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3N9U

Crystal Structure of the Complex between the 25 kDa Subunit and the 59 kDa Subunit (RRM domain) of Human Cleavage Factor Im

Functional Information from GO Data
ChainGOidnamespacecontents
A0003682molecular_functionchromatin binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
A0005849cellular_componentmRNA cleavage factor complex
A0006397biological_processmRNA processing
A0010608biological_processpost-transcriptional regulation of gene expression
A0016604cellular_componentnuclear body
A0030154biological_processcell differentiation
A0031124biological_processmRNA 3'-end processing
A0034451cellular_componentcentriolar satellite
A0035925molecular_functionmRNA 3'-UTR AU-rich region binding
A0042382cellular_componentparaspeckles
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042826molecular_functionhistone deacetylase binding
A0051262biological_processprotein tetramerization
A0051290biological_processprotein heterotetramerization
A0110104biological_processmRNA alternative polyadenylation
A0180010biological_processco-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway
A1900365biological_processobsolete positive regulation of mRNA polyadenylation
A2000738biological_processpositive regulation of stem cell differentiation
A2000975biological_processpositive regulation of pro-B cell differentiation
B0003682molecular_functionchromatin binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005847cellular_componentmRNA cleavage and polyadenylation specificity factor complex
B0005849cellular_componentmRNA cleavage factor complex
B0006397biological_processmRNA processing
B0010608biological_processpost-transcriptional regulation of gene expression
B0016604cellular_componentnuclear body
B0030154biological_processcell differentiation
B0031124biological_processmRNA 3'-end processing
B0034451cellular_componentcentriolar satellite
B0035925molecular_functionmRNA 3'-UTR AU-rich region binding
B0042382cellular_componentparaspeckles
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042826molecular_functionhistone deacetylase binding
B0051262biological_processprotein tetramerization
B0051290biological_processprotein heterotetramerization
B0110104biological_processmRNA alternative polyadenylation
B0180010biological_processco-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway
B1900365biological_processobsolete positive regulation of mRNA polyadenylation
B2000738biological_processpositive regulation of stem cell differentiation
B2000975biological_processpositive regulation of pro-B cell differentiation
C0003676molecular_functionnucleic acid binding
C0003723molecular_functionRNA binding
I0003676molecular_functionnucleic acid binding
I0003723molecular_functionRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 228
ChainResidue
AGLU81
ALYS105
ALEU106
ALYS172
AILE211

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 228
ChainResidue
BILE211
BHOH267
BHOH313
BHOH317
BHOH326
BGLU81
BLYS105
BLEU106
BLYS172

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 229
ChainResidue
ATYR202
BPRO156
BGLN157
BHOH391

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Interaction with RNA => ECO:0000269|PubMed:20479262, ECO:0000312|PDB:3MDG, ECO:0000312|PDB:3MDI
ChainResidueDetails
AGLU55
AARG63
BGLU55
BARG63

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17172643, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS23
BLYS23

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS29
ALYS56
BLYS29
BLYS56

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR40
BTYR40

223166

PDB entries from 2024-07-31

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