6ASY
BiP-ATP2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0006457 | biological_process | protein folding |
| A | 0008180 | cellular_component | COP9 signalosome |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0021589 | biological_process | cerebellum structural organization |
| A | 0021680 | biological_process | cerebellar Purkinje cell layer development |
| A | 0021762 | biological_process | substantia nigra development |
| A | 0030291 | molecular_function | protein serine/threonine kinase inhibitor activity |
| A | 0030335 | biological_process | positive regulation of cell migration |
| A | 0030496 | cellular_component | midbody |
| A | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| A | 0031072 | molecular_function | heat shock protein binding |
| A | 0031204 | biological_process | post-translational protein targeting to membrane, translocation |
| A | 0031333 | biological_process | negative regulation of protein-containing complex assembly |
| A | 0031398 | biological_process | positive regulation of protein ubiquitination |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034663 | cellular_component | endoplasmic reticulum chaperone complex |
| A | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| A | 0034976 | biological_process | response to endoplasmic reticulum stress |
| A | 0035437 | biological_process | maintenance of protein localization in endoplasmic reticulum |
| A | 0036498 | biological_process | IRE1-mediated unfolded protein response |
| A | 0036503 | biological_process | ERAD pathway |
| A | 0042026 | biological_process | protein refolding |
| A | 0042149 | biological_process | cellular response to glucose starvation |
| A | 0042470 | cellular_component | melanosome |
| A | 0043022 | molecular_function | ribosome binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0044183 | molecular_function | protein folding chaperone |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0051603 | biological_process | obsolete proteolysis involved in protein catabolic process |
| A | 0051787 | molecular_function | misfolded protein binding |
| A | 0060904 | biological_process | regulation of protein folding in endoplasmic reticulum |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0140311 | molecular_function | protein sequestering activity |
| A | 1903891 | biological_process | regulation of ATF6-mediated unfolded protein response |
| A | 1903894 | biological_process | regulation of IRE1-mediated unfolded protein response |
| A | 1903895 | biological_process | negative regulation of IRE1-mediated unfolded protein response |
| A | 1903897 | biological_process | regulation of PERK-mediated unfolded protein response |
| A | 1903898 | biological_process | negative regulation of PERK-mediated unfolded protein response |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005925 | cellular_component | focal adhesion |
| B | 0006457 | biological_process | protein folding |
| B | 0008180 | cellular_component | COP9 signalosome |
| B | 0009986 | cellular_component | cell surface |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0021589 | biological_process | cerebellum structural organization |
| B | 0021680 | biological_process | cerebellar Purkinje cell layer development |
| B | 0021762 | biological_process | substantia nigra development |
| B | 0030291 | molecular_function | protein serine/threonine kinase inhibitor activity |
| B | 0030335 | biological_process | positive regulation of cell migration |
| B | 0030496 | cellular_component | midbody |
| B | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
| B | 0031072 | molecular_function | heat shock protein binding |
| B | 0031204 | biological_process | post-translational protein targeting to membrane, translocation |
| B | 0031333 | biological_process | negative regulation of protein-containing complex assembly |
| B | 0031398 | biological_process | positive regulation of protein ubiquitination |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034663 | cellular_component | endoplasmic reticulum chaperone complex |
| B | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| B | 0034976 | biological_process | response to endoplasmic reticulum stress |
| B | 0035437 | biological_process | maintenance of protein localization in endoplasmic reticulum |
| B | 0036498 | biological_process | IRE1-mediated unfolded protein response |
| B | 0036503 | biological_process | ERAD pathway |
| B | 0042026 | biological_process | protein refolding |
| B | 0042149 | biological_process | cellular response to glucose starvation |
| B | 0042470 | cellular_component | melanosome |
| B | 0043022 | molecular_function | ribosome binding |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0051603 | biological_process | obsolete proteolysis involved in protein catabolic process |
| B | 0051787 | molecular_function | misfolded protein binding |
| B | 0060904 | biological_process | regulation of protein folding in endoplasmic reticulum |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0140311 | molecular_function | protein sequestering activity |
| B | 1903891 | biological_process | regulation of ATF6-mediated unfolded protein response |
| B | 1903894 | biological_process | regulation of IRE1-mediated unfolded protein response |
| B | 1903895 | biological_process | negative regulation of IRE1-mediated unfolded protein response |
| B | 1903897 | biological_process | regulation of PERK-mediated unfolded protein response |
| B | 1903898 | biological_process | negative regulation of PERK-mediated unfolded protein response |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 701 |
| Chain | Residue |
| A | LYS353 |
| A | ASN380 |
| A | HOH1216 |
| B | GLY430 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 702 |
| Chain | Residue |
| A | HOH951 |
| A | GLY58 |
| A | ASN59 |
| A | ARG60 |
| A | ILE61 |
