NCAPH

Condensin complex subunit 2 also known as chromosome-associated protein H (CAP-H) or non-SMC condensin I complex subunit H (NCAPH) is a protein that in humans is encoded by the NCAPH gene.[5][6] CAP-H is a subunit of condensin I, a large protein complex involved in chromosome condensation

NCAPH
Identifiers
Aliases	NCAPH, BRRN1, CAP-H, non-SMC condensin I complex subunit H, MCPH23, CAPH
External IDs	OMIM: 602332 MGI: 2444777 HomoloGene: 133986 GeneCards: NCAPH
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q11.2 Start 96,335,766 bp[1] End 96,377,091 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 F1 Start 127,103,809 bp[2] End 127,133,954 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • chromatin binding • DNA topoisomerase binding • DNA topoisomerase (ATP-hydrolyzing) activator activity Cellular component • cytoplasm • membrane • chromosome • condensin complex • nuclear condensin complex • cell nucleus • cytosol Biological process • cell division • cell cycle • chromosome condensation • mitotic chromosome condensation • meiotic chromosome condensation • meiotic chromosome segregation • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity • female meiotic nuclear division • female meiosis chromosome separation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	23397	215387
Ensembl	ENSG00000121152	ENSMUSG00000034906
UniProt	Q15003	Q8C156
RefSeq (mRNA)	NM_001281710 NM_001281711 NM_001281712 NM_015341	NM_144818
RefSeq (protein)	NP_001268639 NP_001268640 NP_001268641 NP_056156	NP_659067
Location (UCSC)	Chr 2: 96.34 – 96.38 Mb	Chr 2: 127.1 – 127.13 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

CAP-H is a member of the barr protein family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. CAP-H is associated with mitotic chromosomes, except during the early phase of chromosome condensation. During interphase, the protein has a distinct punctate nucleolar localization.[6]

Model organisms

Ncaph knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Salmonella infection	Abnormal[7]
Citrobacter infection	Normal[8]
All tests and analysis from[9][10]

Model organisms have been used in the study of NCAPH function. A conditional knockout mouse line, called Ncaph^{tm1a(EUCOMM)Wtsi}[11][12] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty four tests were carried out on mutant mice and three significant abnormalities were observed.[9] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and an increased susceptibility to bacterial infection was observed in male animals.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000121152 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034906 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Cabello OA, Baldini A, Bhat M, Bellen H, Belmont JW (Dec 1997). "Localization of BRRN1, the human homologue of Drosophila barr, to 2q11.2". Genomics. 46 (2): 311–3. doi:10.1006/geno.1997.5021. PMID 9417923.
6. "Entrez Gene: NCAPH non-SMC condensin I complex, subunit H".
7. "Salmonella infection data for Ncaph". Wellcome Trust Sanger Institute.
8. "Citrobacter infection data for Ncaph". Wellcome Trust Sanger Institute.
9. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
10. Mouse Resources Portal, Wellcome Trust Sanger Institute.
11. "International Knockout Mouse Consortium".
12. "Mouse Genome Informatics".
13. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
14. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
15. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
16. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Further reading

• Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S (1995). "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". DNA Research. 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
• Hirano T, Kobayashi R, Hirano M (May 1997). "Condensins, chromosome condensation protein complexes containing XCAP-C, XCAP-E and a Xenopus homolog of the Drosophila Barren protein". Cell. 89 (4): 511–21. doi:10.1016/S0092-8674(00)80233-0. PMID 9160743.
• Kimura K, Cuvier O, Hirano T (Feb 2001). "Chromosome condensation by a human condensin complex in Xenopus egg extracts". The Journal of Biological Chemistry. 276 (8): 5417–20. doi:10.1074/jbc.C000873200. PMID 11136719.
• Cabello OA, Eliseeva E, He WG, Youssoufian H, Plon SE, Brinkley BR, Belmont JW (Nov 2001). "Cell cycle-dependent expression and nucleolar localization of hCAP-H". Molecular Biology of the Cell. 12 (11): 3527–37. doi:10.1091/mbc.12.11.3527. PMC 60273. PMID 11694586.
• Heale JT, Ball AR, Schmiesing JA, Kim JS, Kong X, Zhou S, Hudson DF, Earnshaw WC, Yokomori K (Mar 2006). "Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair". Molecular Cell. 21 (6): 837–48. doi:10.1016/j.molcel.2006.01.036. PMID 16543152.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (Apr 2006). "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.