Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2YGG

Complex of CaMBR and CaM

Functional Information from GO Data
ChainGOidnamespacecontents
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0001975biological_processresponse to amphetamine
B0002027biological_processregulation of heart rate
B0005246molecular_functioncalcium channel regulator activity
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0008076cellular_componentvoltage-gated potassium channel complex
B0008179molecular_functionadenylate cyclase binding
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030017cellular_componentsarcomere
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030426cellular_componentgrowth cone
B0030672cellular_componentsynaptic vesicle membrane
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031800molecular_functiontype 3 metabotropic glutamate receptor binding
B0031966cellular_componentmitochondrial membrane
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035307biological_processpositive regulation of protein dephosphorylation
B0035458biological_processcellular response to interferon-beta
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0043548molecular_functionphosphatidylinositol 3-kinase binding
B0044305cellular_componentcalyx of Held
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050998molecular_functionnitric-oxide synthase binding
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0072542molecular_functionprotein phosphatase activator activity
B0090150biological_processestablishment of protein localization to membrane
B0090151biological_processestablishment of protein localization to mitochondrial membrane
B0097225cellular_componentsperm midpiece
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098901biological_processregulation of cardiac muscle cell action potential
B0099523cellular_componentpresynaptic cytosol
B0099524cellular_componentpostsynaptic cytosol
B0140056biological_processorganelle localization by membrane tethering
B0140238biological_processpresynaptic endocytosis
B1900242biological_processregulation of synaptic vesicle endocytosis
B1902494cellular_componentcatalytic complex
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
B2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 1686
ChainResidue
AGLU630
AILE631
BSER82
BGLU85
BMET146
BTHR147
BHOH2059

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TAM A 1687
ChainResidue
AARG645
ASER648
ATYR649
AHOH2045
AHOH2046
BLEU113
BHOH2038
AGLU629
AARG632

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1151
ChainResidue
BASP94
BASP96
BASN98
BTYR100
BGLU105
BHOH2025

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 1152
ChainResidue
BASP57
BASP59
BASN61
BTHR63
BGLU68
BHOH2007
BHOH2008

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1153
ChainResidue
BASP21
BASP23
BASP25
BTHR27
BGLU32
BHOH2002

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1154
ChainResidue
BASP130
BASP132
BASP134
BGLN136
BGLU141
BHOH2053

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MRD B 1155
ChainResidue
BLYS76
BTHR80
BHOH2010

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TAM B 1156
ChainResidue
AARG651
AHOH2032
BASN138
BTYR139
BGLU140
BHOH2016

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TAM B 1157
ChainResidue
ALEU646
BGLU120
BASP123
BGLU124
BHOH2069

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP21-LEU33
BASP57-PHE69
BASP94-LEU106
BASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH
ChainResidueDetails
BASP21
BASP23
BASP25
BTHR27
BGLU32

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH
ChainResidueDetails
BASP57
BASP59
BASN61
BTHR63
BGLU68

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
BASP94
BASP96
BASN98
BTYR100
BGLU105

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
BASP130
BASP132
BASP134
BGLN136
BGLU141

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8
ChainResidueDetails
BALA2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BLYS22

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
BTHR45

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BSER82

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BLYS95

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
BTYR100

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
BSER102

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BTHR111

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BLYS116

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BTYR139

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
BLYS22

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon