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P40032

- TPA1_YEAST

UniProt

P40032 - TPA1_YEAST

Protein

Prolyl 3,4-dihydroxylase TPA1

Gene

TPA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation of 'Pro-64' of small ribosomal subunit RPS23 (RPS23A and RPS23B), thereby regulating protein translation termination efficiency. Part of a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It associates specifically with components of the translation termination complex and is involved in both translation termination and in regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.3 Publications

    Catalytic activityi

    Peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl 3,4-hydroxy-L-proline + succinate + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication
    Ascorbate.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi159 – 1591Iron1 PublicationPROSITE-ProRule annotation
    Metal bindingi161 – 1611Iron1 PublicationPROSITE-ProRule annotation
    Binding sitei173 – 17312-oxoglutarate1 PublicationPROSITE-ProRule annotation
    Metal bindingi227 – 2271Iron1 PublicationPROSITE-ProRule annotation
    Binding sitei238 – 23812-oxoglutarate1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. peptidyl-proline dioxygenase activity Source: UniProtKB
    4. poly(A) binding Source: SGD

    GO - Biological processi

    1. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: SGD
    2. peptidyl-proline di-hydroxylation Source: UniProtKB
    3. regulation of translational termination Source: UniProtKB
    4. translational termination Source: SGD

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30228-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl 3,4-dihydroxylase TPA1 (EC:1.14.11.-)
    Alternative name(s):
    Termination and polyadenylation protein 1
    Gene namesi
    Name:TPA1
    Ordered Locus Names:YER049W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER049w.
    SGDiS000000851. TPA1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Decrease of translation termination efficacy and an increase in mRNAs half-lives and longer mRNA poly(A) tails.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1613HDD → ADN or ADA: Loss of function.
    Mutagenesisi159 – 1591H → A: Loss of function.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 644644Prolyl 3,4-dihydroxylase TPA1PRO_0000206670Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei607 – 6071Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40032.
    PaxDbiP40032.
    PeptideAtlasiP40032.

    Expressioni

    Gene expression databases

    GenevestigatoriP40032.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with FRK1, eRF1 (SUP1), eRF3 (SUP35) and polyadenylate-binding protein PAB1. Interacts with ETT1.4 Publications

    Protein-protein interaction databases

    BioGridi36788. 55 interactions.
    DIPiDIP-2878N.
    IntActiP40032. 5 interactions.
    MINTiMINT-516781.
    STRINGi4932.YER049W.

    Structurei

    Secondary structure

    1
    644
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 293
    Helixi32 – 354
    Helixi37 – 4812
    Beta strandi51 – 533
    Beta strandi56 – 605
    Helixi64 – 7714
    Beta strandi81 – 844
    Beta strandi86 – 927
    Helixi111 – 12010
    Helixi123 – 13210
    Beta strandi139 – 1424
    Beta strandi145 – 1506
    Beta strandi155 – 1595
    Beta strandi166 – 1738
    Helixi183 – 1853
    Beta strandi189 – 1913
    Beta strandi194 – 1963
    Beta strandi205 – 2084
    Beta strandi214 – 2196
    Turni222 – 2243
    Beta strandi227 – 2293
    Beta strandi238 – 2469
    Helixi259 – 26810
    Helixi269 – 2779
    Helixi278 – 2825
    Helixi294 – 30411
    Helixi332 – 3398
    Helixi344 – 3463
    Helixi349 – 36214
    Beta strandi363 – 3697
    Helixi373 – 38917
    Helixi396 – 3983
    Turni409 – 4113
    Beta strandi415 – 4173
    Beta strandi419 – 4213
    Helixi428 – 4369
    Helixi443 – 45715
    Turni461 – 4633
    Helixi466 – 47914
    Helixi481 – 49111
    Beta strandi492 – 4954
    Beta strandi497 – 5059
    Turni507 – 5093
    Helixi521 – 5233
    Beta strandi527 – 54014
    Turni546 – 5505
    Beta strandi555 – 5584
    Beta strandi588 – 5925
    Beta strandi596 – 6049
    Beta strandi609 – 6124
    Beta strandi623 – 63412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KT1X-ray2.50A21-644[»]
    3KT4X-ray2.73A21-644[»]
    3KT7X-ray1.77A21-644[»]
    3MGUX-ray2.80A1-644[»]
    ProteinModelPortaliP40032.
    SMRiP40032. Positions 22-636.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40032.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini141 – 247107Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TPA1 family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3751.
    GeneTreeiENSGT00390000002349.
    HOGENOMiHOG000165892.
    OMAiPEWGGAL.
    OrthoDBiEOG7J44H4.

