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Q80Z37 (TOPRS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1033 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as an E3 ubiquitin-protein ligase and as a 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.1 Ref.2

Subunit structure

Interacts with TOP1. 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 By similarity. Interacts with p53/TP53. Interacts with PARK7/DJ-1. Ref.1 Ref.2

Subcellular location

Nucleus. NucleusPML body By similarity. Note: Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage By similarity. Ref.1 Ref.2

Induction

By genotoxic agents such as cisplatin and camptothecin. Ref.2

Post-translational modification

Phosphorylation at Ser-99 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 E3 SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation By similarity.

Sumoylated By similarity.

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAH37141.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processDNA damage
Ubl conjugation pathway
   Cellular componentNucleus
   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 sequence or structural similarity. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from direct assay Ref.2. Source: MGI

maintenance of protein location in nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from genetic interaction Ref.2. Source: MGI

positive regulation of ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein monoubiquitination

Inferred from electronic annotation. Source: Ensembl

protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation

Inferred from direct assay Ref.2. Source: MGI

ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentPML body

Inferred from sequence or structural similarity. Source: UniProtKB

centriole

Inferred from electronic annotation. Source: Ensembl

ciliary basal body

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

gamma-tubulin complex

Inferred from electronic annotation. Source: Ensembl

nuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor connecting cilium

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

spindle pole

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

SUMO ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

antigen binding

Inferred from electronic annotation. Source: Ensembl

ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10331033E3 ubiquitin-protein ligase Topors
PRO_0000232627

Regions

Zinc finger104 – 14340RING-type
Region52 – 376325Required for DNA-binding By similarity
Region438 – 654217Interaction with SUMO1 By similarity
Region438 – 574137Sumoylation and localization to discrete nuclear foci By similarity
Region457 – 879423Interaction with TOP1 By similarity
Region457 – 731275Interaction with p53/TP53 By similarity
Region851 – 91464Interaction with UBE2I By similarity
Compositional bias579 – 787209Arg-rich
Compositional bias877 – 89216Lys-rich

Amino acid modifications

Modified residue991Phosphoserine By similarity
Modified residue5001Phosphoserine By similarity
Modified residue5851Phosphoserine By similarity
Modified residue7181Phosphoserine; by PLK1 By similarity
Modified residue8611Phosphoserine By similarity
Modified residue8631Phosphoserine By similarity
Modified residue10161Phosphoserine Ref.5
Cross-link561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict401S → F in BAB69457. Ref.1
Sequence conflict6231L → P in AAH40797. Ref.3
Sequence conflict6571S → A in BAB69457. Ref.1
Sequence conflict6821S → A in AAH40797. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q80Z37 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3A99C00491D7EFD2

FASTA1,033117,082
        10         20         30         40         50         60 
MGSQPPPPGS PLSREEGEAP PLVPAEEGRR RSRRVRLRGS CRHRPSLLSR RELASNGPAV 

        70         80         90        100        110        120 
PATASSEIMA SAAKEFKMDN FSPKAGTSKL QQTVPADASP DSKCPICLDR FDNVSYLDRC 

       130        140        150        160        170        180 
LHKFCFRCVQ EWSKNKAECP LCKQPFDSIF HSVRAEDDFK EYVLRPSYNG SFTNPEVRRF 

       190        200        210        220        230        240 
RYRTTMTRER SASLYSPSST VSRRTTTPPD SGVLFEGLGI STRPRDVDIP QFMRQMALRG 

       250        260        270        280        290        300 
PTTTDERSLR KIQEQDIINF RRTLYRAGVR VRSIEDGGRY RDISAEFFRR NPACLHRLVP 

       310        320        330        340        350        360 
WLKRELTVLF GAHGSLVNIV QHIIMSNVTR YDLESQAFVS DLRPFLLNRT EHFIHEFISF 

       370        380        390        400        410        420 
ARSPFNMAAF DQHANYDCPP SSEEGSRSDS SVITISPDEA ETQELDMNAS TVRQAPWDDE 

       430        440        450        460        470        480 
TPGPSYSSSE QVHVGVSSLL NSSDSSDEEL VSGGTTSQIQ GVQTNDDVNN DSDSSSDNCV 

