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Protein

Probable E3 ubiquitin-protein ligase TRIM8

Gene

Trim8

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

Functioni

Probable E3 ubiquitin-protein ligase which may promote proteasomal degradation of SOCS1.1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 5642RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 13241B box-type 1Add
BLAST
Zinc fingeri140 – 18243B box-type 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

  • innate immune response Source: UniProtKB
  • negative regulation of viral entry into host cell Source: UniProtKB
  • negative regulation of viral release from host cell Source: UniProtKB
  • negative regulation of viral transcription Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of NF-kappaB transcription factor activity Source: MGI
  • positive regulation of protein localization to nucleus Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • stem cell population maintenance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable E3 ubiquitin-protein ligase TRIM8 (EC:6.3.2.-)
Alternative name(s):
Glioblastoma-expressed RING finger protein
RING finger protein 27
Tripartite motif-containing protein 8
Gene namesi
Name:Trim8
Synonyms:Gerp, Rnf27
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1933302. Trim8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • PML body Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Probable E3 ubiquitin-protein ligase TRIM8PRO_0000056207Add
BLAST

Proteomic databases

EPDiQ99PJ2.
MaxQBiQ99PJ2.
PaxDbiQ99PJ2.
PRIDEiQ99PJ2.
TopDownProteomicsiQ99PJ2.

Expressioni

Tissue specificityi

High expression in heart, liver, and thymus. Expressed in embryonic CNS, kidney, lens and gut.2 Publications

Developmental stagei

At 10.5 and 12.5 dpc, expressed in the central nervous system. At 14.5 dpc, expressed in the eye (lens and inner neural layer of the retina), in the primitive glomeruli of the developing kidney, in the villi of the gut and in the dorsal root ganglia.

Gene expression databases

BgeeiQ99PJ2.
CleanExiMM_TRIM8.
GenevisibleiQ99PJ2. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with SOCS1 (via) SH2 domain and SOCS box.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi220231. 1 interaction.
IntActiQ99PJ2. 1 interaction.
MINTiMINT-1634563.
STRINGi10090.ENSMUSP00000026008.

Structurei

3D structure databases

ProteinModelPortaliQ99PJ2.
SMRiQ99PJ2. Positions 7-55, 145-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili181 – 24969Sequence analysisAdd
BLAST
Coiled coili274 – 29522Sequence analysisAdd
BLAST

Domaini

The coiled coil domain is required for homodimerization.By similarity
The region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 2 B box-type zinc fingers.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 5642RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 13241B box-type 1Add
BLAST
Zinc fingeri140 – 18243B box-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410KDQ2. Eukaryota.
ENOG410ZTPN. LUCA.
GeneTreeiENSGT00840000129840.
HOGENOMiHOG000082538.
HOVERGENiHBG056254.
InParanoidiQ99PJ2.
KOiK12001.
OMAiEDINFMK.
OrthoDBiEOG76HQ11.
TreeFamiTF333491.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99PJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENWKNCFE EELICPICLH VFVEPVQLPC KHNFCRGCIG EAWAKDSGLV
60 70 80 90 100
RCPECNQAYN QKPGLEKNLK LTNIVEKFNA LHVEKPPTAL HCVFCRRGPP
110 120 130 140 150
LPAQKVCLRC EAPCCQSHVQ THLQQPSTAR GHLLVEADDV RAWSCPQHNA
160 170 180 190 200
YRLYHCEAEQ VAVCQYCCYY SGAHQGHSVC DVEIRRNEIR KMLMKQQERL
210 220 230 240 250
EEREQDIEDQ LYKLESDKRL VEEKVSQLKE EVRLQYEKLH QLLDEDLRQT
260 270 280 290 300
VEVLDKAQAK FCSENAAQAL HLGERMQEAK KLLGSLQRLF DKTEDVGFMK
310 320 330 340 350
NTKSVKILMD RTQTCTGSSL SPPKIGHLNS KLFLNEVAKK EKQLRKMLEG
360 370 380 390 400
PFSTPVPFLQ SVPLYPCGVN SSGAEKRKHS TAFPEASFLE TSSGPVGGQY
410 420 430 440 450
GAAGTASSEG QSGQPLGPCS STQHLVALPG GTQPVHSSPV FPPSQYPNGS
460 470 480 490 500
TTQQPMLPQY GGRKILVCSV DNCYCSSVAN HGGHQPYPRS GHFPWTVPSQ
510 520 530 540 550
EYSHPLPPTP SVPQSLPGLA VRDWLDASQQ PGHQDFYRVY GQPSTKHYVT

S
Length:551
Mass (Da):61,602
Last modified:July 27, 2011 - v3
Checksum:iA5388F450D6566A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti218 – 2181K → M in AAG53088 (PubMed:11118312).Curated
Sequence conflicti218 – 2181K → M in AAG53489 (PubMed:11331580).Curated
Sequence conflicti259 – 2591A → G in AAG53088 (PubMed:11118312).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281047 mRNA. Translation: AAG53088.1.
AK052763 mRNA. Translation: BAC35138.1.
AK079847 mRNA. Translation: BAC37764.1.
AK155303 mRNA. Translation: BAE33177.1.
BC037065 mRNA. Translation: AAH37065.1.
BC152343 mRNA. Translation: AAI52344.1.
BC152344 mRNA. Translation: AAI52345.1.
AF220035 mRNA. Translation: AAG53489.1.
CCDSiCCDS38009.1.
RefSeqiNP_444330.2. NM_053100.2.
UniGeneiMm.392177.
Mm.481672.

Genome annotation databases

EnsembliENSMUST00000026008; ENSMUSP00000026008; ENSMUSG00000025034.
GeneIDi93679.
KEGGimmu:93679.
UCSCiuc008hts.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281047 mRNA. Translation: AAG53088.1.
AK052763 mRNA. Translation: BAC35138.1.
AK079847 mRNA. Translation: BAC37764.1.
AK155303 mRNA. Translation: BAE33177.1.
BC037065 mRNA. Translation: AAH37065.1.
BC152343 mRNA. Translation: AAI52344.1.
BC152344 mRNA. Translation: AAI52345.1.
AF220035 mRNA. Translation: AAG53489.1.
CCDSiCCDS38009.1.
RefSeqiNP_444330.2. NM_053100.2.
UniGeneiMm.392177.
Mm.481672.

3D structure databases

ProteinModelPortaliQ99PJ2.
SMRiQ99PJ2. Positions 7-55, 145-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220231. 1 interaction.
IntActiQ99PJ2. 1 interaction.
MINTiMINT-1634563.
STRINGi10090.ENSMUSP00000026008.

Proteomic databases

EPDiQ99PJ2.
MaxQBiQ99PJ2.
PaxDbiQ99PJ2.
PRIDEiQ99PJ2.
TopDownProteomicsiQ99PJ2.

Protocols and materials databases

DNASUi93679.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026008; ENSMUSP00000026008; ENSMUSG00000025034.
GeneIDi93679.
KEGGimmu:93679.
UCSCiuc008hts.1. mouse.

Organism-specific databases

CTDi81603.
MGIiMGI:1933302. Trim8.

Phylogenomic databases

eggNOGiENOG410KDQ2. Eukaryota.
ENOG410ZTPN. LUCA.
GeneTreeiENSGT00840000129840.
HOGENOMiHOG000082538.
HOVERGENiHBG056254.
InParanoidiQ99PJ2.
KOiK12001.
OMAiEDINFMK.
OrthoDBiEOG76HQ11.
TreeFamiTF333491.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiTrim8. mouse.
NextBioi351396.
PROiQ99PJ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PJ2.
CleanExiMM_TRIM8.
GenevisibleiQ99PJ2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  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 and NOD.
    Tissue: Kidney.
  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: FVB/N.
    Tissue: Colon.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 196-463, TISSUE SPECIFICITY.
  5. Cited for: FUNCTION, INTERACTION WITH SOCS1, TISSUE SPECIFICITY, INDUCTION, C-TERMINAL DOMAIN.

Entry informationi

Entry nameiTRIM8_MOUSE
AccessioniPrimary (citable) accession number: Q99PJ2
Secondary accession number(s): Q3U2G3
, Q8C508, Q8C700, Q8CGI2, Q99PQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 136 of the entry and version 3 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.