TOPORS
entrez
10210
canonical
uniprot
Q9NS56
canonical
ensembl
ENSG00000197579
resolver
ensp
ENSP00000353735
resolver
ensp
ENSP00000369187
resolver
genesymbol
TOPORS
resolver
genesymbol_syn
LUN
resolver
genesymbol_syn
TP53BPL
resolver
hgnc
HGNC:21653
resolver
uniprot
O43273
resolver
uniprot
Q6P987
resolver
uniprot
Q9NS55
resolver
uniprot
Q9UNR9
resolver
uniprot_entry
TOPRS_HUMAN
resolver
uniprot_sec
O43273
resolver
uniprot_sec
Q6P987
resolver
uniprot_sec
Q9NS55
resolver
uniprot_sec
Q9UNR9
resolver
amino_acid_sequence
MGSQPPLGSPLSREEGEAPPPAPASEGRRRSRRVRLRGSCRHRPSFLGCRELAASAPARPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFVTPDRRFRYRTTLTRERNASVYSPSGPVNRRTTTPPDSGVLFEGLGISTRPRDVEIPQFMRQIAVRRPTTADERSLRKIQEQDIINFRRTLYRAGARVRNIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANYDCPAPSYEEGSHSDSSVITISPDEAETQELDINVATVSQAPWDDETPGPSYSSSEQVHVTMSSLLNTSDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPEFRVQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSRTASTGTDRVRNEKPGGKRKYKTRHLEGTNEVAQPSREFASKAKDSHYQKSSSKLDGNYKNESDTFSDSRSSDRETKHKRRKRKTRSLSVEIVYEGKATDTTKHHKKKKKKHKKKHKKHHGDNASRSPVVITIDSDSDKDSEVKEDTECDNSGPQDPLQNEFLAPSLEPFETKDVVTIEAEFGVLDKECDIATLSNNLNNANKTVDNIPPLAASVEQTLDVREESTFVSDLENQPSNIVSLQTEPSRQLPSPRTSLMSVCLGRDCDMS
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 31 (RP31) [MIM:609923]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:17924349}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Functions as an E3 ubiquitin-protein ligase and as an E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA damage-induced cell death through IKBKE sumoylation. {ECO:0000269|PubMed:15247280, ECO:0000269|PubMed:15735665, ECO:0000269|PubMed:16122737, ECO:0000269|PubMed:17803295, ECO:0000269|PubMed:18077445, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:20188669}.
uniprot
proteins
mass_dalton
119198
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:14516784"; MUTAGEN 98; /note="S->A: Loss of phosphorylation but no effect on E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:19053840"; MUTAGEN 98; /note="S->D: Increase in E3 ubiquitin-protein ligase activity and increased binding to UBE2D1. No effect on SUMO1-protein ligase activity."; /evidence="ECO:0000269|PubMed:19053840"; MUTAGEN 131; /note="W->A: Abrogates E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:15247280"; MUTAGEN 301; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:14516784"; MUTAGEN 485; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:14516784"; MUTAGEN 560; /note="K->R: Strongly reduces sumoylation."; /evidence="ECO:0000269|PubMed:14516784"; MUTAGEN 718; /note="S->A: Loss of phosphorylation by PLK1 and increases in p53/TP53 stability."; /evidence="ECO:0000269|PubMed:19473992"; MUTAGEN 921; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:14516784
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-98 regulates the E3 ubiquitin-protein ligase activity but not the SUMO1-protein ligase activity. Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase activity versus the SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation. {ECO:0000269|PubMed:19053840, ECO:0000269|PubMed:19473992}.; PTM: Sumoylated. {ECO:0000269|PubMed:14516784, ECO:0000269|PubMed:16122737}.
uniprot
proteins
pubmed
10352183
uniprot
proteins
pubmed
10415337
uniprot
proteins
pubmed
11278651
uniprot
proteins
pubmed
12083797
uniprot
proteins
pubmed
14516784
uniprot
proteins
pubmed
15107820
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15247280
uniprot
proteins
pubmed
15364129
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15735665
uniprot
proteins
pubmed
16122737
uniprot
proteins
pubmed
17803295
uniprot
proteins
pubmed
17924349
uniprot
proteins
pubmed
18077445
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19053840
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19473992
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20188669
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
1045
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage.
uniprot
proteins