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1  structure 40  species 0  interactions 73  sequences 2  architectures

Family: hNIFK_binding (PF12196)

Summary: FHA Ki67 binding domain of hNIFK

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This is the Wikipedia entry entitled "MKI67IP". More...

MKI67IP Edit Wikipedia article

MKI67 (FHA domain) interacting nucleolar phosphoprotein

PDB rendering based on 2aff.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols MKI67IP; NIFK; Nopp34
External IDs OMIM611970 MGI1915199 HomoloGene49862 GeneCards: MKI67IP Gene
RNA expression pattern
PBB GE MKI67IP gnf1h00768 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 84365 67949
Ensembl ENSG00000155438 ENSMUSG00000026377
UniProt Q9BYG3 Q91VE6
RefSeq (mRNA) NM_032390 NM_026472
RefSeq (protein) NP_115766 NP_080748
Location (UCSC) Chr 2:
122.48 – 122.49 Mb
Chr 1:
118.32 – 118.33 Mb
PubMed search [1] [2]
FHA Ki67 binding domain of hNIFK
PDB 2aff EBI.jpg
the solution structure of the ki67fha/hnifk(226-269)3p complex
Identifiers
Symbol hNIFK_binding
Pfam PF12196
InterPro IPR021043

MKI67 FHA domain-interacting nucleolar phosphoprotein is a protein that in humans is encoded by the MKI67IP gene.[1][2]

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.[3]

References[edit]

  1. ^ 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. 
  2. ^ "Entrez Gene: MKI67IP MKI67 (FHA domain) interacting nucleolar phosphoprotein". 
  3. ^ 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. 

Further reading[edit]


This article incorporates text from the public domain Pfam and InterPro IPR021043

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

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.

Literature references

  1. 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].

Domain organisation

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Alignments

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(5)
Full
(73)
Representative proteomes NCBI
(53)
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RP15
(1)
RP35
(2)
RP55
(9)
RP75
(31)
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  Seed
(5)
Full
(73)
Representative proteomes NCBI
(53)
Meta
(0)
RP15
(1)
RP35
(2)
RP55
(9)
RP75
(31)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(5)
Full
(73)
Representative proteomes NCBI
(53)
Meta
(0)
RP15
(1)
RP35
(2)
RP55
(9)
RP75
(31)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

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Trees

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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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

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Seed source: pdb_2aff
Previous IDs: none
Type: Domain
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 information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 29.0 27.9
Noise cut-off 20.4 19.6
Model length: 41
Family (HMM) version: 3
Download: download the raw HMM for this family

Species distribution

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Structures

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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