Summary: MIZ/SP-RING zinc finger
This is the Wikipedia entry entitled "MIZ zinc finger". More...
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MIZ zinc finger Edit Wikipedia article
In molecular biology the MIZ-type zinc finger domain is a zinc finger-containing protein with homology to the yeast protein, Nfi-1. Miz1 is a sequence specific DNA binding protein that can function as a positive-acting transcription factor. Miz1 binds to the homeobox protein Msx2, enhancing the specific DNA-binding ability of Msx2. Other proteins containing this domain include the human pias family (protein inhibitor of activated STAT protein). The name MIZ is derived from Msx-interacting-zinc finger. The crystal structure of S. cerevisiae sumo e3 ligase siz1 containing this domain has been solved.
- Stead, M.A., Trinh, C.H., Garnett, J.A., Carr, S.B., Baron, A.J., Edwards, T.A., Wright, S.C. (2007). "A beta-sheet interaction interface directs the tetramerisation of the Miz-1 POZ domain.". J.Mol.Biol. 373: 820–826. doi:10.1016/j.jmb.2007.08.026.
- Wu L, Wu H, Ma L, Sangiorgi F, Wu N, Bell JR, Lyons GE, Maxson R (July 1997). "Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA". Mech. Dev. 65 (1-2): 3–17. doi:10.1016/S0925-4773(97)00032-4. PMID 9256341.
MIZ/SP-RING zinc finger Provide feedback
This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organisation .
Wu L, Wu H, Ma L, Sangiorgi F, Wu N, Bell JR, Lyons GE, Maxson R; , Mech Dev 1997;65:3-17.: Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA. PUBMED:9256341 EPMC:9256341
Zhao X, Blobel G; , Proc Natl Acad Sci U S A 2005;102:4777-4782.: From The Cover: A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. PUBMED:15738391 EPMC:15738391
Cheng CH, Lo YH, Liang SS, Ti SC, Lin FM, Yeh CH, Huang HY, Wang TF; , Genes Dev. 2006;20:2067-2081.: SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae. PUBMED:16847351 EPMC:16847351
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004181
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
This entry represents MIZ-type zinc finger domains. Miz1 (Msx-interacting-zinc finger) is a zinc finger-containing protein with homology to the yeast protein, Nfi-1. Miz1 is a sequence specific DNA binding protein that can function as a positive-acting transcription factor. Miz1 binds to the homeobox protein Msx2, enhancing the specific DNA-binding ability of Msx2 [PUBMED:9256341]. Other proteins containing this domain include the human pias family (protein inhibitor of activated STAT protein).
More information about these proteins can be found at Protein of the Month: Zinc Fingers [PUBMED:].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
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This clan includes the Ring zinc finger domains as well as the U-box domain that appears to have lost the zinc coordinating cysteine residues .
The clan contains the following 38 members:Baculo_IE-1 Baculo_RING DUF1644 FANCL_C IBR Prok-RING_1 Prok-RING_2 Prok-RING_4 RINGv Rtf2 U-box UPF1_Zn_bind zf-ANAPC11 zf-C3H2C3 zf-C3HC4 zf-C3HC4_2 zf-C3HC4_3 zf-C3HC4_4 zf-C3HC4_5 zf-MIZ zf-NOSIP zf-Nse zf-P11 zf-rbx1 zf-RING-like zf-RING_10 zf-RING_11 zf-RING_2 zf-RING_4 zf-RING_5 zf-RING_6 zf-RING_7 zf-RING_9 zf-RING_UBOX zf-UBP zf-UDP zinc_ribbon_16 Zn_ribbon_17
We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Psi-blast Q9UN16|
|Author:||Bateman A, Mistry J, Wood V|
|Number in seed:||33|
|Number in full:||1753|
|Average length of the domain:||50.50 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||7.19 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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 zf-MIZ domain has been found. There are 6 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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