TUT1
entrez
64852
canonical
uniprot
Q9H6E5
canonical
ensembl
ENSG00000149016
resolver
ensp
ENSP00000308000
resolver
ensp
ENSP00000419607
resolver
ensp
ENSP00000748740
resolver
enst
ENST00000308436
resolver
enst
ENST00000476907
resolver
genesymbol
TUT1
resolver
genesymbol
URLC6
resolver
genesymbol_syn
RBM21
resolver
hgnc
HGNC:26184
resolver
uniprot
A0A0A8K9B1
resolver
uniprot
A1A527
resolver
uniprot
A8K995
resolver
uniprot
F5H0R1
resolver
uniprot
Q2NL65
resolver
uniprot
Q7L583
resolver
uniprot
Q9H6H7
resolver
uniprot_entry
A0A0A8K9B1_HUMAN
resolver
uniprot_entry
F5H0R1_HUMAN
resolver
uniprot_entry
STPAP_HUMAN
resolver
uniprot_sec
A1A527
resolver
uniprot_sec
A8K995
resolver
uniprot_sec
Q2NL65
resolver
uniprot_sec
Q7L583
resolver
uniprot_sec
Q9H6H7
resolver
activity_regulation
ACTIVITY REGULATION: Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). {ECO:0000269|PubMed:18288197}.
uniprot
proteins
amino_acid_sequence
MAAVDSDVESLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRAARKAQGLRSVFVSGFPRDVDSAQLSEYFLAFGPVASVVMDKDKGVFAIVEMGDVGAREAVLSQSQHSLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLAKALAEAADVGAQMIKLVGLRELSEAERQLRSLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEEPQPVPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLLEDREEGDLGKASELAETPKEEKAEGAAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASRLEPSINVEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGGLPSNLWEGLRLGPLNLQDPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPLAPFTQLTAALVQVFREALGCHIEQATKRTRSEGGGTGESSQGGTSKRLKVDGQKNCCEEGKEEQQGCAGDGGEDRVEEMVIEVGEMVQDWAMQSPGQPGDLPLTTGKHGAPGEEGQPSHAALAERGPKGHEAAQEWSQGEAGKGASLPSSASWRCALWHRVWQGRRRARRRLQQQTKEGAGGGAGTRAGWLATEAQVTQELKGLSGGEERPETEPLLSFVASVSPADRMLTVTPLQDPQGLFPDLHHFLQVFLPQAIRHLK
uniprot
proteins
ec_number
2.7.7.19
uniprot
proteins
ec_number
2.7.7.52
uniprot
proteins
function
FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs (PubMed:18288197, PubMed:21102410). Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1 (PubMed:18288197). In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs (PubMed:21102410). In addition to adenylyltransferase activity, also has uridylyltransferase activity (PubMed:16790842, PubMed:18288197, PubMed:28589955). However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase (PubMed:18288197). Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA (PubMed:16790842, PubMed:18288197, PubMed:28589955). Not involved in replication-dependent histone mRNA degradation. {ECO:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410, ECO:0000269|PubMed:28589955}.
uniprot
proteins
mass_dalton
93847
uniprot
proteins
mutagenesis
MUTAGEN 216; /note="D->A: Abolishes adenylyltransferase activity; when associated with A-218."; /evidence="ECO:0000269|PubMed:18288197"; MUTAGEN 218; /note="D->A: Abolishes adenylyltransferase activity; when associated with A-216."; /evidence="ECO:0000269|PubMed:18288197"; MUTAGEN 779; /note="R->A: Reduced terminal uridylyltransferase activity; when associated with A-783."; /evidence="ECO:0000269|PubMed:28589955"; MUTAGEN 783; /note="R->A: Reduced terminal uridylyltransferase activity; when associated with A-779."; /evidence="ECO:0000269|PubMed:28589955
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region. {ECO:0000269|PubMed:18305108}.
uniprot
proteins
protein_family
DNA polymerase type-B-like family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16790842
uniprot
proteins
pubmed
18172165
uniprot
proteins
pubmed
18288197
uniprot
proteins
pubmed
18305108
uniprot
proteins
pubmed
21102410
uniprot
proteins
pubmed
28589955
uniprot
proteins
sequence_length
874
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16790842}. Nucleus speckle {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:18305108}.
uniprot
proteins