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1XML

Structure of human Dcps

Functional Information from GO Data
ChainGOidnamespacecontents
A0000288biological_processnuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
A0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
A0000340molecular_functionRNA 7-methylguanosine cap binding
A0000932cellular_componentP-body
A0004532molecular_functionRNA exonuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006397biological_processmRNA processing
A0008380biological_processRNA splicing
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0045292biological_processmRNA cis splicing, via spliceosome
A0048471cellular_componentperinuclear region of cytoplasm
A0110156biological_processmRNA methylguanosine-cap decapping
A0140932molecular_function5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
B0000288biological_processnuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
B0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
B0000340molecular_functionRNA 7-methylguanosine cap binding
B0000932cellular_componentP-body
B0004532molecular_functionRNA exonuclease activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006397biological_processmRNA processing
B0008380biological_processRNA splicing
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0045292biological_processmRNA cis splicing, via spliceosome
B0048471cellular_componentperinuclear region of cytoplasm
B0110156biological_processmRNA methylguanosine-cap decapping
B0140932molecular_function5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 601
ChainResidue
AHIS268
ASER272
AHIS277
AHIS279
AHOH651

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 602
ChainResidue
BARG294
BHOH637
BHOH777
BHIS268
BSER272
BHIS277
BHIS279

Functional Information from PROSITE/UniProt
site_idPS00892
Number of Residues19
DetailsHIT_1 HIT domain signature. RvylhYlPsYyHLHVHFTA
ChainResidueDetails
BARG264-ALA282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsMotif: {"description":"nuclear export sequence (NES)"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"Histidine triad motif"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15068804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15769464","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues22
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DAR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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