6ASY
BiP-ATP2
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0006983 | biological_process | ER overload response |
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 | 0030335 | biological_process | positive regulation of cell migration |
A | 0030496 | cellular_component | midbody |
A | 0030512 | biological_process | negative regulation of transforming growth factor beta receptor signaling pathway |
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 | 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 | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
A | 0051087 | molecular_function | protein-folding chaperone binding |
A | 0051603 | biological_process | 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 | 0071353 | biological_process | cellular response to interleukin-4 |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
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 |
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 | 0006983 | biological_process | ER overload response |
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 | 0030335 | biological_process | positive regulation of cell migration |
B | 0030496 | cellular_component | midbody |
B | 0030512 | biological_process | negative regulation of transforming growth factor beta receptor signaling pathway |
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 | 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 | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
B | 0051087 | molecular_function | protein-folding chaperone binding |
B | 0051603 | biological_process | 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 | 0071353 | biological_process | cellular response to interleukin-4 |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
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 |
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 | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21526763 |
Chain | Residue | Details |
A | GLY36 | |
B | GLY364 | |
A | LYS96 | |
A | GLY227 | |
A | GLU293 | |
A | GLY364 | |
B | GLY36 | |
B | LYS96 | |
B | GLY227 | |
B | GLU293 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06761 |
Chain | Residue | Details |
A | SER86 | |
B | SER86 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P20029 |
Chain | Residue | Details |
A | LYS125 | |
A | LYS213 | |
A | LYS326 | |
B | LYS125 | |
B | LYS213 | |
B | LYS326 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 |
Chain | Residue | Details |
A | TYR160 | |
B | TYR160 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 |
Chain | Residue | Details |
A | LYS271 | |
B | LYS271 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 |
Chain | Residue | Details |
A | LYS353 | |
B | LYS353 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P20029 |
Chain | Residue | Details |
A | LYS447 | |
B | LYS447 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8 |
Chain | Residue | Details |
A | GLN492 | |
B | GLN492 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; alternate => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | ASN518 | |
B | ASN518 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | GLU585 | |
B | GLU585 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | GLU591 | |
B | GLU591 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS352 | |
B | LYS352 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 |
Chain | Residue | Details |
A | LYS353 | |
B | LYS353 |