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

5UYX

Structure of Human T-complex protein 1 subunit epsilon (CCT5)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003730molecular_functionmRNA 3'-UTR binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005832cellular_componentchaperonin-containing T-complex
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006457biological_processprotein folding
A0007339biological_processbinding of sperm to zona pellucida
A0009615biological_processresponse to virus
A0016887molecular_functionATP hydrolysis activity
A0031681molecular_functionG-protein beta-subunit binding
A0032212biological_processpositive regulation of telomere maintenance via telomerase
A0044183molecular_functionprotein folding chaperone
A0044297cellular_componentcell body
A0048027molecular_functionmRNA 5'-UTR binding
A0048487molecular_functionbeta-tubulin binding
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0061077biological_processchaperone-mediated protein folding
A0070062cellular_componentextracellular exosome
A0140662molecular_functionATP-dependent protein folding chaperone
A1904851biological_processpositive regulation of establishment of protein localization to telomere
A1904871biological_processpositive regulation of protein localization to Cajal body
A1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
B0003730molecular_functionmRNA 3'-UTR binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005832cellular_componentchaperonin-containing T-complex
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006457biological_processprotein folding
B0007339biological_processbinding of sperm to zona pellucida
B0009615biological_processresponse to virus
B0016887molecular_functionATP hydrolysis activity
B0031681molecular_functionG-protein beta-subunit binding
B0032212biological_processpositive regulation of telomere maintenance via telomerase
B0044183molecular_functionprotein folding chaperone
B0044297cellular_componentcell body
B0048027molecular_functionmRNA 5'-UTR binding
B0048487molecular_functionbeta-tubulin binding
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0061077biological_processchaperone-mediated protein folding
B0070062cellular_componentextracellular exosome
B0140662molecular_functionATP-dependent protein folding chaperone
B1904851biological_processpositive regulation of establishment of protein localization to telomere
B1904871biological_processpositive regulation of protein localization to Cajal body
B1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
C0003730molecular_functionmRNA 3'-UTR binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0005832cellular_componentchaperonin-containing T-complex
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0006457biological_processprotein folding
C0007339biological_processbinding of sperm to zona pellucida
C0009615biological_processresponse to virus
C0016887molecular_functionATP hydrolysis activity
C0031681molecular_functionG-protein beta-subunit binding
C0032212biological_processpositive regulation of telomere maintenance via telomerase
C0044183molecular_functionprotein folding chaperone
C0044297cellular_componentcell body
C0048027molecular_functionmRNA 5'-UTR binding
C0048487molecular_functionbeta-tubulin binding
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0061077biological_processchaperone-mediated protein folding
C0070062cellular_componentextracellular exosome
C0140662molecular_functionATP-dependent protein folding chaperone
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
D0003730molecular_functionmRNA 3'-UTR binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
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
D0009615biological_processresponse to virus
D0016887molecular_functionATP hydrolysis activity
D0031681molecular_functionG-protein beta-subunit binding
D0032212biological_processpositive regulation of telomere maintenance via telomerase
D0044183molecular_functionprotein folding chaperone
D0044297cellular_componentcell body
D0048027molecular_functionmRNA 5'-UTR binding
D0048487molecular_functionbeta-tubulin binding
D0050821biological_processprotein stabilization
D0051082molecular_functionunfolded protein binding
D0061077biological_processchaperone-mediated protein folding
D0070062cellular_componentextracellular exosome
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
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ADP A 601
ChainResidue
ALEU52
AGLU508
ALYS513
AGLY53
AASP104
AGLY105
ATHR106
ATHR107
AGLY422
ACYS493
AVAL506

site_idAC2
Number of Residues14
Detailsbinding site for residue ADP B 601
ChainResidue
BSER51
BLEU52
BGLY53
BASP104
BGLY105
BTHR106
BTHR107
BGLY108
BGLY422
BLEU462
BCYS493
BLEU494
BVAL506
BGLU508

site_idAC3
Number of Residues10
Detailsbinding site for residue ADP C 601
ChainResidue
CSER51
CLEU52
CGLY53
CGLY105
CTHR106
CTHR107
CGLY108
CGLY422
CCYS493
CGLU508

site_idAC4
Number of Residues13
Detailsbinding site for residue ADP D 601
ChainResidue
DSER51
DLEU52
DGLY53
DASP104
DGLY105
DTHR106
DTHR107
DGLY108
DGLY422
DCYS493
DLEU494
DVAL506
DGLU508

Functional Information from PROSITE/UniProt
site_idPS00750
Number of Residues13
DetailsTCP1_1 Chaperonins TCP-1 signature 1. RTsLGPnGldKMM
ChainResidueDetails
AARG49-MET61

site_idPS00751
Number of Residues17
DetailsTCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILsmMdVdHQ
ChainResidueDetails
AVAL70-GLN86

site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QDdeIGDGT
ChainResidueDetails
AGLN98-THR106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER26
BSER26
CSER26
DSER26

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER346
ASER539
BSER346
BSER539
CSER346
CSER539
DSER346
DSER539

site_idSWS_FT_FI4
Number of Residues32
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS20
BLYS210
BLYS214
BLYS265
BLYS275
BLYS279
BLYS392
CLYS20
CLYS210
CLYS214
CLYS265
CLYS275
CLYS279
CLYS392
DLYS20
DLYS210
DLYS214
DLYS265
ALYS210
DLYS275
DLYS279
DLYS392
ALYS214
ALYS265
ALYS275
ALYS279
ALYS392
BLYS20

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon