| IED ID | IndEnz0002007445 |
| Enzyme Type ID | protease007445 |
| Protein Name |
Cellular tumor antigen p53 Antigen NY-CO-13 Phosphoprotein p53 Tumor suppressor p53 |
| Gene Name | TP53 P53 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD |
| Enzyme Length | 393 |
| Uniprot Accession Number | P04637 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 102..292 |
| EC Number | |
| Enzyme Function | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:9840937}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (6); Beta strand (19); Chain (1); Compositional bias (4); Cross-link (4); DNA binding (1); Helix (13); Metal binding (4); Modified residue (28); Motif (5); Mutagenesis (34); Natural variant (1363); Region (19); Site (1); Turn (7) |
| Keywords | 3D-structure;Acetylation;Activator;Alternative promoter usage;Alternative splicing;Apoptosis;Biological rhythms;Cell cycle;Cytoplasm;Cytoskeleton;DNA-binding;Direct protein sequencing;Disease variant;Endoplasmic reticulum;Glycoprotein;Host-virus interaction;Isopeptide bond;Li-Fraumeni syndrome;Metal-binding;Methylation;Mitochondrion;Necrosis;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Tumor suppressor;Ubl conjugation;Zinc |
| Interact With | Q13155; O95376; P49407; Q9UBL3; O95352-2; O15169; Q8N9N5; P10415; Q07817-1; O14503; P51587; Q9NPI1; Q9BX70; Q9Y297; P55212; Q9BWC9; P17676; Q92793; P55060; Q14999; Q8IWT3; Q9P0U4; Q9UER7; Q92841; P17844; Q9NRR4; Q9BV47; O14641; Q09472; P15036; Q86XK2; P21333-2; P51114; P49841; P32780; Q13547; Q86Z02; P09429; P61978; P61978-2; P38646; P04792; P42858; Q7Z6Z7; Q16666-2; O14920; Q9UHH9; Q6NYC1; Q92993; Q9H7Z6; O60341-1; Q8IZD2; P13473-2; P43356; Q96M61; Q9UBF1; P46821; Q15759; Q8IW41; Q00987; O15151; Q9UHC7; O75970; P04731; P19338; Q9Y618; P23511; P25208; Q9Y3T9; O60936; P06748; P06748-1; Q15466; P22736; O43847; O60285; P49757; Q96FW1; Q8TEW0; P09874; Q96KB5; Q7Z412; P35232; O75925; Q8N2W9; Q92569; Q13526; P53350; P29590; D3DTS7; P30405; P36873-1; Q8WUF5; P30153; Q13362; Q05655; P61289; Q05397; Q06609; Q06330; Q96PM5; Q6PCD5; Q06587; P23396; Q9Y265; Q8N488; P23297; P31949; P29034; P33764; P26447; P33763; P06703; P04271; P25815; Q15424; Q8WTS6; P31947; Q96ST3; Q96EB6; Q15796; Q9NRG4; O95863; Q06945; P08047; Q12772; Q96SB4; P31948; P63165; Q86TM6; P20226; P15884; Q96GM8; Itself; Q12888; Q12888-1; Q13625; Q9H3D4; P13693; O15164; Q15672; P0CG48; P63279; Q05086; P09936; Q96PU4; Q9H9J4; Q9H9J4-2; Q93009; P11473; Q99986; Q14191; Q9NZC7; O14980; P12956; P61981; P63104; Q8TAQ5; Q7L7W2; P29066; Q9ESJ1; P45481; P03126; P06463; P02829; Q08619; P89055; Q923E4; Q8R5A0; P32776; O88898; P26687; Q9PST7; P03070; P26663; Q8QW27; P17844; P17844 |
| Induction | INDUCTION: Up-regulated in response to DNA damage. Isoform 2 is not induced in tumor cells in response to stress. {ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:16131611}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:22726440}. Nucleus {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:21597459}. Nucleus, PML body {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12810724}. Endoplasmic reticulum {ECO:0000269|PubMed:17170702}. Mitochondrion matrix {ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:27323408}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28842590}. Note=Recruited into PML bodies together with CHEK2 (PubMed:12810724). Translocates to mitochondria upon oxidative stress (PubMed:22726440). Translocates to mitochondria in response to mitomycin C treatment (PubMed:27323408). {ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:27323408}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23752197}. Cytoplasm. Note=Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Note=Localized mainly in the nucleus with minor staining in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Note=Localized in the nucleus in most cells but found in the cytoplasm in some cells.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus. Cytoplasm. Note=Predominantly nuclear but translocates to the cytoplasm following cell stress.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus. Cytoplasm. Note=Localized mainly in the nucleus with minor staining in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 8]: Nucleus. Cytoplasm. Note=Localized in both nucleus and cytoplasm in most cells. In some cells, forms foci in the nucleus that are different from nucleoli.; SUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm. |
