TUT4
entrez
23318
canonical
uniprot
Q5TAX3
canonical
ensembl
ENSG00000134744
resolver
ensp
ENSP00000257177
resolver
ensp
ENSP00000360599
resolver
ensp
ENSP00000608184
resolver
genesymbol
TUT4
resolver
genesymbol_syn
KIAA0191
resolver
genesymbol_syn
ZCCHC11
resolver
hgnc
HGNC:28981
resolver
uniprot
A0A0C4DFM7
resolver
uniprot
A2RRP0
resolver
uniprot
B7Z8J5
resolver
uniprot
D3DQ35
resolver
uniprot
Q12764
resolver
uniprot
Q5TAX2
resolver
uniprot
Q5TAX4
resolver
uniprot
Q86XZ3
resolver
uniprot_entry
TUT4_HUMAN
resolver
uniprot_sec
A0A0C4DFM7
resolver
uniprot_sec
A2RRP0
resolver
uniprot_sec
B7Z8J5
resolver
uniprot_sec
D3DQ35
resolver
uniprot_sec
Q12764
resolver
uniprot_sec
Q5TAX2
resolver
uniprot_sec
Q5TAX4
resolver
uniprot_sec
Q86XZ3
resolver
amino_acid_sequence
MEESKTLKSENHEPKKNVICEESKAVQVIGNQTLKARNDKSVKEIENSSPNRNSSKKNKQNDICIEKTEVKSCKVNAANLPGPKDLGLVLRDQSHCKAKKFPNSPVKAEKATISQAKSEKATSLQAKAEKSPKSPNSVKAEKASSYQMKSEKVPSSPAEAEKGPSLLLKDMRQKTELQQIGKKIPSSFTSVDKVNIEAVGGEKCALQNSPRSQKQQTCTDNTGDSDDSASGIEDVSDDLSKMKNDESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNILEKQEESELRSLPPPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDVNIDIKFPPKMNHPDLLIKVLGILKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSAGNDMACLTTDLLTALGKIEPVFIPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLLPCLLGSWIEGFDPKRMDDFQLKGIVEEKFVKWECNSSSATEKNSIAEENKAKADQPKDDTKKTETDNQSNAMKEKHGKSPLALETPNRVSLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKRRIAIEDPFSVKRNVARSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKSTVDFKKREKGKISNKKPVKSNNMATNGCILLGETTEKINAEREQPVQCDEMDCTSQRCIIDNNNLLVNELDFADHGQDSSSLSTSKSSEIEPKLDKKQDDLAPSETCLKKELSQCNCIDLSKSPDPDKSTGTDCRSNLETESSHQSVCTDTSATSCNCKATEDASDLNDDDNLPTQELYYVFDKFILTSGKPPTIVCSICKKDGHSKNDCPEDFRKIDLKPLPPMTNRFREILDLVCKRCFDELSPPCSEQHNREQILIGLEKFIQKEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEIIENLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPVIPVLQEIFDGKQIPQRMVDGWNAFFFDKTEELKKRLPSLGKNTESLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWTSKCIAIEDPFDLNHNLGAGVSRKMTNFIMKAFINGRKLFGTPFYPLIGREAEYFFDSRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKSLLFRLKKKDSEEEKEGNEEEKDSRDVLDPRDLHDTRDFRDPRDLRCFICGDAGHVRRECPEVKLARQRNSSVAAAQLVRNLVNAQQVAGSAQQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAQYSPMHNMGLLPMHPLQIPAPSWPIHGPVIHSAPGSAPSNIGLNDPSIIFAQPAARPVAIPNTSHDGHWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPLVPASWPYGLHQNFMHQGNARFQPNKPFYTQDRCATRRCRERCPHPPRGNVSE
uniprot
proteins
ec_number
2.7.7.52
uniprot
proteins
function
FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:25480299, PubMed:31036859). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (By similarity). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also functions as an integral regulator of microRNA biogenesis using 3 different uridylation mechanisms (PubMed:25979828). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression (PubMed:19703396). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:25979828). Adds oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (PubMed:25979828). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP (PubMed:16643855). Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (By similarity) (PubMed:16643855, PubMed:18172165, PubMed:19703396, PubMed:25480299, PubMed:25979828). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (PubMed:30122351). {ECO:0000250|UniProtKB:B2RX14, ECO:0000269|PubMed:16643855, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:25480299, ECO:0000269|PubMed:25979828, ECO:0000269|PubMed:30122351, ECO:0000269|PubMed:31036859}.
uniprot
proteins
mass_dalton
185166
uniprot
proteins
mutagenesis
MUTAGEN 253..333; /note="Missing: Loss of interaction with LIN28A and pre-let-7 RNA."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 306; /note="C->A: Loss of LIN28A and pre-let-7 RNA binding and loss of pre-let-7 RNA uridylylation; when associated with A-309."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 309; /note="C->A: Loss of LIN28A and pre-let-7 RNA binding and loss of pre-let-7 RNA uridylylation; when associated with A-306."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 321; /note="K->A: Strongly decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-324."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 324; /note="K->A: Strongly decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-321."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 326..327; /note="KR->AA: Strongly decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 329..330; /note="KK->AA: Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 450; /note="H->A: Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-452."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 452; /note="K->A: Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-450."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 669..670; /note="RR->AA: Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation."; /evidence="ECO:0000269|PubMed:31036859"; MUTAGEN 1011; /note="D->A: Loss of nucleotidyltransferase activity and stabilization of pre-let-7 miRNAs. Abolishes inhibition of LIRE1 retrotransposition."; /evidence="ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:25480299, ECO:0000269|PubMed:30122351
uniprot
proteins
protein_family
DNA polymerase type-B-like family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16643855
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18172165
uniprot
proteins
pubmed
19703396
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22118463
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25480299
uniprot
proteins
pubmed
25979828
uniprot
proteins
pubmed
30122351
uniprot
proteins
pubmed
31036859
uniprot
proteins
pubmed
8724849
uniprot
proteins
sequence_length
1644
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16643855}. Cytoplasm {ECO:0000269|PubMed:16643855, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:25480299}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:30122351}. Note=Mainly cytoplasmic (PubMed:19703396, PubMed:25480299). Translocates into the cytoplasm following treatment of the cell with LPS (PubMed:16643855). Co-enriched in cytoplasmic foci with MOV10 (PubMed:30122351). {ECO:0000269|PubMed:30122351}.
uniprot
proteins