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4E50

Calmodulin and Ng peptide complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000086biological_processG2/M transition of mitotic cell cycle
A0000922cellular_componentspindle pole
A0002027biological_processregulation of heart rate
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0008076cellular_componentvoltage-gated potassium channel complex
A0008179molecular_functionadenylate cyclase binding
A0010856molecular_functionadenylate cyclase activator activity
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0016240biological_processautophagosome membrane docking
A0019855molecular_functioncalcium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030426cellular_componentgrowth cone
A0030672cellular_componentsynaptic vesicle membrane
A0031432molecular_functiontitin binding
A0031514cellular_componentmotile cilium
A0031800molecular_functiontype 3 metabotropic glutamate receptor binding
A0031966cellular_componentmitochondrial membrane
A0032465biological_processregulation of cytokinesis
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0035307biological_processpositive regulation of protein dephosphorylation
A0035458biological_processcellular response to interferon-beta
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0043548molecular_functionphosphatidylinositol 3-kinase binding
A0044305cellular_componentcalyx of Held
A0044325molecular_functiontransmembrane transporter binding
A0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0050998molecular_functionnitric-oxide synthase binding
A0051592biological_processresponse to calcium ion
A0055117biological_processregulation of cardiac muscle contraction
A0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0071346biological_processcellular response to type II interferon
A0072542molecular_functionprotein phosphatase activator activity
A0097225cellular_componentsperm midpiece
A0098901biological_processregulation of cardiac muscle cell action potential
A0140056biological_processorganelle localization by membrane tethering
A0140238biological_processpresynaptic endocytosis
A1902494cellular_componentcatalytic complex
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP21-LEU33
AASP57-PHE69
AASP94-LEU106
AASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK
ChainResidueDetails
AASP21
AGLU68
AASP94
AASP96
AASN98
ATYR100
AGLU105
AASP130
AASP132
AASP134
AGLN136
AASP23
AGLU141
AASP25
ATHR27
AGLU32
AASP57
AASP59
AASN61
ATHR63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.5
ChainResidueDetails
AALA2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS22

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
ATHR45

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ASER82

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS95

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:21183079
ChainResidueDetails
ATYR100

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER102

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATHR111

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS116

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATYR139

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ALYS22

site_idSWS_FT_FI13
Number of Residues1
DetailsSITE: Crucial for interaction with calmodulin
ChainResidueDetails
AARG166

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PHK and PKC => ECO:0000269|PubMed:23462742
ChainResidueDetails
ASER164

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PDB entries from 2024-05-01

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