lubert EJ, Skaggs HS, Goodson ML, Hong Y, Park-Sarge OK, Sarge KD (2005). "Mechanism of hsp70i gene bookmarking".Science.307 (5708):421–3.Bibcode:2005Sci...307..421X.doi:10.1126/science.1106478.PMID 15662014.S2CID 37132180.
Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (2006)."Phosphoproteome analysis of the human mitotic spindle".Proc. Natl. Acad. Sci. U.S.A.103 (14):5391–6.Bibcode:2006PNAS..103.5391N.doi:10.1073/pnas.0507066103.PMC 1459365.PMID 16565220.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006)."Global, in vivo, and site-specific phosphorylation dynamics in signaling networks".Cell.127 (3):635–48.doi:10.1016/j.cell.2006.09.026.PMID 17081983.S2CID 7827573.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007)."Large-scale mapping of human protein-protein interactions by mass spectrometry".Mol. Syst. Biol.3 (1): 89.doi:10.1038/msb4100134.PMC 1847948.PMID 17353931.

Structures of thecell nucleus /nuclear protein

Envelope (membrane)/
nuclear lamina

Nucleolus

Other

Chromatin Dot (PML body) Paraspeckle
SMC protein:	Cohesin SMC1A SMC1B SMC3 Condensin NCAPD2 NCAPD3 NCAPG NCAPG2 NCAPH NCAPH2 SMC2 SMC4 DNA repair SMC5 SMC6
Transition nuclear protein:	TNP1 TNP2
Nuclear matrix (Nucleoskeleton) Nucleoplasm (Nucleosol)
LITAF
see alsotranscription factors and intracellular receptors

see alsonucleus diseases

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