INCENP

Inner centromere protein is a protein that in humans is encoded by the INCENP gene.^[5][6][7] It is a regulatory protein in the chromosome passenger complex (CPC).^[8] It is involved in regulation of the catalytic proteins Aurora B and Aurora C.^[9][10][11] It acts in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N-terminal domain of INCENP is the domain involved in formation of this three-helical bundle while its C-terminal domain is responsible for the interaction with Aurora B.^[12][11]

INCENP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2QFA, 4AF3
Identifiers
Aliases	INCENP, inner centromere protein
External IDs	OMIM: 604411; MGI: 1313288; HomoloGene: 9624; GeneCards: INCENP; OMA:INCENP - orthologs
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q12.3 Start 62,123,998 bp[1] End 62,153,169 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19 A|19 6.1 cM Start 9,849,660 bp[2] End 9,876,915 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence sural nerve bone marrow cell mucosa of esophagus cerebellar hemisphere right hemisphere of cerebellum stromal cell of endometrium testicle prefrontal cortex Top expressed in Paneth cell condyle fossa ureter primitive streak fetal liver hematopoietic progenitor cell renal corpuscle Rostral migratory stream primary oocyte internal carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytoplasm central element pericentric heterochromatin spindle nucleoplasm lateral element chromosome chromocenter synaptonemal complex chromosome, centromeric region microtubule cytoskeleton kinetochore nucleus cytosol nuclear body midbody protein-containing complex Biological process chromosome segregation cell division cell cycle mitotic cytokinesis mitotic sister chromatid segregation regulation of mitotic cytokinesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3619 16319 Ensembl ENSG00000149503 ENSMUSG00000024660 UniProt Q9NQS7 Q9WU62 RefSeq (mRNA) NM_001040694 NM_020238 NM_016692 NM_001369356 RefSeq (protein) NP_001035784 NP_064623 NP_057901 Location (UCSC) Chr 11: 62.12 – 62.15 Mb Chr 19: 9.85 – 9.88 Mb PubMed search [3] [4]
Wikidata
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Chromosome passenger complex (CPC) protein INCENP N terminal
Identifiers
Symbol	INCENP_N
Pfam	PF12178
InterPro	IPR022006
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Inner centromere protein, ARK binding region
Identifiers
Symbol	INCENP_ARK-bind
Pfam	PF03941
InterPro	IPR005635
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In mammalian cells, two broad groups of centromere-interacting proteins have been described: constitutively binding centromere proteins and 'passenger' (or transiently interacting) proteins.^[13] The constitutive proteins include CENPA (centromere protein A), CENPB, CENPC1, and CENPD.

The term 'passenger proteins' encompasses a broad collection of proteins that localize to the centromere during specific stages of the cell cycle.^[14] These include CENPE; MCAK; KID; cytoplasmic dynein (e.g., DYNC1H1); CliPs (e.g. CLIP1); and CENPF/mitosin (CENPF). The inner centromere proteins (INCENPs),^[5] the initial members of the passenger protein group, display a broad localization along chromosomes in the early stages of mitosis but gradually become concentrated at centromeres as the cell cycle progresses into mid-metaphase. During telophase, the proteins are located within the midbody in the intercellular bridge, where they are discarded after cytokinesis.^[7][15]

Interactions

INCENP has been shown to interact with H2AFZ,^[16] Survivin^[17] and CDCA8.^[18] The ARK binding region has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.^[19]