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Protein

E3 ubiquitin-protein ligase TRIM71

Gene

TRIM71

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (PubMed:23125361). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. 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 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (PubMed:28431233).By similarity1 Publication2 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 – 95RING-typePROSITE-ProRule annotationAdd BLAST84
Zinc fingeri194 – 241B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri273 – 314B box-type 2PROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM71 (EC:2.3.2.27)
Alternative name(s):
Protein lin-41 homolog
RING-type E3 ubiquitin transferase TRIM71Curated
Tripartite motif-containing protein 71
Gene namesi
Name:TRIM71
Synonyms:LIN41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000206557.5
HGNCiHGNC:32669 TRIM71
neXtProtiNX_Q2Q1W2

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Promotes reprogramming of differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. Inhibits translation of the prodifferentiation transcription factor EGR1 through binding to its mRNA and regulates a broad array of differentiation genes.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi647G → D: Strongly decreases repression on mRNA. 1 Publication1
Mutagenesisi675H → L: Abolishes repression on mRNA. Abolishes interaction with AGO2, PABPC1 and PUM2. Increases interaction with HSP90AA1. 1 Publication1
Mutagenesisi702Y → A: Decreases repression on mRNA. Decreases interaction with HSP90AA1. Abolishes interaction with PABPC1 and PUM2. Increases interaction with AGO2. 1 Publication1
Mutagenesisi751R → A: Decreases repression on mRNA. Abolishes interaction with AGO2, HSP90AA1, PABPC1 and PUM2. 1 Publication1

Organism-specific databases

DisGeNETi131405
OpenTargetsiENSG00000206557
PharmGKBiPA144596246

Polymorphism and mutation databases

BioMutaiTRIM71
DMDMi121941685

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002795112 – 868E3 ubiquitin-protein ligase TRIM71Add BLAST867

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Post-translational modificationi

Autoubiquitinated.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiQ2Q1W2
MaxQBiQ2Q1W2
PaxDbiQ2Q1W2
PeptideAtlasiQ2Q1W2
PRIDEiQ2Q1W2
ProteomicsDBi61436

PTM databases

iPTMnetiQ2Q1W2
PhosphoSitePlusiQ2Q1W2

Expressioni

Tissue specificityi

Specifically expressed in testis.1 Publication

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 (PubMed:17890240, PubMed:24239284). Down-regulated by retinoic acid in Tera-2 cells (PubMed:15722555).3 Publications

Gene expression databases

BgeeiENSG00000206557
CleanExiHS_TRIM71
GenevisibleiQ2Q1W2 HS

Organism-specific databases

HPAiHPA038141
HPA038142

Interactioni

Subunit structurei

Interacts (via NHL repeats) with AGO2; the interaction increases in presence of RNA (PubMed:23125361). Interacts with HSP90AA1. Interacts (via NHL repeats) with MOV10, PABPC1, PUM1, PUM2, STAU2, XRN1 and XRN2 in an RNA-dependent manner (PubMed:23125361). Interacts with SHCBP1; leading to enhance its stability (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi126279, 20 interactors
STRINGi9606.ENSP00000373272

Structurei

3D structure databases

ProteinModelPortaliQ2Q1W2
SMRiQ2Q1W2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati479 – 580FilaminAdd BLAST102
Repeati593 – 636NHL 1Add BLAST44
Repeati640 – 683NHL 2Add BLAST44
Repeati687 – 730NHL 3Add BLAST44
Repeati734 – 777NHL 4Add BLAST44
Repeati781 – 824NHL 5Add BLAST44
Repeati828 – 868NHL 6Add BLAST41

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili391 – 427Sequence analysisAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 42Ser-richAdd BLAST17
Compositional biasi146 – 157His-richAdd BLAST12

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.1 Publication

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri12 – 95RING-typePROSITE-ProRule annotationAdd BLAST84
Zinc fingeri194 – 241B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri273 – 314B box-type 2PROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITG8 Eukaryota
ENOG410XSQC LUCA
GeneTreeiENSGT00920000148978
HOGENOMiHOG000006755
HOVERGENiHBG081916
InParanoidiQ2Q1W2
KOiK12035
OMAiFEGALWK
OrthoDBiEOG091G02WU
PhylomeDBiQ2Q1W2
TreeFamiTF331018

Family and domain databases

CDDicd00021 BBOX, 2 hits
Gene3Di2.120.10.30, 2 hits
2.60.40.10, 1 hit
3.30.40.10, 1 hit
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.

Q2Q1W2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG
60 70 80 90 100
AAARRLHVLP CLHAFCRPCL EAHRLPAAGG GAAGEPLKLR CPVCDQKVVL
110 120 130 140 150
AEAAGMDALP SSAFLLSNLL DAVVATADEP PPKNGRAGAP AGAGGHSNHR
160 170 180 190 200
HHAHHAHPRA SASAPPLPQA PQPPAPSRSA PGGPAASPSA LLLRRPHGCS
210 220 230 240 250
SCDEGNAASS RCLDCQEHLC DNCVRAHQRV RLTKDHYIER GPPGPGAAAA
260 270 280 290 300
AQQLGLGPPF PGPPFSILSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
310 320 330 340 350
CTMGRHGGHS FIYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA
360 370 380 390 400
EQVEMKAKVV QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ
410 420 430 440 450
VEKLRQNLNK LESTISAVQQ VLEEGRALDI LLARDRMLAQ VQELKTVRSL
460 470 480 490 500
LQPQEDDRVM FTPPDQALYL AIKSFGFVSS GAFAPLTKAT GDGLKRALQG
510 520 530 540 550
KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV SDQQNGTYVV
560 570 580 590 600
SYRPQLEGEH LVSVTLCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
610 620 630 640 650
DSDGKLCRPW GVSVDKEGYI IVADRSNNRI QVFKPCGAFH HKFGTLGSRP
660 670 680 690 700
GQFDRPAGVA CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF
710 720 730 740 750
NYPWDVAVNS EGKILVSDTR NHRIQLFGPD GVFLNKYGFE GALWKHFDSP
760 770 780 790 800
RGVAFNHEGH LVVTDFNNHR LLVIHPDCQS ARFLGSEGTG NGQFLRPQGV
810 820 830 840 850
AVDQEGRIIV ADSRNHRVQM FESNGSFLCK FGAQGSGFGQ MDRPSGIAIT
860
PDGMIVVVDF GNNRILVF
Length:868
Mass (Da):93,385
Last modified:January 24, 2006 - v1
Checksum:iA71A1E5CC019F80D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ232881 mRNA Translation: ABB18374.1
CCDSiCCDS43060.1
RefSeqiNP_001034200.1, NM_001039111.2
UniGeneiHs.113170
Hs.567678

Genome annotation databases

EnsembliENST00000383763; ENSP00000373272; ENSG00000206557
GeneIDi131405
KEGGihsa:131405
UCSCiuc003cff.4 human

Similar proteinsi

Entry informationi

Entry nameiLIN41_HUMAN
AccessioniPrimary (citable) accession number: Q2Q1W2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: January 24, 2006
Last modified: June 20, 2018
This is version 115 of the entry and version 1 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

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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