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Reviewed, UniProtKB/Swiss-Prot Q8R3F9 (TUT1_MOUSE)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    U6 snRNA-specific terminal uridylyltransferase 1
      Short name=U6-TUTase
    EC=2.7.7.52
Alternative name(s):
    RNA-binding motif protein 21
      Short name=RNA-binding protein 21
Gene names
Name: Tut1
Synonyms: Rbm21
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Highly specific terminal uridylyltransferase that exclusively accepts U6 snRNA as substrate. U6 snRNA is unique in that nucleotides are both added to and removed from its 3'-end. U6-TUTase is responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA By similarity.

Catalytic activity

UTP + RNA(n) = diphosphate + RNA(n+1).

Subcellular location

Nucleusnucleolus By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.3

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Cellular componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA uridylyltransferase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R3F9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8R3F9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     391-405: LALYNSRFLNLCSEM → YFCVGLKAGSKVWGI
     406-869: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 869869U6 snRNA-specific terminal uridylyltransferase 1
PRO_0000254187

Regions

Domain56 – 12873RRM

Amino acid modifications

Modified residue7441Phosphoserine Ref.3

Natural variations

Alternative sequence391 – 40515LALYN…LCSEM → YFCVGLKAGSKVWGI in isoform 2.
VSP_021201
Alternative sequence406 – 869464Missing in isoform 2.
VSP_021202

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 0D0D2C73AAC78A25

FASTA86994,603
        10         20         30         40         50         60 
MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV 

        70         80         90        100        110        120 
SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHG 

       130        140        150        160        170        180 
LRVRPREQKE FQSPASKSPK GVDSSSHQLV QALAEAADVG AQMVKLVELR ELSEAERQLR 

       190        200        210        220        230        240 
NLVVALMQEV FTEFFPGCVV HPFGSTVNSF DVHGCDLDLF LDMGDMEETE PDPKAPKVPE 

       250        260        270        280        290        300 
TSSLDSALAS SLDPQALACT PASPLDSLSP TSVQESESLD FDTPSSLAPQ TPDSALGSDT 

       310        320        330        340        350        360 
VTSPQSLPPV SPLQEDRKEG KQGKELELAE EASKDEKEEA AAVLELVGSI LRGCVPGVYR 

       370        380        390        400        410        420 
VQTVPSARRP VVKFCHRPSG LHGDVSLSNR LALYNSRFLN LCSEMDGRVR PLVYTLRCWA 

       430        440        450        460        470        480 
QHNGLSGGGP LLNNYALTLL VIYFLQTRDP PVLPTVAQLT QRAGEGEQVE VDGWDCSFPK 

       490        500        510        520        530        540 
DASRLEPSTN VEPLSSLLAQ FFSCVSCLDL SGSLLSLREG RPLMVAEGLP SDLWEGLRLG 

       550        560        570        580        590        600 
PMNLQDPFDL SHNVAANVTG RVAKRLQSCC GAAASYCRSL QYQQRSSRGR DWGLLPLLQP 

       610        620        630        640        650        660 
SSPSSLLSAK LIPLPSAPFP QVIMALVDVL REALGCHIEQ GTKRRRSEGA RIKDSPLGGV 

       670        680        690        700        710        720 
NKRQRLGGQE KSFEEGKEEP QGCAGDHSEN EVEEMVIEVR ETPQDWALLH SGPPEEELPL 

       730        740        750        760        770        780 
MTANCLDKAA EHNPMKPEVA GEGSQGETGK EASHPSSVSW RCALWHQVWQ GRRRARRRLQ 

       790        800        810        820        830        840 
QQTKEEGRGG PTTGAEWLAM EARVTQELKG PNSEQERPPG EPLLSFVASA SQAEQTLTVA 

       850        860 
PLQDSQGLFP GLHHFLQGFI PQALKNLLK 

« Hide

Isoform 2.

Checksum: DE8F28DDC4C52B65
Show »

FASTA40543,617

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Hypothalamus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK138418 mRNA. Translation: BAE23652.1.
BC023900 mRNA. Translation: AAH23900.1.
BC025499 mRNA. Translation: AAH25499.1.
IPIIPI00153749.
IPI00798562.
RefSeqNP_932110.1.
UniGeneMm.165979

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ8R3F9.

Proteomic databases

PRIDEQ8R3F9.

Genome annotation databases

EnsemblENSMUSG00000071645. Mus musculus. [Contig view]
GeneID70044.
KEGGmmu:70044.

Organism-specific databases

MGIMGI:1917294. Tut1.

Phylogenomic databases

HOVERGENQ8R3F9.
OMAQ8R3F9. QGGTSKR.

Enzyme and pathway databases

BRENDA2.7.7.52. 244.

Gene expression databases

ArrayExpressQ8R3F9.
BgeeQ8R3F9.
GermOnlineENSMUSG00000071645. Mus musculus.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR002058. PAP_assoc.
IPR000504. RRM_RNP1.
IPR015880. Znf_C2H2-like.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF03828. PAP_assoc. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio330881.
SOURCESearch...

Entry information

Entry nameTUT1_MOUSE
AccessionPrimary (citable) accession number: Q8R3F9
Secondary accession number(s): Q3UUH3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents