Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase TRIM8

Gene

TRIM8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which plays different roles in immune pathways. Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1 (PubMed:12163497). Plays a positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'lys-63' polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B (PubMed:22084099, PubMed:23152791). Modulates also STAT3 activity through negative regulation of PIAS3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus (PubMed:20516148).4 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

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)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 56RING-typePROSITE-ProRule annotationAdd BLAST42
Zinc fingeri92 – 132B box-type 1Add BLAST41
Zinc fingeri140 – 182B box-type 2Add BLAST43

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • transferase activity Source: UniProtKB-KW
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • innate immune response Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of viral release from host cell Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • protein ubiquitination Source: UniProtKB-UniPathway

Keywordsi

Molecular functionTransferase
Biological processImmunity, Innate immunity, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-877300 Interferon gamma signaling
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM8 (EC:2.3.2.27)
Alternative name(s):
Glioblastoma-expressed RING finger protein
RING finger protein 27
RING-type E3 ubiquitin transferase TRIM8Curated
Tripartite motif-containing protein 8
Gene namesi
Name:TRIM8
Synonyms:GERP, RNF27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000171206.13
HGNCiHGNC:15579 TRIM8
MIMi606125 gene
neXtProtiNX_Q9BZR9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi81603
OpenTargetsiENSG00000171206
PharmGKBiPA37983

Polymorphism and mutation databases

BioMutaiTRIM8
DMDMi18202744

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000562061 – 551E3 ubiquitin-protein ligase TRIM8Add BLAST551

Proteomic databases

EPDiQ9BZR9
MaxQBiQ9BZR9
PaxDbiQ9BZR9
PeptideAtlasiQ9BZR9
PRIDEiQ9BZR9

PTM databases

iPTMnetiQ9BZR9
PhosphoSitePlusiQ9BZR9

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000171206
CleanExiHS_TRIM8
ExpressionAtlasiQ9BZR9 baseline and differential
GenevisibleiQ9BZR9 HS

Organism-specific databases

HPAiHPA023560
HPA023561

Interactioni

Subunit structurei

Homodimer. Interacts with SOCS1 (via) SH2 domain and SOCS box (PubMed:12163497). Interacts with HSP90AB1; prevents nucleus translocation of phosphorylated STAT3 and HSP90AB1. Interacts with MAP3K7/TAK1 (PubMed:22084099). Interacts with PIAS3 (PubMed:20516148).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi123541, 54 interactors
IntActiQ9BZR9, 63 interactors
STRINGi9606.ENSP00000302120

Structurei

3D structure databases

ProteinModelPortaliQ9BZR9
SMRiQ9BZR9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili181 – 249Sequence analysisAdd BLAST69

Domaini

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

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 56RING-typePROSITE-ProRule annotationAdd BLAST42
Zinc fingeri92 – 132B box-type 1Add BLAST41
Zinc fingeri140 – 182B box-type 2Add BLAST43

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITEZ Eukaryota
ENOG410ZTPN LUCA
GeneTreeiENSGT00910000144235
HOGENOMiHOG000082538
HOVERGENiHBG056254
InParanoidiQ9BZR9
KOiK12001
OMAiHPPYPRS
OrthoDBiEOG091G059M
PhylomeDBiQ9BZR9
TreeFamiTF333491

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
SMARTiView protein in SMART
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9BZR9-1 [UniParc]FASTAAdd to basket

« Hide

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

S
Length:551
Mass (Da):61,489
Last modified:September 26, 2001 - v2
Checksum:i1FEF89029EB9BACB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti174H → R in AAG53087 (PubMed:11118312).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281046 mRNA Translation: AAG53087.1
AF220034 mRNA Translation: AAG53488.1
AL391121 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49680.1
BC021925 mRNA Translation: AAH21925.1
CCDSiCCDS31274.1
PIRiJC7562
RefSeqiNP_112174.2, NM_030912.2
UniGeneiHs.336810

Genome annotation databases

EnsembliENST00000302424; ENSP00000302120; ENSG00000171206
GeneIDi81603
KEGGihsa:81603
UCSCiuc001kvz.3 human

Similar proteinsi

Entry informationi

Entry nameiTRIM8_HUMAN
AccessioniPrimary (citable) accession number: Q9BZR9
Secondary accession number(s): A6NI31, Q9C028
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: April 25, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health