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FAQ

Speckle targeted PIP5K1A-regulated poly(A) polymerase


Known also as: RNA-binding motif protein 21, RNA-binding protein 21, U6 snRNA-specific terminal uridylyltransferase 1
Known abbreviations: TUT1, PAPD2, RBM21, Star-PAP, STARPAP, TUTase, U6-TUTase

Yeast homolog: not known

Protein




Structures Models
Domains

Secondary structure

Disorder

This protein is highly disordered (59 % of residues are predicted to be disordered)

Top 3 models:
Template: 2b4v, chain A
Method: hhsearch
Fragment: 132-641
Template: 1cvj, chain A
Method: sparks
Fragment: 1-132
Template: 3bub, chain A
Method: compass
Fragment: 571-798


Sequence length:874 aa
Molecular weight:93.847 kDa
Isoelectric point:5.9

Sequence:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MAAVDSDVESLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRAARKAQGLRSVFVSGFPRDVDSAQLSEYFLAFGPVASVVMDKDKGVFAIVEMGDVGAREAVLSQSQHSLGGHRLRVRPREQKE
FQSPASKSPKGAAPDSHQLAKALAEAADVGAQMIKLVGLRELSEAERQLRSLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEEPQPVPKAPESPSLDSALASPLDPQALACTPAS
PPDSQPPASPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLLEDREEGDLGKASELAETPKEEKAEGAAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLAL
HNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASRLEPSINVEPLSSLLAQFFSCVSCWDLRGSLLSLREGQAL
PVAGGLPSNLWEGLRLGPLNLQDPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPLAPFTQLTAALVQVFREALGCHIEQATKRTRSEGGGTG
ESSQGGTSKRLKVDGQKNCCEEGKEEQQGCAGDGGEDRVEEMVIEVGEMVQDWAMQSPGQPGDLPLTTGKHGAPGEEGQPSHAALAERGPKGHEAAQEWSQGEAGKGASLPSSASWRCALWHRVWQGRRR
ARRRLQQQTKEGAGGGAGTRAGWLATEAQVTQELKGLSGGEERPETEPLLSFVASVSPADRMLTVTPLQDPQGLFPDLHHFLQVFLPQAIRHLK


Enzyme
EC number: 2.7.7.19
Name: Polynucleotide adenylyltransferase
Reaction: ATP + RNA(n) <=> diphosphate + RNA(n+1)
EC number: 2.7.7.52
Name: RNA uridylyltransferase
Reaction: UTP + RNA(n) <=> diphosphate + RNA(n+1)

Gene location: 11q12.2


Summary
TUT1 is a nucleotidyl transferase that functions both as a terminal uridylyltransferase and as a nuclear poly(A) polymerase. The enzyme specifically adds and removes nucleotides from the 3' end of small nuclear RNAs and select mRNAs and may function in controlling gene expression and cell proliferation.

Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. 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.

As the ATP ratio is higher than UTP in cells, suggesting that TUT1 functions primarily as a poly(A) polymerase. 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. Not involved in replication-dependent histone mRNA degradation.

Associates with the cleavage and polyadenylation specificity factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction is direct. Interacts with PIP5K1A; interaction.

Phosphorylated by CK1 in the proline-rich (Pro-rich) region. Phosphorylated upon DNA damage, probably by ATM or ATR.

See this protein in other databases:
         

Literature:

Additional computationally mapped references ...


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