6GHM
Structure of PP1 alpha phosphatase bound to ASPP2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000164 | cellular_component | protein phosphatase type 1 complex |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0001111 | biological_process | RNA polymerase II promoter clearance |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0005912 | cellular_component | adherens junction |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0005979 | biological_process | regulation of glycogen biosynthetic process |
| A | 0005981 | biological_process | regulation of glycogen catabolic process |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0008157 | molecular_function | protein phosphatase 1 binding |
| A | 0010288 | biological_process | response to lead ion |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0032922 | biological_process | circadian regulation of gene expression |
| A | 0032968 | biological_process | positive regulation of transcription elongation by RNA polymerase II |
| A | 0034244 | biological_process | negative regulation of transcription elongation by RNA polymerase II |
| A | 0042587 | cellular_component | glycogen granule |
| A | 0042752 | biological_process | regulation of circadian rhythm |
| A | 0043021 | molecular_function | ribonucleoprotein complex binding |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0043153 | biological_process | entrainment of circadian clock by photoperiod |
| A | 0043197 | cellular_component | dendritic spine |
| A | 0043204 | cellular_component | perikaryon |
| A | 0043247 | biological_process | telomere maintenance in response to DNA damage |
| A | 0043558 | biological_process | regulation of translational initiation in response to stress |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0045725 | biological_process | positive regulation of glycogen biosynthetic process |
| A | 0046579 | biological_process | positive regulation of Ras protein signal transduction |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| A | 0050821 | biological_process | protein stabilization |
| A | 0051301 | biological_process | cell division |
| A | 0060828 | biological_process | regulation of canonical Wnt signaling pathway |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072357 | cellular_component | PTW/PP1 phosphatase complex |
| A | 0098609 | biological_process | cell-cell adhesion |
| A | 0098641 | molecular_function | cadherin binding involved in cell-cell adhesion |
| A | 0098793 | cellular_component | presynapse |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0180007 | molecular_function | RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity |
| A | 2000806 | biological_process | positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled |
| B | 0000164 | cellular_component | protein phosphatase type 1 complex |
| B | 0000781 | cellular_component | chromosome, telomeric region |
| B | 0001111 | biological_process | RNA polymerase II promoter clearance |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0005912 | cellular_component | adherens junction |
| B | 0005977 | biological_process | glycogen metabolic process |
| B | 0005979 | biological_process | regulation of glycogen biosynthetic process |
| B | 0005981 | biological_process | regulation of glycogen catabolic process |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0008157 | molecular_function | protein phosphatase 1 binding |
| B | 0010288 | biological_process | response to lead ion |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0032922 | biological_process | circadian regulation of gene expression |
| B | 0032968 | biological_process | positive regulation of transcription elongation by RNA polymerase II |
| B | 0034244 | biological_process | negative regulation of transcription elongation by RNA polymerase II |
| B | 0042587 | cellular_component | glycogen granule |
| B | 0042752 | biological_process | regulation of circadian rhythm |
| B | 0043021 | molecular_function | ribonucleoprotein complex binding |
| B | 0043025 | cellular_component | neuronal cell body |
| B | 0043153 | biological_process | entrainment of circadian clock by photoperiod |
| B | 0043197 | cellular_component | dendritic spine |
| B | 0043204 | cellular_component | perikaryon |
| B | 0043247 | biological_process | telomere maintenance in response to DNA damage |
| B | 0043558 | biological_process | regulation of translational initiation in response to stress |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0045725 | biological_process | positive regulation of glycogen biosynthetic process |
| B | 0046579 | biological_process | positive regulation of Ras protein signal transduction |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046914 | molecular_function | transition metal ion binding |
| B | 0050821 | biological_process | protein stabilization |
| B | 0051301 | biological_process | cell division |
| B | 0060828 | biological_process | regulation of canonical Wnt signaling pathway |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072357 | cellular_component | PTW/PP1 phosphatase complex |
| B | 0098609 | biological_process | cell-cell adhesion |
| B | 0098641 | molecular_function | cadherin binding involved in cell-cell adhesion |
| B | 0098793 | cellular_component | presynapse |
| B | 0098794 | cellular_component | postsynapse |
| B | 0098978 | cellular_component | glutamatergic synapse |
| B | 0180007 | molecular_function | RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity |
