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

8I6J

The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state

Functional Information from GO Data
ChainGOidnamespacecontents
C0002199cellular_componentzona pellucida receptor complex
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005832cellular_componentchaperonin-containing T-complex
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0006457biological_processprotein folding
C0007339biological_processbinding of sperm to zona pellucida
C0032212biological_processpositive regulation of telomere maintenance via telomerase
C0044183molecular_functionprotein folding chaperone
C0044297cellular_componentcell body
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0061077biological_processchaperone-mediated protein folding
C0070062cellular_componentextracellular exosome
C1904851biological_processpositive regulation of establishment of protein localization to telomere
C1904871biological_processpositive regulation of protein localization to Cajal body
C1904874biological_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. RTcLGPkSmmKML
ChainResidueDetails
CARG38-LEU50

site_idPS00751
Number of Residues17
DetailsTCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
ChainResidueDetails
CMET59-PRO75

site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
ChainResidueDetails
CGLN87-THR95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330
ChainResidueDetails
CMET1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER11
CSER243

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P80318
ChainResidueDetails
CSER170
QSER236

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS222

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CSER244

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CTYR247

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER252

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR430
CTHR459

site_idSWS_FT_FI9
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS15
CLYS248
CLYS249

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211
ChainResidueDetails
CLYS381

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon