Summary: Chromosome passenger complex (CPC) protein INCENP N terminal
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INCENP Edit Wikipedia article
|RNA expression pattern|
|View/Edit Human||View/Edit Mouse|
|Chromosome passenger complex (CPC) protein INCENP N terminal|
|Inner centromere protein, ARK binding region|
In mammalian cells, two broad groups of centromere-interacting proteins have been described: constitutively binding centromere proteins and 'passenger' (or transiently interacting) proteins. 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. These include CENPE; MCAK; KID; cytoplasmic dynein (e.g., DYNC1H1); CliPs (e.g. CLIP1); and CENPF/mitosin (CENPF). The inner centromere proteins (INCENPs), 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.
INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function 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.
INCENP has been shown to interact with H2AFZ, Survivin and CDCA8. 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.
- "Human PubMed Reference:".
- "Mouse PubMed Reference:".
- Earnshaw WC, Cooke CA (Sep 1991). "Analysis of the distribution of the INCENPs throughout mitosis reveals the existence of a pathway of structural changes in the chromosomes during metaphase and early events in cleavage furrow formation". J Cell Sci. 98 (4): 443–61. PMID 1860899.
- Adams RR, Eckley DM, Vagnarelli P, Wheatley SP, Gerloff DL, Mackay AM, Svingen PA, Kaufmann SH, Earnshaw WC (Jul 2001). "Human INCENP colocalizes with the Aurora-B/AIRK2 kinase on chromosomes and is overexpressed in tumour cells". Chromosoma. 110 (2): 65–74. doi:10.1007/s004120100130. PMID 11453556.
- "Entrez Gene: INCENP inner centromere protein antigens 135/155kDa".
- Choo, K. H. Andy (1997). The centromere. Oxford [Oxfordshire]: Oxford University Press. ISBN 0-19-857780-X.
- Earnshaw WC, Mackay AM (September 1994). "Role of nonhistone proteins in the chromosomal events of mitosis". FASEB J. 8 (12): 947–56. PMID 8088460.
- Cutts SM, Fowler KJ, Kile BT, Hii LL, O'Dowd RA, Hudson DF, Saffery R, Kalitsis P, Earle E, Choo KH (July 1999). "Defective chromosome segregation, microtubule bundling and nuclear bridging in inner centromere protein gene (Incenp)-disrupted mice". Hum. Mol. Genet. 8 (7): 1145–55. doi:10.1093/hmg/8.7.1145. PMID 10369859.
- Jeyaprakash, A. A.; Klein, U. R.; Lindner, D.; Ebert, J.; Nigg, E. A.; Conti, E. (2007). "Structure of a Survivin–Borealin–INCENP Core Complex Reveals How Chromosomal Passengers Travel Together". Cell. 131 (2): 271–285. doi:10.1016/j.cell.2007.07.045. PMID 17956729.
- Rangasamy D, Berven L, Ridgway P, Tremethick DJ (April 2003). "Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development". EMBO J. 22 (7): 1599–607. doi:10.1093/emboj/cdg160. PMC . PMID 12660166.
- Wheatley SP, Carvalho A, Vagnarelli P, Earnshaw WC (June 2001). "INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis". Curr. Biol. 11 (11): 886–90. doi:10.1016/S0960-9822(01)00238-X. PMID 11516652.
- Gassmann R, Carvalho A, Henzing AJ, Ruchaud S, Hudson DF, Honda R, Nigg EA, Gerloff DL, Earnshaw WC (July 2004). "Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle". J. Cell Biol. 166 (2): 179–91. doi:10.1083/jcb.200404001. PMC . PMID 15249581.
- Leverson JD, Huang HK, Forsburg SL, Hunter T (April 2002). "The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis". Mol. Biol. Cell. 13 (4): 1132–43. doi:10.1091/mbc.01-07-0330. PMC . PMID 11950927.
- Ainsztein AM, Kandels-Lewis SE, Mackay AM, Earnshaw WC (1999). "INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1.". J. Cell Biol. 143 (7): 1763–74. doi:10.1083/jcb.143.7.1763. PMC . PMID 9864353.
- Martineau-Thuillier S, Andreassen PR, Margolis RL (1999). "Colocalization of TD-60 and INCENP throughout G2 and mitosis: evidence for their possible interaction in signalling cytokinesis.". Chromosoma. 107 (6-7): 461–70. doi:10.1007/s004120050330. PMID 9914378.
- Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC . PMID 10737800.
- Wheatley SP, Kandels-Lewis SE, Adams RR, et al. (2001). "INCENP binds directly to tubulin and requires dynamic microtubules to target to the cleavage furrow.". Exp. Cell Res. 262 (2): 122–7. doi:10.1006/excr.2000.5088. PMID 11139336.
- Wheatley SP, Carvalho A, Vagnarelli P, Earnshaw WC (2001). "INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis.". Curr. Biol. 11 (11): 886–90. doi:10.1016/S0960-9822(01)00238-X. PMID 11516652.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC . PMID 12477932.
- Parra MT, Viera A, Gómez R, et al. (2003). "Dynamic relocalization of the chromosomal passenger complex proteins inner centromere protein (INCENP) and aurora-B kinase during male mouse meiosis.". J. Cell. Sci. 116 (Pt 6): 961–74. doi:10.1242/jcs.00330. PMID 12584241.
- Rangasamy D, Berven L, Ridgway P, Tremethick DJ (2003). "Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development.". EMBO J. 22 (7): 1599–607. doi:10.1093/emboj/cdg160. PMC . PMID 12660166.
- Honda R, Körner R, Nigg EA (2004). "Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis.". Mol. Biol. Cell. 14 (8): 3325–41. doi:10.1091/mbc.E02-11-0769. PMC . PMID 12925766.
- Wheatley SP, Henzing AJ, Dodson H, et al. (2004). "Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo.". J. Biol. Chem. 279 (7): 5655–60. doi:10.1074/jbc.M311299200. PMID 14610074.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gassmann R, Carvalho A, Henzing AJ, et al. (2004). "Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle.". J. Cell Biol. 166 (2): 179–91. doi:10.1083/jcb.200404001. PMC . PMID 15249581.
- Li X, Sakashita G, Matsuzaki H, et al. (2004). "Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C.". J. Biol. Chem. 279 (45): 47201–11. doi:10.1074/jbc.M403029200. PMID 15316025.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC . PMID 15489334.
- Zhu C, Bossy-Wetzel E, Jiang W (2005). "Recruitment of MKLP1 to the spindle midzone/midbody by INCENP is essential for midbody formation and completion of cytokinesis in human cells.". Biochem. J. 389 (Pt 2): 373–81. doi:10.1042/BJ20050097. PMC . PMID 15796717.
- Chen HL, Tang CJ, Chen CY, Tang TK (2005). "Overexpression of an Aurora-C kinase-deficient mutant disrupts the Aurora-B/INCENP complex and induces polyploidy.". J. Biomed. Sci. 12 (2): 297–310. doi:10.1007/s11373-005-0980-0. PMID 15917996.
- Vader G, Kauw JJ, Medema RH, Lens SM (2006). "Survivin mediates targeting of the chromosomal passenger complex to the centromere and midbody.". EMBO Rep. 7 (1): 85–92. doi:10.1038/sj.embor.7400562. PMC . PMID 16239925.
- Goto H, Kiyono T, Tomono Y, et al. (2006). "Complex formation of Plk1 and INCENP required for metaphase-anaphase transition.". Nat. Cell Biol. 8 (2): 180–7. doi:10.1038/ncb1350. PMID 16378098.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Chromosome passenger complex (CPC) protein INCENP N terminal Provide feedback
This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.
Jeyaprakash AA, Klein UR, Lindner D, Ebert J, Nigg EA, Conti E;, Cell. 2007;131:271-285.: Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together. PUBMED:17956729 EPMC:17956729
This tab holds annotation information from the InterPro database.
InterPro entry IPR022006
This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N-terminal domain is the domain involved in formation of this three helical bundle.
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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|Author:||Mistry J, Gavin OL|
|Number in seed:||15|
|Number in full:||86|
|Average length of the domain:||35.80 aa|
|Average identity of full alignment:||49 %|
|Average coverage of the sequence by the domain:||4.53 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
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There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
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Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the INCENP_N domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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