SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
1Q6NUK8_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionPsmd4p2 protein.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016308 1-phosphatidylinositol-4-phosphate 5-kinase... (IEA)
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 von Willebrand factor is a large multimeric glycoprotein found in bloodplasma. Mutant forms are involved in the aetiology of bleeding disorders . In von Willebrand factor.he type A domain (vWF) is the prototype fora protein superfamily. The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteinsthat incorporate vWF domains participate in numerous biological events(e.g. cell adhesion.igration.oming.attern formation.nd signaltransduction).nvolving interaction with a large array of ligands . A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands . Foldrecognition algorithms were used to score sequence compatibility with alibrary of known structures: the vWF domain fold was predicted to be adoubly-wound.pen.wisted beta-sheet flanked by alpha-helices . 3D structures have been determined for the I-domains of integrins CD11b(with bound magnesium) and CD11a (with bound manganese) . The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this siterepresents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands . The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved.ut the manner in which the metal ion is coordinated differs slightly .
  IPR002035:von Willebrand factor, type A
The Ubiquitin Interacting Motif (UIM) was first described in the 26S proteasome subunit PSD4/RPN-10 . It is known to bind multiple ubiquitin and was also found in many proteins involved in the endocytic pathway.ncludingthe PSD4/RPN-10/S5a multiubiquitin binding subunit of the 26S proteasome; the VPS27 vacuolar sorting protein; and ataxin-3. protein involved in ataxia disease.
  IPR003903:Ubiquitin interacting motif
IPR002498:PIPKc 
Evalue:-177.05551732785 
Location:56-397IPR002035:VWA 
Evalue:-6.82390874094432 
Location:490-673IPR003903:UIM 
Evalue:-1.58502662181854 
Location:766-783IPR003903:UIM 
Evalue:0.568201720714569 
Location:695-712
SequencesProtein: Q6NUK8_HUMAN (862 aa)
mRNA: BC068549
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (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: 1117 residues, 95707938-95711287Exon2: 2 residues, -Jump to Q6NUK8_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2627 95780558-96078136 ~-298K 5364(+)Loci: 3909 95707938-95711287 ~-3K 5361(-)Link out to UCSC