    Family and domain databases

    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR019601. Oxoglutarate/Fe-dep_Oase_C.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view]
    PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
    PF10637. Ofd1_CTDD. 1 hit.
    [Graphical view]
    SMARTiSM00702. P4Hc. 1 hit.
    [Graphical view]
    PROSITEiPS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40032-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRKTAEVKG EKERNSKQIS LEEDKIKGMF NPKIWDKTFQ DGLKKEIEDS    50
    QPYNWGTIHE LVNDDLLRAV RKEIETEIHF TKKETDIYRV NQSGDLANLS 100
    GLDWDDLSRL PNLFKLRQIL YSKQYRDFFG YVTKAGKLSG SKTDMSINTY 150
    TKGCHLLTHD DVIGSRRISF ILYLPDPDRK WKSHYGGGLR LFPSILPNVP 200
    HSDPSAKLVP QFNQIAFFKV LPGFSFHDVE EVKVDKHRLS IQGWYHIPQV 250
    GEEGYIPGEE EAWVRNNTST LAQIESNVLE DFEFPKDERN ILSFHEVKHF 300
    EKMLKGDAGA KTDNTPKESM TSVISDSVKL SEAEFTYLSQ YISPEHLSSK 350
    GIEKLQKQFV ENSSLQIESF LNDDKSELLK KVIKQKELEQ ECPYHSKDVK 400
    APWKTAIPPH KARYLYIDGK EYRNFQTEAD ILEALNNNDL PNFQFTKDAI 450
    KIISDASGNS RENNFDAELA LIDLAVFHKS TIFKKYLALL TSLCPVSEQI 500
    LIRRFRPGMD FTLATKCRFN ELLKSNPDII DAVLEGTLCL TPSAGWESGE 550
    LGGYELYMMD DDEDNKQYLK EDVEDASVYR ADDSGDSVLI NDPPAWNTFN 600
    LVLRDESVLE FVKYVSWSAK SSRWDVKMKW DVKSCDEDGQ EDEA 644
    Length:644
    Mass (Da):74,041
    Last modified:February 1, 1995 - v1
    Checksum:i1273410E75479A46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18796 Genomic DNA. Translation: AAB64584.1.
    BK006939 Genomic DNA. Translation: DAA07705.1.
    PIRiS50552.
    RefSeqiNP_010969.1. NM_001178940.1.

    Genome annotation databases

    EnsemblFungiiYER049W; YER049W; YER049W.
    GeneIDi856775.
    KEGGisce:YER049W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18796 Genomic DNA. Translation: AAB64584.1 .
    BK006939 Genomic DNA. Translation: DAA07705.1 .
    PIRi S50552.
    RefSeqi NP_010969.1. NM_001178940.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KT1 X-ray 2.50 A 21-644 [» ]
    3KT4 X-ray 2.73 A 21-644 [» ]
    3KT7 X-ray 1.77 A 21-644 [» ]
    3MGU X-ray 2.80 A 1-644 [» ]
    ProteinModelPortali P40032.
    SMRi P40032. Positions 22-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36788. 55 interactions.
    DIPi DIP-2878N.
    IntActi P40032. 5 interactions.
    MINTi MINT-516781.
    STRINGi 4932.YER049W.

    Proteomic databases

    MaxQBi P40032.
    PaxDbi P40032.
    PeptideAtlasi P40032.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER049W ; YER049W ; YER049W .
    GeneIDi 856775.
    KEGGi sce:YER049W.

    Organism-specific databases

    CYGDi YER049w.
    SGDi S000000851. TPA1.

    Phylogenomic databases

    eggNOGi COG3751.
    GeneTreei ENSGT00390000002349.
    HOGENOMi HOG000165892.
    OMAi PEWGGAL.
    OrthoDBi EOG7J44H4.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30228-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P40032.
    NextBioi 982973.

    Gene expression databases

    Genevestigatori P40032.

    Family and domain databases

    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR019601. Oxoglutarate/Fe-dep_Oase_C.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view ]
    Pfami PF13640. 2OG-FeII_Oxy_3. 1 hit.
    PF10637. Ofd1_CTDD. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae."
      Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.
      Mol. Cell. Biol. 26:5237-5248(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAB1; SUP1 AND SUP35.
    6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FRK1.
    8. Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 159-ASP--HIS-161.
    9. "Structural and functional insights into Saccharomyces cerevisiae Tpa1, a putative prolylhydroxylase influencing translation termination and transcription."
      Henri J., Rispal D., Bayart E., van Tilbeurgh H., Seraphin B., Graille M.
      J. Biol. Chem. 285:30767-30778(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-644, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, MUTAGENESIS OF 159-ASP--HIS-161, INTERACTION WITH ETT1.
    10. "Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex."
      Kim H.S., Kim H.L., Kim K.H., Kim D.J., Lee S.J., Yoon J.Y., Yoon H.J., Lee H.Y., Park S.B., Kim S.J., Lee J.Y., Suh S.W.
      Nucleic Acids Res. 38:2099-2110(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 21-644 IN COMPLEX WITH IRON AND 2-OXOGLUTARATE, SUBUNIT.

    Entry informationi

    Entry nameiTPA1_YEAST
    AccessioniPrimary (citable) accession number: P40032
    Secondary accession number(s): D3DLV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8910 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3