Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1AUI

HUMAN CALCINEURIN HETERODIMER

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005516	molecular_function	calmodulin binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005955	cellular_component	calcineurin complex
A	0006470	biological_process	protein dephosphorylation
A	0008544	biological_process	epidermis development
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010613	biological_process	positive regulation of cardiac muscle hypertrophy
A	0010628	biological_process	positive regulation of gene expression
A	0010629	biological_process	negative regulation of gene expression
A	0016311	biological_process	dephosphorylation
A	0016787	molecular_function	hydrolase activity
A	0019897	cellular_component	extrinsic component of plasma membrane
A	0019899	molecular_function	enzyme binding
A	0023057	biological_process	negative regulation of signaling
A	0030018	cellular_component	Z disc
A	0030216	biological_process	keratinocyte differentiation
A	0030335	biological_process	positive regulation of cell migration
A	0033173	biological_process	calcineurin-NFAT signaling cascade
A	0033192	molecular_function	calmodulin-dependent protein phosphatase activity
A	0042060	biological_process	wound healing
A	0042104	biological_process	positive regulation of activated T cell proliferation
A	0042110	biological_process	T cell activation
A	0042383	cellular_component	sarcolemma
A	0043197	cellular_component	dendritic spine
A	0043403	biological_process	skeletal muscle tissue regeneration
A	0045669	biological_process	positive regulation of osteoblast differentiation
A	0045672	biological_process	positive regulation of osteoclast differentiation
A	0045785	biological_process	positive regulation of cell adhesion
A	0045807	biological_process	positive regulation of endocytosis
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0046878	biological_process	positive regulation of saliva secretion
A	0046983	molecular_function	protein dimerization activity
A	0048741	biological_process	skeletal muscle fiber development
A	0050804	biological_process	modulation of chemical synaptic transmission
A	0051117	molecular_function	ATPase binding
A	0051592	biological_process	response to calcium ion
A	0061006	biological_process	regulation of cell proliferation involved in kidney morphogenesis
A	0070886	biological_process	positive regulation of calcineurin-NFAT signaling cascade
A	0090193	biological_process	positive regulation of glomerulus development
A	0097205	biological_process	renal filtration
A	0097720	biological_process	calcineurin-mediated signaling
A	0098685	cellular_component	Schaffer collateral - CA1 synapse
A	0098978	cellular_component	glutamatergic synapse
A	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
A	0110062	biological_process	negative regulation of angiotensin-activated signaling pathway
A	1903235	biological_process	positive regulation of calcium ion-dependent exocytosis of neurotransmitter
A	1903244	biological_process	positive regulation of cardiac muscle hypertrophy in response to stress
A	1905205	biological_process	positive regulation of connective tissue replacement
A	1905665	biological_process	positive regulation of calcium ion import across plasma membrane
A	1905949	biological_process	negative regulation of calcium ion import across plasma membrane
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0004723	molecular_function	calcium-dependent protein serine/threonine phosphatase activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005516	molecular_function	calmodulin binding
B	0005654	cellular_component	nucleoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005955	cellular_component	calcineurin complex
B	0008597	molecular_function	calcium-dependent protein serine/threonine phosphatase regulator activity
B	0019902	molecular_function	phosphatase binding
B	0019904	molecular_function	protein domain specific binding
B	0033173	biological_process	calcineurin-NFAT signaling cascade
B	0042383	cellular_component	sarcolemma
B	0045202	cellular_component	synapse
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046872	molecular_function	metal ion binding
B	0070886	biological_process	positive regulation of calcineurin-NFAT signaling cascade
B	0098685	cellular_component	Schaffer collateral - CA1 synapse
B	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
B	0098688	cellular_component	parallel fiber to Purkinje cell synapse
B	0098693	biological_process	regulation of synaptic vesicle cycle
B	0098794	cellular_component	postsynapse
B	0098978	cellular_component	glutamatergic synapse
B	0099149	biological_process	regulation of postsynaptic neurotransmitter receptor internalization
B	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
B	1905665	biological_process	positive regulation of calcium ion import across plasma membrane
B	1905949	biological_process	negative regulation of calcium ion import across plasma membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 500

Chain	Residue
B	ASP30
B	ASP32
B	SER34
B	SER36
B	GLU41

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 501

Chain	Residue
B	ASP62
B	ASP64
B	ASN66
B	GLU68
B	GLU73
B	HOH585

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 502

Chain	Residue
B	ASP99
B	ASP101
B	ASP103
B	TYR105
B	GLU110
B	HOH755

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 503

Chain	Residue
B	ASP140
B	ASP142
B	ASP144
B	ARG146
B	GLU151
B	HOH622

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 522

Chain	Residue
A	ASP118
A	ASN150
A	HIS199
A	HIS281
A	FE523
A	HOH778

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE A 523

Chain	Residue
A	ASP90
A	HIS92
A	ASP118
A	ZN522
A	HOH627
A	HOH778
A	HOH796

site_id	CA1
Number of Residues	5
Details	CALCIUM BINDING SITE.

Chain	Residue
B	SER34
B	SER36
B	GLU41
B	ASP30
B	ASP32

site_id	CA2
Number of Residues	5
Details	CALCIUM BINDING SITE.

Chain	Residue
B	ASP62
B	ASP64
B	ASN66
B	GLU68
B	GLU73

site_id	CA3
Number of Residues	5
Details	CALCIUM BINDING SITE.

Chain	Residue
B	ASP99
B	ASP101
B	ASP103
B	TYR105
B	GLU110

site_id	CA4
Number of Residues	5
Details	CALCIUM BINDING SITE.

Chain	Residue
B	ASP140
B	ASP142
B	ASP144
B	ARG146
B	GLU151

site_id	FEB
Number of Residues	3
Details	FE BINDING SITE.

Chain	Residue
A	ASP90
A	HIS92
A	ASP118

site_id	ZNB
Number of Residues	4
Details	ZN BINDING SITE.

Chain	Residue
A	ASP118
A	ASN150
A	HIS199
A	HIS281

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF

Chain	Residue	Details
B	ASP30-PHE42
B	ASP62-PHE74
B	ASP99-LEU111
B	ASP140-PHE152

site_id	PS00125
Number of Residues	6
Details	SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE

Chain	Residue	Details
A	LEU147-GLU152

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	284
Details	Region: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Region: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17502104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Region: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Motif: {"description":"SAPNY motif","evidences":[{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UUQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63329","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	28
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	35
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	35
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	35
Details	Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	5
Details	Region: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Site: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 11015619, 8524402

Chain	Residue	Details
A	HIS151
A	ARG122
A	ARG254
A	ASP121

site_id	MCSA1
Number of Residues	10
Details	M-CSA 406

Chain	Residue	Details
A	ASP90	metal ligand
A	HIS281	metal ligand
A	HIS92	metal ligand
A	ASP118	metal ligand
A	ASP121	electrostatic stabiliser
A	ARG122	transition state stabiliser
A	ASN150	metal ligand
A	HIS151	proton shuttle (general acid/base)
A	HIS199	metal ligand
A	ARG254	transition state stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)