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4D1E

THE CRYSTAL STRUCTURE OF HUMAN MUSCLE ALPHA-ACTININ-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005178molecular_functionintegrin binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0007155biological_processcell adhesion
A0008092molecular_functioncytoskeletal protein binding
A0008307molecular_functionstructural constituent of muscle
A0015629cellular_componentactin cytoskeleton
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0030018cellular_componentZ disc
A0030035biological_processmicrospike assembly
A0030036biological_processactin cytoskeleton organization
A0030054cellular_componentcell junction
A0030175cellular_componentfilopodium
A0030274molecular_functionLIM domain binding
A0030374molecular_functionnuclear receptor coactivator activity
A0030864cellular_componentcortical actin cytoskeleton
A0031093cellular_componentplatelet alpha granule lumen
A0031143cellular_componentpseudopodium
A0031432molecular_functiontitin binding
A0042391biological_processregulation of membrane potential
A0042802molecular_functionidentical protein binding
A0042981biological_processregulation of apoptotic process
A0042995cellular_componentcell projection
A0043197cellular_componentdendritic spine
A0043267biological_processnegative regulation of potassium ion transport
A0043268biological_processpositive regulation of potassium ion transport
A0044325molecular_functiontransmembrane transporter binding
A0045214biological_processsarcomere organization
A0045893biological_processpositive regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0048041biological_processfocal adhesion assembly
A0051015molecular_functionactin filament binding
A0051373molecular_functionFATZ binding
A0051695biological_processactin filament uncapping
A0055001biological_processmuscle cell development
A0055013biological_processcardiac muscle cell development
A0070062cellular_componentextracellular exosome
A0070080molecular_functiontitin Z domain binding
A0072659biological_processprotein localization to plasma membrane
A0086097biological_processphospholipase C-activating angiotensin-activated signaling pathway
A0098839cellular_componentpostsynaptic density membrane
A0098871cellular_componentpostsynaptic actin cytoskeleton
A0098973molecular_functionstructural constituent of postsynaptic actin cytoskeleton
A0098974biological_processpostsynaptic actin cytoskeleton organization
A0098978cellular_componentglutamatergic synapse
A0099092cellular_componentpostsynaptic density, intracellular component
A1901017biological_processnegative regulation of potassium ion transmembrane transporter activity
A1901018biological_processpositive regulation of potassium ion transmembrane transporter activity
A2000009biological_processnegative regulation of protein localization to cell surface
A2001137biological_processpositive regulation of endocytic recycling
A2001259biological_processpositive regulation of cation channel activity
Functional Information from PROSITE/UniProt
site_idPS00019
Number of Residues10
DetailsACTININ_1 Actinin-type actin-binding domain signature 1. QRkTFTAWCN
ChainResidueDetails
AGLN40-ASN49

site_idPS00020
Number of Residues25
DetailsACTININ_2 Actinin-type actin-binding domain signature 2. LvSIGAeEIvDgnvkMtLGMIWtII
ChainResidueDetails
ALEU114-ILE138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP766
AASN770
AASP777
AASP802
AASN804
ATHR808

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9JI91
ChainResidueDetails
ATHR237

227111

PDB entries from 2024-11-06

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