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Q9NS56 (TOPRS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase Topors

EC=6.3.2.-
Alternative name(s):
SUMO1-protein E3 ligase Topors
Topoisomerase I-binding RING finger protein
Topoisomerase I-binding arginine/serine-rich protein
Tumor suppressor p53-binding protein 3
Short name=p53-binding protein 3
Short name=p53BP3
Gene names
Name:TOPORS
Synonyms:LUN, TP53BPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1045 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.11 Ref.12 Ref.14 Ref.16 Ref.19 Ref.21

Subunit structure

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. Ref.1 Ref.5 Ref.7 Ref.14 Ref.16 Ref.19 Ref.21

Subcellular location

Nucleus. NucleusPML body. Note: Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.16 Ref.19 Ref.21

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. Ref.2 Ref.5 Ref.10

Induction

By genotoxic agents such as cisplatin and camptothecin. Ref.12

Post-translational modification

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.

Sumoylated. Ref.7 Ref.11

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Contains 1 RING-type zinc finger.

Caution

Was originally (Ref.2) thought to bind to the palindromic consensus sequence 5'-TCCCAGCACTTTGGGA-3' and to regulate the transcription of numerous genes in the lung.

Sequence caution

The sequence AAC98530.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA damage
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseRetinitis pigmentosa
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from direct assay Ref.12. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay Ref.21. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

maintenance of protein location in nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity PubMed 21159800. Source: BHF-UCL

photoreceptor cell outer segment organization

Inferred from sequence or structural similarity PubMed 21159800. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of ubiquitin-protein transferase activity

Inferred from direct assay Ref.8. Source: BHF-UCL

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.16. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from direct assay Ref.8. Source: BHF-UCL

protein localization to nucleus

Inferred from mutant phenotype Ref.21. Source: UniProtKB

protein monoubiquitination

Inferred from direct assay Ref.8. Source: BHF-UCL

protein sumoylation

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

retina layer formation

Inferred from sequence or structural similarity PubMed 21159800. Source: BHF-UCL

retinal cone cell development

Inferred from sequence or structural similarity PubMed 21159800. Source: BHF-UCL

retinal rod cell development

Inferred from sequence or structural similarity PubMed 21159800. Source: BHF-UCL

transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.19. Source: UniProtKB

   Cellular_componentPML body

Inferred from direct assay Ref.21. Source: UniProtKB

centriole

Inferred from direct assay PubMed 21159800. Source: BHF-UCL

ciliary basal body

Inferred from direct assay PubMed 21159800. Source: BHF-UCL

gamma-tubulin complex

Inferred from direct assay PubMed 21159800. Source: BHF-UCL

midbody

Traceable author statement PubMed 21159800. Source: BHF-UCL

nuclear speck

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

photoreceptor connecting cilium

Inferred from direct assay PubMed 21159800. Source: BHF-UCL

spindle pole

Inferred from direct assay PubMed 21159800. Source: BHF-UCL

ubiquitin ligase complex

Inferred from direct assay Ref.8. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from direct assay Ref.2. Source: UniProtKB

DNA topoisomerase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

SUMO ligase activity

Inferred from direct assay Ref.14. Source: UniProtKB

antigen binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.14Ref.16Ref.19Ref.21. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.16. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NS56-1)

Also known as: LUN-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.
Isoform 2 (identifier: Q9NS56-2)

Also known as: LUN-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.
     66-66: E → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10451045E3 ubiquitin-protein ligase Topors
PRO_0000232626

Regions

Zinc finger103 – 14240RING-type
Region1 – 195195E3 ubiquitin-protein ligase activity
Region51 – 374324Required for DNA-binding
Region437 – 654218Interaction with SUMO1
Region437 – 574138Required for sumoylation and localization to discrete nuclear foci
Region456 – 882427Interaction with TOP1
Region456 – 731276Interaction with p53/TP53
Region854 – 91764Interaction with UBE2I
Compositional bias579 – 788210Arg-rich
Compositional bias854 – 89542Lys-rich