| A | HOH812 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 703 |
| Chain | Residue |
| A | GLU358 |
| A | SER385 |
| A | ARG386 |
| B | ARG49 |
| B | VAL50 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 704 |
| Chain | Residue |
| A | GLU73 |
| A | ARG558 |
| B | LYS512 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 705 |
| Chain | Residue |
| A | LYS340 |
| A | GLN343 |
| A | HOH844 |
| A | HOH1004 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | binding site for residue ATP A 706 |
| Chain | Residue |
| A | GLY36 |
| A | THR37 |
| A | THR38 |
| A | TYR39 |
| A | LYS96 |
| A | GLU201 |
| A | GLY226 |
| A | GLY227 |
| A | GLY228 |
| A | THR229 |
| A | GLY255 |
| A | GLU293 |
| A | LYS296 |
| A | ARG297 |
| A | SER300 |
| A | GLY363 |
| A | GLY364 |
| A | SER365 |
| A | ARG367 |
| A | ILE368 |
| A | HOH815 |
| A | HOH841 |
| A | HOH871 |
| A | HOH882 |
| A | HOH939 |
| A | HOH1098 |
| A | HOH1137 |
| A | HOH1231 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 707 |
| Chain | Residue |
| A | ARG386 |
| A | GLY387 |
| A | HOH849 |
| A | HOH892 |
| B | ARG60 |
| B | ASN389 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 708 |
| Chain | Residue |
| A | HIS265 |
| A | LYS326 |
| A | LEU330 |
| A | HOH964 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 709 |
| Chain | Residue |
| A | LYS276 |
| A | LYS280 |
| A | TYR313 |
| A | GLU314 |
| A | HOH823 |
| A | HOH827 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 710 |
| Chain | Residue |
| A | GLN302 |
| A | HIS303 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 711 |
| Chain | Residue |
| A | ASP111 |
| A | GLU256 |
| A | ASP257 |
| A | HOH802 |
| A | HOH885 |
| A | HOH1100 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 712 |
| Chain | Residue |
| A | LYS344 |
| A | HOH828 |
| A | HOH837 |
| A | HOH850 |
| B | ARG466 |
| B | ASP471 |
| B | HOH1032 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 713 |
| Chain | Residue |
| A | ARG466 |
| A | ASP471 |
| A | HOH819 |
| A | HOH860 |
| A | HOH1177 |
| B | LYS344 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 714 |
| Chain | Residue |
| A | GLN182 |
| A | LYS185 |
| A | HOH830 |
| A | HOH918 |
| A | HOH953 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 A 715 |
| Chain | Residue |
| A | HOH1015 |
| B | GLU89 |
| A | GLU25 |
| A | VAL27 |
| A | HIS167 |
| A | ASN194 |
| A | MET196 |
| A | HOH986 |
| A | HOH990 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 716 |
| Chain | Residue |
| A | GLY387 |
| A | ILE388 |
| A | ASN389 |
| B | SO4705 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 701 |
| Chain | Residue |
| B | GLY58 |
| B | ASN59 |
| B | ARG60 |
| B | ILE61 |
| B | HOH860 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 702 |
| Chain | Residue |
| A | LYS512 |
| B | GLU73 |
| B | ARG558 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 703 |
| Chain | Residue |
| A | GLY430 |
| B | LYS353 |
| B | ASN380 |
| site_id | AE2 |
| Number of Residues | 28 |
| Details | binding site for residue ATP B 704 |
| Chain | Residue |
| B | GLY36 |
| B | THR37 |
| B | THR38 |
| B | TYR39 |
| B | LYS96 |
| B | GLU201 |
| B | GLY226 |
| B | GLY227 |
| B | GLY228 |
| B | THR229 |
| B | GLY255 |
| B | GLU293 |
| B | LYS296 |
| B | ARG297 |
| B | SER300 |
| B | GLY363 |
| B | GLY364 |
| B | SER365 |
| B | ARG367 |
| B | ILE368 |
| B | ASP391 |
| B | HOH803 |
| B | HOH841 |
| B | HOH899 |
| B | HOH900 |
| B | HOH944 |
| B | HOH1017 |
| B | HOH1169 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 705 |
| Chain | Residue |
| A | ARG60 |
| A | ASN389 |
| A | PO4716 |
| B | ARG386 |
| B | GLY387 |
| B | HOH947 |
| B | HOH970 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 706 |
| Chain | Residue |
| B | LYS280 |
| B | TYR313 |
| B | GLU314 |
| B | HOH806 |
| B | HOH810 |
| B | HOH836 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 707 |
| Chain | Residue |
| B | GLN302 |
| B | HIS303 |
| B | HOH824 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 708 |
| Chain | Residue |
| B | HIS265 |
| B | LYS326 |
| B | HOH1059 |
| B | HOH1140 |
| B | HOH1206 |
| B | HOH1222 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 709 |
| Chain | Residue |
| B | GLU256 |
| B | ASP257 |
| B | HOH927 |
| site_id | AE8 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 B 710 |
| Chain | Residue |
| A | GLU89 |
| B | GLU25 |
| B | VAL27 |
| B | HIS167 |
| B | ASN194 |
| B | HOH864 |
| B | HOH874 |
| B | HOH975 |
| B | HOH1024 |
| B | HOH1156 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 711 |
| Chain | Residue |
| B | GLN182 |
| B | LYS185 |
| B | HOH823 |
| B | HOH926 |
| B | HOH1075 |
| B | HOH1224 |
| site_id | AF1 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 712 |
| Chain | Residue |
| A | ARG49 |
| A | HOH861 |
| B | GLU358 |
| B | SER385 |
| B | ARG386 |
| B | HOH954 |
| B | HOH1159 |
Functional Information from PROSITE/UniProt
| site_id | PS00297 |
| Number of Residues | 8 |
| Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
| Chain | Residue | Details |
| A | ILE33-SER40 |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL |
| Chain | Residue | Details |
| A | VAL222-LEU235 |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ |
| Chain | Residue | Details |
| A | ILE359-GLN373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 310 |
| Details | Region: {"description":"Nucleotide-binding (NBD)","evidences":[{"source":"PubMed","id":"28286085","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Region: {"description":"Interdomain linker","evidences":[{"source":"UniProtKB","id":"G3I8R9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21526763","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06761","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DMV8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P0DMV8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; alternate","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
