1MCX
STRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001786 | molecular_function | phosphatidylserine binding |
A | 0001891 | cellular_component | phagocytic cup |
A | 0002250 | biological_process | adaptive immune response |
A | 0002548 | biological_process | monocyte chemotaxis |
A | 0002685 | biological_process | regulation of leukocyte migration |
A | 0004859 | molecular_function | phospholipase inhibitor activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005544 | molecular_function | calcium-dependent phospholipid binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005768 | cellular_component | endosome |
A | 0005769 | cellular_component | early endosome |
A | 0005886 | cellular_component | plasma membrane |
A | 0005929 | cellular_component | cilium |
A | 0006909 | biological_process | phagocytosis |
A | 0006954 | biological_process | inflammatory response |
A | 0007165 | biological_process | signal transduction |
A | 0007187 | biological_process | G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger |
A | 0008360 | biological_process | regulation of cell shape |
A | 0012506 | cellular_component | vesicle membrane |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0016328 | cellular_component | lateral plasma membrane |
A | 0019834 | molecular_function | phospholipase A2 inhibitor activity |
A | 0030036 | biological_process | actin cytoskeleton organization |
A | 0030659 | cellular_component | cytoplasmic vesicle membrane |
A | 0031514 | cellular_component | motile cilium |
A | 0031901 | cellular_component | early endosome membrane |
A | 0032652 | biological_process | regulation of interleukin-1 production |
A | 0032743 | biological_process | positive regulation of interleukin-2 production |
A | 0042102 | biological_process | positive regulation of T cell proliferation |
A | 0042119 | biological_process | neutrophil activation |
A | 0045087 | biological_process | innate immune response |
A | 0045627 | biological_process | positive regulation of T-helper 1 cell differentiation |
A | 0045629 | biological_process | negative regulation of T-helper 2 cell differentiation |
A | 0045920 | biological_process | negative regulation of exocytosis |
A | 0046872 | molecular_function | metal ion binding |
A | 0046883 | biological_process | regulation of hormone secretion |
A | 0050727 | biological_process | regulation of inflammatory response |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071385 | biological_process | cellular response to glucocorticoid stimulus |
A | 0071621 | biological_process | granulocyte chemotaxis |
A | 0090303 | biological_process | positive regulation of wound healing |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 347 |
Chain | Residue |
A | GLY59 |
A | VAL60 |
A | GLU62 |
A | HOH355 |
A | HOH356 |
A | HOH656 |
A | HOH657 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 348 |
Chain | Residue |
A | GLU105 |
A | ASP196 |
A | HOH357 |
A | HOH358 |
A | HOH658 |
A | LYS97 |
A | LEU100 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 349 |
Chain | Residue |
A | MET127 |
A | GLY129 |
A | GLY131 |
A | ASP171 |
A | HOH359 |
A | HOH404 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 350 |
Chain | Residue |
A | THR132 |
A | GLU134 |
A | HOH360 |
A | HOH361 |
A | HOH362 |
A | HOH385 |
A | HOH560 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 351 |
Chain | Residue |
A | GLY210 |
A | ARG213 |
A | GLY215 |
A | GLU255 |
A | HOH363 |
A | HOH644 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 352 |
Chain | Residue |
A | MET286 |
A | GLY288 |
A | GLY290 |
A | GLU330 |
A | HOH364 |
A | HOH365 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 353 |
Chain | Residue |
A | LEU328 |
A | THR331 |
A | GLU336 |
A | HOH366 |
A | HOH367 |
A | HOH492 |
A | HOH531 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 354 |
Chain | Residue |
A | ASP253 |
A | LEU256 |
A | GLU261 |
A | HOH368 |
A | HOH588 |
A | HOH660 |
Functional Information from PROSITE/UniProt
site_id | PS00223 |
Number of Residues | 53 |
Details | ANNEXIN_1 Annexin repeat signature. GVdeatiieiLtkRtnaQrqQikaaYlqekgkpLdeaLkkaltGhleevAlaL |
Chain | Residue | Details |
A | GLY59-LEU111 | |
A | GLY131-LEU183 | |
A | GLY215-VAL267 | |
A | GLY290-LEU342 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 26 |
Details | BINDING: BINDING => ECO:0007744|PDB:1MCX |
Chain | Residue | Details |
A | GLY59 | |
A | THR132 | |
A | GLU134 | |
A | ASP171 | |
A | GLY210 | |
A | ARG213 | |
A | GLY215 | |
A | ASP253 | |
A | GLU255 | |
A | LEU256 | |
A | GLU261 | |
A | VAL60 | |
A | MET286 | |
A | GLY288 | |
A | GLY290 | |
A | LEU328 | |
A | GLU330 | |
A | THR331 | |
A | GLU336 | |
A | GLU62 | |
A | LYS97 | |
A | LEU100 | |
A | GLU105 | |
A | MET127 | |
A | GLY129 | |
A | GLY131 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by CTSG => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | LYS26 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by TRPM7 => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | SER5 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:3020049 |
Chain | Residue | Details |
A | TYR21 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | SER34 | |
A | SER37 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | THR41 | |
A | THR136 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10107 |
Chain | Residue | Details |
A | LYS58 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | LYS239 | |
A | LYS312 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CROSSLNK: Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250 |
Chain | Residue | Details |
A | GLN19 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | LYS332 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04083 |
Chain | Residue | Details |
A | LYS214 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P10107 |
Chain | Residue | Details |
A | LYS257 |