Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3F3F

Crystal structure of the nucleoporin pair Nup85-Seh1, space group P21

Functional Information from GO Data
ChainGOidnamespacecontents
A0005198molecular_functionstructural molecule activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005773cellular_componentvacuole
A0005774cellular_componentvacuolar membrane
A0006913biological_processnucleocytoplasmic transport
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0017056molecular_functionstructural constituent of nuclear pore
A0031080cellular_componentnuclear pore outer ring
A0031965cellular_componentnuclear membrane
A0034198biological_processcellular response to amino acid starvation
A0035859cellular_componentSeh1-associated complex
A0051028biological_processmRNA transport
A1903432biological_processregulation of TORC1 signaling
A1904263biological_processpositive regulation of TORC1 signaling
B0005198molecular_functionstructural molecule activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005643cellular_componentnuclear pore
B0005773cellular_componentvacuole
B0005774cellular_componentvacuolar membrane
B0006913biological_processnucleocytoplasmic transport
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0017056molecular_functionstructural constituent of nuclear pore
B0031080cellular_componentnuclear pore outer ring
B0031965cellular_componentnuclear membrane
B0034198biological_processcellular response to amino acid starvation
B0035859cellular_componentSeh1-associated complex
B0051028biological_processmRNA transport
B1903432biological_processregulation of TORC1 signaling
B1904263biological_processpositive regulation of TORC1 signaling
E0005198molecular_functionstructural molecule activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005635cellular_componentnuclear envelope
E0005643cellular_componentnuclear pore
E0005773cellular_componentvacuole
E0005774cellular_componentvacuolar membrane
E0006913biological_processnucleocytoplasmic transport
E0015031biological_processprotein transport
E0016020cellular_componentmembrane
E0017056molecular_functionstructural constituent of nuclear pore
E0031080cellular_componentnuclear pore outer ring
E0031965cellular_componentnuclear membrane
E0034198biological_processcellular response to amino acid starvation
E0035859cellular_componentSeh1-associated complex
E0051028biological_processmRNA transport
E1903432biological_processregulation of TORC1 signaling
E1904263biological_processpositive regulation of TORC1 signaling
F0005198molecular_functionstructural molecule activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005635cellular_componentnuclear envelope
F0005643cellular_componentnuclear pore
F0005773cellular_componentvacuole
F0005774cellular_componentvacuolar membrane
F0006913biological_processnucleocytoplasmic transport
F0015031biological_processprotein transport
F0016020cellular_componentmembrane
F0017056molecular_functionstructural constituent of nuclear pore
F0031080cellular_componentnuclear pore outer ring
F0031965cellular_componentnuclear membrane
F0034198biological_processcellular response to amino acid starvation
F0035859cellular_componentSeh1-associated complex
F0051028biological_processmRNA transport
F1903432biological_processregulation of TORC1 signaling
F1904263biological_processpositive regulation of TORC1 signaling
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER257
BSER257
ESER257
FSER257

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon