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0GUC2D_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGUCY2D
DescriptionRetinal guanylyl cyclase 1 precursor (ec 4.6.1.2) (guanylate cyclase 2d, retinal) (retgc-1) (rod outer segment membrane guanylate cyclase) (ros-gc).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005640 nuclear outer membrane (TAS)
0004383 guanylate cyclase activity (TAS)
0004872 receptor activity (TAS)
0007168 receptor guanylyl cyclase signaling pathway (TAS)
0007601 visual perception (TAS)

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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:
Guanylate cyclases () catalyse the formation of cyclic GMP (cGMP) from GTP. cGMP acts as an intracellular messenger.ctivating cGMP-dependent kinases and regulating cGMP-sensitive ion channels. The role of cGMP as a second messenger in vascular smooth muscle relaxation and retinal photo-transduction is well established. Guanylate cyclase is found both in thesoluble and particulate fractions of eukaryotic cells. The soluble and plasmamembrane-bound forms differ in structure.egulation and other properties . Most currently known plasma membrane-boundforms are receptors for small polypeptides. The soluble forms of guanylate cyclase arecytoplasmic heterodimers having alpha and beta subunits. In all characterized eukaryote guanylyl- and adenylyl cyclases.yclic nucleotide synthesis is carried out by the conserved class III cyclase domain.
  IPR001054:Adenylyl cyclase class-3/4/guanylyl cyclase
This describes a ligand binding domain and includes extracellular ligand binding domains of a wide range of receptors.s well as the bacterial amino acid binding proteins of known structure .
  IPR001828:Extracellular ligand-binding receptor
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
IPR001054:CYCc 
Evalue:-101.920818753952 
Location:844-1039IPR001828:ANF_receptor 
Evalue:-52.7958793640137 
Location:72-409IPR000719:Pkinase 
Evalue:-12.5528421401978 
Location:584-805
SequencesProtein: GUC2D_HUMAN (1103 aa)
mRNA: NM_000180
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK01769
  Level 3 annotation:
    guanylate cyclase
  Level 2 annotation:
    Purine metabolism
    Gap junction
    Long-term depression
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 21 residues, 7846716-7846777Exon2: 245 residues, 7847081-7847811Exon3: 103 residues, 7847894-7848199Exon4: 119 residues, 7850405-7850757Exon5: 30 residues, 7851102-7851187Exon6: 36 residues, 7851468-7851571Exon7: 36 residues, 7851973-7852075Exon8: 29 residues, 7853548-7853629Exon9: 71 residues, 7856186-7856393Exon10: 54 residues, 7856492-7856649Exon11: 52 residues, 7857145-7857295Exon12: 51 residues, 7857922-7858071Exon13: 56 residues, 7858643-7858807Exon14: 66 residues, 7858901-7859094Exon15: 60 residues, 7859370-7859545Exon16: 35 residues, 7859785-7859884Exon17: 33 residues, 7859969-7860064Exon18: 30 residues, 7860247-7860333Exon19: 39 residues, 7860485-7860597Exon20: 72 residues, 7864170-7864382Exon21: 2 residues, -Jump to GUC2D_HUMAN  
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Loci Cluster (Details)Loci: 4258 6644024-6675784 ~-32K 14997(TEKT1)(-)Loci: 4259 7033935-7063745 ~-30K 15014(DLG4)(-)Loci: 2974 7063876-7069308 ~-5K 15016(ACADVL)(+)Loci: 4260 7084462-7086477 ~-2K 15021(GABARAP)(-)Loci: 2975 7252225-7263903 ~-12K 15047(NLGN2)(+)Loci: 2976 7289129-7301655 ~-13K 15051(CHRNB1)(+)Loci: 2977 7427889-7432228 ~-4K 15066(MPDU1)(+)Loci: 2978 7474184-7477419 ~-3K 15071(SHBG)(+)Loci: 4261 7512446-7531642 ~-19K 15074(TP53)(-)Loci: 4262 7774391-7775983 ~-2K 15094(TRAPPC1)(-)Loci: 2979 7846716-7864382 ~-18K 15097(GUCY2D)(+)Loci: 4263 8004447-8006987 ~-3K 15108(VAMP2)(-)Loci: 2980 8093361-8114528 ~-21K 15119(PFAS)(+)Loci: 2981 8279988-8330396 ~-50K 15135(+)Loci: 2973 6620295-6631688 ~-11K 14996(FBXO39)(+)Link out to UCSC