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Protein

E3 ubiquitin/ISG15 ligase TRIM25

Gene

Trim25

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity).By similarity

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine.

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 5442RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_275137. TRAF6 mediated NF-kB activation.
REACT_289760. Negative regulators of RIG-I/MDA5 signaling.
REACT_308796. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_311325. TRAF3-dependent IRF activation pathway.
REACT_311354. TRAF6 mediated IRF7 activation.
REACT_332213. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_349056. Interferon gamma signaling.
REACT_362050. Termination of translesion DNA synthesis.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin/ISG15 ligase TRIM25 (EC:6.3.2.19, EC:6.3.2.n3)
Alternative name(s):
Estrogen-responsive finger protein
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:102749. Trim25.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Colocalized with DDX58 at cytoplasmic perinuclear bodies.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 634634E3 ubiquitin/ISG15 ligase TRIM25PRO_0000056234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991PhosphoserineBy similarity
Cross-linki116 – 116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)By similarity
Modified residuei272 – 2721N6-acetyllysineBy similarity
Modified residuei277 – 2771PhosphotyrosineBy similarity
Modified residuei572 – 5721N6-acetyllysineBy similarity

Post-translational modificationi

Auto-ISGylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61510.
PaxDbiQ61510.
PRIDEiQ61510.

PTM databases

PhosphoSiteiQ61510.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ61510.
CleanExiMM_TRIM25.
ExpressionAtlasiQ61510. baseline and differential.
GenevisibleiQ61510. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi229840. 11 interactions.
IntActiQ61510. 3 interactions.
MINTiMINT-240797.
STRINGi10090.ENSMUSP00000103528.

Structurei

Secondary structure

1
634
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi441 – 45010Combined sources
Helixi454 – 4574Combined sources
Helixi458 – 4603Combined sources
Turni468 – 4703Combined sources
Beta strandi475 – 4784Combined sources
Turni479 – 4824Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi501 – 5099Combined sources
Beta strandi514 – 52310Combined sources
Beta strandi528 – 5358Combined sources
Beta strandi540 – 5423Combined sources
Helixi543 – 5453Combined sources
Beta strandi553 – 5597Combined sources
Beta strandi562 – 5676Combined sources
Beta strandi570 – 5745Combined sources
Beta strandi581 – 5877Combined sources
Turni588 – 5914Combined sources
Beta strandi592 – 60918Combined sources
Beta strandi616 – 6249Combined sources
Beta strandi628 – 6314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B8EX-ray1.78A/B440-634[»]
ProteinModelPortaliQ61510.
SMRiQ61510. Positions 4-53, 156-356, 440-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 634191B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili215 – 30591Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 5442RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG253760.
GeneTreeiENSGT00760000118995.
HOGENOMiHOG000132974.
HOVERGENiHBG101063.
InParanoidiQ61510.
KOiK10652.
OMAiEANSTRK.
OrthoDBiEOG7CG6ZK.
TreeFamiTF351086.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341M → T in BAA09941 (PubMed:7592654).Curated
Sequence conflicti165 – 1651L → F in BAA09941 (PubMed:7592654).Curated
Sequence conflicti261 – 2611K → R in BAA09941 (PubMed:7592654).Curated
Sequence conflicti439 – 4391V → I in BAA09941 (PubMed:7592654).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63902 mRNA. Translation: BAA09941.1.
AK169562 mRNA. Translation: BAE41230.1.
AL646096 Genomic DNA. Translation: CAI24266.1.
CCDSiCCDS36278.1.
PIRiI49642.
RefSeqiNP_033572.2. NM_009546.2.
UniGeneiMm.248445.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63902 mRNA. Translation: BAA09941.1.
AK169562 mRNA. Translation: BAE41230.1.
AL646096 Genomic DNA. Translation: CAI24266.1.
CCDSiCCDS36278.1.
PIRiI49642.
RefSeqiNP_033572.2. NM_009546.2.
UniGeneiMm.248445.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B8EX-ray1.78A/B440-634[»]
ProteinModelPortaliQ61510.
SMRiQ61510. Positions 4-53, 156-356, 440-633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229840. 11 interactions.
IntActiQ61510. 3 interactions.
MINTiMINT-240797.
STRINGi10090.ENSMUSP00000103528.

PTM databases

PhosphoSiteiQ61510.

Proteomic databases

MaxQBiQ61510.
PaxDbiQ61510.
PRIDEiQ61510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7706.
MGIiMGI:102749. Trim25.

Phylogenomic databases

eggNOGiNOG253760.
GeneTreeiENSGT00760000118995.
HOGENOMiHOG000132974.
HOVERGENiHBG101063.
InParanoidiQ61510.
KOiK10652.
OMAiEANSTRK.
OrthoDBiEOG7CG6ZK.
TreeFamiTF351086.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_275137. TRAF6 mediated NF-kB activation.
REACT_289760. Negative regulators of RIG-I/MDA5 signaling.
REACT_308796. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_311325. TRAF3-dependent IRF activation pathway.
REACT_311354. TRAF6 mediated IRF7 activation.
REACT_332213. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_349056. Interferon gamma signaling.
REACT_362050. Termination of translesion DNA synthesis.

Miscellaneous databases

NextBioi375545.
PROiQ61510.
SOURCEiSearch...

Gene expression databases

BgeeiQ61510.
CleanExiMM_TRIM25.
ExpressionAtlasiQ61510. baseline and differential.
GenevisibleiQ61510. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, structure, and expression of mouse estrogen-responsive finger protein Efp. Co-localization with estrogen receptor mRNA in target organs."
    Orimo A., Inoue S., Ikeda K., Noji S., Muramatsu M.
    J. Biol. Chem. 270:24406-24413(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Ovary, Placenta and Uterus.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiTRI25_MOUSE
AccessioniPrimary (citable) accession number: Q61510
Secondary accession number(s): Q5SU70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 132 of the entry and version 2 of the sequence. [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
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.