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Q9H6E5 (STPAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length874 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. Ref.5 Ref.6 Ref.7 Ref.9

Catalytic activity

UTP + RNA(n) = diphosphate + RNA(n+1). Ref.7

ATP + RNA(n) = diphosphate + RNA(n+1). Ref.7

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Ref.7

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. Ref.7 Ref.9

Subcellular location

Nucleusnucleolus. Nucleus speckle Ref.5 Ref.7 Ref.8.

Tissue specificity

Widely expressed. Ref.7

Post-translational modification

Phosphorylated by CK1 in the proline-rich (Pro-rich) region. Ref.8

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.

Sequence caution

The sequence BAB15282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionNucleotidyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA cleavage

Inferred from direct assay Ref.9. Source: UniProtKB

mRNA polyadenylation

Inferred from direct assay Ref.9. Source: UniProtKB

snRNA processing

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentintercellular bridge

Inferred from direct assay. Source: HPA

nuclear speck

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.5. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from direct assay Ref.7. Source: UniProtKB

RNA uridylyltransferase activity

Inferred from direct assay Ref.5Ref.7. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.8. Source: UniProtKB

mRNA 3'-UTR binding

Inferred from direct assay Ref.9. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polynucleotide adenylyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Speckle targeted PIP5K1A-regulated poly(A) polymerase
PRO_0000254186

Regions

Domain56 – 12873RRM
Domain491 – 54959PAP-associated
Zinc finger16 – 4025C2H2-type
Compositional bias229 – 31082Pro-rich

Sites

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

Natural variations

Natural variant4421L → F.
Corresponds to variant rs3197865 [ dbSNP | Ensembl ].
VAR_028833

Experimental info

Mutagenesis2161D → A: Abolishes adenylyltransferase activity; when associated with A-218. Ref.7
Mutagenesis2181D → A: Abolishes adenylyltransferase activity; when associated with A-216. Ref.7
Sequence conflict661D → G in BAB15314. Ref.1
Sequence conflict8091Q → R in BAF85299. Ref.1

Secondary structure

............. 874
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H6E5 [UniParc].

Last modified February 20, 2007. Version 2.
Checksum: 85A4117A040FC90D

FASTA87493,847
        10         20         30         40         50         60 
MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR KAQGLRSVFV 

        70         80         90        100        110        120 
SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG DVGAREAVLS QSQHSLGGHR 

       130        140        150        160        170        180 
LRVRPREQKE FQSPASKSPK GAAPDSHQLA KALAEAADVG AQMIKLVGLR ELSEAERQLR 

       190        200        210        220        230        240 
SLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS 

       250        260        270        280        290        300 
LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA 

       310        320        330        340        350        360 
SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG CVPGVYRVQT 

       370        380        390        400        410        420 
VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR 

       430        440        450        460        470        480 
GLSGSGPLLS NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS 

       490        500        510        520        530        540 
RLEPSINVEP LSSLLAQFFS CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN 

       550        560        570        580        590        600 
LQDPFDLSHN VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP 

       610        620        630        640        650        660 
SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG ESSQGGTSKR 

       670        680        690        700        710        720 
LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV QDWAMQSPGQ PGDLPLTTGK 

       730        740        750        760        770        780 
HGAPGEEGQP SHAALAERGP KGHEAAQEWS QGEAGKGASL PSSASWRCAL WHRVWQGRRR 

       790        800        810        820        830        840 
ARRRLQQQTK EGAGGGAGTR AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD 

       850        860        870 
RMLTVTPLQD PQGLFPDLHH FLQVFLPQAI RHLK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Colon and Eye.
[5]"Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase."
Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R., Benecke B.-J.
RNA 12:1494-1504(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, SUBCELLULAR LOCATION.
[6]"Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
Mullen T.E., Marzluff W.F.
Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
[7]"A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
[8]"CKIalpha is associated with and phosphorylates star-PAP and is also required for expression of select star-PAP target messenger RNAs."
Gonzales M.L., Mellman D.L., Anderson R.A.
J. Biol. Chem. 283:12665-12673(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CK1.
[9]"The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
Laishram R.S., Anderson R.A.
EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS ADENYLYLTRANSFERASE, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
[10]"Solution structure of RNA binding domain in RNA binding motif protein 21."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 54-141.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK025920 mRNA. Translation: BAB15282.1. Different initiation.
AK026000 mRNA. Translation: BAB15314.1.
AK292610 mRNA. Translation: BAF85299.1.
AP002990 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74029.1.
BC005013 mRNA. Translation: AAH05013.2.
BC110910 mRNA. Translation: AAI10911.1.
BC128263 mRNA. Translation: AAI28264.1.
RefSeqNP_073741.2. NM_022830.2.
UniGeneHs.728983.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5GNMR-A55-141[»]
ProteinModelPortalQ9H6E5.
SMRQ9H6E5. Positions 23-141, 148-226, 333-610.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122325. 14 interactions.
DIPDIP-53651N.
IntActQ9H6E5. 12 interactions.
MINTMINT-7900460.
STRING9606.ENSP00000278279.

Polymorphism databases

DMDM126302611.

Proteomic databases

MaxQBQ9H6E5.
PaxDbQ9H6E5.
PRIDEQ9H6E5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000476907; ENSP00000419607; ENSG00000149016.
GeneID64852.
KEGGhsa:64852.

Organism-specific databases

CTD64852.
GeneCardsGC11M062342.
HGNCHGNC:26184. TUT1.
HPAHPA039253.
MIM610641. gene.
neXtProtNX_Q9H6E5.
PharmGKBPA162407405.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5260.
HOGENOMHOG000115998.
HOVERGENHBG079670.
InParanoidQ9H6E5.
OrthoDBEOG7353WD.
PhylomeDBQ9H6E5.

Gene expression databases

ArrayExpressQ9H6E5.
BgeeQ9H6E5.
CleanExHS_TUT1.
GenevestigatorQ9H6E5.

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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H6E5.
GenomeRNAi64852.
NextBio66977.
PROQ9H6E5.
SOURCESearch...

Entry information

Entry nameSTPAP_HUMAN
AccessionPrimary (citable) accession number: Q9H6E5
Secondary accession number(s): A1A527 expand/collapse secondary AC list , A8K995, Q2NL65, Q7L583, Q9H6H7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM