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E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)

 LIN41_HUMAN             Reviewed;         868 AA.
Q2Q1W2;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 1.
12-SEP-2018, entry version 117.
RecName: Full=E3 ubiquitin-protein ligase TRIM71;
EC=2.3.2.27;
AltName: Full=Protein lin-41 homolog;
AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 71;
Name=TRIM71; Synonyms=LIN41;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Lerner M., Corcoran M., Nielsen M., Zubarev R., Uhlen M., Hober S.,
Grander D., Sangfelt O.;
"The RBCC gene RFP2 (LEU5/TRIM13), frequently deleted in various
malignancies, encodes a ring E3 ubiquitin ligase.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[2]
IDENTIFICATION.
PubMed=16245339; DOI=10.1002/dvdy.20591;
Lancman J.J., Caruccio N.C., Harfe B.D., Pasquinelli A.E.,
Schageman J.J., Pertsemlidis A., Fallon J.F.;
"Analysis of the regulation of lin-41 during chick and mouse limb
development.";
Dev. Dyn. 234:948-960(2005).
[3]
IDENTIFICATION.
PubMed=16247770; DOI=10.1002/dvdy.20599;
Maller Schulman B.R., Esquela-Kerscher A., Slack F.J.;
"Reciprocal expression of lin-41 and the microRNAs let-7 and mir-125
during mouse embryogenesis.";
Dev. Dyn. 234:1046-1054(2005).
[4]
TISSUE SPECIFICITY, AND DOWN-REGULATION BY RETINOIC ACID.
PubMed=15722555; DOI=10.1074/jbc.M412247200;
Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.;
"Depletion of human micro-RNA miR-125b reveals that it is critical for
the proliferation of differentiated cells but not for the down-
regulation of putative targets during differentiation.";
J. Biol. Chem. 280:16635-16641(2005).
[5]
INDUCTION.
PubMed=17890240; DOI=10.1093/molbev/msm195;
Lin Y.C., Hsieh L.C., Kuo M.W., Yu J., Kuo H.H., Lo W.L., Lin R.J.,
Yu A.L., Li W.H.;
"Human TRIM71 and its nematode homologue are targets of let-7 microRNA
and its zebrafish orthologue is essential for development.";
Mol. Biol. Evol. 24:2525-2534(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AGO2; HSP90AA1;
MOV10; PABPC1; PUM1; PUM2; STAU2; XRN1 AND XRN2, RNA-BINDING, DOMAIN,
AND MUTAGENESIS OF GLY-647; HIS-675; TYR-702 AND ARG-751.
PubMed=23125361; DOI=10.1093/nar/gks1032;
Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
"The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
function.";
Nucleic Acids Res. 41:518-532(2013).
[9]
FUNCTION, BIOTECHNOLOGY, SUBCELLULAR LOCATION, AND INDUCTION BY LET-7.
PubMed=24239284; DOI=10.1016/j.stem.2013.11.001;
Worringer K.A., Rand T.A., Hayashi Y., Sami S., Takahashi K.,
Tanabe K., Narita M., Srivastava D., Yamanaka S.;
"The let-7/LIN-41 pathway regulates reprogramming to human induced
pluripotent stem cells by controlling expression of prodifferentiation
genes.";
Cell Stem Cell 14:40-52(2014).
[10]
FUNCTION, AND MIRNA-BINDING.
PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L.,
Eichner N., Lehmann G., Schall K., Urlaub H., Meister G.;
"A Compendium of RNA-Binding Proteins that Regulate MicroRNA
Biogenesis.";
Mol. Cell 66:270-284(2017).
-!- FUNCTION: 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). {ECO:0000250|UniProtKB:Q1PSW8,
ECO:0000269|PubMed:23125361, ECO:0000269|PubMed:28431233,
ECO:0000305|PubMed:24239284}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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). {ECO:0000250|UniProtKB:Q1PSW8,
ECO:0000269|PubMed:23125361}.
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:23125361, ECO:0000269|PubMed:24239284}.
-!- TISSUE SPECIFICITY: Specifically expressed in testis.
{ECO:0000269|PubMed:15722555}.
-!- INDUCTION: 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).
{ECO:0000269|PubMed:15722555, ECO:0000269|PubMed:17890240,
ECO:0000269|PubMed:24239284}.
-!- DOMAIN: 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. {ECO:0000269|PubMed:23125361}.
-!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}.
-!- BIOTECHNOLOGY: 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.
{ECO:0000269|PubMed:24239284}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ232881; ABB18374.1; -; mRNA.
CCDS; CCDS43060.1; -.
RefSeq; NP_001034200.1; NM_001039111.2.
UniGene; Hs.113170; -.
UniGene; Hs.567678; -.
ProteinModelPortal; Q2Q1W2; -.
SMR; Q2Q1W2; -.
BioGrid; 126279; 30.
STRING; 9606.ENSP00000373272; -.
iPTMnet; Q2Q1W2; -.
PhosphoSitePlus; Q2Q1W2; -.
BioMuta; TRIM71; -.
DMDM; 121941685; -.
EPD; Q2Q1W2; -.
MaxQB; Q2Q1W2; -.
PaxDb; Q2Q1W2; -.
PeptideAtlas; Q2Q1W2; -.
PRIDE; Q2Q1W2; -.
ProteomicsDB; 61436; -.
