SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
1O95712_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionCytosolic phospholipase a2 beta.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005829 cytosol (ISS)
0005576 extracellular region (TAS)
0005509 calcium ion binding (NAS)
0047498 calcium-dependent phospholipase A2 activity (IDA)
0005544 calcium-dependent phospholipid binding (NAS)
0019369 arachidonic acid metabolism (NAS)
0019722 calcium-mediated signaling (NAS)
0046475 glycerophospholipid catabolism (IDA)
0006954 inflammatory response (NAS)
0007567 parturition (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/ [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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:
This family consists of lysophospholipase / phospholipase B and cytosolic phospholipase A2 which also has a C2 domain . Phospholipase B enzymes catalyse the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells . Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids .he aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in .
  IPR002642:Lysophospholipase, catalytic region
The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes.ncluding phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies ofthe C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see )and the protein kinase catalytic domain (see ). Regions withsignificant homology to the C2-domain have been found in many proteins.The C2 domain is thought to be involved in calcium-dependent phospholipidbinding and in membrane targetting processes such as subcellular localisation. The 3D structure of theC2 domain of synaptotagmin has been reported.he domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . Calcium binds ina cup-shaped depression formed by the N- and C-terminal loops of theC2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.
  IPR000008:C2 calcium-dependent membrane targeting
This entry contains:Aspartyl (asparaginyl) beta-hydroxylase (AAH). AAH is an alpha-ketoglutarate-dependent dioxygenase that hydroxylates aspartate and asparagine residues in EGF-like domains of proteins . and The transcription factor Jumonji which is required for neural tube formation in mice .There is evidence of domain swapping within the jumonji family of transcription factors . This domain is often associated with JmjN (see ).
  IPR003347:Transcription factor jumonji/aspartyl beta-hydroxylase
SequencesProtein: O95712_HUMAN (1012 aa)
mRNA: NM_005090
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: 25 residues, 39907605-39907678Exon2: 53 residues, 39914229-39914383Exon3: 86 residues, 39914459-39914713Exon4: 21 residues, 39915077-39915134Exon5: 34 residues, 39915637-39915733Exon6: 27 residues, 39915964-39916041Exon7: 26 residues, 39919647-39919720Exon8: 47 residues, 39920013-39920150Exon9: 46 residues, 39920263-39920395Exon10: 15 residues, 39920544-39920585Exon11: 16 residues, 39920720-39920763Exon12: 20 residues, 39921006-39921061Exon13: 45 residues, 39921308-39921439Exon14: 30 residues, 39921682-39921766Exon15: 14 residues, 39922043-39922081Exon16: 47 residues, 39923165-39923301Exon17: 47 residues, 39923960-39924097Exon18: 76 residues, 39924337-39924560Exon19: 41 residues, 39924692-39924810Exon20: 48 residues, 39925127-39925265Exon21: 37 residues, 39925432-39925537Exon22: 62 residues, 39925692-39925872Exon23: 57 residues, 39926158-39926325Exon24: 64 residues, 39926826-39927013Exon25: 166 residues, 39927138-39927630Exon26: 2 residues, -Jump to O95712_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2879 39907605-39927630 ~-20K 12149(+)Loci: 4164 39927636-39973567 ~-46K 12151(SPTBN5)(-)Loci: 4165 40238191-40287794 ~-50K 12159(VPS39)(-)Loci: 2880 40438989-40491807 ~-53K 12167(CAPN3)(+)Loci: 2881 40575126-40612548 ~-37K 12175(SNAP23)(+)Loci: 2882 40655148-40752587 ~-97K 12179(+)Loci: 2878 39638523-39658828 ~-20K 12142(TYRO3)(+)Link out to UCSC