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Q61510

- TRI25_MOUSE

UniProt

Q61510 - TRI25_MOUSE

Protein

E3 ubiquitin/ISG15 ligase TRIM25

Gene

Trim25

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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.

    Pathwayi

    Regions

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

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. innate immune response Source: UniProt
    3. negative regulation of viral entry into host cell Source: UniProt
    4. negative regulation of viral release from host cell Source: UniProt
    5. protein ubiquitination Source: UniProtKB-UniPathway
    6. response to estrogen Source: Ensembl
    7. response to vitamin D Source: Ensembl

    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_198521. TRAF6 mediated IRF7 activation.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    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: 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

    1. cell junction Source: Ensembl
    2. cytoplasm Source: MGI
    3. nucleus Source: Ensembl

    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 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

    ArrayExpressiQ61510.
    BgeeiQ61510.
    CleanExiMM_TRIM25.
    GenevestigatoriQ61510.

    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 – 45010
    Helixi454 – 4574
    Helixi458 – 4603
    Turni468 – 4703
    Beta strandi475 – 4784
    Turni479 – 4824
    Beta strandi483 – 4864
    Beta strandi501 – 5099
    Beta strandi514 – 52310
    Beta strandi528 – 5358
    Beta strandi540 – 5423
    Helixi543 – 5453
    Beta strandi553 – 5597
    Beta strandi562 – 5676
    Beta strandi570 – 5745
    Beta strandi581 – 5877
    Turni588 – 5914
    Beta strandi592 – 60918
    Beta strandi616 – 6249
    Beta strandi628 – 6314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B8EX-ray1.78A/B440-634[»]
    ProteinModelPortaliQ61510.
    SMRiQ61510. Positions 4-53, 189-356, 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.
    GeneTreeiENSGT00730000110450.
    HOGENOMiHOG000132974.
    HOVERGENiHBG101063.
    InParanoidiQ5SU70.
    KOiK10652.
    OMAiEANSTRK.
    OrthoDBiEOG7CG6ZK.
    TreeFamiTF351086.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001870. 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]
    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

    MAELNPLAEE LSCSVCLELF KEPVTTPCGH NFCMSCLDET WVVQGPPYRC    50
    PQCRKVYQVR PQLQKNTVMC AVVEQFLQAE QARTPVDDWT PPARFSASSA 100
    ATQVACDHCL TEIAVKTCLV CMASFCQEHL RPHFDSPAFQ DHPLQSPIRD 150
    LLRRKCTQHN RLRELFCPEH GECICHICLV EHKTCSPTTL SQASADLEYK 200
    LRNKLTIMHS HINGATKALE DVRSKQQCVQ DSMKRKMEQL RQEYMEMKAV 250
    IDAAETSSLR KLKEEEKRVY GKFDTIYQVL VKKKSEMQKL KAEVELIMDK 300
    GDEFEFLEKA AKLQGESTKP VYIPKIDLDH DLIMGIYQGA ADLKSELKHS 350
    IKKLQKKSEE HNGSGNKGDQ TQSTFKPVQP SKKTIQEKKT KKTPVAPGPP 400
    SHFSPNKLPT FGAPGQSLDS KATSPDAAPK ASAAQPDSVG VKAKVLENFL 450
    TKSRTELLEY FVKVIFDYNT AHNKVSLSNK YTTASVSDGL QHYRSHPQRF 500
    TYCSQVLGLH CYKNGIHYWE VELQKNNFCG VGICYGSMER QGPESRLGRN 550
    PNSWCVEWFN NKISAWHNNV EKTLPSTKAT RVGVLLNCDH GFVIFFAVTE 600
    KVHLMYKFKV DFTEALYPAF WVFSAGTTLS ICSK 634
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63902 mRNA. Translation: BAA09941.1 .
    AK169562 mRNA. Translation: BAE41230.1 .
    AL646096 Genomic DNA. Translation: CAI24266.1 .
    CCDSi CCDS36278.1.
    PIRi I49642.
    RefSeqi NP_033572.2. NM_009546.2.
    UniGenei Mm.248445.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B8E X-ray 1.78 A/B 440-634 [» ]
    ProteinModelPortali Q61510.
    SMRi Q61510. Positions 4-53, 189-356, 440-633.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229840. 11 interactions.
    IntActi Q61510. 3 interactions.
    MINTi MINT-240797.
    STRINGi 10090.ENSMUSP00000103528.

    PTM databases

    PhosphoSitei Q61510.

    Proteomic databases

    MaxQBi Q61510.
    PaxDbi Q61510.
    PRIDEi Q61510.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000107896 ; ENSMUSP00000103528 ; ENSMUSG00000000275 .
    GeneIDi 217069.
    KEGGi mmu:217069.
    UCSCi uc007kwc.1. mouse.

    Organism-specific databases

    CTDi 7706.
    MGIi MGI:102749. Trim25.

    Phylogenomic databases

    eggNOGi NOG253760.
    GeneTreei ENSGT00730000110450.
    HOGENOMi HOG000132974.
    HOVERGENi HBG101063.
    InParanoidi Q5SU70.
    KOi K10652.
    OMAi EANSTRK.
    OrthoDBi EOG7CG6ZK.
    TreeFami TF351086.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Miscellaneous databases

    NextBioi 375545.
    PROi Q61510.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61510.
    Bgeei Q61510.
    CleanExi MM_TRIM25.
    Genevestigatori Q61510.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001870. 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 ]
    Pfami PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00589. PRY. 1 hit.
    SM00184. RING. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 124 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