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Details on Person UniProt:Q15021 NCAPD2

Class:IdReferenceGeneProduct:87692
_chainChangeLogchain:1-1401 added on Fri February 6 2015
_displayNameUniProt:Q15021 NCAPD2
_timestamp2024-11-03 20:13:47
chainchain:1-1401
checksum35E31642B94B513D
commentFUNCTION 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).SUBUNIT 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. Interacts with histones H1 and H3.INTERACTION 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.DOMAIN The C-terminal domain interacts with histones H1 and H3, and may be responsible for condensin complex targeting to mitotic chromosomes. This domain is independent from the bipartite nuclear localization signal, although they are contained within the same region.PTM Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPH and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity).DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the CND1 (condensin subunit 1) family.SEQUENCE CAUTION Extended N-terminus.
descriptionrecommendedName: Condensin complex subunit 1 alternativeName: Chromosome condensation-related SMC-associated protein 1 alternativeName: Chromosome-associated protein D2 shortName: hCAP-D2 alternativeName: Non-SMC condensin I complex subunit D2 alternativeName: XCAP-D2 homolog
geneNameNCAPD2
CAPD2
CNAP1
KIAA0159
identifierQ15021
isSequenceChangedFALSE
keywordCell cycle
Cell division
Chromosome
Cytoplasm
Direct protein sequencing
Disease variant
DNA condensation
Mitosis
Nucleus
Phosphoprotein
Primary microcephaly
Proteomics identification
Reference proteome
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
nameNCAPD2
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8997078] ENSEMBL:ENSG00000010292 NCAPD2 [Homo sapiens]
secondaryIdentifierCND1_HUMAN
D3DUR4
Q8N6U3
sequenceLength1401
species[Species:48887] Homo sapiens
(referenceEntity)[EntityWithAccessionedSequence:1638140] NCAPD2 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:2517887] p-T1339,T1384,T1389-NCAPD2 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:2529011] p-S-NCAPD2 [cytosol] [Homo sapiens]
(referenceSequence)[ModifiedResidue:2517880] O-phospho-L-threonine at 1339
[ModifiedResidue:2517881] O-phospho-L-threonine at 1389
[ModifiedResidue:2517884] O-phospho-L-threonine at 1384
[ModifiedResidue:2529010] O-phospho-L-serine at unknown position
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No pathways have been reviewed or authored by UniProt:Q15021 NCAPD2 (87692)