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6URG

Cryo-EM structure of human CPSF160-WDR33-CPSF30-CPSF100 PIM complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
A0006397biological_processmRNA processing
A0019899molecular_functionenzyme binding
A0035925molecular_functionmRNA 3'-UTR AU-rich region binding
A0180012biological_processco-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway
B0031124biological_processmRNA 3'-end processing
C0003676molecular_functionnucleic acid binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
C0006397biological_processmRNA processing
C0008270molecular_functionzinc ion binding
C0043231cellular_componentintracellular membrane-bounded organelle
C0046872molecular_functionmetal ion binding
C1990837molecular_functionsequence-specific double-stranded DNA binding
F0003723molecular_functionRNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
F0006397biological_processmRNA processing
F0006398biological_processmRNA 3'-end processing by stem-loop binding and cleavage
F0016020cellular_componentmembrane
F0098794cellular_componentpostsynapse
F0098978cellular_componentglutamatergic synapse
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue ZN C 301
ChainResidue
CCYS41
CCYS55
CHIS59

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues13
DetailsLIPOCALIN Lipocalin signature. EVKl.NLNGNWLLT
ChainResidueDetails
BGLU293-THR305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
FSER419
FSER420

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
FSER423

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
FSER660

site_idSWS_FT_FI4
Number of Residues24
DetailsZN_FING: C3H1-type 4 => ECO:0000255|PROSITE-ProRule:PRU00723
ChainResidueDetails
CGLU118-HIS142
BLYS560

site_idSWS_FT_FI5
Number of Residues26
DetailsZN_FING: C3H1-type 5 => ECO:0000255|PROSITE-ProRule:PRU00723
ChainResidueDetails
CTHR143-PHE169

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CMET200

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
CSER202

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CPRO212

227111

PDB entries from 2024-11-06

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