TOPORS | ENSG00000197579 | NCBI 10210

Details for: TOPORS

Gene ID: 10210

Symbol: TOPORS

Ensembl ID: ENSG00000197579

Description: TOP1 binding arginine/serine rich protein, E3 ubiquitin ligase

Associated with

Metabolism of proteins
(R-HSA-392499)
Post-translational protein modification
(R-HSA-597592)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of immune response proteins
(R-HSA-4755510)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of transcription cofactors
(R-HSA-3899300)
Antigen binding
(GO:0003823)
Centriole
(GO:0005814)
Ciliary basal body
(GO:0036064)
Dna-templated transcription
(GO:0006351)
Dna binding
(GO:0003677)
Dna damage response
(GO:0006974)
Dna topoisomerase binding
(GO:0044547)
Gamma-tubulin complex
(GO:0000930)
Intrinsic apoptotic signaling pathway in response to dna damage
(GO:0008630)
Intrinsic apoptotic signaling pathway in response to dna damage by p53 class mediator
(GO:0042771)
Maintenance of protein location in nucleus
(GO:0051457)
Metal ion binding
(GO:0046872)
Midbody
(GO:0030496)
Nuclear speck
(GO:0016607)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Photoreceptor connecting cilium
(GO:0032391)
Pml body
(GO:0016605)
Positive regulation of dna-templated transcription
(GO:0045893)
Positive regulation of ubiquitin-protein transferase activity
(GO:0051443)
Proteasome-mediated ubiquitin-dependent protein catabolic process
(GO:0043161)
Protein binding
(GO:0005515)
Protein k48-linked ubiquitination
(GO:0070936)
Protein localization to nucleus
(GO:0034504)
Protein monoubiquitination
(GO:0006513)
Protein polyubiquitination
(GO:0000209)
Protein sumoylation
(GO:0016925)
Regulation of cell population proliferation
(GO:0042127)
Spindle pole
(GO:0000922)
Sumo transferase activity
(GO:0019789)
Ubiquitin-dependent protein catabolic process
(GO:0006511)
Ubiquitin-protein transferase activity
(GO:0004842)
Ubiquitin ligase complex
(GO:0000151)
Ubiquitin protein ligase activity
(GO:0061630)

Other Information

Proteins

E3 ubiquitin-protein ligase Topors

Genular Protein ID: 1389906506

Symbol: TOPRS_HUMAN

Name: E3 ubiquitin-protein ligase Topors

UniProtKB Accession Codes:

Q9NS56 O43273 Q6P987 Q9NS55 Q9UNR9

Database IDs:

Citations:

PubMed ID: 10352183

Title: Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein.

PubMed ID: 10352183

DOI: 10.1093/nar/27.12.2538

PubMed ID: 11278651

Title: Cloning and characterization of LUN, a novel RING-finger protein that is highly expressed in lung and specifically binds to a palindromic sequence.

PubMed ID: 11278651

DOI: 10.1074/jbc.m010262200

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 10415337

Title: Identification of a novel gene encoding a p53-associated protein.

PubMed ID: 10415337

DOI: 10.1016/s0378-1119(99)00203-6

PubMed ID: 12083797

Title: The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies.

PubMed ID: 12083797

DOI: 10.1006/excr.2002.5550

PubMed ID: 14516784

Title: The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation.

PubMed ID: 14516784

DOI: 10.1016/s0014-4827(03)00292-1

PubMed ID: 15247280

Title: Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53.

PubMed ID: 15247280

DOI: 10.1074/jbc.c400300200

PubMed ID: 15364129

Title: Expression of LUN gene that encodes a novel RING finger protein is correlated with development and progression of non-small cell lung cancer.

PubMed ID: 15364129

DOI: 10.1016/j.lungcan.2004.03.009

PubMed ID: 15107820

Title: The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor.

PubMed ID: 15107820

DOI: 10.1038/sj.onc.1207700

PubMed ID: 16122737

Title: Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo.

PubMed ID: 16122737

DOI: 10.1016/j.febslet.2005.07.088

PubMed ID: 15735665

Title: Topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damage.

PubMed ID: 15735665

DOI: 10.1038/sj.onc.1208554

PubMed ID: 17924349

Title: Mutations in TOPORS cause autosomal dominant retinitis pigmentosa with perivascular retinal pigment epithelium atrophy.

PubMed ID: 17924349

DOI: 10.1086/521953

PubMed ID: 17803295

Title: TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins.

PubMed ID: 17803295

DOI: 10.1021/pr0703674

PubMed ID: 19053840

Title: Identification of phosphorylation sites of TOPORS and a role for serine 98 in the regulation of ubiquitin but not SUMO E3 ligase activity.

