Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000226 | biological_process | microtubule cytoskeleton organization |
A | 0000278 | biological_process | mitotic cell cycle |
A | 0005200 | molecular_function | structural constituent of cytoskeleton |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005874 | cellular_component | microtubule |
A | 0007017 | biological_process | microtubule-based process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000226 | biological_process | microtubule cytoskeleton organization |
B | 0000278 | biological_process | mitotic cell cycle |
B | 0001764 | biological_process | neuron migration |
B | 0003924 | molecular_function | GTPase activity |
B | 0005200 | molecular_function | structural constituent of cytoskeleton |
B | 0005515 | molecular_function | protein binding |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005874 | cellular_component | microtubule |
B | 0007017 | biological_process | microtubule-based process |
B | 0046872 | molecular_function | metal ion binding |
K | 0003777 | molecular_function | microtubule motor activity |
K | 0005524 | molecular_function | ATP binding |
K | 0007018 | biological_process | microtubule-based movement |
K | 0008017 | molecular_function | microtubule binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | GLN11 |
A | GTP502 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GTP A 502 |
Chain | Residue |
A | ALA180 |
A | ASN206 |
A | GLU207 |
A | ILE209 |
A | TYR210 |
A | CYS213 |
A | THR223 |
A | TYR224 |
A | ASN226 |
A | LEU227 |
A | MG501 |
B | LEU248 |
A | GLY142 |
A | GLY143 |
A | GLY144 |
A | ALA174 |
A | VAL177 |
A | SER178 |
A | THR179 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | GLN11 |
B | GLU71 |
B | THR74 |
B | G2P602 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE G2P B 602 |
Chain | Residue |
B | GLY10 |
B | GLN11 |
B | CYS12 |
B | GLN15 |
B | ASP69 |
B | GLU71 |
B | ALA99 |
B | SER140 |
B | GLY142 |
B | GLY144 |
B | THR145 |
B | ASP179 |
B | GLU183 |
B | ASN206 |
B | TYR224 |
B | LEU227 |
B | ASN228 |
B | MG601 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 K 500 |
Chain | Residue |
K | SER89 |
K | SER90 |
K | GLY91 |
K | LYS92 |
K | THR93 |
Functional Information from PROSITE/UniProt
site_id | PS00227 |
Number of Residues | 7 |
Details | TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG |
Chain | Residue | Details |
B | GLY142-GLY148 | |
A | GLY142-GLY148 | |
site_id | PS00411 |
Number of Residues | 12 |
Details | KINESIN_MOTOR_1 Kinesin motor domain signature. GKLyLVDLAGSE |
Chain | Residue | Details |
K | GLY226-GLU237 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q13885","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P56536","evidenceCode":"ECO:0000250"}]} |