Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8R3F9 (STPAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Speckle targeted PIP5K1A-regulated poly(A) polymerase
Short name=Star-PAP
EC=2.7.7.19
Alternative name(s):
RNA-binding motif protein 21
Short name=RNA-binding protein 21
U6 snRNA-specific terminal uridylyltransferase 1
Short name=U6-TUTase
EC=2.7.7.52
Gene names
Name:Tut1
Synonyms:Rbm21
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. 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. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it 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 By similarity.

Catalytic activity

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

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

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) By similarity.

Subunit structure

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

Subcellular location

Nucleus › nucleolus By similarity. Nucleus speckle By similarity.

Post-translational modification

Phosphorylated by CK1 in the proline-rich (Pro-rich) region By similarity.

Sequence similarities

Belongs to the DNA polymerase type-B-like family.

Contains 1 C2H2-type zinc finger.

Contains 1 PAP-associated domain.

Contains 1 RRM (RNA recognition motif) domain.

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 – 869869Speckle targeted PIP5K1A-regulated poly(A) polymerase
PRO_0000254187

Regions

Domain56 – 12873RRM
Domain494 – 55259PAP-associated
Zinc finger16 – 4025C2H2-type
Compositional bias229 – 31284Pro-rich

Sites

Metal binding2161Magnesium or manganese; catalytic By similarity
Metal binding2181Magnesium or manganese; catalytic By similarity

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 [UniParc].

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK138418 mRNA. Translation: BAE23652.1.
BC023900 mRNA. Translation: AAH23900.1.
BC025499 mRNA. Translation: AAH25499.1.
IPIIPI00153749.
IPI00798562.
RefSeqNP_932110.1. NM_197993.2.
UniGeneMm.165979.

3D structure databases

ProteinModelPortalQ8R3F9.
SMRQ8R3F9. Positions 23-141, 326-582.
ModBaseSearch...

PTM databases

PhosphoSiteQ8R3F9.

Proteomic databases

PaxDbQ8R3F9.
PRIDEQ8R3F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000096239; ENSMUSP00000093958; ENSMUSG00000071645.
GeneID70044.
KEGGmmu:70044.
UCSCuc008gog.1. mouse.
uc008goh.1. mouse.

Organism-specific databases

CTD64852.
MGIMGI:1917294. Tut1.

Phylogenomic databases

eggNOGCOG5260.
GeneTreeENSGT00550000074490.
HOVERGENHBG079670.
InParanoidQ8R3F9.
OMAEQQGCAG.
OrthoDBEOG480HWB.

Gene expression databases

BgeeQ8R3F9.
GenevestigatorQ8R3F9.
GermOnlineENSMUSG00000071645. Mus musculus.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF03828. PAP_assoc. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. False negative.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio330881.
SOURCESearch...

Entry information

Entry nameSTPAP_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: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents