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Protein

E3 ubiquitin-protein ligase TRIM71

Gene

Trim71

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

Functioni

E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (PubMed:19898466). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression (PubMed:22735451). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (PubMed:23125361). Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (PubMed:22735451). Specific regulator of miRNA biogenesis. miRNA Binds MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity).By similarity3 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 fingeri12 – 94RING-typePROSITE-ProRule annotationAdd BLAST83
Zinc fingeri181 – 228B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri260 – 301B box-type 2PROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

  • miRNA binding Source: UniProtKB
  • translation repressor activity Source: MGI
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • 3'-UTR-mediated mRNA destabilization Source: MGI
  • cellular response to organic substance Source: MGI
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • miRNA mediated inhibition of translation Source: UniProtKB
  • miRNA metabolic process Source: UniProtKB
  • negative regulation of translation Source: MGI
  • neural tube closure Source: MGI
  • neural tube development Source: UniProtKB
  • positive regulation of gene silencing by miRNA Source: MGI
  • posttranscriptional regulation of gene expression Source: MGI
  • production of miRNAs involved in gene silencing by miRNA Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • regulation of gene silencing by miRNA Source: UniProtKB
  • regulation of neural precursor cell proliferation Source: UniProtKB
  • regulation of protein metabolic process Source: MGI
  • stem cell proliferation Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, RNA-binding, Transferase
Biological processRNA-mediated gene silencing, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM71 (EC:2.3.2.27)
Alternative name(s):
Protein lin-41 homolog
Short name:
mLin41
RING-type E3 ubiquitin transferase TRIM71Curated
Tripartite motif-containing protein 71
Gene namesi
Name:Trim71
Synonyms:Gm1127, Lin41
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2685973. Trim71.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at E9.5, due to a neural tube closure defect in the anterior craniofacial region of the neural tube, corresponding to the forebrain/midbrain boundary. Reduced cell proliferation in the neuroepithelium.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12C → L: Abolishes E3 ubiquitin-protein ligase activity; when associated with A-15. 1 Publication1
Mutagenesisi15C → A: Abolishes E3 ubiquitin-protein ligase activity; when associated with L-12. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002795122 – 855E3 ubiquitin-protein ligase TRIM71Add BLAST854

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Post-translational modificationi

Autoubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

PaxDbiQ1PSW8.
PeptideAtlasiQ1PSW8.
PRIDEiQ1PSW8.

PTM databases

iPTMnetiQ1PSW8.
PhosphoSitePlusiQ1PSW8.

Expressioni

Tissue specificityi

Highly expressed in undifferentiated embryonic stem cells (ESCs). Expressed in the epiblast and in interfollicular epidermal stem cells during early development. Also expressed in male germ cells and in the reproductive tract. Highly expressed in neuroepithelial cells, and its expression declines as neurogenesis proceeds (at protein level). Expressed in ependymal cells of the brain (PubMed:25883935).4 Publications

Developmental stagei

Expression is first detected at E8.5, increases to highest levels at E14.5 and remains elevated through the newborn stage. Expressed in developing limb buds and tail buds starting from E9.5. At E9.5, expression is prominent in the entire embryo, with the exception of the primordial cardiac sac. At E10.5, expression reduces to the neuroepithelium, branchial arches, spinal cord, somites, limb, and tail buds. At the onset of central nervous system development, the neuroepithelium shows a prominent staining between E9.5 and E10.5. Thereafter, expression is unevenly distributed in a progressively thinner layer along the inner surface of the ventricle. Expression is intense at the bumps corresponding to the nascent limb buds around E10.5. Shortly thereafter, as the limb buds emerge from the body and expand, expression declines and is limited to the most distal surface at E12.5. At E13.5 it is no longer possible to identify expression in either the developing nervous system, the limb or the tail buds. From postnatal day 10 (P10) to the adulthood, expressed in cells lining the wall of the four ventricles of the postnatal brain (PubMed:25883935).3 Publications

Inductioni

Negatively regulated by the microRNA (miRNA) let-7 which causes degradation of the mRNA encoding this protein. This requires a let-7 complementary site (LCS) in the 3'-UTR of the mRNA encoding this protein.1 Publication

Gene expression databases

BgeeiENSMUSG00000079259.
CleanExiMM_TRIM71.
GenevisibleiQ1PSW8. MM.

Interactioni

Subunit structurei

Interacts (via NHL repeats) with AGO2; the interaction increases in presence of RNA (PubMed:19898466, PubMed:22508726, PubMed:22735451). Interacts with HSP90AA1. Interacts (via NHL repeats) with MOV10, PABPC1, PUM1, PUM2, STAU2, XRN1 and XRN2 in an RNA-dependent manner (By similarity). Interacts with SHCBP1; leading to enhance its stability (PubMed:22508726).By similarity3 Publications

Protein-protein interaction databases

BioGridi561929. 11 interactors.
STRINGi10090.ENSMUSP00000107447.

Structurei

3D structure databases

ProteinModelPortaliQ1PSW8.
SMRiQ1PSW8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati466 – 567FilaminAdd BLAST102
Repeati580 – 623NHL 1Add BLAST44
Repeati627 – 670NHL 2Add BLAST44
Repeati674 – 717NHL 3Add BLAST44
Repeati721 – 764NHL 4Add BLAST44
Repeati768 – 811NHL 5Add BLAST44
Repeati815 – 855NHL 6Add BLAST41

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili314 – 352Sequence analysisAdd BLAST39
Coiled coili378 – 411Sequence analysisAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 42Ser-richAdd BLAST17

Domaini

The NHL domain, containing the 6 NHL repeats, is necessary and sufficient to target RNA but not to repress mRNA. The minimal region needed to execute repression consists of the coiled coil domain and the Filamin repeat. The RING-type domain is dispensable for mRNA repression.By similarity

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri12 – 94RING-typePROSITE-ProRule annotationAdd BLAST83
Zinc fingeri181 – 228B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri260 – 301B box-type 2PROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITG8. Eukaryota.
ENOG410XSQC. LUCA.
GeneTreeiENSGT00890000139359.
HOGENOMiHOG000006755.
HOVERGENiHBG081916.
InParanoidiQ1PSW8.
KOiK12035.
OMAiFEGALWK.
OrthoDBiEOG091G02WU.
PhylomeDBiQ1PSW8.
TreeFamiTF331018.

Family and domain databases

CDDicd00021. BBOX. 2 hits.
Gene3Di2.120.10.30. 3 hits.
2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
InterProiView protein in InterPro
IPR011042. 6-blade_b-propeller_TolB-like.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
PfamiView protein in Pfam
PF00630. Filamin. 1 hit.
PF01436. NHL. 6 hits.
PF00643. zf-B_box. 1 hit.
SMARTiView protein in SMART
SM00336. BBOX. 2 hits.
SM00557. IG_FLMN. 1 hit.
SM00184. RING. 1 hit.
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiView protein in PROSITE
PS50194. FILAMIN_REPEAT. 1 hit.
PS51125. NHL. 6 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q1PSW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSAGGGGPGA
60 70 80 90 100
AARRLHVLPC LHAFCRPCLE AHRLPAPGGA GPAEALKLRC PVCDQKVVLA
110 120 130 140 150
EAAGMDALPS SAFLLSNLLD AVVATAEEPP PKNGRAGGGP GGAGGHSNHR
160 170 180 190 200
HHAHHPAQRA AAPAPQPPPG PAASPGSLLM RRPHGCSSCD EGNAASSRCL
210 220 230 240 250
DCQEHLCDNC VRAHQRVRLT KDHYIERGPP GPAAASAAQQ LGLGPPFAGA
260 270 280 290 300
PFSILSVFPE RLGFCQHHDD EVLHLYCDTC SVPICRECTL GRHGGHSFAY
310 320 330 340 350
LQDALQDSRA LTIQLLADAQ QGRQALQLSI EQAQTVAEQV EMKAKVVQSE
360 370 380 390 400
VKAVTARHKK ALEDRECELL WKVEKIRQVK AKSLFLQVEK LRQSLSKLES
410 420 430 440 450
TISAVQQVLE EGRALDILLA RDRMLAQVQE LKTIRGLLQP QEDDRIMFTP
460 470 480 490 500
PDQALYLALK SIGFVSSGAF APLTKATGDG IKRALQGKVA SFTVMGYDHD
510 520 530 540 550
GEPRHSGGDL MSVVVLGPDG NLFGAEVSDQ QNGTYIVSYR PQLEGEHLVS
560 570 580 590 600
VTLYNQHIEN SPFKVVVKSG RSYVGIGLPG LSFGSEGDGE GKLCRPWGVS
610 620 630 640 650
VDKEGFIIVA DRSNNRIQVF KPCGSFHHKF GTLGSRPGQF DRPAGVACDA
660 670 680 690 700
SRRIIVADKD NHRIQIFTFE GQFLLKFGEK GTKNGQFNYP WDVAVNSEGK
710 720 730 740 750
ILVSDTRNHR IQLFGPDGVF LNKYGFEGSL WKHFDSPRGV AFNNEGHLVV
760 770 780 790 800
TDFNNHRLLV IHPDCQSARF LGSEGSGNGQ FLRPQGVAVD QEGRIIVADS
810 820 830 840 850
RNHRVQMFEA NGSFLCKFGA QGSGFGQMDR PSGIAVTPDG LIVVVDFGNN

RILIF
Length:855
Mass (Da):92,054
Last modified:May 16, 2006 - v1
Checksum:i151BA48E28C34904
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ005956 mRNA. Translation: AAY55947.1.
CCDSiCCDS40793.1.
RefSeqiNP_001035968.1. NM_001042503.2.
UniGeneiMm.17857.

Genome annotation databases

EnsembliENSMUST00000111816; ENSMUSP00000107447; ENSMUSG00000079259.
GeneIDi636931.
KEGGimmu:636931.
UCSCiuc009rxp.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiLIN41_MOUSE
AccessioniPrimary (citable) accession number: Q1PSW8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: May 16, 2006
Last modified: November 22, 2017
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Reported to mediate ubiquitination and subsequent degradation of AGO2 (PubMed:19898466). However, this result is subject to discussion and later reports suggest that, while it interacts with AGO2, it is not involved in AGO2 ubiquitination (PubMed:22508726, PubMed:22735451).3 Publications

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