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Protein

Trehalose synthase complex regulatory subunit TPS3

Gene

TPS3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex.1 Publication

GO - Molecular functioni

  • catalytic activity Source: InterPro
  • enzyme regulator activity Source: SGD

GO - Biological processi

  • dephosphorylation Source: GOC
  • regulation of catalytic activity Source: GOC
  • trehalose biosynthetic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17134.
YEAST:MONOMER3O-4030.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose synthase complex regulatory subunit TPS3
Alternative name(s):
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 115 kDa subunit
Gene namesi
Name:TPS3
Ordered Locus Names:YMR261C
ORF Names:YM8156.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR261C.
SGDiS000004874. TPS3.

Subcellular locationi

GO - Cellular componenti

  • alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10541054Trehalose synthase complex regulatory subunit TPS3PRO_0000122510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei150 – 1501PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources
Modified residuei265 – 2651PhosphothreonineCombined sources
Modified residuei267 – 2671PhosphoserineCombined sources
Modified residuei273 – 2731PhosphoserineCombined sources
Modified residuei960 – 9601PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38426.
PeptideAtlasiP38426.

PTM databases

iPTMnetiP38426.

Expressioni

Inductioni

Repressed by glucose.

Interactioni

Subunit structurei

The trehalose synthase complex is composed of the two catalytic subunits TPS1 and TPS2 and at least one of the two regulatory subunits TPS3 or TSL1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TPS1Q007646EBI-19448,EBI-19430
TPS2P316885EBI-19448,EBI-19440

Protein-protein interaction databases

BioGridi35439. 51 interactions.
DIPiDIP-891N.
IntActiP38426. 7 interactions.
MINTiMINT-638595.

Structurei

3D structure databases

ProteinModelPortaliP38426.
SMRiP38426. Positions 388-760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 778492GlycosyltransferaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi125 – 249125Ser-richAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 20 family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075394.
HOGENOMiHOG000179930.
InParanoidiP38426.
KOiK16055.
OMAiKMLAYER.
OrthoDBiEOG76QFS6.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequencei

Sequence statusi: Complete.

P38426-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIIVASLFL PYTPQFEADV TNSDTAKLVE SSMIKVDCNN QELSNNKQER
60 70 80 90 100
SSSVTSASSH YIGLPQEAQI NGEPLQRANV GSPATGVNYH NEMEMLSSEQ
110 120 130 140 150
FLEELTANAT HAANSGIPPA NNPVSSGSTA QRPSVEEFFS APSARVCSPS
160 170 180 190 200
QEASASSISA SRSSAHHNDL SSSLMKNPNL SFDSHPPRVR SSSKSAVITP
210 220 230 240 250
VSKSVPDVDP AVVDVAKVRE EFQQQASLPS MKRVSGSTAG DSSIASSSSN
260 270 280 290 300
LRYSQQFQDN FIEDTDSEDD IDSDLETDAT KKYNVPKFGG YSNNAKLRAS
310 320 330 340 350
LMRNSYELFK HLPWTIVDSD KGNGSLKNAV NIAVAEKTVK EPVSWVGTMG
360 370 380 390 400
IPTDELPHEV CHKISKKLEQ DFSSFPVVTD DITFKGAYKN YAKQILWPTL
410 420 430 440 450
HYQIPDNPNS KAFEDHSWDY YQKVNQKFSD RIVSVYKPGD TIWIHDYHLM
460 470 480 490 500
LVPQMVREKL PKAKIGFFLH VSFPSSEVFR CLANRERILE GIIGANFVGF
510 520 530 540 550
QTKEYKRHFL QTCNRLLAAD VSNDEVKYHC NIVSVMYAPI GIDYYHLTSQ
560 570 580 590 600
LRNGSVLEWR QLIKERWRNK KLIVCRDQFD RIRGLQKKML AYERFLIENP
610 620 630 640 650
EYIEKVVLIQ ICIGKSSDPE YERQIMVVVD RINSLSSNIS ISQPVVFLHQ
660 670 680 690 700
DLDFAQYLAL NCEADVFLVD ALREGMNLTC HEFIVSSFEK NAPLLLSEFT
710 720 730 740 750
GSSSVLKEGA ILINPWDINH VAQSIKRSLE MSPEEKRRRW KKLFKSVIEH
760 770 780 790 800
DSDNWITKCF EYINNAWESN QETSTVFNLA PEKFCADYKA SKKHLFIFKI
810 820 830 840 850
SEPPTSRMLS LLSELSSNNI VYVLSSFTKN TFESLYNGVL NIGLIAENGA
860 870 880 890 900
YVRVNGSWYN IVEELDWMKE VAKIFDEKVE RLPGSYYKIA DSMIRFHTEN
910 920 930 940 950
ADDQDRVPTV IGEAITHINT LFDDRDIHAY VHKDIVFVQQ TGLALAAAEF
960 970 980 990 1000
LMKFYNSGVS PTDNSRISLS RTSSSMSVGN NKKHFQNQVD FVCVSGSTSP
1010 1020 1030 1040 1050
IIEPLFKLVK QEVEKNNLKF GYTILYGSSR STYAKEHING VNELFTILHD

