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Q61510 (TRI25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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/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 names
Name:Trim25
Synonyms:Efp, Zfp147, Znf147
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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

Subcellular location

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

Tissue specificity

Ubiquitous. Ref.1

Domain

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.

Post-translational modification

Auto-ISGylated By similarity.

Sequence similarities

Contains 1 B30.2/SPRY domain.

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 634634E3 ubiquitin/ISG15 ligase TRIM25
PRO_0000056234

Regions

Domain444 – 634191B30.2/SPRY
Zinc finger13 – 5442RING-type
Coiled coil215 – 30591 Potential

Amino acid modifications

Modified residue991Phosphoserine By similarity
Modified residue2721N6-acetyllysine By similarity
Modified residue5721N6-acetyllysine By similarity
Cross-link116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) By similarity

Experimental info

Sequence conflict341M → T in BAA09941. Ref.1
Sequence conflict1651L → F in BAA09941. Ref.1
Sequence conflict2611K → R in BAA09941. Ref.1
Sequence conflict4391V → I in BAA09941. Ref.1

Secondary structure

................................... 634
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61510 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 3B764531AAE8582E

FASTA63471,726
        10         20         30         40         50         60 
MAELNPLAEE LSCSVCLELF KEPVTTPCGH NFCMSCLDET WVVQGPPYRC PQCRKVYQVR 

        70         80         90        100        110        120 
PQLQKNTVMC AVVEQFLQAE QARTPVDDWT PPARFSASSA ATQVACDHCL TEIAVKTCLV 

       130        140        150        160        170        180 
CMASFCQEHL RPHFDSPAFQ DHPLQSPIRD LLRRKCTQHN RLRELFCPEH GECICHICLV 

       190        200        210        220        230        240 
EHKTCSPTTL SQASADLEYK LRNKLTIMHS HINGATKALE DVRSKQQCVQ DSMKRKMEQL 

       250        260        270        280        290        300 
RQEYMEMKAV IDAAETSSLR KLKEEEKRVY GKFDTIYQVL VKKKSEMQKL KAEVELIMDK 

       310        320        330        340        350        360 
GDEFEFLEKA AKLQGESTKP VYIPKIDLDH DLIMGIYQGA ADLKSELKHS IKKLQKKSEE 

       370        380        390        400        410        420 
HNGSGNKGDQ TQSTFKPVQP SKKTIQEKKT KKTPVAPGPP SHFSPNKLPT FGAPGQSLDS 

       430        440        450        460        470        480 
KATSPDAAPK ASAAQPDSVG VKAKVLENFL TKSRTELLEY FVKVIFDYNT AHNKVSLSNK 

       490        500        510        520        530        540 
YTTASVSDGL QHYRSHPQRF TYCSQVLGLH CYKNGIHYWE VELQKNNFCG VGICYGSMER 

       550        560        570        580        590        600 
QGPESRLGRN PNSWCVEWFN NKISAWHNNV EKTLPSTKAT RVGVLLNCDH GFVIFFAVTE 

       610        620        630 
KVHLMYKFKV DFTEALYPAF WVFSAGTTLS ICSK 

« Hide

References

« Hide 'large scale' references
[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. 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].
Strain: C57BL/6J.
Tissue: Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63902 mRNA. Translation: BAA09941.1.
AK169562 mRNA. Translation: BAE41230.1.
AL646096 Genomic DNA. Translation: CAI24266.1.
CCDSCCDS36278.1.
PIRI49642.
RefSeqNP_033572.2. NM_009546.2.
UniGeneMm.248445.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B8EX-ray1.78A/B440-634[»]
ProteinModelPortalQ61510.
SMRQ61510. Positions 4-53, 189-356, 440-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229840. 11 interactions.
IntActQ61510. 3 interactions.
MINTMINT-240797.
STRING10090.ENSMUSP00000103528.

PTM databases

PhosphoSiteQ61510.

Proteomic databases

MaxQBQ61510.
PaxDbQ61510.
PRIDEQ61510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000107896; ENSMUSP00000103528; ENSMUSG00000000275.
GeneID217069.
KEGGmmu:217069.
UCSCuc007kwc.1. mouse.

Organism-specific databases

CTD7706.
MGIMGI:102749. Trim25.

Phylogenomic databases

eggNOGNOG253760.
GeneTreeENSGT00730000110450.
HOGENOMHOG000132974.
HOVERGENHBG101063.
InParanoidQ5SU70.
KOK10652.
OMAEANSTRK.
OrthoDBEOG7CG6ZK.
TreeFamTF351086.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ61510.
BgeeQ61510.
CleanExMM_TRIM25.
GenevestigatorQ61510.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio375545.
PROQ61510.
SOURCESearch...

Entry information

Entry nameTRI25_MOUSE
AccessionPrimary (citable) accession number: Q61510
Secondary accession number(s): Q5SU70
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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