Q02880 · TOP2B_HUMAN
- ProteinDNA topoisomerase 2-beta
- GeneTOP2B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1626 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 112 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 141 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 169-171 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SSN | ||||||
Binding site | 182-189 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRNGYGAK | ||||||
Binding site | 397-399 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QTK | ||||||
Binding site | 482 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 510 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 513 | Interaction with DNA | ||||
Sequence: N | ||||||
Binding site | 562 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 562 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 564 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 682 | Interaction with DNA | ||||
Sequence: R | ||||||
Site | 683 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 744 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 778 | Interaction with DNA | ||||
Sequence: Y | ||||||
Site | 825 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 826 | O-(5'-phospho-DNA)-tyrosine intermediate | ||||
Sequence: Y | ||||||
Site | 877 | Important for DNA bending; intercalates between base pairs of target DNA | ||||
Sequence: I | ||||||
Site | 952 | Interaction with DNA | ||||
Sequence: W |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA topoisomerase 2-beta
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ02880
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
B-cell immunodeficiency, distal limb anomalies, and urogenital malformations (BILU)
- Note
- DescriptionAn autosomal dominant disorder characterized by humoral immunodeficiency with undetectable B cells, distal limb anomalies, dysmorphic facial features, and urogenital malformations.
- See alsoMIM:609296
Natural variants in BILU
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086569 | 488 | S>L | in BILU; loss-of-function variant in a yeast complementation assay; dbSNP:rs2125377904 | |
VAR_086570 | 490 | A>P | in BILU; decreased protein abundance; severely decreased DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; dbSNP:rs2125377898 | |
VAR_086571 | 593 | missing | in BILU; loss-of-function variant in a yeast complementation assay | |
VAR_086572 | 638 | G>S | in BILU; loss-of-function variant in a yeast complementation assay; dbSNP:rs2125373730 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_079273 | 63 | found in patients with global developmental delay and autism spectrum disorder; likely pathogenic; dbSNP:rs886039770 | |||
Sequence: H → Y | ||||||
Mutagenesis | 482 | Strongly reduced enzyme activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 485 | Slightly reduced enzyme activity. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_086569 | 488 | in BILU; loss-of-function variant in a yeast complementation assay; dbSNP:rs2125377904 | |||
Sequence: S → L | ||||||
Natural variant | VAR_086570 | 490 | in BILU; decreased protein abundance; severely decreased DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; dbSNP:rs2125377898 | |||
Sequence: A → P | ||||||
Mutagenesis | 508 | Slightly reduced enzyme activity. | ||||
Sequence: R → E | ||||||
Mutagenesis | 510 | Strongly reduced enzyme activity. | ||||
Sequence: K → E | ||||||
Mutagenesis | 515 | Slightly reduced enzyme activity. | ||||
Sequence: R → Q | ||||||
Natural variant | VAR_086571 | 593 | in BILU; loss-of-function variant in a yeast complementation assay | |||
Sequence: Missing | ||||||
Natural variant | VAR_086572 | 638 | in BILU; loss-of-function variant in a yeast complementation assay; dbSNP:rs2125373730 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,326 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000145369 | 2-1626 | UniProt | DNA topoisomerase 2-beta | |||
Sequence: AKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLAAFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKKKKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYFAESDEEEDDVDFAMFN | |||||||
Modified residue | 3 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 28 | UniProt | In isoform Q02880-2; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: Q | |||||||
Cross-link | 29 | UniProt | In isoform Q02880-2; Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: N | |||||||
Cross-link | 33 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 34 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 177 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 178 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 228 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 299 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 367 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 373 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 437 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 439 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 446 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 600 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 605 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 635 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 643 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 646 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 676 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 712 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1092 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1214 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1217 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1226 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1227 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1236 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1238 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 1250 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1262 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1271 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1292 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1292 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1323 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1327 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1336 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1340 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1340 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1342 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1344 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1358 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1370 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1375 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1398 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1403 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1403 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1413 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1413 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1421 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1421 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1422 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1424 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1424 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1431 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1435 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1440 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1441 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1441 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1449 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1452 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1452 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1453 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1454 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1454 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1456 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1457 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1461 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1461 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1466 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1466 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1473 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1473 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1476 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1476 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1478 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1490 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1522 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1522 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1524 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1526 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1526 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1550 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1550 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1552 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1552 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1558 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1575 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1575 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1576 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1581 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1581 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1592 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1596 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1609 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1613 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1613 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Also found in breast, colon and lung carcinomas, Hodgkin's disease, large-cell non-Hodgkin's lymphoma, lymphocytic lymphomas and seminomas (PubMed:9155056).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with KIAA1210 (By similarity).