LTAA
Length:1,054
Mass (Da):118,835
Last modified:April 18, 2006 - v3
Checksum:i02E1098B94838EA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861P → L in AAA35224 (Ref. 1) Curated
Sequence conflicti765 – 7651N → D in AAA35224 (Ref. 1) Curated
Sequence conflicti834 – 8341S → G in AAA35224 (Ref. 1) Curated
Sequence conflicti902 – 9021D → E in AAA35224 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88172 Genomic DNA. Translation: AAA35224.1.
Z49260 Genomic DNA. Translation: CAA89244.1.
AY692968 Genomic DNA. Translation: AAT92987.1.
BK006946 Genomic DNA. Translation: DAA10161.1.
RefSeqiNP_013988.1. NM_001182768.1.

Genome annotation databases

EnsemblFungiiYMR261C; YMR261C; YMR261C.
GeneIDi855303.
KEGGisce:YMR261C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88172 Genomic DNA. Translation: AAA35224.1.
Z49260 Genomic DNA. Translation: CAA89244.1.
AY692968 Genomic DNA. Translation: AAT92987.1.
BK006946 Genomic DNA. Translation: DAA10161.1.
RefSeqiNP_013988.1. NM_001182768.1.

3D structure databases

ProteinModelPortaliP38426.
SMRiP38426. Positions 388-760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35439. 51 interactions.
DIPiDIP-891N.
IntActiP38426. 7 interactions.
MINTiMINT-638595.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

PTM databases

iPTMnetiP38426.

Proteomic databases

MaxQBiP38426.
PeptideAtlasiP38426.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR261C; YMR261C; YMR261C.
GeneIDi855303.
KEGGisce:YMR261C.

Organism-specific databases

EuPathDBiFungiDB:YMR261C.
SGDiS000004874. TPS3.

Phylogenomic databases

GeneTreeiENSGT00550000075394.
HOGENOMiHOG000179930.
InParanoidiP38426.
KOiK16055.
OMAiKMLAYER.
OrthoDBiEOG76QFS6.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17134.
YEAST:MONOMER3O-4030.

Miscellaneous databases

PROiP38426.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A large open reading frame in the yeast genome containing homology to the cif1 gene."
    Manning A.M., Rosenbloom C.L., Beaudet A.L.
    Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Structural analysis of the subunits of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae and their function during heat shock."
    Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T., Wiemken A., De Virgilio C.
    Mol. Microbiol. 24:687-695(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TPS1 AND TPS2.
  6. "Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex."
    Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C., Wiemken A., Thevelein J.M.
    J. Biol. Chem. 273:33311-33319(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-181 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-150; THR-265; SER-267 AND SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPS3_YEAST
AccessioniPrimary (citable) accession number: P38426
Secondary accession number(s): D6W087, Q6B1W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 18, 2006
Last modified: June 8, 2016
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.