CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006012
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Trehalose-phosphatase 
Protein Synonyms/Alias
 Trehalose synthase complex catalytic subunit TPS2; Trehalose-6-phosphate phosphatase; TPP 
Gene Name
 TPS2 
Gene Synonyms/Alias
 PFK3; YDR074W; YD8554.07 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
323ILKDAFTKDIDSKVLubiquitination[1]
520EKSNLESKLWKEVPTubiquitination[1]
626RDQKFLNKWLGGKLPacetylation[2]
881LKSKLASKAYVMKRSacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6- phosphate and UDP-glucose in a two step process. 
Sequence Annotation
 REGION 1 554 Glycosyltransferase.  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 896 AA 
Protein Sequence
MTTTAQDNSP KKRQRIINCV TQLPYKIQLG ESNDDWKISA TTGNSALFSS LEYLQFDSTE 60
YEQHVVGWTG EITRTERNLF TREAKEKPQD LDDDPLYLTK EQINGLTTTL QDHMKSDKEA 120
KTDTTQTAPV TNNVHPVWLL RKNQSRWRNY AEKVIWPTFH YILNPSNEGE QEKNWWYDYV 180
KFNEAYAQKI GEVYRKGDII WIHDYYLLLL PQLLRMKFND ESIIIGYFHH APWPSNEYFR 240
CLPRRKQILD GLVGANRICF QNESFSRHFV SSCKRLLDAT AKKSKNSSNS DQYQVSVYGG 300
DVLVDSLPIG VNTTQILKDA FTKDIDSKVL SIKQAYQNKK IIIGRDRLDS VRGVVQKLRA 360
FETFLAMYPE WRDQVVLIQV SSPTANRNSP QTIRLEQQVN ELVNSINSEY GNLNFSPVQH 420
YYMRIPKDVY LSLLRVADLC LITSVRDGMN TTALEYVTVK SHMSNFLCYG NPLILSEFSG 480
SSNVLKDAIV VNPWDSVAVA KSINMALKLD KEEKSNLESK LWKEVPTIQD WTNKFLSSLK 540
EQASSNDDME RKMTPALNRP VLLENYKQAK RRLFLFDYDG TLTPIVKDPA AAIPSARLYT 600
ILQKLCADPH NQIWIISGRD QKFLNKWLGG KLPQLGLSAE HGCFMKDVSC QDWVNLTEKV 660
DMSWQVRVNE VMEEFTTRTP GSFIERKKVA LTWHYRRTVP ELGEFHAKEL KEKLLSFTDD 720
FDLEVMDGKA NIEVRPRFVN KGEIVKRLVW HQHGKPQDML KGISEKLPKD EMPDFVLCLG 780
DDFTDEDMFR QLNTIETCWK EKYPDQKNQW GNYGFYPVTV GSASKKTVAK AHLTDPQQVL 840
ETLGLLVGDV SLFQSAGTVD LDSRGHVKNS ESSLKSKLAS KAYVMKRSAS YTGAKV 896 
Gene Ontology
 GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IPI:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0004805; F:trehalose-phosphatase activity; IMP:SGD.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0005992; P:trehalose biosynthetic process; IMP:SGD. 
Interpro
 IPR001830; Glyco_trans_20.
 IPR023214; HAD-like_dom.
 IPR006379; HAD-SF_hydro_IIB.
 IPR003337; Trehalose_PPase. 
Pfam
 PF00982; Glyco_transf_20
 PF02358; Trehalose_PPase 
SMART
  
PROSITE
  
PRINTS