Condensin complex subunit 2 (NCAPH)

The protein contains 741 amino acids for an estimated molecular weight of 82563 Da.

 

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 (PubMed:11136719). Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). (updated: Nov. 7, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 48%
Model score: 0
No model available.

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VariantDescription
dbSNP:rs2305935
MCPH23

The reference OMIM entry for this protein is 602332

Non-smc condensin i complex subunit h; ncaph
Condensin i complex, non-smc subunit h
Chromosome-associated protein h; caph
Barren, drosophila, homolog of, 1; brrn1

CLONING

Bhat et al. (1996) established that in Drosophila the product of 'barr' (barren) is necessary for sister chromatid separation and modulates topoisomerase II (126430) activity. The barr gene is evolutionarily conserved and sequence similarity searches identified a 2.7-kb human homolog.

MAPPING

Cabello et al. (1997) reported the genomic localization of this human member of the barr gene family, symbolized BRRN1 by them. By Southern analysis of monochromosomal human/rodent hybrid cells, they mapped the BRRN1 gene to chromosome 2. By fluorescence in situ hybridization, they localized the assignment to 2q11.2. This assignment was confirmed and refined by radiation hybrid analysis.

GENE FUNCTION

Aono et al. (2002) reported that Cnd2, the fission yeast homolog of Drosophila barren and the budding yeast protein Brn1, is required for both interphase and mitotic condensation. In Cnd2 mutants, ultraviolet-induced DNA damage was not repaired and cells arrested by hydroxyurea did not recover. Cds1 (604373) activation was abolished in the presence of hydroxyurea in Cnd2 mutant cells and in cells where other condensin subunits had been disrupted. In the absence of hydroxyurea, a G2 checkpoint delay occurred in Cnd2 mutants in a manner dependent on Cds1 and Rad3 but not Chk1 (603078), before the mitotic condensation defect. Furthermore, the Cnd2 mutation was synthetic-lethal with mutations of excision repair, RecQ helicase (see 600537), and DNA replication enzymes. ... More on the omim web site

Subscribe to this protein entry history

Nov. 16, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602332 was added.