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E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (Tumor suppressor p53-binding protein 3) (p53-binding protein 3) (p53BP3)

 TOPRS_HUMAN             Reviewed;        1045 AA.
Q9NS56; O43273; Q6P987; Q9NS55; Q9UNR9;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=E3 ubiquitin-protein ligase Topors;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase Topors {ECO:0000305};
AltName: Full=SUMO1-protein E3 ligase Topors;
AltName: Full=Topoisomerase I-binding RING finger protein;
AltName: Full=Topoisomerase I-binding arginine/serine-rich protein;
AltName: Full=Tumor suppressor p53-binding protein 3;
Short=p53-binding protein 3;
Short=p53BP3;
Name=TOPORS; Synonyms=LUN, TP53BPL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TOP1, AND
SUBCELLULAR LOCATION.
PubMed=10352183; DOI=10.1093/nar/27.12.2538;
Haluska P. Jr., Saleem A., Rasheed Z., Ahmed F., Su E.W., Liu L.F.,
Rubin E.H.;
"Interaction between human topoisomerase I and a novel RING
finger/arginine-serine protein.";
Nucleic Acids Res. 27:2538-2544(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PUTATIVE DNA-BINDING,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=11278651; DOI=10.1074/jbc.M010262200;
Chu D., Kakazu N., Gorrin-Rivas M.J., Lu H.P., Kawata M., Abe T.,
Ueda K., Adachi Y.;
"Cloning and characterization of LUN, a novel RING-finger protein that
is highly expressed in lung and specifically binds to a palindromic
sequence.";
J. Biol. Chem. 276:14004-14013(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
THR-154; LYS-517 AND ASP-749.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-1045 (ISOFORM 1), INTERACTION WITH
TP53, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10415337; DOI=10.1016/S0378-1119(99)00203-6;
Zhou R., Wen H., Ao S.-Z.;
"Identification of a novel gene encoding a p53-associated protein.";
Gene 235:93-101(1999).
[6]
SUBCELLULAR LOCATION.
PubMed=12083797; DOI=10.1006/excr.2002.5550;
Rasheed Z.A., Saleem A., Ravee Y., Pandolfi P.P., Rubin E.H.;
"The topoisomerase I-binding RING protein, topors, is associated with
promyelocytic leukemia nuclear bodies.";
Exp. Cell Res. 277:152-160(2002).
[7]
INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION,
AND MUTAGENESIS OF LYS-76; LYS-301; LYS-485; LYS-560 AND LYS-921.
PubMed=14516784; DOI=10.1016/S0014-4827(03)00292-1;
Weger S., Hammer E., Engstler M.;
"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.";
Exp. Cell Res. 290:13-27(2003).
[8]
FUNCTION, AND MUTAGENESIS OF TRP-131.
PubMed=15247280; DOI=10.1074/jbc.C400300200;
Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z.,
Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H.;
"Topors functions as an E3 ubiquitin ligase with specific E2 enzymes
and ubiquitinates p53.";
J. Biol. Chem. 279:36440-36444(2004).
[9]
REDUCED EXPRESSION IN LUNG CANCERS.
PubMed=15364129; DOI=10.1016/j.lungcan.2004.03.009;
Oyanagi H., Takenaka K., Ishikawa S., Kawano Y., Adachi Y., Ueda K.,
Wada H., Tanaka F.;
"Expression of LUN gene that encodes a novel RING finger protein is
correlated with development and progression of non-small cell lung
cancer.";
Lung Cancer 46:21-28(2004).
[10]
TISSUE SPECIFICITY, AND REDUCED EXPRESSION IN COLON CANCERS.
PubMed=15107820; DOI=10.1038/sj.onc.1207700;
Saleem A., Dutta J., Malegaonkar D., Rasheed F., Rasheed Z.,
Rajendra R., Marshall H., Luo M., Li H., Rubin E.H.;
"The topoisomerase I- and p53-binding protein topors is differentially
expressed in normal and malignant human tissues and may function as a
tumor suppressor.";
Oncogene 23:5293-5300(2004).
[11]
FUNCTION, AND SUMOYLATION.
PubMed=16122737; DOI=10.1016/j.febslet.2005.07.088;
Weger S., Hammer E., Heilbronn R.;
"Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo.";
FEBS Lett. 579:5007-5012(2005).
[12]
FUNCTION, AND INDUCTION.
PubMed=15735665; DOI=10.1038/sj.onc.1208554;
Lin L., Ozaki T., Takada Y., Kageyama H., Nakamura Y., Hata A.,
Zhang J.H., Simonds W.F., Nakagawara A., Koseki H.;
"Topors, a p53 and topoisomerase I-binding RING finger protein, is a
coactivator of p53 in growth suppression induced by DNA damage.";
Oncogene 24:3385-3396(2005).
[13]
INVOLVEMENT IN RP31.
PubMed=17924349; DOI=10.1086/521953;
Chakarova C.F., Papaioannou M.G., Khanna H., Lopez I., Waseem N.,
Shah A., Theis T., Friedman J., Maubaret C., Bujakowska K.,
Veraitch B., El-Aziz M.M.A., Prescott de Q., Parapuram S.K.,
Bickmore W.A., Munro P.M.G., Gal A., Hamel C.P., Marigo V.,
Ponting C.P., Wissinger B., Zrenner E., Matter K., Swaroop A.,
Koenekoop R.K., Bhattacharya S.S.;
"Mutations in TOPORS cause autosomal dominant retinitis pigmentosa
with perivascular retinal pigment epithelium atrophy.";
Am. J. Hum. Genet. 81:1098-1103(2007).
[14]
FUNCTION, AND INTERACTION WITH SIN3A.
PubMed=17803295; DOI=10.1021/pr0703674;
Pungaliya P., Kulkarni D., Park H.J., Marshall H., Zheng H.,
Lackland H., Saleem A., Rubin E.H.;
"TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying
proteins.";
J. Proteome Res. 6:3918-3923(2007).
[15]
PHOSPHORYLATION AT SER-98; SER-499; SER-585 AND SER-866, MUTAGENESIS
OF SER-98, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19053840; DOI=10.1021/bi801904q;
Park H.J., Zheng H., Kulkarni D., Kerrigan J., Pungaliya P.,
Saleem A., Rubin E.H.;
"Identification of phosphorylation sites of TOPORS and a role for
serine 98 in the regulation of ubiquitin but not SUMO E3 ligase
activity.";
Biochemistry 47:13887-13896(2008).
[16]
FUNCTION, INTERACTION WITH NKX3-1, AND SUBCELLULAR LOCATION.
PubMed=18077445; DOI=10.1074/jbc.M708630200;
Guan B., Pungaliya P., Li X., Uquillas C., Mutton L.N., Rubin E.H.,
Bieberich C.J.;
"Ubiquitination by TOPORS regulates the prostate tumor suppressor
NKX3.1.";
J. Biol. Chem. 283:4834-4840(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
FUNCTION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-718 BY PLK1,
MUTAGENESIS OF SER-718, AND SUBCELLULAR LOCATION.
PubMed=19473992; DOI=10.1074/jbc.C109.001560;
Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.;
"Plk1-mediated phosphorylation of Topors regulates p53 stability.";
J. Biol. Chem. 284:18588-18592(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-864 AND SER-866,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
FUNCTION, INTERACTION WITH IKBKE, AND SUBCELLULAR LOCATION.
PubMed=20188669; DOI=10.1016/j.molcel.2010.01.018;
Renner F., Moreno R., Schmitz M.L.;
"SUMOylation-dependent localization of IKKepsilon in PML nuclear
bodies is essential for protection against DNA-damage-triggered cell
death.";
Mol. Cell 37:503-515(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-864 AND SER-866,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-194; SER-585 AND
SER-734, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-83; LYS-249 AND
LYS-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-701, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-701, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"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.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-76; LYS-83; LYS-88;
LYS-159; LYS-249; LYS-701; LYS-819 AND LYS-837, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- 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}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: Interacts with PARK7/DJ-1 (By similarity). Interacts with
TOP1. Interacts with p53/TP53; can both ubiquitinate and sumoylate
p53/TP53. Interacts with the SUMO1 conjugating enzyme UBE2I.
Interacts with SUMO1. Interacts with NKX3-1; polyubiquitinates
NKX3-1 and induces its proteasomal degradation. Interacts with
SIN3A; sumoylates SIN3A. Interacts with IKBKE; induced by DNA
damage. {ECO:0000250|UniProtKB:Q80Z37,
ECO:0000269|PubMed:10352183, ECO:0000269|PubMed:10415337,
ECO:0000269|PubMed:14516784, ECO:0000269|PubMed:17803295,
ECO:0000269|PubMed:18077445, ECO:0000269|PubMed:19473992,
ECO:0000269|PubMed:20188669}.