PubMed ID: 19053840

DOI: 10.1021/bi801904q

PubMed ID: 18077445

Title: Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1.

PubMed ID: 18077445

DOI: 10.1074/jbc.m708630200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19473992

Title: Plk1-mediated phosphorylation of Topors regulates p53 stability.

PubMed ID: 19473992

DOI: 10.1074/jbc.c109.001560

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20188669

Title: SUMOylation-dependent localization of IKKepsilon in PML nuclear bodies is essential for protection against DNA-damage-triggered cell death.

PubMed ID: 20188669

DOI: 10.1016/j.molcel.2010.01.018

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

Sequence Information:

Length: 1045
Mass: 119198
Checksum: 3DA635FDB5C83B77
Sequence:

MGSQPPLGSP LSREEGEAPP PAPASEGRRR SRRVRLRGSC RHRPSFLGCR ELAASAPARP 
APASSEIMAS AAKEFKMDNF SPKAGTSKLQ QTVPADASPD SKCPICLDRF DNVSYLDRCL 
HKFCFRCVQE WSKNKAECPL CKQPFDSIFH SVRAEDDFKE YVLRPSYNGS FVTPDRRFRY 
RTTLTRERNA SVYSPSGPVN RRTTTPPDSG VLFEGLGIST RPRDVEIPQF MRQIAVRRPT 
TADERSLRKI QEQDIINFRR TLYRAGARVR NIEDGGRYRD ISAEFFRRNP ACLHRLVPWL 
KRELTVLFGA HGSLVNIVQH IIMSNVTRYD LESQAFVSDL RPFLLNRTEH FIHEFISFAR 
SPFNMAAFDQ HANYDCPAPS YEEGSHSDSS VITISPDEAE TQELDINVAT VSQAPWDDET 
PGPSYSSSEQ VHVTMSSLLN TSDSSDEELV TGGATSQIQG VQTNDDLNND SDDSSDNCVI 
VGFVKPLAER TPELVELSSD SEDLGSYEKM ETVKTQEQEQ SYSSGDSDVS RCSSPHSVLG 
KDEQINKGHC DSSTRIKSKK EEKRSTSLSS PRNLNSSVRG DRVYSPYNHR HRKRGRSRSS 
DSRSQSRSGH DQKNHRKHHG KKRMKSKRSR SRESSRPRGR RDKKRSRTRD SSWSRRSQTL 
SLSSESTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSRY KWEYTYYSRN KDRDGYESSY 
RRRTLSRAHY SRQSSSPEFR VQSFSERTNA RKKNNHSERK YYYYERHRSR SLSSNRSRTA 
STGTDRVRNE KPGGKRKYKT RHLEGTNEVA QPSREFASKA KDSHYQKSSS KLDGNYKNES 
DTFSDSRSSD RETKHKRRKR KTRSLSVEIV YEGKATDTTK HHKKKKKKHK KKHKKHHGDN 
ASRSPVVITI DSDSDKDSEV KEDTECDNSG PQDPLQNEFL APSLEPFETK DVVTIEAEFG 
VLDKECDIAT LSNNLNNANK TVDNIPPLAA SVEQTLDVRE ESTFVSDLEN QPSNIVSLQT 
EPSRQLPSPR TSLMSVCLGR DCDMS

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: TOPORS

Associated with

Other Information

Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein. PubMed ID: 10352183

Cloning and characterization of LUN, a novel RING-finger protein that is highly expressed in lung and specifically binds to a palindromic sequence. PubMed ID: 11278651

DNA sequence and analysis of human chromosome 9. PubMed ID: 15164053

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Identification of a novel gene encoding a p53-associated protein. PubMed ID: 10415337

The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies. PubMed ID: 12083797

The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation. PubMed ID: 14516784

Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53. PubMed ID: 15247280

Expression of LUN gene that encodes a novel RING finger protein is correlated with development and progression of non-small cell lung cancer. PubMed ID: 15364129

The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor. PubMed ID: 15107820

Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. PubMed ID: 16122737

Topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damage. PubMed ID: 15735665

Mutations in TOPORS cause autosomal dominant retinitis pigmentosa with perivascular retinal pigment epithelium atrophy. PubMed ID: 17924349

TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins. PubMed ID: 17803295

Identification of phosphorylation sites of TOPORS and a role for serine 98 in the regulation of ubiquitin but not SUMO E3 ligase activity. PubMed ID: 19053840

Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1. PubMed ID: 18077445

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Plk1-mediated phosphorylation of Topors regulates p53 stability. PubMed ID: 19473992

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

SUMOylation-dependent localization of IKKepsilon in PML nuclear bodies is essential for protection against DNA-damage-triggered cell death. PubMed ID: 20188669

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733