4ABN
Crystal structure of full length mouse Strap (TTC5)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009267 | biological_process | cellular response to starvation |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0043022 | molecular_function | ribosome binding |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0061014 | biological_process | positive regulation of mRNA catabolic process |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003682 | molecular_function | chromatin binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009267 | biological_process | cellular response to starvation |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0043022 | molecular_function | ribosome binding |
| B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| B | 0061014 | biological_process | positive regulation of mRNA catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1433 |
| Chain | Residue |
| A | SER208 |
| A | GLN212 |
| A | EDO1434 |
| A | HOH2068 |
| A | HOH2138 |
| A | HOH2142 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1434 |
| Chain | Residue |
| A | LYS115 |
| A | LYS116 |
| A | EDO1433 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | SITE: Mediates interaction with N-terminal MREI motif of beta-tubulin nascent chain => ECO:0000250|UniProtKB:Q8N0Z6 |
| Chain | Residue | Details |
| A | ARG147 | |
| A | ASP225 | |
| A | GLU259 | |
| B | ARG147 | |
| B | ASP225 | |
| B | GLU259 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by ATM => ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:22362889 |
| Chain | Residue | Details |
| A | SER203 | |
| B | SER203 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CHEK2 => ECO:0000269|PubMed:18833288, ECO:0000269|PubMed:22362889 |
| Chain | Residue | Details |
| A | SER221 | |
| B | SER221 |