| Modified Residue | MOD_RES 9; /note="Phosphoserine; by HIPK4"; /evidence="ECO:0000269|PubMed:18022393"; MOD_RES 15; /note="Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM"; /evidence="ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:28842590"; MOD_RES 18; /note="Phosphothreonine; by CK1, VRK1 and VRK2"; /evidence="ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422"; MOD_RES 20; /note="Phosphoserine; by CHEK2, CK1 and PLK3"; /evidence="ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275"; MOD_RES 33; /note="Phosphoserine; by CDK5 and CDK7"; /evidence="ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:9372954"; MOD_RES 37; /note="Phosphoserine; by MAPKAPK5"; /evidence="ECO:0000269|PubMed:17254968"; MOD_RES 46; /note="Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG"; /evidence="ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690"; MOD_RES 55; /note="Phosphothreonine; by TAF1 and GRK5"; /evidence="ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:20124405"; MOD_RES 120; /note="N6-acetyllysine; by KAT6A"; /evidence="ECO:0000269|PubMed:23431171"; MOD_RES 183; /note="Phosphoserine; by AURKB"; /evidence="ECO:0000269|PubMed:20959462"; MOD_RES 269; /note="Phosphoserine; by AURKB"; /evidence="ECO:0000269|PubMed:20959462"; MOD_RES 284; /note="Phosphothreonine; by AURKB"; /evidence="ECO:0000269|PubMed:20959462"; MOD_RES 305; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:12724314"; MOD_RES 315; /note="Phosphoserine; by AURKA, CDK1 and CDK2"; /evidence="ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:14702041"; MOD_RES 321; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P02340"; MOD_RES 333; /note="Omega-N-methylarginine; by PRMT5"; /evidence="ECO:0000269|PubMed:19011621"; MOD_RES 335; /note="Symmetric dimethylarginine; by PRMT5"; /evidence="ECO:0000269|PubMed:19011621"; MOD_RES 337; /note="Symmetric dimethylarginine; by PRMT5"; /evidence="ECO:0000269|PubMed:19011621"; MOD_RES 370; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:22864287"; MOD_RES 370; /note="N6-methyllysine; by SMYD2; alternate"; /evidence="ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:22864287"; MOD_RES 372; /note="N6-methyllysine; by SETD7"; /evidence="ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16415881"; MOD_RES 373; /note="N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate"; /evidence="ECO:0000269|PubMed:20118233"; MOD_RES 373; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:10656795"; MOD_RES 381; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 382; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287"; MOD_RES 382; /note="N6-acetyllysine; by KAT6A; alternate"; /evidence="ECO:0000269|PubMed:10656795, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:23431171, ECO:0007744|PubMed:19608861"; MOD_RES 382; /note="N6-methyllysine; by KMT5A; alternate"; /evidence="ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287"; MOD_RES 392; /note="Phosphoserine; by CK2, CDK2 and NUAK1"; /evidence="ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:22214662" |
| Post Translational Modification | PTM: Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Acetylation of Lys-382 by EP300. Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner. {ECO:0000269|PubMed:10656795, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:23431171}.; PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 (By similarity). Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was initially thought to be mediated by STK11/LKB1 but it was later shown that it is indirect and that STK11/LKB1-dependent phosphorylation is probably mediated by downstream NUAK1 (PubMed:21317932). It is unclear whether AMP directly mediates phosphorylation at Ser-15. Phosphorylated on Thr-18 by isoform 1 and isoform 2 of VRK2. Phosphorylation on Thr-18 by isoform 2 of VRK2 results in a reduction in ubiquitination by MDM2 and an increase in acetylation by EP300. