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8QJ7

Cryo-EM structure of human DNA polymerase alpha-primase in pre-initiation stage 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000731biological_processDNA synthesis involved in DNA repair
A0000785cellular_componentchromatin
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003688molecular_functionDNA replication origin binding
A0003697molecular_functionsingle-stranded DNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005658cellular_componentalpha DNA polymerase:primase complex
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006261biological_processDNA-templated DNA replication
A0006269biological_processDNA replication, synthesis of primer
A0006270biological_processDNA replication initiation
A0006271biological_processDNA strand elongation involved in DNA replication
A0006272biological_processleading strand elongation
A0006273biological_processlagging strand elongation
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0008270molecular_functionzinc ion binding
A0016363cellular_componentnuclear matrix
A0019901molecular_functionprotein kinase binding
A0031981cellular_componentnuclear lumen
A0032479biological_processregulation of type I interferon production
A0046872molecular_functionmetal ion binding
A1902975biological_processmitotic DNA replication initiation
A1904161biological_processDNA synthesis involved in UV-damage excision repair
B0003674molecular_functionmolecular_function
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005658cellular_componentalpha DNA polymerase:primase complex
B0005829cellular_componentcytosol
B0006260biological_processDNA replication
B0006269biological_processDNA replication, synthesis of primer
B0006270biological_processDNA replication initiation
B0006606biological_processprotein import into nucleus
C0000287molecular_functionmagnesium ion binding
C0000428cellular_componentDNA-directed RNA polymerase complex
C0003896molecular_functionDNA primase activity
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005658cellular_componentalpha DNA polymerase:primase complex
C0006260biological_processDNA replication
C0006269biological_processDNA replication, synthesis of primer
C0006270biological_processDNA replication initiation
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
C0016779molecular_functionnucleotidyltransferase activity
C0032553molecular_functionribonucleotide binding
C0046872molecular_functionmetal ion binding
C1990077cellular_componentprimosome complex
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005658cellular_componentalpha DNA polymerase:primase complex
D0006260biological_processDNA replication
D0006261biological_processDNA-templated DNA replication
D0006269biological_processDNA replication, synthesis of primer
D0006270biological_processDNA replication initiation
D0046872molecular_functionmetal ion binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
D0071667molecular_functionDNA/RNA hybrid binding
D1903934biological_processpositive regulation of DNA primase activity
D1990077cellular_componentprimosome complex
Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIMI
ChainResidueDetails
ATYR1000-ILE1008

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377
ChainResidueDetails
DCYS287
DCYS367
DCYS424

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159
ChainResidueDetails
DCYS384
BTHR130
ACYS1310
ACYS1315
ACYS1348
ACYS1353
ACYS1371
ACYS1374

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR470
CCYS122
CCYS128
CCYS131

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER147

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER152

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER154

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER209

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P33609
ChainResidueDetails
ALYS224

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR406

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P33609
ChainResidueDetails
ALYS970

224201

PDB entries from 2024-08-28

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