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3CHW

Complex of Dictyostelium discoideum Actin with Profilin and the Last Poly-Pro of Human VASP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000281biological_processmitotic cytokinesis
A0000902biological_processcell morphogenesis
A0001778biological_processplasma membrane repair
A0001891cellular_componentphagocytic cup
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005911cellular_componentcell-cell junction
A0005938cellular_componentcell cortex
A0006897biological_processendocytosis
A0006909biological_processphagocytosis
A0006935biological_processchemotaxis
A0006972biological_processhyperosmotic response
A0007010biological_processcytoskeleton organization
A0015629cellular_componentactin cytoskeleton
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0017022molecular_functionmyosin binding
A0030027cellular_componentlamellipodium
A0030139cellular_componentendocytic vesicle
A0030864cellular_componentcortical actin cytoskeleton
A0031143cellular_componentpseudopodium
A0031252cellular_componentcell leading edge
A0032009cellular_componentearly phagosome
A0032010cellular_componentphagolysosome
A0042331biological_processphototaxis
A0045335cellular_componentphagocytic vesicle
A0051591biological_processresponse to cAMP
A0060187cellular_componentcell pole
A0061836cellular_componentintranuclear rod
A0061851cellular_componentleading edge of lamellipodium
A0070685cellular_componentmacropinocytic cup
P0000774molecular_functionadenyl-nucleotide exchange factor activity
P0001784molecular_functionphosphotyrosine residue binding
P0001843biological_processneural tube closure
P0003723molecular_functionRNA binding
P0003779molecular_functionactin binding
P0003785molecular_functionactin monomer binding
P0005515molecular_functionprotein binding
P0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
P0005634cellular_componentnucleus
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0005856cellular_componentcytoskeleton
P0005925cellular_componentfocal adhesion
P0005938cellular_componentcell cortex
P0006357biological_processregulation of transcription by RNA polymerase II
P0010634biological_processpositive regulation of epithelial cell migration
P0016020cellular_componentmembrane
P0030036biological_processactin cytoskeleton organization
P0030833biological_processregulation of actin filament polymerization
P0030837biological_processnegative regulation of actin filament polymerization
P0030838biological_processpositive regulation of actin filament polymerization
P0031267molecular_functionsmall GTPase binding
P0032232biological_processnegative regulation of actin filament bundle assembly
P0032233biological_processpositive regulation of actin filament bundle assembly
P0032781biological_processpositive regulation of ATP-dependent activity
P0044087biological_processregulation of cellular component biogenesis
P0045296molecular_functioncadherin binding
P0050804biological_processmodulation of chemical synaptic transmission
P0050821biological_processprotein stabilization
P0051497biological_processnegative regulation of stress fiber assembly
P0060074biological_processsynapse maturation
P0070062cellular_componentextracellular exosome
P0070064molecular_functionproline-rich region binding
P0072562cellular_componentblood microparticle
P0098885biological_processmodification of postsynaptic actin cytoskeleton
P0098978cellular_componentglutamatergic synapse
P0110053biological_processregulation of actin filament organization
P1900029biological_processpositive regulation of ruffle assembly
Functional Information from PDB Data
site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 402
ChainResidue
AGLY13
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
APHE306
ALYS336
ASER14
AGLY15
AMET16
ALYS18
AGLY156
AASP157
AGLY158
AGLY182

Functional Information from PROSITE/UniProt
site_idPS00414
Number of Residues8
DetailsPROFILIN Profilin signature. .AgWNaYiD
ChainResidueDetails
PALA1-ASP8

site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKeEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:3342873, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712
ChainResidueDetails
PALA1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62963
ChainResidueDetails
PSER27

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
PSER56

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
PSER84

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
PLYS104
PLYS107

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
PTYR128

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ROCK1 => ECO:0000269|PubMed:18573880
ChainResidueDetails
PSER137

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
PLYS53

219140

PDB entries from 2024-05-01

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