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage. Phosphorylation at Ser-15 is required for interaction with DDX3X and gamma-tubulin (PubMed:28842590). {ECO:0000250, ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11546806, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:16377624, ECO:0000269|PubMed:16704422, ECO:0000269|PubMed:1705009, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:18022393, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:2141171, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:9372954}.; PTM: Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.; PTM: May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line. {ECO:0000269|PubMed:8632915}.; PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation (PubMed:10722742, PubMed:12810724, PubMed:15340061, PubMed:17170702, PubMed:19880522). Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome (PubMed:10722742, PubMed:12810724, PubMed:20173098). Ubiquitinated by MKRN1 at Lys-291 and Lys-292, which leads to proteasomal degradation (PubMed:19536131). Deubiquitinated by USP10, leading to its stabilization (PubMed:20096447). Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation (PubMed:19556538). Ubiquitination by TOPORS induces degradation (PubMed:19473992). Deubiquitination by USP7, leading to stabilization (PubMed:15053880). Isoform 4 is monoubiquitinated in an MDM2-independent manner (PubMed:15340061). Ubiquitinated by COP1, which leads to proteasomal degradation (PubMed:19837670). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (By similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to proteasomal degradation (PubMed:21597459). {ECO:0000250|UniProtKB:P02340, ECO:0000269|PubMed:10722742, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19536131, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:25591766, ECO:0000269|PubMed:25732823}.; PTM: Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation (PubMed:15525938, PubMed:16415881). Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity (PubMed:17108971). Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370 (PubMed:17108971). Dimethylated at Lys-373 by EHMT1 and EHMT2 (PubMed:20118233). Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity (PubMed:17707234). Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20 (PubMed:22864287). Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (PubMed:17805299). Monomethylated at Arg-333 and dimethylated at Arg-335 and Arg-337 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (PubMed:19011621). {ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16415881, ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22864287}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9. {ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (30); Electron microscopy (2); X-ray crystallography (194) |
| Cross Reference PDB | 1A1U; 1AIE; 1C26; 1DT7; 1GZH; 1H26; 1HS5; 1JSP; 1KZY; 1MA3; 1OLG; 1OLH; 1PES; 1PET; 1SAE; 1SAF; 1SAK; 1SAL; 1TSR; 1TUP; 1UOL; 1XQH; 1YC5; 1YCQ; 1YCR; 1YCS; 2AC0; 2ADY; 2AHI; 2ATA; 2B3G; 2BIM; 2BIN; 2BIO; 2BIP; 2BIQ; 2F1X; 2FEJ; 2FOJ; 2FOO; 2GS0; 2H1L; 2H2D; 2H2F; 2H4F; 2H4H; 2H4J; 2H59; 2J0Z; 2J10; 2J11; 2J1W; 2J1X; 2J1Y; 2J1Z; 2J20; 2J21; 2K8F; 2L14; 2LY4; 2MEJ; 2MWO; 2MWP; 2MWY; 2MZD; 2OCJ; 2PCX; 2RUK; 2VUK; 2WGX; 2X0U; 2X0V; 2X0W; 2XWR; 2YBG; 2YDR; 2Z5S; 2Z5T; 3D05; 3D06; 3D07; 3D08; 3D09; 3D0A; 3DAB; 3DAC; 3IGK; 3IGL; 3KMD; 3KZ8; 3LW1; 3OQ5; 3PDH; 3Q01; 3Q05; 3Q06; 3SAK; 3TG5; 3TS8; 3ZME; 4AGL; 4AGM; 4AGN; 4AGO; 4AGP; 4AGQ; 4BUZ; 4BV2; 4HFZ; 4HJE; 4IBQ; 4IBS; 4IBT; 4IBU; 4IBV; 4IBW; 4IBY; 4IBZ; 4IJT; 4KVP; 4LO9; 4LOE; 4LOF; 4MZI; 4MZR; 4QO1; 4RP6; 4RP7; 4X34; 4XR8; 4ZZJ; 5A7B; 5AB9; 5ABA; 5AOI; 5AOJ; 5AOK; 5AOL; 5AOM; 5BUA; 5ECG; 5G4M; 5G4N; 5G4O; 5HOU; 5HP0; 5HPD; 5LAP; 5LGY; 5MCT; 5MCU; 5MCV; 5MCW; 5MF7; 5MG7; 5MHC; 5MOC; 5O1A; 5O1B; 5O1C; 5O1D; 5O1E; 5O1F; 5O1G; 5O1H; 5O1I; 5OL0; 5UN8; 5XZC; 6FF9; 6FJ5; 6GGA; 6GGB; 6GGC; 6GGD; 6GGE; 6GGF; 6LHD; 6R5L; 6RJZ; 6RK8; 6RKI; 6RKK; 6RKM; 6RL3; 6RL4; 6RL6; 6RM5; 6RM7; 6RWH; 6RWI; 6RWS; 6RWU; 6RX2; 6RZ3; 6S39; 6S3C; 6S40; 6S9Q; 6SHZ; 6SI0; 6SI1; 6SI2; 6SI3; 6SI4; 6SIN; 6SIO; 6SIP; 6SIQ; 6SL6; 6SLV; 6T58; 6V4F; 6V4H; 6VQO; 6VR1; 6VR5; 6VRM; 6VRN; 6W51; 6XRE; 7BWN; 7DHY; 7DHZ; 7DVD; 7EL4; |
| Mapped Pubmed ID | !!!TOLONGITDOESNOTFITINEXCELL,NOTREPRESENTABLEINEXCELL!!!; |
| Motif | MOTIF 17..25; /note=TADI; MOTIF 48..56; /note=TADII; MOTIF 305..321; /note=Bipartite nuclear localization signal; MOTIF 339..350; /note=Nuclear export signal; MOTIF 370..372; /note=[KR]-[STA]-K motif |
| Gene Encoded By | |
| Mass | 43,653 |
| Kinetics | |
| Metal Binding | METAL 176; /note=Zinc; METAL 179; /note=Zinc; METAL 238; /note=Zinc; METAL 242; /note=Zinc |
| Rhea ID | |
| Cross Reference Brenda |