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1AUI

HUMAN CALCINEURIN HETERODIMER

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0001975biological_processresponse to amphetamine
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005955cellular_componentcalcineurin complex
A0006470biological_processprotein dephosphorylation
A0006606biological_processprotein import into nucleus
A0006816biological_processcalcium ion transport
A0008287cellular_componentprotein serine/threonine phosphatase complex
A0008544biological_processepidermis development
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0010628biological_processpositive regulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0014883biological_processtransition between fast and slow fiber
A0014898biological_processcardiac muscle hypertrophy in response to stress
A0016018molecular_functioncyclosporin A binding
A0016020cellular_componentmembrane
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0017018molecular_functionmyosin phosphatase activity
A0019722biological_processcalcium-mediated signaling
A0019897cellular_componentextrinsic component of plasma membrane
A0019899molecular_functionenzyme binding
A0023057biological_processnegative regulation of signaling
A0030018cellular_componentZ disc
A0030216biological_processkeratinocyte differentiation
A0030335biological_processpositive regulation of cell migration
A0033173biological_processcalcineurin-NFAT signaling cascade
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0033555biological_processmulticellular organismal response to stress
A0036057cellular_componentslit diaphragm
A0042060biological_processwound healing
A0042104biological_processpositive regulation of activated T cell proliferation
A0042110biological_processT cell activation
A0042383cellular_componentsarcolemma
A0042995cellular_componentcell projection
A0043197cellular_componentdendritic spine
A0043403biological_processskeletal muscle tissue regeneration
A0044877molecular_functionprotein-containing complex binding
A0045202cellular_componentsynapse
A0045669biological_processpositive regulation of osteoblast differentiation
A0045672biological_processpositive regulation of osteoclast differentiation
A0045785biological_processpositive regulation of cell adhesion
A0045807biological_processpositive regulation of endocytosis
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0046878biological_processpositive regulation of saliva secretion
A0046983molecular_functionprotein dimerization activity
A0048741biological_processskeletal muscle fiber development
A0048813biological_processdendrite morphogenesis
A0050774biological_processnegative regulation of dendrite morphogenesis
A0050804biological_processmodulation of chemical synaptic transmission
A0051117molecular_functionATPase binding
A0051592biological_processresponse to calcium ion
A0060079biological_processexcitatory postsynaptic potential
A0061006biological_processregulation of cell proliferation involved in kidney morphogenesis
A0070262biological_processpeptidyl-serine dephosphorylation
A0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
A0071333biological_processcellular response to glucose stimulus
A0090193biological_processpositive regulation of glomerulus development
A0097205biological_processrenal filtration
A0097720biological_processcalcineurin-mediated signaling
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098978cellular_componentglutamatergic synapse
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0110062biological_processnegative regulation of angiotensin-activated signaling pathway
A1903244biological_processpositive regulation of cardiac muscle hypertrophy in response to stress
A1905205biological_processpositive regulation of connective tissue replacement
A1905665biological_processpositive regulation of calcium ion import across plasma membrane
A1905949biological_processnegative regulation of calcium ion import across plasma membrane
B0001569biological_processbranching involved in blood vessel morphogenesis
B0001837biological_processepithelial to mesenchymal transition
B0004721molecular_functionphosphoprotein phosphatase activity
B0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005955cellular_componentcalcineurin complex
B0006606biological_processprotein import into nucleus
B0007507biological_processheart development
B0008287cellular_componentprotein serine/threonine phosphatase complex
B0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
B0014044biological_processSchwann cell development
B0016018molecular_functioncyclosporin A binding
B0016020cellular_componentmembrane
B0019902molecular_functionphosphatase binding
B0019904molecular_functionprotein domain specific binding
B0022011biological_processmyelination in peripheral nervous system
B0033173biological_processcalcineurin-NFAT signaling cascade
B0034504biological_processprotein localization to nucleus
B0042383cellular_componentsarcolemma
B0045202cellular_componentsynapse
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0060487biological_processlung epithelial cell differentiation
B0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
B0097720biological_processcalcineurin-mediated signaling
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098686cellular_componenthippocampal mossy fiber to CA3 synapse
B0098688cellular_componentparallel fiber to Purkinje cell synapse
B0098693biological_processregulation of synaptic vesicle cycle
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
B0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B1905665biological_processpositive regulation of calcium ion import across plasma membrane
B1905949biological_processnegative regulation of calcium ion import across plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 500
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73
BHOH585

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 502
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110
BHOH755

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151
BHOH622

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 522
ChainResidue
AASP118
AASN150
AHIS199
AHIS281
AFE523
AHOH778

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE A 523
ChainResidue
AASP90
AHIS92
AASP118
AZN522
AHOH627
AHOH778
AHOH796

site_idCA1
Number of Residues5
DetailsCALCIUM BINDING SITE.
ChainResidue
BSER34
BSER36
BGLU41
BASP30
BASP32

site_idCA2
Number of Residues5
DetailsCALCIUM BINDING SITE.
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73

site_idCA3
Number of Residues5
DetailsCALCIUM BINDING SITE.
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110

site_idCA4
Number of Residues5
DetailsCALCIUM BINDING SITE.
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151

site_idFEB
Number of Residues3
DetailsFE BINDING SITE.
ChainResidue
AASP90
AHIS92
AASP118

site_idZNB
Number of Residues4
DetailsZN BINDING SITE.
ChainResidue
AASP118
AASN150
AHIS199
AHIS281

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
ChainResidueDetails
BASP30-PHE42
BASP62-PHE74
BASP99-LEU111
BASP140-PHE152

site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU147-GLU152

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
ChainResidueDetails
BLEU31
BPHE74
BLYS141
BGLY143
BGLY145
BILE147
BPHE152
BASN33
BGLY35
BLEU37
BPHE42
BTHR63
BGLY65
BGLY67
BVAL69

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
ChainResidueDetails
BMET100
BLYS102
BGLY104
BILE106
BLEU111
AHIS281

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000269|PubMed:23468591
ChainResidueDetails
BMET118
BASN122

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q63810
ChainResidueDetails
BILE106

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:25255805
ChainResidueDetails
BASN2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63329
ChainResidueDetails
ASER469

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER492

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 406
ChainResidueDetails
AASP90metal ligand
AHIS281metal ligand
AHIS92metal ligand
AASP118metal ligand
AASP121electrostatic stabiliser
AARG122transition state stabiliser
AASN150metal ligand
AHIS151proton shuttle (general acid/base)
AHIS199metal ligand
AARG254transition state stabiliser

218196

PDB entries from 2024-04-10

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