-!- INTERACTION:
P03132:Rep68 (xeno); NbExp=3; IntAct=EBI-1996473, EBI-7387242;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LUN-1;
IsoId=Q9NS56-1; Sequence=Displayed;
Name=2; Synonyms=LUN-2;
IsoId=Q9NS56-2; Sequence=VSP_017916, VSP_017917;
-!- TISSUE SPECIFICITY: Expressed at highest levels in testis and at
lower levels in adrenal gland, bone marrow, brain, colon, heart,
kidney, liver, muscle, ovary, pancreas, placenta, prostate,
skeletal muscle, skin, small intestine, spleen, stomach, testis,
thymus, thyroid and uterus. Expressed in the alveolar epithelium
of the lung. Expression is commonly decreased in colon
adenocarcinomas and lung cancers. {ECO:0000269|PubMed:10415337,
ECO:0000269|PubMed:11278651, ECO:0000269|PubMed:15107820}.
-!- INDUCTION: By genotoxic agents such as cisplatin and camptothecin.
{ECO:0000269|PubMed:15735665}.
-!- 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}.
-!- 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 mutations affecting the gene represented in this entry.
-!- CAUTION: Was originally thought to bind to the palindromic
consensus sequence 5'-TCCCAGCACTTTGGGA-3' and to regulate the
transcription of numerous genes in the lung.
{ECO:0000305|PubMed:11278651}.
-!- SEQUENCE CAUTION:
Sequence=AAC98530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TOPORSID42663ch9p21.html";
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EMBL; AF098300; AAD23379.1; -; mRNA.
EMBL; AB045732; BAB03714.1; -; mRNA.
EMBL; AB045733; BAB03715.1; -; mRNA.
EMBL; AL353671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC060884; AAH60884.1; -; mRNA.
EMBL; U82939; AAC98530.1; ALT_INIT; mRNA.
CCDS; CCDS56566.1; -. [Q9NS56-2]
CCDS; CCDS6527.1; -. [Q9NS56-1]
RefSeq; NP_001182551.1; NM_001195622.1. [Q9NS56-2]
RefSeq; NP_005793.2; NM_005802.4. [Q9NS56-1]
UniGene; Hs.589962; -.
ProteinModelPortal; Q9NS56; -.
SMR; Q9NS56; -.
BioGrid; 115505; 65.
IntAct; Q9NS56; 19.
MINT; MINT-94004; -.
STRING; 9606.ENSP00000353735; -.
iPTMnet; Q9NS56; -.
PhosphoSitePlus; Q9NS56; -.
BioMuta; TOPORS; -.
DMDM; 74752935; -.
EPD; Q9NS56; -.
MaxQB; Q9NS56; -.
PaxDb; Q9NS56; -.
PeptideAtlas; Q9NS56; -.
PRIDE; Q9NS56; -.
Ensembl; ENST00000360538; ENSP00000353735; ENSG00000197579. [Q9NS56-1]
Ensembl; ENST00000379858; ENSP00000369187; ENSG00000197579. [Q9NS56-2]
GeneID; 10210; -.
KEGG; hsa:10210; -.
UCSC; uc003zrb.4; human. [Q9NS56-1]
CTD; 10210; -.
DisGeNET; 10210; -.
EuPathDB; HostDB:ENSG00000197579.7; -.
GeneCards; TOPORS; -.
GeneReviews; TOPORS; -.
HGNC; HGNC:21653; TOPORS.
HPA; HPA060640; -.
HPA; HPA065661; -.
MalaCards; TOPORS; -.
MIM; 609507; gene.
MIM; 609923; phenotype.
neXtProt; NX_Q9NS56; -.
OpenTargets; ENSG00000197579; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA134979531; -.
eggNOG; KOG4430; Eukaryota.
eggNOG; ENOG410XQZR; LUCA.
GeneTree; ENSGT00530000064170; -.
HOGENOM; HOG000231723; -.
HOVERGEN; HBG080410; -.
InParanoid; Q9NS56; -.
KO; K10631; -.
OMA; FIHEFIS; -.
OrthoDB; EOG091G089U; -.
PhylomeDB; Q9NS56; -.
TreeFam; TF339497; -.
SIGNOR; Q9NS56; -.
ChiTaRS; TOPORS; human.
GeneWiki; TOPORS; -.
GenomeRNAi; 10210; -.
PRO; PR:Q9NS56; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000197579; -.
CleanEx; HS_TOPORS; -.
Genevisible; Q9NS56; HS.
GO; GO:0005814; C:centriole; IDA:BHF-UCL.
GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
GO; GO:0000930; C:gamma-tubulin complex; IDA:BHF-UCL.
GO; GO:0030496; C:midbody; TAS:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:BHF-UCL.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:BHF-UCL.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:BHF-UCL.
GO; GO:0003823; F:antigen binding; IPI:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0044547; F:DNA topoisomerase binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019789; F:SUMO transferase activity; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:BHF-UCL.
GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:BHF-UCL.
GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010842; P:retina layer formation; ISS:BHF-UCL.
GO; GO:0046549; P:retinal cone cell development; ISS:BHF-UCL.
GO; GO:0046548; P:retinal rod cell development; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA damage; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Retinitis pigmentosa; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1045 E3 ubiquitin-protein ligase Topors.
/FTId=PRO_0000232626.
ZN_FING 103 142 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 1 195 E3 ubiquitin-protein ligase activity.
REGION 51 374 Required for DNA-binding.
REGION 437 654 Interaction with SUMO1.
{ECO:0000269|PubMed:14516784}.
REGION 437 574 Required for sumoylation and localization
to discrete nuclear foci.
REGION 456 882 Interaction with TOP1.
{ECO:0000269|PubMed:10352183}.
REGION 456 731 Interaction with p53/TP53.
{ECO:0000269|PubMed:10415337}.
REGION 854 917 Interaction with UBE2I.
{ECO:0000269|PubMed:14516784}.
COMPBIAS 579 788 Arg-rich.
COMPBIAS 854 895 Lys-rich.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19053840}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000269|PubMed:19053840}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19053840}.
MOD_RES 718 718 Phosphoserine; by PLK1.
{ECO:0000269|PubMed:19473992}.
MOD_RES 734 734 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 864 864 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:19053840}.
MOD_RES 912 912 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Z37}.
MOD_RES 914 914 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Z37}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Z37}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 83 83 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 88 88 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 560 560 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
CROSSLNK 701 701 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 819 819 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 837 837 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 65 Missing (in isoform 2).
{ECO:0000303|PubMed:11278651}.
/FTId=VSP_017916.
VAR_SEQ 66 66 E -> M (in isoform 2).
{ECO:0000303|PubMed:11278651}.
/FTId=VSP_017917.
VARIANT 154 154 A -> T (in dbSNP:rs17855104).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037629.
VARIANT 517 517 E -> K (in dbSNP:rs17855103).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037630.
VARIANT 749 749 N -> D (in dbSNP:rs17857515).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037631.
VARIANT 812 812 P -> R (in dbSNP:rs36034138).
/FTId=VAR_037632.
MUTAGEN 76 76 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:14516784}.
MUTAGEN 98 98 S->A: Loss of phosphorylation but no
effect on E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:19053840}.
MUTAGEN 98 98 S->D: Increase in E3 ubiquitin-protein
ligase activity and increased binding to
UBE2D1. No effect on SUMO1-protein ligase
activity. {ECO:0000269|PubMed:19053840}.
MUTAGEN 131 131 W->A: Abrogates E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:15247280}.
MUTAGEN 301 301 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:14516784}.
MUTAGEN 485 485 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:14516784}.
MUTAGEN 560 560 K->R: Strongly reduces sumoylation.
{ECO:0000269|PubMed:14516784}.
MUTAGEN 718 718 S->A: Loss of phosphorylation by PLK1 and
increases in p53/TP53 stability.
{ECO:0000269|PubMed:19473992}.
MUTAGEN 921 921 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:14516784}.
CONFLICT 124 125 CF -> K (in Ref. 5; AAC98530).
{ECO:0000305}.
CONFLICT 257 257 N -> S (in Ref. 1; AAD23379).
{ECO:0000305}.
CONFLICT 308 308 F -> S (in Ref. 1; AAD23379).
{ECO:0000305}.
CONFLICT 922 922 E -> G (in Ref. 1; AAD23379).
{ECO:0000305}.
CONFLICT 1040 1040 R -> K (in Ref. 1; AAD23379).
{ECO:0000305}.
SEQUENCE 1045 AA; 119198 MW; 3DA635FDB5C83B77 CRC64;
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


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