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0MYST4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMYST4
DescriptionHistone acetyltransferase myst4 (ec 2.3.1.48) (ec 2.3.1.-) (myst protein 4) (moz, ybf2/sas3, sas2 and tip60 protein 4) (histone acetyltransferase moz2) (monocytic leukemia zinc finger protein- related factor) (histone acetyltransferase morf).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0000786 nucleosome (ISS)
0004402 histone acetyltransferase activity (ISS)
0016563 transcriptional activator activity (ISS)
0016564 transcriptional repressor activity (ISS)
0016573 histone acetylation (ISS)
0016481 negative regulation of transcription (ISS)
0006334 nucleosome assembly (ISS)
0045941 positive regulation of transcription (ISS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Moz is a monocytic leukemia Zn_finger protein and the SAS protein from Saccharomyces cerevisiae is involved in silencing the Hmr locus. These proteins were reported to be homologous to acetyltransferases but this similarity is not supported by standard sequence analysis.
  IPR002717:MOZ/SAS-like protein
Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures.Histone H5 performs the same function as histone H1.nd replaces H1 in certain cells. The structure of GH5.he globular domain of the linker histone H5 is known . The fold is similar to the DNA-binding domain of the catabolite gene activator protein.AP.hus providing a possible model for the binding of GH5 to DNA.
  IPR005818:Histone H1/H5
The homeodomain (PHD) finger .s a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of.ut distinct from the C3HC4 type RING finger.The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively.he interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain.he PHD finger is thought to bind two zinc ions.
  IPR001965:Zinc finger, PHD-type
Zinc finger domains (ZnFs) are common.elatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA-binding module.nFs have recently been shown to mediate protein:protein and protein:lipid interactions. There are at least 14 different classes of Zn fingers.hich differ in the nature and arrangement of their zinc-binding residues .The FYVE zinc finger domain is conserved from yeast to man.nd is named after four proteins that it has been found in: Fab1.OTB/ZK632.12.ac1.nd EEA1. It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P).hich is found mainly on endosomes .The plant homeodomain (PHD) zinc finger domain has a C4HC3-type motif.nd is widely distributed in eukaryotes.eing found in many chromatin regulatory factors .Both the FYVE and the PHD zinc finger motifs display strikingly similar dimetal(zinc)-bound alpha+beta folds.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011011:Zinc finger, FYVE/PHD-type
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif.here the "wings".r loops.re small beta-sheets. The winged helix motif consists of two wings (W1.2).hree alpha helices (H1.2.3) and three beta-sheets (S1.2.3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 . The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA.hile the wings make different DNA contacts.ften with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain.ncluding transcriptional repressors such as biotin repressor.exA repressor and the arginine repressor ; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell differentiation.eat-shock transcription factor.nd the general transcription factors TFIIE and TFIIF . helicases such as RuvB that promotes branch migration at the Holliday junction.nd CDC6 in the pre-replication complex . endonucleases such as FokI and TnsA ; histones; and Mu transposase.here the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
IPR002717:MOZ_SAS 
Evalue:-132.522872924805 
Location:773-960IPR001965:PHD 
Evalue:-12.6382722854614 
Location:274-320IPR005818:H15 
Evalue:-7.33724216831843 
Location:93-170IPR001965:PHD 
Evalue:-6.55284214019775 
Location:215-272
SequencesProtein: MYST4_HUMAN (2073 aa)
mRNA: NM_012330
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK00653
  Level 3 annotation:
    histone acetyltransferase
  Level 2 annotation:
    Other enzymes
K00680
  Level 3 annotation:
    
  Level 2 annotation:
    Butanoate metabolism
    Glycerophospholipid metabolism
    Valine
     leucine and isoleucine degradation
    Lysine degradation
    Histidine metabolism
    Tyrosine metabolism
    Phenylalanine metabolism
    Limonene and pinene degradation
    Alkaloid biosynthesis II
    Ethylbenzene degradation
    Benzoate degradation via CoA ligation
    1- and 2-Methylnaphthalene degradation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 18 residues, 76268463-76268516Exon2: 295 residues, 76272363-76273242Exon3: 38 residues, 76389733-76389842Exon4: 40 residues, 76399423-76399539Exon5: 29 residues, 76399783-76399865Exon6: 46 residues, 76402270-76402403Exon7: 312 residues, 76405162-76406094Exon8: 42 residues, 76407079-76407201Exon9: 40 residues, 76408987-76409103Exon10: 49 residues, 76411550-76411692Exon11: 56 residues, 76414843-76415005Exon12: 33 residues, 76418782-76418876Exon13: 79 residues, 76450345-76450577Exon14: 55 residues, 76450889-76451049Exon15: 119 residues, 76451644-76451995Exon16: 99 residues, 76454721-76455013Exon17: 854 residues, 76458252-76460810Exon18: 2 residues, -Jump to MYST4_HUMAN  
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