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Q80Z37

- TOPRS_MOUSE

UniProt

Q80Z37 - TOPRS_MOUSE

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Protein
E3 ubiquitin-protein ligase Topors
Gene
Topors
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 14340RING-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. SUMO ligase activity Source: UniProtKB
  3. antigen binding Source: Ensembl
  4. protein binding Source: MGI
  5. ubiquitin-protein transferase activity Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  3. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  4. maintenance of protein location in nucleus Source: Ensembl
  5. positive regulation of transcription, DNA-templated Source: MGI
  6. positive regulation of ubiquitin-protein transferase activity Source: Ensembl
  7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  8. protein K48-linked ubiquitination Source: Ensembl
  9. protein localization to nucleus Source: UniProtKB
  10. protein monoubiquitination Source: Ensembl
  11. protein sumoylation Source: UniProtKB
  12. regulation of cell proliferation Source: MGI
  13. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Topors
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2146189. Topors.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB
  2. centriole Source: Ensembl
  3. ciliary basal body Source: BHF-UCL
  4. gamma-tubulin complex Source: Ensembl
  5. nuclear speck Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. photoreceptor connecting cilium Source: BHF-UCL
  8. spindle pole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10331033E3 ubiquitin-protein ligase Topors
PRO_0000232627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine By similarity
Modified residuei500 – 5001Phosphoserine By similarity
Cross-linki561 – 561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei585 – 5851Phosphoserine By similarity
Modified residuei718 – 7181Phosphoserine; by PLK1 By similarity
Modified residuei861 – 8611Phosphoserine By similarity
Modified residuei863 – 8631Phosphoserine By similarity
Modified residuei1016 – 10161Phosphoserine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ80Z37.

PTM databases

PhosphoSiteiQ80Z37.

Expressioni

Inductioni

By genotoxic agents such as cisplatin and camptothecin.1 Publication

Gene expression databases

BgeeiQ80Z37.
CleanExiMM_TOPORS.
GenevestigatoriQ80Z37.

Interactioni

Subunit structurei

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-1.2 Publications

Protein-protein interaction databases

BioGridi222976. 2 interactions.
IntActiQ80Z37. 1 interaction.
MINTiMINT-1789728.
STRINGi10090.ENSMUSP00000046843.

Structurei

3D structure databases

ProteinModelPortaliQ80Z37.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 376325Required for DNA-binding By similarity
Add
BLAST
Regioni438 – 654217Interaction with SUMO1 By similarity
Add
BLAST
Regioni438 – 574137Sumoylation and localization to discrete nuclear foci By similarity
Add
BLAST
Regioni457 – 879423Interaction with TOP1 By similarity
Add
BLAST
Regioni457 – 731275Interaction with p53/TP53 By similarity
Add
BLAST
Regioni851 – 91464Interaction with UBE2I By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi579 – 787209Arg-rich
Add
BLAST
Compositional biasi877 – 89216Lys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG244178.
GeneTreeiENSGT00530000064170.
HOVERGENiHBG080410.
InParanoidiQ80Z37.
KOiK10631.
OMAiLLNRTEH.
OrthoDBiEOG722J8G.
PhylomeDBiQ80Z37.
TreeFamiTF339497.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80Z37-1 [UniParc]FASTAAdd to Basket

« Hide

MGSQPPPPGS PLSREEGEAP PLVPAEEGRR RSRRVRLRGS CRHRPSLLSR     50
RELASNGPAV PATASSEIMA SAAKEFKMDN FSPKAGTSKL QQTVPADASP 100
DSKCPICLDR FDNVSYLDRC LHKFCFRCVQ EWSKNKAECP LCKQPFDSIF 150
HSVRAEDDFK EYVLRPSYNG SFTNPEVRRF RYRTTMTRER SASLYSPSST 200
VSRRTTTPPD SGVLFEGLGI STRPRDVDIP QFMRQMALRG PTTTDERSLR 250
KIQEQDIINF RRTLYRAGVR VRSIEDGGRY RDISAEFFRR NPACLHRLVP 300
WLKRELTVLF GAHGSLVNIV QHIIMSNVTR YDLESQAFVS DLRPFLLNRT 350
EHFIHEFISF ARSPFNMAAF DQHANYDCPP SSEEGSRSDS SVITISPDEA 400
ETQELDMNAS TVRQAPWDDE TPGPSYSSSE QVHVGVSSLL NSSDSSDEEL 450
VSGGTTSQIQ GVQTNDDVNN DSDSSSDNCV IVGFVKPLAE RTPELVELSS 500
DSEELGPYEK VETVKTQEQE QSYSSGDSDV SRASSPRSVL GKDEQMSKSH 550
CDSDTRISSK KEEKRSTSLP APRDSSSTRG DRVCSPYNHR HRKGGRSRSS 600
DSRSQSRSGH DPRNHRKHGK KRLRNKRSRS RESSSRPRAR KDKKRSRTRD 650
SSWSRRSQTL SLSSGSTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSKY 700
KWEYTYYSRN KDRDGYESSY RRRTLSRAHY SRQSSSPEFR IQSFSERTNA 750
RKKNHSERKY YYYERRRSRS VSSNRSRTTS AGPDRVRNEK PGGKRKYKTR 800
HLEGTSEEAQ PAREFTSKGK DSHYQKSKLD GSYKNESDSF SDSRSSDRET 850
KHKRRRRRTR SLSVEIVYEG KATDTSKHHK KKKKKHKKKH KKHHGDNTSR 900
SPVVITIDSD SDGESEVKAG IECSNGSLPQ PIQDGAFETK DVVTIEDELG 950
VLDKDCDVTA LADDLSTSQT VENCDSPAVP VEQTLDVREE STFASDLESQ 1000
SSNVSIQAEP SRPVPSPRTS LSSVSPGRDC DVS 1033
Length:1,033
Mass (Da):117,082
Last modified:June 1, 2003 - v1
Checksum:i3A99C00491D7EFD2
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401S → F in BAB69457. 1 Publication
Sequence conflicti623 – 6231L → P in AAH40797. 1 Publication
Sequence conflicti657 – 6571S → A in BAB69457. 1 Publication
Sequence conflicti682 – 6821S → A in AAH40797. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS38710.1.
RefSeqiNP_598858.2. NM_134097.3.
UniGeneiMm.251548.

Genome annotation databases

EnsembliENSMUST00000042575; ENSMUSP00000046843; ENSMUSG00000036822.
GeneIDi106021.
KEGGimmu:106021.
UCSCiuc008shi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS38710.1.
RefSeqi NP_598858.2. NM_134097.3.
UniGenei Mm.251548.

3D structure databases

ProteinModelPortali Q80Z37.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 222976. 2 interactions.
IntActi Q80Z37. 1 interaction.
MINTi MINT-1789728.
STRINGi 10090.ENSMUSP00000046843.

PTM databases

PhosphoSitei Q80Z37.

Proteomic databases

PRIDEi Q80Z37.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000042575 ; ENSMUSP00000046843 ; ENSMUSG00000036822 .
GeneIDi 106021.
KEGGi mmu:106021.
UCSCi uc008shi.1. mouse.

Organism-specific databases

CTDi 10210.
MGIi MGI:2146189. Topors.

Phylogenomic databases

eggNOGi NOG244178.
GeneTreei ENSGT00530000064170.
HOVERGENi HBG080410.
InParanoidi Q80Z37.
KOi K10631.
OMAi LLNRTEH.
OrthoDBi EOG722J8G.
PhylomeDBi Q80Z37.
TreeFami TF339497.

Miscellaneous databases

NextBioi 358016.
PROi Q80Z37.
SOURCEi Search...

Gene expression databases

Bgeei Q80Z37.
CleanExi MM_TOPORS.
Genevestigatori Q80Z37.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTOPRS_MOUSE
AccessioniPrimary (citable) accession number: Q80Z37
Secondary accession number(s): Q3U5B5
, Q3UPZ1, Q3USN3, Q3UZ55, Q8BXP2, Q8CFF5, Q8CGC8, Q920L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi