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3BHO

Crystal Structure of the 25kDa Subunit of Human Cleavage factor Im with Ap4A

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
A1900365biological_processobsolete positive regulation of mRNA polyadenylation
A1990120biological_processobsolete messenger ribonucleoprotein complex assembly
A2000738biological_processpositive regulation of stem cell differentiation
A2000975biological_processpositive regulation of pro-B cell differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE B4P A 800
ChainResidue
AARG63
APHE103
AARG150
AGLN157
ALYS172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with RNA => ECO:0000269|PubMed:20479262, ECO:0000312|PDB:3MDG, ECO:0000312|PDB:3MDI
ChainResidueDetails
AGLU55
AARG63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17172643, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS23

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS29
ALYS56

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR40

218853

PDB entries from 2024-04-24

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