TPS2/YDR074W Protein Information Help

Standard Name Tps2p
Systematic Name Ydr074wp
Alias Hog2p , Pfk3p
ORF Classification Verified
Description Phosphatase subunit of the trehalose-6-P synthase/phosphatase complex; involved in synthesis of the storage carbohydrate trehalose; expression is induced by stress conditions and repressed by the Ras-cAMP pathway; protein abundance increases in response to DNA replication stress (1, 2, 3)
Name Description Trehalose-6-phosphate PhoSphatase
Experimental Data
Molecules/cell 22700 4
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 896
Molecular Weight (Da) 102,976
Isoelectric Point (pI) 8.19

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Tps2p (InterPro)
Physical Interactions There are 38 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052E97 | P31688
MIPS: YDR074W
NCBI: 1431537 | 1730010 | 406769 | 4212 | 577801 | 6320279 | NP_010359.1
GenBank/EMBL/DDBJ: DAA11920.1 | X58858 | X70694 | Z46796 | Z74370
External Classifications EC: 3.1.3.12 [Trehalose-phosphatase]
Amino Acid Sequence (or in FASTA format)
 
       1  MTTTAQDNSP KKRQRIINCV TQLPYKIQLG ESNDDWKISA TTGNSALFSS
      51  LEYLQFDSTE YEQHVVGWTG EITRTERNLF TREAKEKPQD LDDDPLYLTK
     101  EQINGLTTTL QDHMKSDKEA KTDTTQTAPV TNNVHPVWLL RKNQSRWRNY
     151  AEKVIWPTFH YILNPSNEGE QEKNWWYDYV KFNEAYAQKI GEVYRKGDII
     201  WIHDYYLLLL PQLLRMKFND ESIIIGYFHH APWPSNEYFR CLPRRKQILD
     251  GLVGANRICF QNESFSRHFV SSCKRLLDAT AKKSKNSSNS DQYQVSVYGG
     301  DVLVDSLPIG VNTTQILKDA FTKDIDSKVL SIKQAYQNKK IIIGRDRLDS
     351  VRGVVQKLRA FETFLAMYPE WRDQVVLIQV SSPTANRNSP QTIRLEQQVN
     401  ELVNSINSEY GNLNFSPVQH YYMRIPKDVY LSLLRVADLC LITSVRDGMN
     451  TTALEYVTVK SHMSNFLCYG NPLILSEFSG SSNVLKDAIV VNPWDSVAVA
     501  KSINMALKLD KEEKSNLESK LWKEVPTIQD WTNKFLSSLK EQASSNDDME
     551  RKMTPALNRP VLLENYKQAK RRLFLFDYDG TLTPIVKDPA AAIPSARLYT
     601  ILQKLCADPH NQIWIISGRD QKFLNKWLGG KLPQLGLSAE HGCFMKDVSC
     651  QDWVNLTEKV DMSWQVRVNE VMEEFTTRTP GSFIERKKVA LTWHYRRTVP
     701  ELGEFHAKEL KEKLLSFTDD FDLEVMDGKA NIEVRPRFVN KGEIVKRLVW
     751  HQHGKPQDML KGISEKLPKD EMPDFVLCLG DDFTDEDMFR QLNTIETCWK
     801  EKYPDQKNQW GNYGFYPVTV GSASKKTVAK AHLTDPQQVL ETLGLLVGDV
     851  SLFQSAGTVD LDSRGHVKNS ESSLKSKLAS KAYVMKRSAS YTGAKV*

external links for Tps2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Tps2p
1) Winderickx J, et al.  (1996) Regulation of genes encoding subunits of the trehalose synthase complex in Saccharomyces cerevisiae: novel variations of STRE-mediated transcription control? Mol Gen Genet 252(4):470-82
2) De Virgilio C, et al.  (1993) Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur J Biochem 212(2):315-23
3) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
4) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41