Summary: FHA Ki67 binding domain of hNIFK
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MKI67IP Edit Wikipedia article
|MKI67 (FHA domain) interacting nucleolar phosphoprotein|
PDB rendering based on 2aff.
|RNA expression pattern|
|FHA Ki67 binding domain of hNIFK|
the solution structure of the ki67fha/hnifk(226-269)3p complex
MKI67 FHA domain-interacting nucleolar phosphoprotein contains an RNA recognition motif (RRM) near to the N-terminus and a FHA Ki67 binding domain near to the C-terminus. There are two conserved sequence motifs within the FHA Ki67 binding domain: TPVCTP and LERRKS, this domain binds to the forkhead-associated domain of human Ki67. High-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. This interaction is involved in cell cycle regulation.
- Takagi M, Sueishi M, Saiwaki T, Kametaka A, Yoneda Y (Jul 2001). "A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis". J Biol Chem 276 (27): 25386–91. doi:10.1074/jbc.M102227200. PMID 11342549.
- "Entrez Gene: MKI67IP MKI67 (FHA domain) interacting nucleolar phosphoprotein".
- Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD (November 2005). "Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67". Nat. Struct. Mol. Biol. 12 (11): 987–93. doi:10.1038/nsmb1008. PMID 16244663.
- Scherl A, Couté Y, Déon C, et al. (2003). "Functional proteomic analysis of human nucleolus.". Mol. Biol. Cell 13 (11): 4100–9. doi:10.1091/mbc.E02-05-0271. PMC 133617. PMID 12429849.
- 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 139241. PMID 12477932.
- Li H, Byeon IJ, Ju Y, Tsai MD (2004). "Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions.". J. Mol. Biol. 335 (1): 371–81. doi:10.1016/j.jmb.2003.10.032. PMID 14659764.
- 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 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
- Byeon IJ, Li H, Song H, et al. (2006). "Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.". Nat. Struct. Mol. Biol. 12 (11): 987–93. doi:10.1038/nsmb1008. PMID 16244663.
- Nousiainen M, Silljé HH, Sauer G, et al. (2006). "Phosphoproteome analysis of the human mitotic spindle.". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
|This article on a gene on chromosome 2 is a stub. You can help Wikipedia by expanding it.|
FHA Ki67 binding domain of hNIFK Provide feedback
This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with PF00076. There are two conserved sequence motifs: TPVCTP and LERRKS. This domain is found on the human nucleolar protein hNIFK. It binds to the fork-head-associated domain of human Ki67. High-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. This interaction is involved in cell cycle regulation.
Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD;, Nat Struct Mol Biol. 2005;12:987-993.: Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. PUBMED:16244663 EPMC:16244663
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR021043
This entry represents eukaryotic proteins that contain a domain of approximately 40 amino acids in length. These proteins are found in association with . There are two conserved sequence motifs: TPVCTP and LERRKS. This domain is found on the human nucleolar protein hNIFK. It binds to the fork-head-associated domain of human Ki67. High-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. This interaction is involved in cell cycle regulation [PUBMED:16244663].
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Curation and family details
|Author:||Mistry J, Gavin OL|
|Number in seed:||5|
|Number in full:||73|
|Average length of the domain:||39.30 aa|
|Average identity of full alignment:||63 %|
|Average coverage of the sequence by the domain:||14.58 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
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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 hNIFK_binding 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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