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2CT9

The crystal structure of calcineurin B homologous proein 1 (CHP1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001578biological_processmicrotubule bundle formation
A0001933biological_processnegative regulation of protein phosphorylation
A0004860molecular_functionprotein kinase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006469biological_processnegative regulation of protein kinase activity
A0006611biological_processprotein export from nucleus
A0006903biological_processvesicle targeting
A0006906biological_processvesicle fusion
A0008017molecular_functionmicrotubule binding
A0010923biological_processnegative regulation of phosphatase activity
A0012505cellular_componentendomembrane system
A0015031biological_processprotein transport
A0015385molecular_functionsodium:proton antiporter activity
A0015630cellular_componentmicrotubule cytoskeleton
A0019900molecular_functionkinase binding
A0022406biological_processmembrane docking
A0030133cellular_componenttransport vesicle
A0031122biological_processcytoplasmic microtubule organization
A0031397biological_processnegative regulation of protein ubiquitination
A0031953biological_processnegative regulation of protein autophosphorylation
A0032088biological_processnegative regulation of NF-kappaB transcription factor activity
A0032417biological_processpositive regulation of sodium:proton antiporter activity
A0035725biological_processsodium ion transmembrane transport
A0042308biological_processnegative regulation of protein import into nucleus
A0045121cellular_componentmembrane raft
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0050821biological_processprotein stabilization
A0051222biological_processpositive regulation of protein transport
A0051259biological_processprotein complex oligomerization
A0051453biological_processregulation of intracellular pH
A0060050biological_processpositive regulation of protein glycosylation
A0061024biological_processmembrane organization
A0061025biological_processmembrane fusion
A0070885biological_processnegative regulation of calcineurin-NFAT signaling cascade
A0071073biological_processpositive regulation of phospholipid biosynthetic process
A0071468biological_processcellular response to acidic pH
A0090314biological_processpositive regulation of protein targeting to membrane
A1990351cellular_componenttransporter complex
B0000139cellular_componentGolgi membrane
B0001578biological_processmicrotubule bundle formation
B0001933biological_processnegative regulation of protein phosphorylation
B0004860molecular_functionprotein kinase inhibitor activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006469biological_processnegative regulation of protein kinase activity
B0006611biological_processprotein export from nucleus
B0006903biological_processvesicle targeting
B0006906biological_processvesicle fusion
B0008017molecular_functionmicrotubule binding
B0010923biological_processnegative regulation of phosphatase activity
B0012505cellular_componentendomembrane system
B0015031biological_processprotein transport
B0015385molecular_functionsodium:proton antiporter activity
B0015630cellular_componentmicrotubule cytoskeleton
B0019900molecular_functionkinase binding
B0022406biological_processmembrane docking
B0030133cellular_componenttransport vesicle
B0031122biological_processcytoplasmic microtubule organization
B0031397biological_processnegative regulation of protein ubiquitination
B0031953biological_processnegative regulation of protein autophosphorylation
B0032088biological_processnegative regulation of NF-kappaB transcription factor activity
B0032417biological_processpositive regulation of sodium:proton antiporter activity
B0035725biological_processsodium ion transmembrane transport
B0042308biological_processnegative regulation of protein import into nucleus
B0045121cellular_componentmembrane raft
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050821biological_processprotein stabilization
B0051222biological_processpositive regulation of protein transport
B0051259biological_processprotein complex oligomerization
B0051453biological_processregulation of intracellular pH
B0060050biological_processpositive regulation of protein glycosylation
B0061024biological_processmembrane organization
B0061025biological_processmembrane fusion
B0070885biological_processnegative regulation of calcineurin-NFAT signaling cascade
B0071073biological_processpositive regulation of phospholipid biosynthetic process
B0071468biological_processcellular response to acidic pH
B0090314biological_processpositive regulation of protein targeting to membrane
B1990351cellular_componenttransporter complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AASP123
AASP125
AASP127
ALYS129
AGLU134
AHOH325

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AALA170
AGLU175
AHOH343
AASP164
AASP166
AASP168

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP123
BASP125
BASP127
BLYS129
BGLU134
BHOH375

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP164
BASP166
BASP168
BALA170
BGLU175
BHOH344

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDKDDKISrdEL
ChainResidueDetails
AASP123-LEU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
ALEU124
BLEU135
ALYS126
AASP128
AILE130
ALEU135
BLEU124
BLYS126
BASP128
BILE130

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLN165
AGLY167
ASER169
APHE176
BGLN165
BGLY167
BSER169
BPHE176

site_idSWS_FT_FI3
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:Q99653
ChainResidueDetails
ASER3
BSER3

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PDB entries from 2024-10-16

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