       490        500        510        520        530        540 
IVGFVKPLAE RTPELVELSS DSEELGPYEK VETVKTQEQE QSYSSGDSDV SRASSPRSVL 

       550        560        570        580        590        600 
GKDEQMSKSH CDSDTRISSK KEEKRSTSLP APRDSSSTRG DRVCSPYNHR HRKGGRSRSS 

       610        620        630        640        650        660 
DSRSQSRSGH DPRNHRKHGK KRLRNKRSRS RESSSRPRAR KDKKRSRTRD SSWSRRSQTL 

       670        680        690        700        710        720 
SLSSGSTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSKY KWEYTYYSRN KDRDGYESSY 

       730        740        750        760        770        780 
RRRTLSRAHY SRQSSSPEFR IQSFSERTNA RKKNHSERKY YYYERRRSRS VSSNRSRTTS 

       790        800        810        820        830        840 
AGPDRVRNEK PGGKRKYKTR HLEGTSEEAQ PAREFTSKGK DSHYQKSKLD GSYKNESDSF 

       850        860        870        880        890        900 
SDSRSSDRET KHKRRRRRTR SLSVEIVYEG KATDTSKHHK KKKKKHKKKH KKHHGDNTSR 

       910        920        930        940        950        960 
SPVVITIDSD SDGESEVKAG IECSNGSLPQ PIQDGAFETK DVVTIEDELG VLDKDCDVTA 

       970        980        990       1000       1010       1020 
LADDLSTSQT VENCDSPAVP VEQTLDVREE STFASDLESQ SSNVSIQAEP SRPVPSPRTS 

      1030 
LSSVSPGRDC DVS 

« Hide

References

« Hide 'large scale' references
[1]"DJ-1 restores p53 transcription activity inhibited by Topors/p53BP3."
Shinbo Y., Taira T., Niki T., Iguchi-Ariga S.M.M., Ariga H.
Int. J. Oncol. 26:641-648(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PARK7 AND TP53, SUBCELLULAR LOCATION.
Strain: C57BL/6.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION, INDUCTION.
[3]"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].
Tissue: Mammary gland and Mammary tumor.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-824.
Strain: C57BL/6J.
Tissue: Corpora quadrigemina, Lung, Retina and Thymus.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB072395 mRNA. Translation: BAB69457.1.
AB104865 mRNA. Translation: BAC65157.1.
BC037141 mRNA. Translation: AAH37141.1. Sequence problems.
BC040797 mRNA. Translation: AAH40797.1.
AK044564 mRNA. Translation: BAC31981.2.
AK134075 mRNA. Translation: BAE22003.1.
AK140250 mRNA. Translation: BAE24298.1.
AK143025 mRNA. Translation: BAE25253.1.
AK153743 mRNA. Translation: BAE32164.1.
RefSeqNP_598858.2. NM_134097.3.
UniGeneMm.251548.

3D structure databases

ProteinModelPortalQ80Z37.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222976. 2 interactions.
IntActQ80Z37. 1 interaction.
MINTMINT-1789728.
STRING10090.ENSMUSP00000046843.

PTM databases

PhosphoSiteQ80Z37.

Proteomic databases

PRIDEQ80Z37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042575; ENSMUSP00000046843; ENSMUSG00000036822.
GeneID106021.
KEGGmmu:106021.
UCSCuc008shi.1. mouse.

Organism-specific databases

CTD10210.
MGIMGI:2146189. Topors.

Phylogenomic databases

eggNOGNOG244178.
GeneTreeENSGT00530000064170.
HOVERGENHBG080410.
InParanoidQ80Z37.
KOK10631.
OMADIINFRR.
OrthoDBEOG722J8G.
PhylomeDBQ80Z37.
TreeFamTF339497.

Gene expression databases

BgeeQ80Z37.
CleanExMM_TOPORS.
GenevestigatorQ80Z37.

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

NextBio358016.
PROQ80Z37.
SOURCESearch...

Entry information

Entry nameTOPRS_MOUSE
AccessionPrimary (citable) accession number: Q80Z37
Secondary accession number(s): Q3U5B5 expand/collapse secondary AC list , Q3UPZ1, Q3USN3, Q3UZ55, Q8BXP2, Q8CFF5, Q8CGC8, Q920L3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot