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P40032 (TPA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PKHD-type hydroxylase TPA1
EC=1.14.11.-
Alternative name(s):
Termination and polyadenylation protein 1
Gene names
Name:TPA1
Ordered Locus Names:YER049W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Ascorbate Potential.

Subunit structure

Interacts with FRK1, eRF1 (SUP1), eRF3 (SUP35) and polyadenylate-binding protein PAB1. Ref.5 Ref.7

Subcellular location

Nucleus Ref.3.

Miscellaneous

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

Sequence similarities

Belongs to the TPA1 family.

Contains 1 Fe2OG dioxygenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 644644PKHD-type hydroxylase TPA1
PRO_0000206670

Regions

Domain141 – 247107Fe2OG dioxygenase

Sites

Metal binding1591Iron By similarity
Metal binding1611Iron By similarity
Metal binding2271Iron By similarity
Binding site23612-oxoglutarate Potential

Amino acid modifications

Modified residue2931Phosphoserine Ref.6
Modified residue5771Phosphoserine Ref.6
Modified residue6071Phosphoserine Ref.6

Secondary structure

1 ................................................................................................... 644
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40032 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 1273410E75479A46

FASTA64474,041
        10         20         30         40         50         60 
MKRKTAEVKG EKERNSKQIS LEEDKIKGMF NPKIWDKTFQ DGLKKEIEDS QPYNWGTIHE 

        70         80         90        100        110        120 
LVNDDLLRAV RKEIETEIHF TKKETDIYRV NQSGDLANLS GLDWDDLSRL PNLFKLRQIL 

       130        140        150        160        170        180 
YSKQYRDFFG YVTKAGKLSG SKTDMSINTY TKGCHLLTHD DVIGSRRISF ILYLPDPDRK 

       190        200        210        220        230        240 
WKSHYGGGLR LFPSILPNVP HSDPSAKLVP QFNQIAFFKV LPGFSFHDVE EVKVDKHRLS 

       250        260        270        280        290        300 
IQGWYHIPQV GEEGYIPGEE EAWVRNNTST LAQIESNVLE DFEFPKDERN ILSFHEVKHF 

       310        320        330        340        350        360 
EKMLKGDAGA KTDNTPKESM TSVISDSVKL SEAEFTYLSQ YISPEHLSSK GIEKLQKQFV 

       370        380        390        400        410        420 
ENSSLQIESF LNDDKSELLK KVIKQKELEQ ECPYHSKDVK APWKTAIPPH KARYLYIDGK 

       430        440        450        460        470        480 
EYRNFQTEAD ILEALNNNDL PNFQFTKDAI KIISDASGNS RENNFDAELA LIDLAVFHKS 

       490        500        510        520        530        540 
TIFKKYLALL TSLCPVSEQI LIRRFRPGMD FTLATKCRFN ELLKSNPDII DAVLEGTLCL 

       550        560        570        580        590        600 
TPSAGWESGE LGGYELYMMD DDEDNKQYLK EDVEDASVYR ADDSGDSVLI NDPPAWNTFN 

       610        620        630        640 
LVLRDESVLE FVKYVSWSAK SSRWDVKMKW DVKSCDEDGQ EDEA

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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-293; SER-577 AND SER-607, MASS SPECTROMETRY.
[7]"A global protein kinase and phosphatase interaction network in yeast."
Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B., Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D., Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C., Nesvizhskii A.I., Tyers M.
Science 328:1043-1046(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FRK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U18796 Genomic DNA. Translation: AAB64584.1.
BK006939 Genomic DNA. Translation: DAA07705.1.
PIRS50552.
RefSeqNP_010969.1. NM_001178940.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KT1X-ray2.50A21-644[»]
3KT4X-ray2.73A21-644[»]
3KT7X-ray1.77A21-644[»]
3MGUX-ray2.80A1-644[»]
ProteinModelPortalP40032.
SMRP40032. Positions 22-636.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2878N.
IntActP40032. 6 interactions.
MINTMINT-516781.
STRING4932.YER049W.

Proteomic databases

PaxDbP40032.
PeptideAtlasP40032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER049W; YER049W; YER049W.
GeneID856775.
KEGGsce:YER049W.

Organism-specific databases

CYGDYER049w.
SGDS000000851. TPA1.

Phylogenomic databases

eggNOGCOG3751.
GeneTreeENSGT00390000002349.
HOGENOMHOG000165892.
OMAFHDVEEV.
OrthoDBEOG4004SX.

Gene expression databases

GenevestigatorP40032.
GermOnlineYER049W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR019601. Oxoglutarate/Fe-dep_Oase_C.
IPR006620. Pro_4_hyd_alph.
[Graphical view]
PfamPF13640. 2OG-FeII_Oxy_3. 1 hit.
PF10637. Ofd1_CTDD. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40032.
NextBio982973.

Entry information

Entry nameTPA1_YEAST
AccessionPrimary (citable) accession number: P40032
Secondary accession number(s): D3DLV1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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