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Protein

E3 ubiquitin-protein ligase Topors

Gene

Topors

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri104 – 143RING-typePROSITE-ProRule annotationAdd BLAST40

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2146189. Topors.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: MGI
  • ciliary basal body Source: BHF-UCL
  • gamma-tubulin complex Source: MGI
  • nuclear speck Source: UniProtKB
  • nucleus Source: UniProtKB
  • photoreceptor connecting cilium Source: BHF-UCL
  • PML body Source: UniProtKB
  • spindle pole Source: MGI
  • ubiquitin ligase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002326271 – 1033E3 ubiquitin-protein ligase ToporsAdd BLAST1033

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei99PhosphoserineCombined sources1
Modified residuei196PhosphoserineBy similarity1
Cross-linki251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei500PhosphoserineBy similarity1
Cross-linki561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei585PhosphoserineBy similarity1
Cross-linki701Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei718Phosphoserine; by PLK1By similarity1
Modified residuei734PhosphoserineBy similarity1
Modified residuei861PhosphoserineCombined sources1
Modified residuei863PhosphoserineCombined sources1
Modified residuei909PhosphoserineCombined sources1
Modified residuei911PhosphoserineCombined sources1
Modified residuei999PhosphoserineCombined sources1
Modified residuei1016PhosphoserineCombined sources1
Modified residuei1025PhosphoserineCombined sources1

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).By similarity
Sumoylated.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ80Z37.
MaxQBiQ80Z37.
PaxDbiQ80Z37.
PeptideAtlasiQ80Z37.
PRIDEiQ80Z37.

PTM databases

iPTMnetiQ80Z37.
PhosphoSitePlusiQ80Z37.

Expressioni

Inductioni

By genotoxic agents such as cisplatin and camptothecin.1 Publication

Gene expression databases

BgeeiENSMUSG00000036822.
CleanExiMM_TOPORS.
GenevisibleiQ80Z37. MM.

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.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi222976. 3 interactors.
IntActiQ80Z37. 1 interactor.
MINTiMINT-1789728.
STRINGi10090.ENSMUSP00000046843.

Structurei

3D structure databases

ProteinModelPortaliQ80Z37.
SMRiQ80Z37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 376Required for DNA-bindingBy similarityAdd BLAST325
Regioni438 – 654Interaction with SUMO1By similarityAdd BLAST217
Regioni438 – 574Sumoylation and localization to discrete nuclear fociBy similarityAdd BLAST137
Regioni457 – 879Interaction with TOP1By similarityAdd BLAST423
Regioni457 – 731Interaction with p53/TP53By similarityAdd BLAST275
Regioni851 – 914Interaction with UBE2IBy similarityAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi579 – 787Arg-richAdd BLAST209
Compositional biasi877 – 892Lys-richAdd BLAST16

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri104 – 143RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4430. Eukaryota.
ENOG410XQZR. LUCA.
GeneTreeiENSGT00530000064170.
HOVERGENiHBG080410.
InParanoidiQ80Z37.
KOiK10631.
OMAiDIINFRR.
OrthoDBiEOG091G089U.
PhylomeDBiQ80Z37.
TreeFamiTF339497.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[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