Interacts with PLSCR1 (PubMed:19690332).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q02880 | PIAS4 Q8N2W9 | 2 | EBI-2307774, EBI-473160 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 363-365 | Interaction with DNA | ||||
Sequence: KKK | ||||||
Domain | 476-593 | Toprim | ||||
Sequence: CTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEE | ||||||
Domain | 736-1189 | Topo IIA-type catalytic | ||||
Sequence: IPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDL | ||||||
Region | 1011-1020 | Interaction with DNA | ||||
Sequence: KLQTTLTCNS | ||||||
Motif | 1034-1044 | Nuclear export signal | ||||
Sequence: ETVQDILKEFF | ||||||
Compositional bias | 1110-1129 | Basic and acidic residues | ||||
Sequence: AWKEAQEKAAEEDETQNQHD | ||||||
Region | 1110-1140 | Disordered | ||||
Sequence: AWKEAQEKAAEEDETQNQHDDSSSDSGTPSG | ||||||
Region | 1274-1604 | Disordered | ||||
Sequence: FDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRAR | ||||||
Compositional bias | 1300-1314 | Basic and acidic residues | ||||
Sequence: GPKPKREKKEPGTRV | ||||||
Compositional bias | 1330-1374 | Basic and acidic residues | ||||
Sequence: KKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDF | ||||||
Compositional bias | 1375-1391 | Acidic residues | ||||
Sequence: SEEEDDDADDDDDDNND | ||||||
Compositional bias | 1468-1485 | Polar residues | ||||
Sequence: EEDSASVFSPSFGLKQTD | ||||||
Compositional bias | 1501-1521 | Basic and acidic residues | ||||
Sequence: SDTVPKPKRAPKQKKVVEAVN | ||||||
Region | 1506-1512 | Interaction with PLSCR1 | ||||
Sequence: KPKRAPK |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q02880-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameBeta-2
- Length1,626
- Mass (Da)183,267
- Last updated2002-01-31 v3
- ChecksumE60E9262CC68B05D
Q02880-2
- NameBeta-1
- Differences from canonical
- 24-28: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H7BZ82 | H7BZ82_HUMAN | TOP2B | 70 | ||
A0A8V8TPE3 | A0A8V8TPE3_HUMAN | TOP2B | 1382 | ||
A0A8V8TP20 | A0A8V8TP20_HUMAN | TOP2B | 1517 | ||
A0A8V8TN33 | A0A8V8TN33_HUMAN | TOP2B | 1010 | ||
E9PCY5 | E9PCY5_HUMAN | TOP2B | 1150 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006532 | 24-28 | in isoform Beta-1 | |||
Sequence: Missing | ||||||
Compositional bias | 1110-1129 | Basic and acidic residues | ||||
Sequence: AWKEAQEKAAEEDETQNQHD | ||||||
Compositional bias | 1300-1314 | Basic and acidic residues | ||||
Sequence: GPKPKREKKEPGTRV | ||||||
Compositional bias | 1330-1374 | Basic and acidic residues | ||||
Sequence: KKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDF | ||||||
Compositional bias | 1375-1391 | Acidic residues | ||||
Sequence: SEEEDDDADDDDDDNND | ||||||
Sequence conflict | 1431 | in Ref. 4; CAA78821/CAA09753 | ||||
Sequence: T → S | ||||||
Compositional bias | 1468-1485 | Polar residues | ||||
Sequence: EEDSASVFSPSFGLKQTD | ||||||
Compositional bias | 1501-1521 | Basic and acidic residues | ||||
Sequence: SDTVPKPKRAPKQKKVVEAVN | ||||||
Sequence conflict | 1611 | in Ref. 1; CAA48197 | ||||
Sequence: A → T | ||||||
Sequence conflict | 1621 | in Ref. 4; CAA09753 | ||||
Sequence: D → H |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X68060 EMBL· GenBank· DDBJ | CAA48197.1 EMBL· GenBank· DDBJ | mRNA | ||
X71911 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z15111 EMBL· GenBank· DDBJ | CAA78815.1 EMBL· GenBank· DDBJ | mRNA | ||
Z15115 EMBL· GenBank· DDBJ | CAA78821.1 EMBL· GenBank· DDBJ | mRNA | ||
M27504 EMBL· GenBank· DDBJ | AAA61210.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ011721 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011722 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011723 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011724 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011725 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011726 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011727 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011728 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011729 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011730 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011731 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ011732 EMBL· GenBank· DDBJ | CAA09753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X53662 EMBL· GenBank· DDBJ | CAA37706.1 EMBL· GenBank· DDBJ | mRNA | ||
U54831 EMBL· GenBank· DDBJ | AAB01982.1 EMBL· GenBank· DDBJ | mRNA |