Amino acid modifications

Modified residue981Phosphoserine Ref.15 Ref.17 Ref.20 Ref.22 Ref.23
Modified residue4991Phosphoserine Ref.15
Modified residue5851Phosphoserine Ref.15
Modified residue7181Phosphoserine; by PLK1 Ref.19
Modified residue8641Phosphoserine Ref.20 Ref.23
Modified residue8661Phosphoserine Ref.15 Ref.20 Ref.23
Modified residue10281Phosphoserine By similarity
Cross-link560Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Natural variations

Alternative sequence1 – 6565Missing in isoform 2.
VSP_017916
Alternative sequence661E → M in isoform 2.
VSP_017917
Natural variant1541A → T. Ref.4
Corresponds to variant rs17855104 [ dbSNP | Ensembl ].
VAR_037629
Natural variant5171E → K. Ref.4
Corresponds to variant rs17855103 [ dbSNP | Ensembl ].
VAR_037630
Natural variant7491N → D. Ref.4
Corresponds to variant rs17857515 [ dbSNP | Ensembl ].
VAR_037631
Natural variant8121P → R.
Corresponds to variant rs36034138 [ dbSNP | Ensembl ].
VAR_037632

Experimental info

Mutagenesis761K → R: No effect on sumoylation. Ref.7
Mutagenesis981S → A: Loss of phosphorylation but no effect on E3 ubiquitin-protein ligase activity. Ref.15
Mutagenesis981S → D: Increase in E3 ubiquitin-protein ligase activity and increased binding to UBE2D1. No effect on SUMO1-protein ligase activity. Ref.15
Mutagenesis1311W → A: Abrogates E3 ubiquitin-protein ligase activity. Ref.8
Mutagenesis3011K → R: No effect on sumoylation. Ref.7
Mutagenesis4851K → R: No effect on sumoylation. Ref.7
Mutagenesis5601K → R: Strongly reduces sumoylation. Ref.7
Mutagenesis7181S → A: Loss of phosphorylation by PLK1 and increases in p53/TP53 stability. Ref.19
Mutagenesis9211K → R: No effect on sumoylation. Ref.7
Sequence conflict124 – 1252CF → K in AAC98530. Ref.5
Sequence conflict2571N → S in AAD23379. Ref.1
Sequence conflict3081F → S in AAD23379. Ref.1
Sequence conflict9221E → G in AAD23379. Ref.1
Sequence conflict10401R → K in AAD23379. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LUN-1) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3DA635FDB5C83B77

FASTA1,045119,198
        10         20         30         40         50         60 
MGSQPPLGSP LSREEGEAPP PAPASEGRRR SRRVRLRGSC RHRPSFLGCR ELAASAPARP 

        70         80         90        100        110        120 
APASSEIMAS AAKEFKMDNF SPKAGTSKLQ QTVPADASPD SKCPICLDRF DNVSYLDRCL 

       130        140        150        160        170        180 
HKFCFRCVQE WSKNKAECPL CKQPFDSIFH SVRAEDDFKE YVLRPSYNGS FVTPDRRFRY 

       190        200        210        220        230        240 
RTTLTRERNA SVYSPSGPVN RRTTTPPDSG VLFEGLGIST RPRDVEIPQF MRQIAVRRPT 

       250        260        270        280        290        300 
TADERSLRKI QEQDIINFRR TLYRAGARVR NIEDGGRYRD ISAEFFRRNP ACLHRLVPWL 

       310        320        330        340        350        360 
KRELTVLFGA HGSLVNIVQH IIMSNVTRYD LESQAFVSDL RPFLLNRTEH FIHEFISFAR 

       370        380        390        400        410        420 
SPFNMAAFDQ HANYDCPAPS YEEGSHSDSS VITISPDEAE TQELDINVAT VSQAPWDDET 

       430        440        450        460        470        480 
PGPSYSSSEQ VHVTMSSLLN TSDSSDEELV TGGATSQIQG VQTNDDLNND SDDSSDNCVI 

       490        500        510        520        530        540 
VGFVKPLAER TPELVELSSD SEDLGSYEKM ETVKTQEQEQ SYSSGDSDVS RCSSPHSVLG 

       550        560        570        580        590        600 
KDEQINKGHC DSSTRIKSKK EEKRSTSLSS PRNLNSSVRG DRVYSPYNHR HRKRGRSRSS 

