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8I9Q

The focused refinement of CCT4-PhLP2A from TRiC-PhLP2A complex in the open state

Functional Information from GO Data
ChainGOidnamespacecontents
D0002199cellular_componentzona pellucida receptor complex
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005829cellular_componentcytosol
D0005832cellular_componentchaperonin-containing T-complex
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0006457biological_processprotein folding
D0007339biological_processbinding of sperm to zona pellucida
D0016887molecular_functionATP hydrolysis activity
D0032212biological_processpositive regulation of telomere maintenance via telomerase
D0042470cellular_componentmelanosome
D0042995cellular_componentcell projection
D0044183molecular_functionprotein folding chaperone
D0044297cellular_componentcell body
D0050821biological_processprotein stabilization
D0051082molecular_functionunfolded protein binding
D0051973biological_processpositive regulation of telomerase activity
D0061077biological_processchaperone-mediated protein folding
D0070062cellular_componentextracellular exosome
D0090666biological_processscaRNA localization to Cajal body
D0140662molecular_functionATP-dependent protein folding chaperone
D1904851biological_processpositive regulation of establishment of protein localization to telomere
D1904871biological_processpositive regulation of protein localization to Cajal body
D1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
Q0001525biological_processangiogenesis
Q0001938biological_processpositive regulation of endothelial cell proliferation
Q0005515molecular_functionprotein binding
Q0005654cellular_componentnucleoplasm
Q0005737cellular_componentcytoplasm
Q0005783cellular_componentendoplasmic reticulum
Q0005829cellular_componentcytosol
Q0006457biological_processprotein folding
Q0006915biological_processapoptotic process
Q0010628biological_processpositive regulation of gene expression
Q0030036biological_processactin cytoskeleton organization
Q0032991cellular_componentprotein-containing complex
Q0043184molecular_functionvascular endothelial growth factor receptor 2 binding
Q0044183molecular_functionprotein folding chaperone
Q0045766biological_processpositive regulation of angiogenesis
Q0048471cellular_componentperinuclear region of cytoplasm
Q0050730biological_processregulation of peptidyl-tyrosine phosphorylation
Q0050821biological_processprotein stabilization
Q0061077biological_processchaperone-mediated protein folding
Q0097356cellular_componentperinucleolar compartment
Q1903645biological_processnegative regulation of chaperone-mediated protein folding
Q2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
Functional Information from PROSITE/UniProt
site_idPS00750
Number of Residues13
DetailsTCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI
ChainResidueDetails
DARG49-ILE61

site_idPS00751
Number of Residues17
DetailsTCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP
ChainResidueDetails
DILE70-PRO86

site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT
ChainResidueDetails
DGLN98-THR106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:26059764
ChainResidueDetails
QMET1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
QSER43

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
QSER234
QSER236
DSER202
DSER444

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS288
DLYS302
DLYS319
DLYS326

219869

PDB entries from 2024-05-15

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