Condensin complex subunit 1 (NCAPD2)
The protein contains 1401 amino acids for an estimated molecular weight of 157182 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. May target the condensin complex to DNA via its C-terminal domain (PubMed:11136719). May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Required for decatenation of non-centromeric ultrafine DNA bridges during anaphase. 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:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
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Biological Process
Cell division
Chromosome separation
Meiotic chromosome condensation
Mitotic cell cycle
Mitotic chromosome condensation
The reference OMIM entry for this protein is 615638
Non-smc condensin i complex subunit d2; ncapd2
Chromosome condensation-related smc-associated protein 1; cnap1
Kiaa0159
DESCRIPTION
NCAPD2 is a subunit of the condensin multiprotein complex required for mitotic chromosome condensation (Schmiesing et al., 2000).CLONING
By sequencing clones obtained from a size-fractionated KG-1 human immature myeloid leukemia cell line cDNA library, Nagase et al. (1995) obtained an NCAPD2 clone, which they designated KIAA0159. The 3-prime end of the transcript contains an Alu sequence, and the deduced 1,401-amino acid protein is predicted to have a transmembrane segment. Northern blot analysis detected NCAPD2 expression in all human tissues and cell lines examined. Database analysis detected an ortholog of NCAPD2 in yeast. By Western blot analysis of HeLa cell nuclear extracts, Schmiesing et al. (2000) found that NCAPD2, which they called CNAP1, had an apparent molecular mass of 155 kD.GENE FUNCTION
By coimmunoprecipitation and Western blot analysis of HeLa cell nuclear extract, Schmiesing et al. (2000) found that CNAP1 interacted with the condensin subunits CAPC (SMC4; 605575) and CAPE (SMC2; 605576) in a stoichiometric manner. In synchronized HeLa cells, the 3 condensin proteins localized to the cytoplasm during interphase, but a subpopulation of the complex colocalized at specific chromosomal foci. During late G2/early prophase, these foci colocalized with phosphorylated histone H3 (see 602810) and, like phosphorylated histone H3, the condensin foci grew to cover the entire length of chromosomes during mitosis. Following mitosis, the majority of condensin subunits relocalized to the cytoplasm.MAPPING
By PCR of a human/rodent hybrid panel, Nagase et al. (1995) mapped the NCAPD2 gene to chromosome 12. Hartz (2014) mapped the NCAPD2 gene to chromosome 12p13.31 based on an alignment of the NCAPD2 sequence (GenBank GENBANK D63880) with the genomic sequence (GRCh37). ... More on the omim web site
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 615638 was added.