       610        620        630        640        650        660 
DSRSQSRSGH DQKNHRKHHG KKRMKSKRSR SRESSRPRGR RDKKRSRTRD SSWSRRSQTL 

       670        680        690        700        710        720 
SLSSESTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSRY KWEYTYYSRN KDRDGYESSY 

       730        740        750        760        770        780 
RRRTLSRAHY SRQSSSPEFR VQSFSERTNA RKKNNHSERK YYYYERHRSR SLSSNRSRTA 

       790        800        810        820        830        840 
STGTDRVRNE KPGGKRKYKT RHLEGTNEVA QPSREFASKA KDSHYQKSSS KLDGNYKNES 

       850        860        870        880        890        900 
DTFSDSRSSD RETKHKRRKR KTRSLSVEIV YEGKATDTTK HHKKKKKKHK KKHKKHHGDN 

       910        920        930        940        950        960 
ASRSPVVITI DSDSDKDSEV KEDTECDNSG PQDPLQNEFL APSLEPFETK DVVTIEAEFG 

       970        980        990       1000       1010       1020 
VLDKECDIAT LSNNLNNANK TVDNIPPLAA SVEQTLDVRE ESTFVSDLEN QPSNIVSLQT 

      1030       1040 
EPSRQLPSPR TSLMSVCLGR DCDMS 

« Hide

Isoform 2 (LUN-2) [UniParc].

Checksum: 85E2A39A2978B20E
Show »

FASTA980112,344

References

« Hide 'large scale' references
[1]"Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein."
Haluska P. Jr., Saleem A., Rasheed Z., Ahmed F., Su E.W., Liu L.F., Rubin E.H.
Nucleic Acids Res. 27:2538-2544(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TOP1, SUBCELLULAR LOCATION.
[2]"Cloning and characterization of LUN, a novel RING-finger protein that is highly expressed in lung and specifically binds to a palindromic sequence."
Chu D., Kakazu N., Gorrin-Rivas M.J., Lu H.P., Kawata M., Abe T., Ueda K., Adachi Y.
J. Biol. Chem. 276:14004-14013(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PUTATIVE DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Lung.
[3]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS THR-154; LYS-517 AND ASP-749.
Tissue: Placenta.
[5]"Identification of a novel gene encoding a p53-associated protein."
Zhou R., Wen H., Ao S.-Z.
Gene 235:93-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-1045 (ISOFORM 1), INTERACTION WITH TP53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies."
Rasheed Z.A., Saleem A., Ravee Y., Pandolfi P.P., Rubin E.H.
Exp. Cell Res. 277:152-160(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"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."
Weger S., Hammer E., Engstler M.
Exp. Cell Res. 290:13-27(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION, MUTAGENESIS OF LYS-76; LYS-301; LYS-485; LYS-560 AND LYS-921.
[8]"Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53."
Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z., Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H.
J. Biol. Chem. 279:36440-36444(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-131.
[9]"Expression of LUN gene that encodes a novel RING finger protein is correlated with development and progression of non-small cell lung cancer."
Oyanagi H., Takenaka K., Ishikawa S., Kawano Y., Adachi Y., Ueda K., Wada H., Tanaka F.
Lung Cancer 46:21-28(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCED EXPRESSION IN LUNG CANCERS.
[10]"The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor."
Saleem A., Dutta J., Malegaonkar D., Rasheed F., Rasheed Z., Rajendra R., Marshall H., Luo M., Li H., Rubin E.H.
Oncogene 23:5293-5300(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, REDUCED EXPRESSION IN COLON CANCERS.
[11]"Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo."
Weger S., Hammer E., Heilbronn R.
FEBS Lett. 579:5007-5012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUMOYLATION.
[12]"Topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damage."
Lin L., Ozaki T., Takada Y., Kageyama H., Nakamura Y., Hata A., Zhang J.H., Simonds W.F., Nakagawara A., Koseki H.
Oncogene 24:3385-3396(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[13]"Mutations in TOPORS cause autosomal dominant retinitis pigmentosa with perivascular retinal pigment epithelium atrophy."
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. expand/collapse author list , Marigo V., Ponting C.P., Wissinger B., Zrenner E., Matter K., Swaroop A., Koenekoop R.K., Bhattacharya S.S.
Am. J. Hum. Genet. 81:1098-1103(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RP31.
[14]"TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins."
Pungaliya P., Kulkarni D., Park H.J., Marshall H., Zheng H., Lackland H., Saleem A., Rubin E.H.
J. Proteome Res. 6:3918-3923(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIN3A.
[15]"Identification of phosphorylation sites of TOPORS and a role for serine 98 in the regulation of ubiquitin but not SUMO E3 ligase activity."
Park H.J., Zheng H., Kulkarni D., Kerrigan J., Pungaliya P., Saleem A., Rubin E.H.
Biochemistry 47:13887-13896(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-98; SER-499; SER-585 AND SER-866, MUTAGENESIS OF SER-98, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1."
Guan B., Pungaliya P., Li X., Uquillas C., Mutton L.N., Rubin E.H., Bieberich C.J.
J. Biol. Chem. 283:4834-4840(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NKX3-1, SUBCELLULAR LOCATION.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Plk1-mediated phosphorylation of Topors regulates p53 stability."
Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.
J. Biol. Chem. 284:18588-18592(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-718 BY PLK1, MUTAGENESIS OF SER-718, SUBCELLULAR LOCATION.
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-864 AND SER-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"SUMOylation-dependent localization of IKKepsilon in PML nuclear bodies is essential for protection against DNA-damage-triggered cell death."
Renner F., Moreno R., Schmitz M.L.
Mol. Cell 37:503-515(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKE, SUBCELLULAR LOCATION.
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-864 AND SER-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF098300 mRNA. Translation: AAD23379.1.
AB045732 mRNA. Translation: BAB03714.1.
AB045733 mRNA. Translation: BAB03715.1.
AL353671 Genomic DNA. Translation: CAH71253.1.
AL353671 Genomic DNA. Translation: CAH71254.1.
BC060884 mRNA. Translation: AAH60884.1.
U82939 mRNA. Translation: AAC98530.1. Different initiation.
CCDSCCDS56566.1. [Q9NS56-2]
CCDS6527.1. [Q9NS56-1]
RefSeqNP_001182551.1. NM_001195622.1. [Q9NS56-2]
NP_005793.2. NM_005802.4. [Q9NS56-1]
UniGeneHs.589962.