Ensembl; ENST00000383763; ENSP00000373272; ENSG00000206557.
GeneID; 131405; -.
KEGG; hsa:131405; -.
UCSC; uc003cff.4; human.
CTD; 131405; -.
DisGeNET; 131405; -.
EuPathDB; HostDB:ENSG00000206557.5; -.
GeneCards; TRIM71; -.
HGNC; HGNC:32669; TRIM71.
HPA; HPA038141; -.
HPA; HPA038142; -.
neXtProt; NX_Q2Q1W2; -.
OpenTargets; ENSG00000206557; -.
PharmGKB; PA144596246; -.
eggNOG; ENOG410ITG8; Eukaryota.
eggNOG; ENOG410XSQC; LUCA.
GeneTree; ENSGT00920000148978; -.
HOGENOM; HOG000006755; -.
HOVERGEN; HBG081916; -.
InParanoid; Q2Q1W2; -.
KO; K12035; -.
OMA; FEGALWK; -.
OrthoDB; EOG091G02WU; -.
PhylomeDB; Q2Q1W2; -.
TreeFam; TF331018; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; TRIM71; human.
GenomeRNAi; 131405; -.
PRO; PR:Q2Q1W2; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000206557; Expressed in 55 organ(s), highest expression level in female gonad.
CleanEx; HS_TRIM71; -.
Genevisible; Q2Q1W2; HS.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0030371; F:translation repressor activity; IDA:CACAO.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:CACAO.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:CACAO.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0021915; P:neural tube development; ISS:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IEA:Ensembl.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; IMP:UniProtKB.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
GO; GO:0072089; P:stem cell proliferation; ISS:UniProtKB.
CDD; cd00021; BBOX; 2.
Gene3D; 2.120.10.30; -; 2.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR001298; Filamin/ABP280_rpt.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR001258; NHL_repeat.
InterPro; IPR013017; NHL_repeat_subgr.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00630; Filamin; 1.
Pfam; PF01436; NHL; 6.
Pfam; PF00643; zf-B_box; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00557; IG_FLMN; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50194; FILAMIN_REPEAT; 1.
PROSITE; PS51125; NHL; 6.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Developmental protein; Metal-binding; Reference proteome; Repeat;
RNA-binding; RNA-mediated gene silencing; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21406692}.
CHAIN 2 868 E3 ubiquitin-protein ligase TRIM71.
/FTId=PRO_0000279511.
REPEAT 479 580 Filamin.
REPEAT 593 636 NHL 1.
REPEAT 640 683 NHL 2.
REPEAT 687 730 NHL 3.
REPEAT 734 777 NHL 4.
REPEAT 781 824 NHL 5.
REPEAT 828 868 NHL 6.
ZN_FING 12 95 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 194 241 B box-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
ZN_FING 273 314 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 391 427 {ECO:0000255}.
COMPBIAS 26 42 Ser-rich.
COMPBIAS 146 157 His-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:21406692}.
MUTAGEN 647 647 G->D: Strongly decreases repression on
mRNA. {ECO:0000269|PubMed:23125361}.
MUTAGEN 675 675 H->L: Abolishes repression on mRNA.
Abolishes interaction with AGO2, PABPC1
and PUM2. Increases interaction with
HSP90AA1. {ECO:0000269|PubMed:23125361}.
MUTAGEN 702 702 Y->A: Decreases repression on mRNA.
Decreases interaction with HSP90AA1.
Abolishes interaction with PABPC1 and
PUM2. Increases interaction with AGO2.
{ECO:0000269|PubMed:23125361}.
MUTAGEN 751 751 R->A: Decreases repression on mRNA.
Abolishes interaction with AGO2,
HSP90AA1, PABPC1 and PUM2.
{ECO:0000269|PubMed:23125361}.
SEQUENCE 868 AA; 93385 MW; A71A1E5CC019F80D CRC64;
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG AAARRLHVLP
CLHAFCRPCL EAHRLPAAGG GAAGEPLKLR CPVCDQKVVL AEAAGMDALP SSAFLLSNLL
DAVVATADEP PPKNGRAGAP AGAGGHSNHR HHAHHAHPRA SASAPPLPQA PQPPAPSRSA
PGGPAASPSA LLLRRPHGCS SCDEGNAASS RCLDCQEHLC DNCVRAHQRV RLTKDHYIER
GPPGPGAAAA AQQLGLGPPF PGPPFSILSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
CTMGRHGGHS FIYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA EQVEMKAKVV
QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ VEKLRQNLNK LESTISAVQQ
VLEEGRALDI LLARDRMLAQ VQELKTVRSL LQPQEDDRVM FTPPDQALYL AIKSFGFVSS
GAFAPLTKAT GDGLKRALQG KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV
SDQQNGTYVV SYRPQLEGEH LVSVTLCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
DSDGKLCRPW GVSVDKEGYI IVADRSNNRI QVFKPCGAFH HKFGTLGSRP GQFDRPAGVA
CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF NYPWDVAVNS EGKILVSDTR
NHRIQLFGPD GVFLNKYGFE GALWKHFDSP RGVAFNHEGH LVVTDFNNHR LLVIHPDCQS
ARFLGSEGTG NGQFLRPQGV AVDQEGRIIV ADSRNHRVQM FESNGSFLCK FGAQGSGFGQ
MDRPSGIAIT PDGMIVVVDF GNNRILVF


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