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2Y4V

CRYSTAL STRUCTURE OF HUMAN CALMODULIN IN COMPLEX WITH A DAP KINASE-1 MUTANT (W305Y) PEPTIDE

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
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0008076cellular_componentvoltage-gated potassium channel complex
A0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
A0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
A0010856molecular_functionadenylate cyclase activator activity
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0016020cellular_componentmembrane
A0016240biological_processautophagosome membrane docking
A0019855molecular_functioncalcium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0021762biological_processsubstantia nigra development
A0030017cellular_componentsarcomere
A0031432molecular_functiontitin binding
A0031514cellular_componentmotile cilium
A0031954biological_processpositive regulation of protein autophosphorylation
A0031982cellular_componentvesicle
A0032465biological_processregulation of cytokinesis
A0032516biological_processobsolete positive regulation of phosphoprotein phosphatase activity
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0035307biological_processobsolete positive regulation of protein dephosphorylation
A0035458biological_processcellular response to interferon-beta
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
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
A0050848biological_processregulation of calcium-mediated signaling
A0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
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
A0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
A0071346biological_processcellular response to type II interferon
A0071902biological_processpositive regulation of protein serine/threonine kinase activity
A0072542molecular_functionprotein phosphatase activator activity
A0097225cellular_componentsperm midpiece
A0098901biological_processregulation of cardiac muscle cell action potential
A0099523cellular_componentpresynaptic cytosol
A0140056biological_processorganelle localization by membrane tethering
A0140238biological_processpresynaptic endocytosis
A1901020biological_processnegative regulation of calcium ion transmembrane transporter activity
A1901842biological_processnegative regulation of high voltage-gated calcium channel activity
A1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
A1902494cellular_componentcatalytic complex
A1905913biological_processnegative regulation of calcium ion export across plasma membrane
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1150
ChainResidue
AASP130
AASP132
AASP134
AGLN136
AGLU141
AHOH2153

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1151
ChainResidue
ATHR27
AGLU32
AHOH2031
AASP21
AASP23
AASP25

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1152
ChainResidue
AASP57
AASP59
AASN61
ATHR63
AGLU68
AHOH2095

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1153
ChainResidue
AASP94
AASP96
AASN98
ATYR100
AGLU105
AHOH2113

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 Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11579085, ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:17056602
ChainResidueDetails
BSER308
AGLU68
AASP23
AASP25
ATHR27
AGLU32
AASP57
AASP59
AASN61
ATHR63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER319
AASP96
AASN98
ATYR100
AGLU105

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
AASP130
AASP132
AASP134
AGLN136
AGLU141

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS22

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
ATHR45

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER82

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS95

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR100

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER102

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR111

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS116

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR139

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ALYS22

226707

PDB entries from 2024-10-30

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