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Protein

Tripartite motif-containing protein 59

Gene

Trim59

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May serve as a multifunctional regulator for innate immune signaling pathways.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 6051RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 13443B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • innate immune response Source: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • negative regulation of viral entry into host cell Source: UniProtKB
  • protein ubiquitination Source: GOC
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite motif-containing protein 59
Alternative name(s):
RING finger protein 1
Gene namesi
Name:Trim59
Synonyms:Mrf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1914199. Trim59.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei329 – 34921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Tripartite motif-containing protein 59PRO_0000249680Add
BLAST

Proteomic databases

EPDiQ922Y2.
MaxQBiQ922Y2.
PaxDbiQ922Y2.
PRIDEiQ922Y2.

PTM databases

PhosphoSiteiQ922Y2.

Expressioni

Tissue specificityi

Moderately expressed in the spleen, brain and heart and very highly expressed in the testis (PubMed:12095697).1 Publication

Gene expression databases

BgeeiQ922Y2.
CleanExiMM_TRIM59.
ExpressionAtlasiQ922Y2. baseline and differential.
GenevisibleiQ922Y2. MM.

Interactioni

Subunit structurei

Interacts with ECSIT (PubMed:22588174).1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000103432.

Structurei

3D structure databases

ProteinModelPortaliQ922Y2.
SMRiQ922Y2. Positions 2-155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili163 – 24684Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 6051RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 13443B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITG5. Eukaryota.
ENOG410YH9X. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000013095.
HOVERGENiHBG060002.
InParanoidiQ922Y2.
KOiK12028.
OMAiKEFMWKI.
OrthoDBiEOG7KWSHJ.
TreeFamiTF331669.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q922Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHNFEEELTC PICYSIFEDP RVLPCSHTFC RNCLENVLQA SGNFYIWRPL
60 70 80 90 100
RIPLKCPNCR SIIEIASTGI ESLPVNFALR AIIEKYQQED HPDVVTCPEH
110 120 130 140 150
YRQPLNVYCL LDKKLVCGHC LTIGQHHGHP IDDLQSAYLK EKDTPQKLLK
160 170 180 190 200
QLTDTHWTDI TRLIEKLEEQ KCHSEKIVQG DKEVVLQYFK ELIDTLEQKK
210 220 230 240 250
KYFLAALCDV GKMINQEYTP QIQGMKEIRE QQLELMTITT SLQDESPLKF
260 270 280 290 300
LEKIDEVRQR VQMLKQRPLP EVQPVEIYPR VSNVLKEEWS RIEIGRIKKA
310 320 330 340 350
VIPEMRVSSK RTPCSWSDND EKEMELFKIL NIAIVSLISV ILMLILLFNH
360 370 380 390 400
HIITFLNEIT SICFSEVFLS VYQSLSKNLY DLNNTVCYTL YLLKEFMWKI

VSR
Length:403
Mass (Da):47,238
Last modified:July 27, 2011 - v2
Checksum:i60AF4F97398DDDBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531P → E in BAB30354 (PubMed:16141072).Curated
Sequence conflicti57 – 571P → A in BAB30354 (PubMed:16141072).Curated
Sequence conflicti61 – 611S → N in BAB30354 (PubMed:16141072).Curated
Sequence conflicti68 – 681T → S in BAB30354 (PubMed:16141072).Curated
Sequence conflicti71 – 711E → K in BAB30354 (PubMed:16141072).Curated
Sequence conflicti75 – 751V → I in BAB30354 (PubMed:16141072).Curated
Sequence conflicti96 – 961T → S in BAB30354 (PubMed:16141072).Curated
Sequence conflicti128 – 1281G → V in BAB30354 (PubMed:16141072).Curated
Sequence conflicti193 – 1931I → T in AAH06700 (PubMed:15489334).Curated
Sequence conflicti193 – 1931I → T in AAH25430 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009637 mRNA. Translation: BAB26408.2.
AK012269 mRNA. Translation: BAB28131.1.
AK016642 mRNA. Translation: BAB30354.1.
AC122876 Genomic DNA. No translation available.
BC006700 mRNA. Translation: AAH06700.1.
BC025430 mRNA. Translation: AAH25430.1.
CCDSiCCDS17402.1.
RefSeqiNP_080139.3. NM_025863.3.
XP_006501980.1. XM_006501917.2.
XP_011238502.1. XM_011240200.1.
XP_011238503.1. XM_011240201.1.
UniGeneiMm.176695.

Genome annotation databases

EnsembliENSMUST00000107802; ENSMUSP00000103432; ENSMUSG00000034317.
GeneIDi66949.
KEGGimmu:66949.
UCSCiuc008pmd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009637 mRNA. Translation: BAB26408.2.
AK012269 mRNA. Translation: BAB28131.1.
AK016642 mRNA. Translation: BAB30354.1.
AC122876 Genomic DNA. No translation available.
BC006700 mRNA. Translation: AAH06700.1.
BC025430 mRNA. Translation: AAH25430.1.
CCDSiCCDS17402.1.
RefSeqiNP_080139.3. NM_025863.3.
XP_006501980.1. XM_006501917.2.
XP_011238502.1. XM_011240200.1.
XP_011238503.1. XM_011240201.1.
UniGeneiMm.176695.

3D structure databases

ProteinModelPortaliQ922Y2.
SMRiQ922Y2. Positions 2-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000103432.

PTM databases

PhosphoSiteiQ922Y2.

Proteomic databases

EPDiQ922Y2.
MaxQBiQ922Y2.
PaxDbiQ922Y2.
PRIDEiQ922Y2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000107802; ENSMUSP00000103432; ENSMUSG00000034317.
GeneIDi66949.
KEGGimmu:66949.
UCSCiuc008pmd.2. mouse.

Organism-specific databases

CTDi286827.
MGIiMGI:1914199. Trim59.

Phylogenomic databases

eggNOGiENOG410ITG5. Eukaryota.
ENOG410YH9X. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000013095.
HOVERGENiHBG060002.
InParanoidiQ922Y2.
KOiK12028.
OMAiKEFMWKI.
OrthoDBiEOG7KWSHJ.
TreeFamiTF331669.

Miscellaneous databases

NextBioi323100.
PROiQ922Y2.
SOURCEiSearch...

Gene expression databases

BgeeiQ922Y2.
CleanExiMM_TRIM59.
ExpressionAtlasiQ922Y2. baseline and differential.
GenevisibleiQ922Y2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Embryo, Testis and Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. "Molecular cloning, mapping and characterization of a novel mouse RING finger gene, Mrf1."
    Chang R., Xu X., Li M.D.
    Gene 291:241-249(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "TRIM59 interacts with ECSIT and negatively regulates NF-kappaB and IRF-3/7-mediated signal pathways."
    Kondo T., Watanabe M., Hatakeyama S.
    Biochem. Biophys. Res. Commun. 422:501-507(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECSIT, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTRI59_MOUSE
AccessioniPrimary (citable) accession number: Q922Y2
Secondary accession number(s): E9QKA7
, Q9CSP2, Q9CUD5, Q9D740
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 118 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

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.