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Q9H6E5

- STPAP_HUMAN

UniProt

Q9H6E5 - STPAP_HUMAN

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Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

TUT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Enzyme regulationi

Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi216 – 2161Magnesium or manganese; catalyticBy similarity
Metal bindingi218 – 2181Magnesium or manganese; catalyticBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 4025C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. mRNA 3'-UTR binding Source: UniProtKB
  5. polynucleotide adenylyltransferase activity Source: UniProtKB
  6. RNA binding Source: UniProtKB
  7. RNA uridylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. mRNA cleavage Source: UniProtKB
  2. mRNA polyadenylation Source: UniProtKB
  3. snRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Speckle targeted PIP5K1A-regulated poly(A) polymerase (EC:2.7.7.19)
Short name:
Star-PAP
Alternative name(s):
RNA-binding motif protein 21
Short name:
RNA-binding protein 21
U6 snRNA-specific terminal uridylyltransferase 1 (EC:2.7.7.52)
Short name:
U6-TUTase
Gene namesi
Name:TUT1
Synonyms:RBM21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:26184. TUT1.

Subcellular locationi

GO - Cellular componenti

  1. intercellular bridge Source: HPA
  2. nuclear speck Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi216 – 2161D → A: Abolishes adenylyltransferase activity; when associated with A-218. 1 Publication
Mutagenesisi218 – 2181D → A: Abolishes adenylyltransferase activity; when associated with A-216. 1 Publication

Organism-specific databases

PharmGKBiPA162407405.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 874874Speckle targeted PIP5K1A-regulated poly(A) polymerasePRO_0000254186Add
BLAST

Post-translational modificationi

Phosphorylated by CK1 in the proline-rich (Pro-rich) region.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H6E5.
PaxDbiQ9H6E5.
PRIDEiQ9H6E5.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9H6E5.
CleanExiHS_TUT1.
ExpressionAtlasiQ9H6E5. baseline and differential.
GenevestigatoriQ9H6E5.

Organism-specific databases

HPAiHPA039253.

Interactioni

Subunit structurei

Associates with the cleavage and polyadenylation specificity factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction is direct. Interacts with PIP5K1A; interaction.2 Publications

Protein-protein interaction databases

BioGridi122325. 17 interactions.
DIPiDIP-53651N.
IntActiQ9H6E5. 12 interactions.
MINTiMINT-7900460.
STRINGi9606.ENSP00000278279.

Structurei

Secondary structure

1
874
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 615Combined sources
Helixi69 – 757Combined sources
Helixi76 – 783Combined sources
Beta strandi82 – 876Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 1018Combined sources
Helixi102 – 1098Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5GNMR-A55-141[»]
ProteinModelPortaliQ9H6E5.
SMRiQ9H6E5. Positions 23-141, 148-226, 333-610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H6E5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 12873RRMPROSITE-ProRule annotationAdd
BLAST
Domaini491 – 54959PAP-associatedAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi229 – 31082Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-B-like family.Curated
Contains 1 C2H2-type zinc finger.Curated
Contains 1 PAP-associated domain.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 4025C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
HOGENOMiHOG000115998.
HOVERGENiHBG079670.
InParanoidiQ9H6E5.
OrthoDBiEOG7353WD.
PhylomeDBiQ9H6E5.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H6E5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR
60 70 80 90 100
KAQGLRSVFV SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG
110 120 130 140 150
DVGAREAVLS QSQHSLGGHR LRVRPREQKE FQSPASKSPK GAAPDSHQLA
160 170 180 190 200
KALAEAADVG AQMIKLVGLR ELSEAERQLR SLVVALMQEV FTEFFPGCVV
210 220 230 240 250
HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS LDSALASPLD
260 270 280 290 300
PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA
310 320 330 340 350
SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG
360 370 380 390 400
CVPGVYRVQT VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS
410 420 430 440 450
ELDGRVRPLV YTLRCWAQGR GLSGSGPLLS NYALTLLVIY FLQTRDPPVL
460 470 480 490 500
PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS RLEPSINVEP LSSLLAQFFS
510 520 530 540 550
CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN LQDPFDLSHN
560 570 580 590 600
VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP
610 620 630 640 650
SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG
660 670 680 690 700
ESSQGGTSKR LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV
710 720 730 740 750
QDWAMQSPGQ PGDLPLTTGK HGAPGEEGQP SHAALAERGP KGHEAAQEWS
760 770 780 790 800
QGEAGKGASL PSSASWRCAL WHRVWQGRRR ARRRLQQQTK EGAGGGAGTR
810 820 830 840 850
AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD RMLTVTPLQD
860 870
PQGLFPDLHH FLQVFLPQAI RHLK
Length:874
Mass (Da):93,847
Last modified:February 20, 2007 - v2
Checksum:i85A4117A040FC90D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661D → G in BAB15314. (PubMed:14702039)Curated
Sequence conflicti809 – 8091Q → R in BAF85299. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti442 – 4421L → F.
Corresponds to variant rs3197865 [ dbSNP | Ensembl ].
VAR_028833

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_073741.2. NM_022830.2.
UniGeneiHs.728983.

Genome annotation databases

EnsembliENST00000476907; ENSP00000419607; ENSG00000149016.
GeneIDi64852.
KEGGihsa:64852.

Polymorphism databases

DMDMi126302611.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
RefSeqi NP_073741.2. NM_022830.2.
UniGenei Hs.728983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E5G NMR - A 55-141 [» ]
ProteinModelPortali Q9H6E5.
SMRi Q9H6E5. Positions 23-141, 148-226, 333-610.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122325. 17 interactions.
DIPi DIP-53651N.
IntActi Q9H6E5. 12 interactions.
MINTi MINT-7900460.
STRINGi 9606.ENSP00000278279.

Polymorphism databases

DMDMi 126302611.

Proteomic databases

MaxQBi Q9H6E5.
PaxDbi Q9H6E5.
PRIDEi Q9H6E5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000476907 ; ENSP00000419607 ; ENSG00000149016 .
GeneIDi 64852.
KEGGi hsa:64852.

Organism-specific databases

CTDi 64852.
GeneCardsi GC11M062342.
HGNCi HGNC:26184. TUT1.
HPAi HPA039253.
MIMi 610641. gene.
neXtProti NX_Q9H6E5.
PharmGKBi PA162407405.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5260.
GeneTreei ENSGT00550000074490.
HOGENOMi HOG000115998.
HOVERGENi HBG079670.
InParanoidi Q9H6E5.
OrthoDBi EOG7353WD.
PhylomeDBi Q9H6E5.

Miscellaneous databases

EvolutionaryTracei Q9H6E5.
GenomeRNAii 64852.
NextBioi 66977.
PROi Q9H6E5.
SOURCEi Search...

Gene expression databases

Bgeei Q9H6E5.
CleanExi HS_TUT1.
ExpressionAtlasi Q9H6E5. baseline and differential.
Genevestigatori Q9H6E5.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
[Graphical view ]
Pfami PF03828. PAP_assoc. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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.

Entry informationi

Entry nameiSTPAP_HUMAN
AccessioniPrimary (citable) accession number: Q9H6E5
Secondary accession number(s): A1A527
, A8K995, Q2NL65, Q7L583, Q9H6H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 20, 2007
Last modified: November 26, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3