3W5K
Crystal structure of Snail1 and importin beta complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005635 | cellular_component | nuclear envelope |
A | 0005643 | cellular_component | nuclear pore |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006404 | biological_process | RNA import into nucleus |
A | 0006606 | biological_process | protein import into nucleus |
A | 0006607 | biological_process | NLS-bearing protein import into nucleus |
A | 0006610 | biological_process | ribosomal protein import into nucleus |
A | 0006886 | biological_process | intracellular protein transport |
A | 0007079 | biological_process | mitotic chromosome movement towards spindle pole |
A | 0007080 | biological_process | mitotic metaphase chromosome alignment |
A | 0008139 | molecular_function | nuclear localization sequence binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0010494 | cellular_component | cytoplasmic stress granule |
A | 0015031 | biological_process | protein transport |
A | 0016020 | cellular_component | membrane |
A | 0019899 | molecular_function | enzyme binding |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030953 | biological_process | astral microtubule organization |
A | 0031267 | molecular_function | small GTPase binding |
A | 0031965 | cellular_component | nuclear membrane |
A | 0032991 | cellular_component | protein-containing complex |
A | 0035332 | biological_process | positive regulation of hippo signaling |
A | 0035580 | cellular_component | specific granule lumen |
A | 0040001 | biological_process | establishment of mitotic spindle localization |
A | 0042564 | cellular_component | NLS-dependent protein nuclear import complex |
A | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0051879 | molecular_function | Hsp90 protein binding |
A | 0061608 | molecular_function | nuclear import signal receptor activity |
A | 0061676 | molecular_function | importin-alpha family protein binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071782 | cellular_component | endoplasmic reticulum tubular network |
A | 0090307 | biological_process | mitotic spindle assembly |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
B | 0000977 | molecular_function | RNA polymerase II transcription regulatory region sequence-specific DNA binding |
B | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
B | 0001227 | molecular_function | DNA-binding transcription repressor activity, RNA polymerase II-specific |
B | 0001649 | biological_process | osteoblast differentiation |
B | 0001650 | cellular_component | fibrillar center |
B | 0001707 | biological_process | mesoderm formation |
B | 0001837 | biological_process | epithelial to mesenchymal transition |
B | 0003180 | biological_process | aortic valve morphogenesis |
B | 0003198 | biological_process | epithelial to mesenchymal transition involved in endocardial cushion formation |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005721 | cellular_component | pericentric heterochromatin |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0007219 | biological_process | Notch signaling pathway |
B | 0007498 | biological_process | mesoderm development |
B | 0008270 | molecular_function | zinc ion binding |
B | 0010631 | biological_process | epithelial cell migration |
B | 0010718 | biological_process | positive regulation of epithelial to mesenchymal transition |
B | 0010957 | biological_process | negative regulation of vitamin D biosynthetic process |
B | 0019900 | molecular_function | kinase binding |
B | 0030335 | biological_process | positive regulation of cell migration |
B | 0031069 | biological_process | hair follicle morphogenesis |
B | 0043518 | biological_process | negative regulation of DNA damage response, signal transduction by p53 class mediator |
B | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0046872 | molecular_function | metal ion binding |
B | 0048762 | biological_process | mesenchymal cell differentiation |
B | 0060021 | biological_process | roof of mouth development |
B | 0060070 | biological_process | canonical Wnt signaling pathway |
B | 0060536 | biological_process | cartilage morphogenesis |
B | 0060707 | biological_process | trophoblast giant cell differentiation |
B | 0060806 | biological_process | negative regulation of cell differentiation involved in embryonic placenta development |
B | 0060972 | biological_process | left/right pattern formation |
B | 0070828 | biological_process | heterochromatin organization |
B | 0070888 | molecular_function | E-box binding |
B | 1902230 | biological_process | negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage |
B | 1990837 | molecular_function | sequence-specific double-stranded DNA binding |
B | 2000810 | biological_process | regulation of bicellular tight junction assembly |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 501 |
Chain | Residue |
B | CYS156 |
B | CYS159 |
B | LYS161 |
B | HIS172 |
B | HIS176 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | HIS202 |
B | CYS182 |
B | THR184 |
B | CYS185 |
B | HIS198 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 503 |
Chain | Residue |
B | CYS210 |
B | CYS213 |
B | HIS226 |
B | HIS230 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 504 |
Chain | Residue |
B | CYS238 |
B | CYS241 |
B | HIS254 |
B | CYS259 |
Functional Information from PROSITE/UniProt
site_id | PS00028 |
Number of Residues | 21 |
Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cky..CnkeYlslgalkmHirs..H |
Chain | Residue | Details |
B | CYS156-HIS176 | |
B | CYS180-HIS202 | |
B | CYS210-HIS230 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 80 |
Details | Domain: {"description":"Importin N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00115","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | Repeat: {"description":"HEAT 2","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 38 |
Details | Repeat: {"description":"HEAT 3","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 31 |
Details | Repeat: {"description":"HEAT 4","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 32 |
Details | Repeat: {"description":"HEAT 5","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 35 |
Details | Repeat: {"description":"HEAT 6","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 49 |
Details | Repeat: {"description":"HEAT 7","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 46 |
Details | Repeat: {"description":"HEAT 8","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 30 |
Details | Repeat: {"description":"HEAT 9","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 36 |
Details | Repeat: {"description":"HEAT 10","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 36 |
Details | Repeat: {"description":"HEAT 11","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 37 |
Details | Repeat: {"description":"HEAT 12","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 48 |
Details | Repeat: {"description":"HEAT 13","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 39 |
Details | Repeat: {"description":"HEAT 14","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 37 |
Details | Repeat: {"description":"HEAT 15","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 38 |
Details | Repeat: {"description":"HEAT 16","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 44 |
Details | Repeat: {"description":"HEAT 17","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 43 |
Details | Repeat: {"description":"HEAT 18","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 42 |
Details | Repeat: {"description":"HEAT 19","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 176 |
Details | Region: {"description":"Essential for high affinity interaction with RPL23A","evidences":[{"source":"PubMed","id":"9687515","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 13 |
Details | Region: {"description":"IAB-binding"} |
Chain | Residue | Details |
site_id | SWS_FT_FI22 |
Number of Residues | 85 |
Details | Region: {"description":"Ran-GTP binding"} |
Chain | Residue | Details |
site_id | SWS_FT_FI23 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI24 |
Number of Residues | 22 |
Details | Zinc finger: {"description":"C2H2-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI25 |
Number of Residues | 24 |
Details | Zinc finger: {"description":"C2H2-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI26 |
Number of Residues | 22 |
Details | Zinc finger: {"description":"C2H2-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI27 |
Number of Residues | 23 |
Details | Zinc finger: {"description":"C2H2-type 4; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI28 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by LATS2","evidences":[{"source":"PubMed","id":"21952048","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI29 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by PAK1","evidences":[{"source":"PubMed","id":"15833848","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |