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Protein

E3 ubiquitin/ISG15 ligase TRIM25

Gene

Trim25

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3.By similarity

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.By similarity
ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri13 – 54RING-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase, Transferase
Biological processAntiviral defense, Immunity, Innate immunity, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1169408 ISG15 antiviral mechanism
R-MMU-5656169 Termination of translesion DNA synthesis
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin/ISG15 ligase TRIM25 (EC:6.3.2.n3By similarity)
Alternative name(s):
Estrogen-responsive finger protein
RING-type E3 ubiquitin transferase (EC:2.3.2.27By similarity)
RING-type E3 ubiquitin transferase TRIM25Curated
Tripartite motif-containing protein 25
Ubiquitin/ISG15-conjugating enzyme TRIM25
Zinc finger protein 147
Gene namesi
Name:Trim25
Synonyms:Efp, Zfp147, Znf147
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:102749 Trim25

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000562341 – 634E3 ubiquitin/ISG15 ligase TRIM25Add BLAST634

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei90PhosphothreonineBy similarity1
Modified residuei99PhosphoserineBy similarity1
Cross-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)By similarity
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei277PhosphotyrosineBy similarity1
Modified residuei572N6-acetyllysineBy similarity1

Post-translational modificationi

Auto-ISGylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ61510
MaxQBiQ61510
PaxDbiQ61510
PeptideAtlasiQ61510
PRIDEiQ61510

PTM databases

iPTMnetiQ61510
PhosphoSitePlusiQ61510
SwissPalmiQ61510

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSMUSG00000000275
CleanExiMM_TRIM25
ExpressionAtlasiQ61510 baseline and differential
GenevisibleiQ61510 MM

Interactioni

Subunit structurei

Interacts (via SPRY domain) with DDX58 (via CARD domain). Interacts with ZFHX3.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229840, 3 interactors
IntActiQ61510, 4 interactors
MINTiQ61510
STRINGi10090.ENSMUSP00000103528

Structurei

Secondary structure

1634
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi441 – 450Combined sources10
Helixi454 – 457Combined sources4
Helixi458 – 460Combined sources3
Turni468 – 470Combined sources3
Beta strandi475 – 478Combined sources4
Turni479 – 482Combined sources4
Beta strandi483 – 486Combined sources4
Beta strandi501 – 509Combined sources9
Beta strandi514 – 523Combined sources10
Beta strandi528 – 535Combined sources8
Beta strandi540 – 542Combined sources3
Helixi543 – 545Combined sources3
Beta strandi553 – 559Combined sources7
Beta strandi562 – 567Combined sources6
Beta strandi570 – 574Combined sources5
Beta strandi581 – 587Combined sources7
Turni588 – 591Combined sources4
Beta strandi592 – 609Combined sources18
Beta strandi616 – 624Combined sources9
Beta strandi628 – 631Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B8EX-ray1.78A/B440-634[»]
ProteinModelPortaliQ61510
SMRiQ61510
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini444 – 634B30.2/SPRYPROSITE-ProRule annotationAdd BLAST191

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili215 – 305Sequence analysisAdd BLAST91

Domaini

The RING-type zinc finger is important for ISG15 E3 ligase activity and autoISGylation. AutoISGylation negatively regulates ISG15 E3 ligase activity.By similarity
The C-terminal B30.2/SPRY domain interacts with the first N-terminal CARD domain of DDX58.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri13 – 54RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITFP Eukaryota
ENOG410XQS1 LUCA
GeneTreeiENSGT00760000118995
HOGENOMiHOG000132974
HOVERGENiHBG101063
InParanoidiQ61510
KOiK10652
OMAiSPAFQDH
OrthoDBiEOG091G05F6
TreeFamiTF351086

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR003879 Butyrophylin_SPRY
IPR013320 ConA-like_dom_sf
IPR006574 PRY
IPR003877 SPRY_dom
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF13765 PRY, 1 hit
PF00622 SPRY, 1 hit
PRINTSiPR01407 BUTYPHLNCDUF
SMARTiView protein in SMART
SM00589 PRY, 1 hit
SM00184 RING, 1 hit
SM00449 SPRY, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q61510-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELNPLAEE LSCSVCLELF KEPVTTPCGH NFCMSCLDET WVVQGPPYRC
60 70 80 90 100
PQCRKVYQVR PQLQKNTVMC AVVEQFLQAE QARTPVDDWT PPARFSASSA
110 120 130 140 150
ATQVACDHCL TEIAVKTCLV CMASFCQEHL RPHFDSPAFQ DHPLQSPIRD
160 170 180 190 200
LLRRKCTQHN RLRELFCPEH GECICHICLV EHKTCSPTTL SQASADLEYK
210 220 230 240 250
LRNKLTIMHS HINGATKALE DVRSKQQCVQ DSMKRKMEQL RQEYMEMKAV
260 270 280 290 300
IDAAETSSLR KLKEEEKRVY GKFDTIYQVL VKKKSEMQKL KAEVELIMDK
310 320 330 340 350
GDEFEFLEKA AKLQGESTKP VYIPKIDLDH DLIMGIYQGA ADLKSELKHS
360 370 380 390 400
IKKLQKKSEE HNGSGNKGDQ TQSTFKPVQP SKKTIQEKKT KKTPVAPGPP
410 420 430 440 450
SHFSPNKLPT FGAPGQSLDS KATSPDAAPK ASAAQPDSVG VKAKVLENFL
460 470 480 490 500
TKSRTELLEY FVKVIFDYNT AHNKVSLSNK YTTASVSDGL QHYRSHPQRF
510 520 530 540 550
TYCSQVLGLH CYKNGIHYWE VELQKNNFCG VGICYGSMER QGPESRLGRN
560 570 580 590 600
PNSWCVEWFN NKISAWHNNV EKTLPSTKAT RVGVLLNCDH GFVIFFAVTE
610 620 630
KVHLMYKFKV DFTEALYPAF WVFSAGTTLS ICSK
Length:634
Mass (Da):71,726
Last modified:July 27, 2011 - v2
Checksum:i3B764531AAE8582E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34M → T in BAA09941 (PubMed:7592654).Curated1
Sequence conflicti165L → F in BAA09941 (PubMed:7592654).Curated1
Sequence conflicti261K → R in BAA09941 (PubMed:7592654).Curated1
Sequence conflicti439V → I in BAA09941 (PubMed:7592654).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63902 mRNA Translation: BAA09941.1
AK169562 mRNA Translation: BAE41230.1
AL646096 Genomic DNA No translation available.
CCDSiCCDS36278.1
PIRiI49642
RefSeqiNP_033572.2, NM_009546.2
UniGeneiMm.248445

Genome annotation databases

EnsembliENSMUST00000107896; ENSMUSP00000103528; ENSMUSG00000000275
GeneIDi217069
KEGGimmu:217069
UCSCiuc007kwc.1 mouse

Similar proteinsi

Entry informationi

Entry nameiTRI25_MOUSE
AccessioniPrimary (citable) accession number: Q61510
Secondary accession number(s): Q5SU70
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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