| B | 2000806 | biological_process | positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled |
| C | 0002039 | molecular_function | p53 binding |
| C | 0042981 | biological_process | regulation of apoptotic process |
| D | 0002039 | molecular_function | p53 binding |
| D | 0042981 | biological_process | regulation of apoptotic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | ASP208 |
| A | GLU218 |
| A | ASN219 |
| A | ASP220 |
| A | THR226 |
| A | GLN249 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | ASP10 |
| B | PRO82 |
| B | GLU84 |
| B | HOH502 |
| A | LEU7 |
| A | ASN8 |
| A | LEU9 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | SER177 |
| A | LEU180 |
| A | PHE235 |
| A | HOH527 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLU54 |
| A | GLU116 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | GLN249 |
| A | GLU256 |
| A | HOH526 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | GLY67 |
| A | GLN68 |
| A | TYR69 |
| A | TYR70 |
| A | GLY97 |
| A | LYS98 |
| A | GLN99 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | ASP253 |
| A | TYR255 |
| A | GLU256 |
| A | PHE257 |
| D | ASP932 |
| D | HOH1301 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 408 |
| Chain | Residue |
| A | GLU56 |
| A | ALA57 |
| A | ASP166 |
| A | GLU287 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 409 |
| Chain | Residue |
| A | ILE130 |
| A | TYR134 |
| A | ARG221 |
| B | PRO178 |
| B | ASP179 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue NHE A 410 |
| Chain | Residue |
| A | SER129 |
| A | ILE130 |
| A | VAL195 |
| A | PRO196 |
| A | ASP197 |
| A | TRP206 |
| A | HOH506 |
| B | GLN181 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for residue NHE A 411 |
| Chain | Residue |
| A | HIS66 |
| A | ASP92 |
| A | ARG96 |
| A | ASN124 |
| A | HIS125 |
| A | ARG221 |
| A | HIS248 |
| A | GLN249 |
| A | VAL250 |
| A | MN412 |
| A | MN413 |
| A | HOH501 |
| A | HOH551 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 412 |
| Chain | Residue |
| A | ASP64 |
| A | HIS66 |
| A | ASP92 |
| A | NHE411 |
| A | MN413 |
| A | HOH501 |
| A | HOH551 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 413 |
| Chain | Residue |
| A | ASP92 |
| A | ASN124 |
| A | HIS173 |
| A | HIS248 |
| A | NHE411 |
| A | MN412 |
| A | HOH501 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| B | LYS41 |
| B | GLU44 |
| B | ILE45 |
| B | SER48 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | LEU47 |
| B | MET190 |
| B | ARG191 |
| B | HOH519 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | GLN249 |
| B | GLU256 |
| B | PHE257 |
| B | HOH528 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | ASP253 |
| B | TYR255 |
| B | GLU256 |
| B | PHE257 |
| C | HOH1201 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| A | GLY215 |
| A | TRP216 |
| B | SER129 |
| site_id | AE1 |
| Number of Residues | 14 |
| Details | binding site for residue NHE B 406 |
| Chain | Residue |
| B | HIS66 |
| B | ASP92 |
| B | ARG96 |
| B | ASN124 |
| B | HIS125 |
| B | ARG221 |
| B | HIS248 |
| B | GLN249 |
| B | VAL250 |
| B | TYR272 |
| B | MN409 |
| B | MN410 |
| B | HOH511 |
| B | HOH538 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue NHE B 407 |
| Chain | Residue |
| A | LYS234 |
| B | SER129 |
| B | VAL195 |
| B | PRO196 |
| B | ASP197 |
| B | TRP206 |
| B | HOH540 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue NHE B 408 |
| Chain | Residue |
| B | ASP242 |
| B | LYS260 |
| B | ARG261 |
| C | VAL922 |
| C | PHE924 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 409 |
| Chain | Residue |
| B | ASP64 |
| B | HIS66 |
| B | ASP92 |
| B | NHE406 |
| B | MN410 |
| B | HOH511 |
| B | HOH538 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 410 |
| Chain | Residue |
| B | ASP92 |
| B | ASN124 |
| B | HIS173 |
| B | HIS248 |
| B | NHE406 |
| B | MN409 |
| B | HOH511 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 1201 |
| Chain | Residue |
| D | ASN1058 |
| D | VAL1061 |
| D | TYR1063 |
| D | LEU1116 |
| D | TYR1117 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 1202 |
| Chain | Residue |
| D | CYS1002 |
| D | ASN1003 |
| D | ASN1004 |
| D | GLU1038 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue NHE D 1203 |
| Chain | Residue |
| A | LYS150 |
| D | GLY1055 |
| D | ILE1056 |
| D | ILE1086 |
| D | ILE1087 |
| D | HIS1088 |
Functional Information from PROSITE/UniProt
| site_id | PS00125 |
| Number of Residues | 6 |
| Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
| Chain | Residue | Details |
| A | LEU121-GLU126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P36873","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30100357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35830882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35831509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36175670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39446389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SW5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16732323","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 62 |
| Details | Repeat: {"description":"ANK 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 64 |
| Details | Repeat: {"description":"ANK 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"ANK 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 84 |
| Details | Repeat: {"description":"ANK 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 124 |
| Details | Domain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
