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P40032

- TPA1_YEAST

UniProt

P40032 - TPA1_YEAST

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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. 2 Publications
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. 56 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.
InParanoidiP40032.
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

        10         20         30         40         50
MKRKTAEVKG EKERNSKQIS LEEDKIKGMF NPKIWDKTFQ DGLKKEIEDS
60 70 80 90 100
QPYNWGTIHE LVNDDLLRAV RKEIETEIHF TKKETDIYRV NQSGDLANLS
110 120 130 140 150
GLDWDDLSRL PNLFKLRQIL YSKQYRDFFG YVTKAGKLSG SKTDMSINTY
160 170 180 190 200
TKGCHLLTHD DVIGSRRISF ILYLPDPDRK WKSHYGGGLR LFPSILPNVP
210 220 230 240 250
HSDPSAKLVP QFNQIAFFKV LPGFSFHDVE EVKVDKHRLS IQGWYHIPQV
260 270 280 290 300
GEEGYIPGEE EAWVRNNTST LAQIESNVLE DFEFPKDERN ILSFHEVKHF
310 320 330 340 350
EKMLKGDAGA KTDNTPKESM TSVISDSVKL SEAEFTYLSQ YISPEHLSSK
360 370 380 390 400
GIEKLQKQFV ENSSLQIESF LNDDKSELLK KVIKQKELEQ ECPYHSKDVK
410 420 430 440 450
APWKTAIPPH KARYLYIDGK EYRNFQTEAD ILEALNNNDL PNFQFTKDAI
460 470 480 490 500
KIISDASGNS RENNFDAELA LIDLAVFHKS TIFKKYLALL TSLCPVSEQI
510 520 530 540 550
LIRRFRPGMD FTLATKCRFN ELLKSNPDII DAVLEGTLCL TPSAGWESGE
560 570 580 590 600
LGGYELYMMD DDEDNKQYLK EDVEDASVYR ADDSGDSVLI NDPPAWNTFN
610 620 630 640
LVLRDESVLE FVKYVSWSAK SSRWDVKMKW DVKSCDEDGQ EDEA
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. 56 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.
InParanoidi P40032.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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