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0FYV1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionFyve finger-containing phosphoinositide kinase (ec (1- phosphatidylinositol-4-phosphate 5-kinase) (pip5k) (ptdins(4)p-5- kinase) (pikfyve) (p235).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0045121 lipid raft (IDA)
0016308 1-phosphatidylinositol-4-phosphate 5-kinase... (TAS)
0005515 protein binding (IPI)
0019722 calcium-mediated signaling (TAS)
0007242 intracellular signaling cascade (TAS)

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Domain Architecture (Details)
InterPro domains unassigned to SynO:
The family consists of various type I.I and III phosphatidylinositol-4-phosphate 5-kinases (PIP5K enzymes). They contain a region from the common kinase core found in the typeI phosphatidylinositol-4-phosphate 5-kinase (PIP5K) family as described in. PIP5K catalyse the formation of phosphoinositol-4.-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signaling pathway.
  IPR002498:Phosphatidylinositol-4-phosphate 5-kinase
The FYVE zinc finger is named after four proteins that it has been found in: Fab1.OTB/ZK632.12.ac1.nd EEA1. The FYVE finger has been shown to bind two Zn2+ ions . The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif + represents a charged residue and X any residue.
  IPR000306:Zinc finger, FYVE-type
This is a domain of unknown function present in signaling proteins including pleckstrinproteins. Segment polarity dishevelled protein is required to establish coherent arrays of polarized cells andsegments in embryos.nd plays a role in wingless signaling. Egl-10 regulates G-protein signaling in the centralnervous system. Mammalian regulators of G-protein signaling also contain these domains.nd regulate signaltransduction by increasing the GTPase activity of G-protein alpha subunits.hereby driving them into theirinactive GDP-bound form.
  IPR000591:Pleckstrin/ G-protein, interacting region
The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases.owever.tructural information from other protein molecules is required for correct folding and subsequent assembly into oligomers . These helper molecules are referred to as molecular chaperones. subfamily of which are the chaperonins .hich include 10 kDa and 60 kDa proteins. These are found in abundance in prokaryotes.hloroplasts and mitochondria. They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees centigrade ).nd are stress-induced.cting to stabilise or protect disassembled polypeptides under heat-shock conditions .The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 to 8 identical subunits.hereas the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings.ach ring containing 7 identical subunits . These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The cpn10 and cpn60 oligomers also require Mg2+-ATP in order to interact to form a functional complex.lthough the mechanism of this interaction is as yet unknown . This chaperonin complex is essential for the correct folding and assembly of polypeptides into oligomeric structures.f which the chaperonins themselves are not a part . The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.The 60 kDa form of chaperonin is the immunodominant antigen of patients with Legionnaires disease .nd is thought to play a role in the protection of the Legionella bacteria from oxygen radicals within macrophages. This hypothesis is based on the finding that the cpn60 gene is upregulated in response to hydrogen peroxide. source of oxygen radicals. Cpn60 has also been found to display strong antigenicity in many bacterial species .nd has the potential for inducing immune protection against unrelated bacterial infections. The RuBisCO subunit binding protein (which has been implicated in the assembly of RuBisCO) and cpn60 have been found to be evolutionary homologues.he RuBisCO subunit binding protein having the C-terminal Gly-Gly-Met repeat found in all bacterial cpn60 sequences. Although the precise function of this repeat is unknown.t is thought to be important as it is also found in 70 kDa heat-shock proteins . The crystal structure of Escherichia coli GroEL has been resolved to 2.8A . The TCP-1 family of proteins act as molecular chaperones for tubulin.ctin and probably some other proteins. They are weakly.ut significantly.elated to the cpn60/groEL chaperonin family.
  IPR002423:Chaperonin Cpn60/TCP-1
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 the "wings".r 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 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 the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
SequencesProtein: FYV1_HUMAN (2098 aa)
mRNA: NM_015040
Local Annotation
Synapse Ontology
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
KO assignmentK00889
  Level 3 annotation:
    1-phosphatidylinositol-4-phosphate 5-kinase
  Level 2 annotation:
    Inositol phosphate metabolism
    Phosphatidylinositol signaling system
    Regulation of actin cytoskeleton
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 50 residues, 208839235-208839384Exon2: 62 residues, 208844479-208844660Exon3: 52 residues, 208846552-208846702Exon4: 41 residues, 208849680-208849799Exon5: 59 residues, 208850505-208850677Exon6: 71 residues, 208858694-208858902Exon7: 32 residues, 208861697-208861787Exon8: 48 residues, 208871609-208871748Exon9: 54 residues, 208873905-208874063Exon10: 39 residues, 208875210-208875322Exon11: 51 residues, 208877139-208877287Exon12: 58 residues, 208877814-208877982Exon13: 22 residues, 208885204-208885264Exon14: 45 residues, 208887262-208887392Exon15: 62 residues, 208888161-208888342Exon16: 27 residues, 208890835-208890910Exon17: 38 residues, 208893220-208893328Exon18: 49 residues, 208897110-208897251Exon19: 44 residues, 208897879-208898006Exon20: 388 residues, 208898238-208899398Exon21: 35 residues, 208901148-208901249Exon22: 26 residues, 208902810-208902882Exon23: 59 residues, 208903491-208903663Exon24: 61 residues, 208906283-208906462Exon25: 40 residues, 208908274-208908388Exon26: 38 residues, 208908761-208908870Exon27: 53 residues, 208909014-208909169Exon28: 32 residues, 208909806-208909897Exon29: 22 residues, 208911476-208911537Exon30: 48 residues, 208912386-208912524Exon31: 42 residues, 208912979-208913100Exon32: 34 residues, 208915522-208915618Exon33: 30 residues, 208918079-208918163Exon34: 34 residues, 208919018-208919116Exon35: 57 residues, 208920827-208920992Exon36: 22 residues, 208922992-208923052Exon37: 61 residues, 208923739-208923916Exon38: 36 residues, 208924320-208924424Exon39: 45 residues, 208925622-208925751Exon40: 89 residues, 208926866-208927128Exon41: 27 residues, 208927539-208927614Exon42: 1189 residues, 208928158-208931719Exon43: 2 residues, -Jump to FYV1_HUMAN  
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