Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CF0

HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000774molecular_functionadenyl-nucleotide exchange factor activity
A0001784molecular_functionphosphotyrosine residue binding
A0001843biological_processneural tube closure
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0003785molecular_functionactin monomer binding
A0005515molecular_functionprotein binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005925cellular_componentfocal adhesion
A0005938cellular_componentcell cortex
A0006357biological_processregulation of transcription by RNA polymerase II
A0010634biological_processpositive regulation of epithelial cell migration
A0016020cellular_componentmembrane
A0030036biological_processactin cytoskeleton organization
A0030833biological_processregulation of actin filament polymerization
A0030837biological_processnegative regulation of actin filament polymerization
A0030838biological_processpositive regulation of actin filament polymerization
A0031267molecular_functionsmall GTPase binding
A0032232biological_processnegative regulation of actin filament bundle assembly
A0032233biological_processpositive regulation of actin filament bundle assembly
A0032781biological_processpositive regulation of ATP-dependent activity
A0044087biological_processregulation of cellular component biogenesis
A0045296molecular_functioncadherin binding
A0050804biological_processmodulation of chemical synaptic transmission
A0050821biological_processprotein stabilization
A0051497biological_processnegative regulation of stress fiber assembly
A0060074biological_processsynapse maturation
A0070062cellular_componentextracellular exosome
A0070064molecular_functionproline-rich region binding
A0072562cellular_componentblood microparticle
A0098885biological_processmodification of postsynaptic actin cytoskeleton
A0098978cellular_componentglutamatergic synapse
A0110053biological_processregulation of actin filament organization
A1900029biological_processpositive regulation of ruffle assembly
B0000774molecular_functionadenyl-nucleotide exchange factor activity
B0001784molecular_functionphosphotyrosine residue binding
B0001843biological_processneural tube closure
B0003723molecular_functionRNA binding
B0003779molecular_functionactin binding
B0003785molecular_functionactin monomer binding
B0005515molecular_functionprotein binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005925cellular_componentfocal adhesion
B0005938cellular_componentcell cortex
B0006357biological_processregulation of transcription by RNA polymerase II
B0010634biological_processpositive regulation of epithelial cell migration
B0016020cellular_componentmembrane
B0030036biological_processactin cytoskeleton organization
B0030833biological_processregulation of actin filament polymerization
B0030837biological_processnegative regulation of actin filament polymerization
B0030838biological_processpositive regulation of actin filament polymerization
B0031267molecular_functionsmall GTPase binding
B0032232biological_processnegative regulation of actin filament bundle assembly
B0032233biological_processpositive regulation of actin filament bundle assembly
B0032781biological_processpositive regulation of ATP-dependent activity
B0044087biological_processregulation of cellular component biogenesis
B0045296molecular_functioncadherin binding
B0050804biological_processmodulation of chemical synaptic transmission
B0050821biological_processprotein stabilization
B0051497biological_processnegative regulation of stress fiber assembly
B0060074biological_processsynapse maturation
B0070062cellular_componentextracellular exosome
B0070064molecular_functionproline-rich region binding
B0072562cellular_componentblood microparticle
B0098885biological_processmodification of postsynaptic actin cytoskeleton
B0098978cellular_componentglutamatergic synapse
B0110053biological_processregulation of actin filament organization
B1900029biological_processpositive regulation of ruffle assembly
Functional Information from PDB Data
site_idPPA
Number of Residues5
DetailsPOLY-L-PROLINE BINDING SITE.
ChainResidue
ATRP3
ATRP31
ATYR6
AHIS133
ATYR139

site_idPPB
Number of Residues5
DetailsPOLY-L-PROLINE BINDING SITE.
ChainResidue
BTYR139
BTRP3
BTRP31
BTYR6
BHIS133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:3342873, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712
ChainResidueDetails
AGLY2
BGLY2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62963
ChainResidueDetails
APRO28
BPRO28

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER57
BSER57

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
AMET85
BMET85

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ATHR105
ATHR108
BTHR105
BTHR108

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
AGLU129
BGLU129

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by ROCK1 => ECO:0000269|PubMed:18573880
ChainResidueDetails
AGLN138
BGLN138

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
AASP54
BASP54

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon