Serine/threonine-protein kinase TDA1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q03533 (TDA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase TDA1

Alternative name(s):
Topoisomerase I damage affected protein 1
EC=2.7.11.1

Gene names

Name:	TDA1
Ordered Locus Names:	YMR291W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine protein kinase shown to have protein phosphorylation activity in vitro. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with RIM11. Ref.11
Subcellular location	Cytoplasm. Nucleus Ref.4.
Disruption phenotype	Leads to cell death when overexpressing the camptothecin mimetic TOP1-T(722)A mutant. Ref.10
Miscellaneous	Present with 10200 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay Ref.4. Source: SGD nucleus Inferred from direct assay Ref.4. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from direct assay PubMed 16319894. Source: SGD protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 586

586

Serine/threonine-protein kinase TDA1

PRO_0000086153

Regions

Domain

39 – 351

313

Protein kinase

Nucleotide binding

45 – 53

ATP By similarity

Sites

Active site

180

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

380

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

383

Phosphoserine Ref.9

Modified residue

408

Phosphoserine Ref.9

Modified residue

409

Phosphoserine Ref.9

Modified residue

411

Phosphothreonine Ref.9

Modified residue

449

Phosphoserine Ref.8 Ref.9

Modified residue

452

Phosphoserine Ref.8

Modified residue

483

Phosphoserine Ref.7

Modified residue

484

Phosphothreonine Ref.7

Modified residue

503

Phosphothreonine Ref.9

Modified residue

504

Phosphothreonine Ref.9

Modified residue

507

Phosphoserine Ref.9

Modified residue

513

Phosphothreonine Ref.9

Modified residue

516

Phosphothreonine Ref.8

Modified residue

518

Phosphoserine Ref.7

Modified residue

522

Phosphoserine Ref.7

Modified residue

523

Phosphoserine Ref.8

Modified residue

525

Phosphoserine Ref.8

Modified residue

538

Phosphothreonine Ref.6

Modified residue

541

Phosphothreonine Ref.9

Modified residue

543

Phosphoserine Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

Q03533 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 584D620D5F798EF6
Show »

FASTA

586

66,220

        10         20         30         40         50         60 
MTTASSSASQ LQQRLPEEKP WPQLSGSNAD AQTFKCKYVT NHNSLGDGNF SVVKECMNIH 

        70         80         90        100        110        120 
TKDLYAMKLI KKQTVKNKIQ LIQREFDLLR SISEKIRDME KKNEHSLDIF EGHHHILQLF 

       130        140        150        160        170        180 
DYFETADNIV LITQLCQKGD LYEKIVENQC LDLETQVTSY CACLVSVLEF LHSQGIVHRD 

       190        200        210        220        230        240 
LKAENVLFRL RVNENEKNLQ GEHHGDFKYD LLAHDLVLAD FGLAAEYNTS KVNSLKEFVG 

       250        260        270        280        290        300 
TISYIAPEIV KCKGVGEMTP DQVGKLDKYG CPVDIWALGV LTYFMAFGYT PFDCTTDDET 

       310        320        330        340        350        360 
LECISKCDYY VDEQMMHDPK YEQFWNFVQC CFTIDPAVRR SAKNLKQHPF IKDYFATSNS 

       370        380        390        400        410        420 
LNTKDTPNFS FHPTIRRVSS TASMHTLRSP SKSRKTTTLA YLNMDGGSSE TSTAFSSKMD 

       430        440        450        460        470        480 
LPDLYVDRTI NSRERSLNRI RDTLKKTLSM TSLKPAGTFD YLHANKNGTS LSSSKSGLVK 

       490        500        510        520        530        540 
KNSTFVLDPK PPKNSLMNGC FSTTPESRSN FNTPKTLSRQ GSSTSVKKYV NEVDLLLTPR 

       550        560        570        580 
TASMSSNDTT AINDYDTTND KNPARKHAAS FQVNVDDSDG DETMQI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(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]	"Analysis of yeast protein kinases using protein chips." Zhu H., Klemic J.F., Chang S., Bertone P., Casamayor A., Klemic K.G., Smith D., Gerstein M., Reed M.A., Snyder M. Nat. Genet. 26:283-289(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"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].
[5]	"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].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND THR-538, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-483; THR-484; SER-518 AND SER-522, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-449; SER-452; THR-516; SER-523; SER-525 AND SER-543, MASS SPECTROMETRY.
[9]	"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-7; SER-380; SER-383; SER-408; SER-409; THR-411; SER-449; THR-503; THR-504; SER-507; THR-513 AND THR-541, MASS SPECTROMETRY.
[10]	"Selective ploidy ablation, a high-throughput plasmid transfer protocol, identifies new genes affecting topoisomerase I-induced DNA damage." Reid R.J., Gonzalez-Barrera S., Sunjevaric I., Alvaro D., Ciccone S., Wagner M., Rothstein R. Genome Res. 21:477-486(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[11]	"Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes." Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M., Gerstein M., Snyder M. Genes Dev. 25:767-778(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIM11.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80836 Genomic DNA. Translation: CAA56800.1. BK006946 Genomic DNA. Translation: DAA10192.1.
PIR	S47452.
RefSeq	NP_014019.1. NM_001182799.1.
3D structure databases
ProteinModelPortal	Q03533.
SMR	Q03533. Positions 4-404.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1641N.
IntAct	Q03533. 6 interactions.
MINT	MINT-388269.
STRING	4932.YMR291W.
Proteomic databases
PaxDb	Q03533.
PeptideAtlas	Q03533.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR291W; YMR291W; YMR291W.
GeneID	855336.
KEGG	sce:YMR291W.
Organism-specific databases
CYGD	YMR291w.
SGD	S000004905. TDA1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000106221.
KO	K08286.
OMA	FSVVKEC.
OrthoDB	EOG4G1QRB.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32961-MONOMER.
Gene expression databases
Genevestigator	Q03533.
GermOnline	YMR291W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR020675. Myosin_light_ch_kinase-rel. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. IPR020679. Ser/Thr_kinase_YMR291W_prd. [Graphical view]
PANTHER	PTHR22964. PTHR22964. 1 hit. PTHR22964:SF7. PTHR22964:SF7. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979067.

Entry information

Entry name

TDA1_YEAST

Accession

Primary (citable) accession number: Q03533
Secondary accession number(s): D6W0B8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents