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1CJY

HUMAN CYTOSOLIC PHOSPHOLIPASE A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001516biological_processprostaglandin biosynthetic process
A0002827biological_processpositive regulation of T-helper 1 type immune response
A0004620molecular_functionphospholipase activity
A0004622molecular_functionlysophospholipase activity
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005743cellular_componentmitochondrial inner membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006071biological_processglycerol metabolic process
A0006640biological_processmonoacylglycerol biosynthetic process
A0006650biological_processglycerophospholipid metabolic process
A0006663biological_processplatelet activating factor biosynthetic process
A0006690biological_processicosanoid metabolic process
A0008289molecular_functionlipid binding
A0008374molecular_functionO-acyltransferase activity
A0009395biological_processphospholipid catabolic process
A0010314molecular_functionphosphatidylinositol-5-phosphate binding
A0010572biological_processpositive regulation of platelet activation
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019369biological_processarachidonate metabolic process
A0019370biological_processleukotriene biosynthetic process
A0032266molecular_functionphosphatidylinositol-3-phosphate binding
A0032308biological_processpositive regulation of prostaglandin secretion
A0034478biological_processphosphatidylglycerol catabolic process
A0034638biological_processphosphatidylcholine catabolic process
A0036151biological_processphosphatidylcholine acyl-chain remodeling
A0042127biological_processregulation of cell population proliferation
A0043032biological_processpositive regulation of macrophage activation
A0043231cellular_componentintracellular membrane-bounded organelle
A0046456biological_processicosanoid biosynthetic process
A0046475biological_processglycerophospholipid catabolic process
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0051649biological_processestablishment of localization in cell
A0070273molecular_functionphosphatidylinositol-4-phosphate binding
A0071236biological_processcellular response to antibiotic
A1902387molecular_functionceramide 1-phosphate binding
B0000139cellular_componentGolgi membrane
B0001516biological_processprostaglandin biosynthetic process
B0002827biological_processpositive regulation of T-helper 1 type immune response
B0004620molecular_functionphospholipase activity
B0004622molecular_functionlysophospholipase activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005737cellular_componentcytoplasm
B0005743cellular_componentmitochondrial inner membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006071biological_processglycerol metabolic process
B0006640biological_processmonoacylglycerol biosynthetic process
B0006650biological_processglycerophospholipid metabolic process
B0006663biological_processplatelet activating factor biosynthetic process
B0006690biological_processicosanoid metabolic process
B0008289molecular_functionlipid binding
B0008374molecular_functionO-acyltransferase activity
B0009395biological_processphospholipid catabolic process
B0010314molecular_functionphosphatidylinositol-5-phosphate binding
B0010572biological_processpositive regulation of platelet activation
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019369biological_processarachidonate metabolic process
B0019370biological_processleukotriene biosynthetic process
B0032266molecular_functionphosphatidylinositol-3-phosphate binding
B0032308biological_processpositive regulation of prostaglandin secretion
B0034478biological_processphosphatidylglycerol catabolic process
B0034638biological_processphosphatidylcholine catabolic process
B0036151biological_processphosphatidylcholine acyl-chain remodeling
B0042127biological_processregulation of cell population proliferation
B0043032biological_processpositive regulation of macrophage activation
B0043231cellular_componentintracellular membrane-bounded organelle
B0046456biological_processicosanoid biosynthetic process
B0046475biological_processglycerophospholipid catabolic process
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0047499molecular_functioncalcium-independent phospholipase A2 activity
B0050482biological_processarachidonate secretion
B0051649biological_processestablishment of localization in cell
B0070273molecular_functionphosphatidylinositol-4-phosphate binding
B0071236biological_processcellular response to antibiotic
B1902387molecular_functionceramide 1-phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 950
ChainResidue
AASP40
ATHR41
AASP43
AASN65
AMES3000
AHOH3026

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 951
ChainResidue
AALA94
AASN95
AASP40
AASP43
AASP93

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1950
ChainResidue
BHOH53
BASP1040
BTHR1041
BASP1043
BASN1065
BMES4000

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1951
ChainResidue
BHOH54
BASP1040
BASP1043
BASP1093
BALA1094
BASN1095

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 3000
ChainResidue
AASP40
AASP43
AASN64
AASN65
AALA94
ATYR96
ACA950
AHOH3026
BLYS1281

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MES B 4000
ChainResidue
ALYS281
BHOH53
BASP1040
BASP1043
BHIS1062
BASN1064
BASN1065
BALA1094
BASN1095
BTYR1096
BCA1950

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues11
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IHVVDSGLtf.N
ChainResidueDetails
AILE545-ASN555

site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DDDELDA
ChainResidueDetails
AASP517-ALA523

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:10319815, ECO:0000269|PubMed:8083230, ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602
ChainResidueDetails
ASER228
BSER1228

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:10319815, ECO:0000269|PubMed:8702602
ChainResidueDetails
AASP549
BASP1549

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AASP40
BASP1043
BASN1065
BASP1093
BALA1094
BASN1095
ATHR41
AASP43
AASN65
AASP93
AALA94
AASN95
BASP1040
BTHR1041

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2
ASER435
BSER1002
BSER1435

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR268
BTHR1268

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50393
ChainResidueDetails
ASER434
ASER515
BSER1434
BSER1515

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER437
BSER1437

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK => ECO:0000269|PubMed:8381049, ECO:0000269|PubMed:9468497
ChainResidueDetails
ASER505
BSER1505

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9468497, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER727
BSER1727

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER729
BSER1729

site_idSWS_FT_FI11
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS541
ALYS606
BLYS1541
BLYS1606

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10319815, 8619991, 8702602, 11080675
ChainResidueDetails
ASER228
AGLY198
AGLY197
AASP549

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10319815, 8619991, 8702602, 11080675
ChainResidueDetails
BGLY1197
BGLY1198
BSER1228
BASP1549

site_idMCSA1
Number of Residues5
DetailsM-CSA 529
ChainResidueDetails
AGLY197electrostatic stabiliser
AGLY198electrostatic stabiliser
AARG200electrostatic stabiliser
ASER228covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AASP549proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 529
ChainResidueDetails
BGLY1197electrostatic stabiliser
BGLY1198electrostatic stabiliser
BARG1200electrostatic stabiliser
BSER1228covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BASP1549proton acceptor, proton donor

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PDB entries from 2024-10-30

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