        10         20         30         40         50
MGSQPPPPGS PLSREEGEAP PLVPAEEGRR RSRRVRLRGS CRHRPSLLSR
60 70 80 90 100
RELASNGPAV PATASSEIMA SAAKEFKMDN FSPKAGTSKL QQTVPADASP
110 120 130 140 150
DSKCPICLDR FDNVSYLDRC LHKFCFRCVQ EWSKNKAECP LCKQPFDSIF
160 170 180 190 200
HSVRAEDDFK EYVLRPSYNG SFTNPEVRRF RYRTTMTRER SASLYSPSST
210 220 230 240 250
VSRRTTTPPD SGVLFEGLGI STRPRDVDIP QFMRQMALRG PTTTDERSLR
260 270 280 290 300
KIQEQDIINF RRTLYRAGVR VRSIEDGGRY RDISAEFFRR NPACLHRLVP
310 320 330 340 350
WLKRELTVLF GAHGSLVNIV QHIIMSNVTR YDLESQAFVS DLRPFLLNRT
360 370 380 390 400
EHFIHEFISF ARSPFNMAAF DQHANYDCPP SSEEGSRSDS SVITISPDEA
410 420 430 440 450
ETQELDMNAS TVRQAPWDDE TPGPSYSSSE QVHVGVSSLL NSSDSSDEEL
460 470 480 490 500
VSGGTTSQIQ GVQTNDDVNN DSDSSSDNCV IVGFVKPLAE RTPELVELSS
510 520 530 540 550
DSEELGPYEK VETVKTQEQE QSYSSGDSDV SRASSPRSVL GKDEQMSKSH
560 570 580 590 600
CDSDTRISSK KEEKRSTSLP APRDSSSTRG DRVCSPYNHR HRKGGRSRSS
610 620 630 640 650
DSRSQSRSGH DPRNHRKHGK KRLRNKRSRS RESSSRPRAR KDKKRSRTRD
660 670 680 690 700
SSWSRRSQTL SLSSGSTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSKY
710 720 730 740 750
KWEYTYYSRN KDRDGYESSY RRRTLSRAHY SRQSSSPEFR IQSFSERTNA
760 770 780 790 800
RKKNHSERKY YYYERRRSRS VSSNRSRTTS AGPDRVRNEK PGGKRKYKTR
810 820 830 840 850
HLEGTSEEAQ PAREFTSKGK DSHYQKSKLD GSYKNESDSF SDSRSSDRET
860 870 880 890 900
KHKRRRRRTR SLSVEIVYEG KATDTSKHHK KKKKKHKKKH KKHHGDNTSR
910 920 930 940 950
SPVVITIDSD SDGESEVKAG IECSNGSLPQ PIQDGAFETK DVVTIEDELG
960 970 980 990 1000
VLDKDCDVTA LADDLSTSQT VENCDSPAVP VEQTLDVREE STFASDLESQ
1010 1020 1030
SSNVSIQAEP SRPVPSPRTS LSSVSPGRDC DVS
Length:1,033
Mass (Da):117,082
Last modified:June 1, 2003 - v1
Checksum:i3A99C00491D7EFD2
GO

Sequence cautioni

The sequence AAH37141 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40S → F in BAB69457 (PubMed:15703819).Curated1
Sequence conflicti623L → P in AAH40797 (PubMed:15489334).Curated1
Sequence conflicti657S → A in BAB69457 (PubMed:15703819).Curated1
Sequence conflicti682S → A in AAH40797 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ80Z37.
SMRiQ80Z37.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222976. 3 interactors.
IntActiQ80Z37. 1 interactor.
MINTiMINT-1789728.
STRINGi10090.ENSMUSP00000046843.

PTM databases

iPTMnetiQ80Z37.
PhosphoSitePlusiQ80Z37.

Proteomic databases

EPDiQ80Z37.
MaxQBiQ80Z37.
PaxDbiQ80Z37.
PeptideAtlasiQ80Z37.
PRIDEiQ80Z37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10210.
MGIiMGI:2146189. Topors.

Phylogenomic databases

eggNOGiKOG4430. Eukaryota.
ENOG410XQZR. LUCA.
GeneTreeiENSGT00530000064170.
HOVERGENiHBG080410.
InParanoidiQ80Z37.
KOiK10631.
OMAiDIINFRR.
OrthoDBiEOG091G089U.
PhylomeDBiQ80Z37.
TreeFamiTF339497.

Miscellaneous databases

PROiQ80Z37.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000036822.
CleanExiMM_TOPORS.
GenevisibleiQ80Z37. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 114 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.