3D structure databases

ProteinModelPortalQ9NS56.
SMRQ9NS56. Positions 100-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115505. 48 interactions.
IntActQ9NS56. 14 interactions.
MINTMINT-94004.
STRING9606.ENSP00000353735.

PTM databases

PhosphoSiteQ9NS56.

Polymorphism databases

DMDM74752935.

Proteomic databases

MaxQBQ9NS56.
PaxDbQ9NS56.
PRIDEQ9NS56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360538; ENSP00000353735; ENSG00000197579. [Q9NS56-1]
ENST00000379858; ENSP00000369187; ENSG00000197579. [Q9NS56-2]
GeneID10210.
KEGGhsa:10210.
UCSCuc003zrb.3. human. [Q9NS56-1]
uc003zrc.3. human. [Q9NS56-2]

Organism-specific databases

CTD10210.
GeneCardsGC09M032496.
GeneReviewsTOPORS.
HGNCHGNC:21653. TOPORS.
MIM609507. gene.
609923. phenotype.
neXtProtNX_Q9NS56.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA134979531.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244178.
HOGENOMHOG000231723.
HOVERGENHBG080410.
InParanoidQ9NS56.
KOK10631.
OMALLNRTEH.
OrthoDBEOG722J8G.
PhylomeDBQ9NS56.
TreeFamTF339497.

Gene expression databases

BgeeQ9NS56.
CleanExHS_TOPORS.
GenevestigatorQ9NS56.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTOPORS. human.
GeneWikiTOPORS.
GenomeRNAi10210.
NextBio38656.
PROQ9NS56.
SOURCESearch...

Entry information

Entry nameTOPRS_HUMAN
AccessionPrimary (citable) accession number: Q9NS56
Secondary accession number(s): O43273 expand/collapse secondary AC list , Q6P987, Q9NS55, Q9UNR9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM