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0ZNF31_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameZNF31
DescriptionZinc finger protein 31 (zinc finger protein kox29) (zinc finger and scan domain containing protein 20).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
A number of C2H2-zinc finger proteins contain a highly conserved N-terminal motif termed the SCAN domain. The SCAN domain may play an important role in the assembly and function of this newly defined subclass of transcriptional regulators .
  IPR003309:Transcriptional regulator SCAN
Zinc finger domains .re nucleic acid-binding protein structures first identified in the Xenopus laevis transcription factor TFIIIA. These domains have since been found in numerous nucleic acid-binding proteins. A zinc finger domain is composed of 25 to 30 amino-acid residues including 2 conserved Cys and 2 conserved His residues in a C-2-C-12-H-3-H type motif. The 12 residues separating the second Cys and the first His are mainly polar and basic.mplicating this region in particular in nucleic acid binding. The zinc finger motif is an unusually small.elf-folding domain in which Zn is a crucial component of its tertiary structure. All bind 1 atom of Zn in a tetrahedral array to yield a finger-like projection.hich interacts with nucleotides in the major groove of the nucleic acid. The Zn binds to the conserved Cys and His residues. Fingers have been found to bind to about 5 base pairs of nucleic acid containing short runs of guanine residues. They have the ability to bind to both RNA and DNA.nd it has been suggested that the zinc finger may thus represent the original nucleic acid binding protein. It has also been suggested that a Zn-centred domain could be used in a protein interaction..g. in protein kinase C. Many classes of zinc fingers are characterized according to the number and positions of the histidine and cysteine residues involved in the zinc atom coordination. In the first class to be characterized.alled C2H2.he first pair of zinc coordinating residues are cysteines.hile the second pair are histidines.
  IPR007086:Zinc finger, C2H2-subtype
Zinc finger domains .re nucleic acid-binding protein structures first identified in the Xenopus laevis transcription factor TFIIIA. These domains have since been found in numerous nucleic acid-binding proteins. A zinc finger domain is composed of 25 to 30 amino-acid residues including 2 conserved Cys and 2 conserved His residues in a C-2-C-12-H-3-H type motif. The 12 residues separating the second Cys and the first His are mainly polar and basic.mplicating this region in particular in nucleic acid binding. The zinc finger motif is an unusually small.elf-folding domain in which Zn is a crucial component of its tertiary structure. All bind 1 atom of Zn in a tetrahedral array to yield a finger-like projection.hich interacts with nucleotides in the major groove of the nucleic acid. The Zn binds to the conserved Cys and His residues. Fingers have been found to bind to about 5 base pairs of nucleic acid containing short runs of guanine residues. They have the ability to bind to both RNA and DNA.nd it has been suggested that the zinc finger may thus represent the original nucleic acid binding protein. It has also been suggested that a Zn-centred domain could be used in a protein interaction..g. in protein kinase C. Many classes of zinc fingers are characterized according to the number and positions of the histidine and cysteine residues involved in the zinc atom coordination. In the first class to be characterized.alled C2H2.he first pair of zinc coordinating residues are cysteines.hile the second pair are histidines.
  IPR007087:Zinc finger, C2H2-type
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR009057:Homeodomain-like
The retroviral oncogene v-myb.nd its cellular counterpart c-myb.ncode nuclear DNA-binding proteins. These belong to the SANT domain family that specifically recognize the sequence YAAC(G/T)G . In myb.ne of the most conserved regions consisting of three tandem repeats has been shown to be involved in DNA-binding .
  IPR001005:Myb, DNA-binding
The Krueppel-associated box (KRAB) is a domain of around 75 amino acids that is found in the N-terminal part of about one third of eukaryotic Krueppel-type C2H2 zinc finger proteins (ZFPs) . It is enriched in charged amino acids and can be divided into subregions A and B.hich are predicted to fold into two amphipathic alpha-helices. The KRAB A and B boxes can be separated by variable spacer segments and many KRAB proteins contain only the A box .The functions currently known for members of the KRAB-containing protein family include transcriptional repression of RNA polymerase I.I.nd III promoters.inding and splicing of RNA.nd control of nucleolus function. The KRAB domain functions as a transcriptional repressor when tethered to the template DNA by a DNA-binding domain. A sequence of 45 amino acids in the KRAB A subdomain has been shown to be necessary and sufficient for transcriptional repression. The B box does not repress by itself but does potentiate the repression exerted by the KRAB A subdomain . Gene silencing requires the binding of the KRAB domain to the RING-B box-coiled coil (RBCC) domain of the KAP-1/TIF1-beta corepressor. As KAP-1 binds to the heterochromatin proteins HP1.t has been proposed that the KRAB-ZFP-bound target gene could be silenced following recruitment to heterochromatin .KRAB-ZFPs probably constitute the single largest class of transcription factors within the human genome . Although the function of KRAB-ZFPs is largely unknown.hey appear to play important roles during cell differentiation and development. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B.
  IPR001909:KRAB box
IPR003309:SCAN 
Evalue:-8.88605690002441 
Location:3-74IPR007087:zf-C2H2 
Evalue:-7.55284214019775 
Location:837-859IPR007087:zf-C2H2 
Evalue:-7.55284214019775 
Location:672-694IPR007087:zf-C2H2 
Evalue:-7.45593214035034 
Location:700-722IPR007087:zf-C2H2 
Evalue:-7.17392539978027 
Location:893-915IPR007087:zf-C2H2 
Evalue:-7.16749095916748 
Location:728-750IPR007087:zf-C2H2 
Evalue:-7.13076829910278 
Location:809-831IPR007087:zf-C2H2 
Evalue:-6.82390880584717 
Location:921-943IPR007087:zf-C2H2 
Evalue:-6.24412536621094 
Location:865-887IPR007087:zf-C2H2 
Evalue:-5.76955127716064 
Location:949-971IPR007087:zf-C2H2 
Evalue:-4.72124624252319 
Location:644-666IPR001005:SANT 
Evalue:-1.17392519729917 
Location:416-480IPR009057:Homeodomain_like 
Evalue:0 
Location:250-329IPR001909:KRAB 
Evalue:0.322219294733919 
Location:149-210
SequencesProtein: ZNF31_HUMAN (977 aa)
mRNA: AK131405 NM_145238
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 15 residues, 33710832-33710875Exon2: 177 residues, 33717366-33717893Exon3: 64 residues, 33726651-33726838Exon4: 27 residues, 33727301-33727378Exon5: 30 residues, 33727704-33727789Exon6: 228 residues, 33729211-33729889Exon7: 145 residues, 33731373-33731802Exon8: 480 residues, 33732404-33733840Exon9: 2 residues, -Jump to ZNF31_HUMANExon1: 12 residues, 33710845-33710879Exon2: 63 residues, 33717366-33717551Exon3: 50 residues, 33717749-33717893Exon4: 64 residues, 33726651-33726838Exon5: 27 residues, 33727301-33727378Exon6: 30 residues, 33727704-33727789Exon7: 228 residues, 33729211-33729889Exon8: 145 residues, 33731373-33731802Exon9: 727 residues, 33732404-33734580Exon10: 2 residues, -Jump to ZNF31_HUMAN  
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