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O23617

- TPS5_ARATH

UniProt

O23617 - TPS5_ARATH

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Protein
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5
Gene
TPS5, At4g17770, dl4920W, FCAALL.9
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

GO - Molecular functioni

  1. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

GO - Biological processi

  1. trehalose biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5 (EC:2.4.1.15)
Alternative name(s):
Trehalose-6-phosphate synthase 5
Short name:
AtTPS5
Gene namesi
Name:TPS5
Ordered Locus Names:At4g17770
ORF Names:dl4920W, FCAALL.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G17770.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51S → A: Abolishes binding to GRF/14-3-3. 1 Publication
Mutagenesisi32 – 321T → A: Abolishes binding to GRF/14-3-3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5
PRO_0000324826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei32 – 321Phosphothreonine1 Publication

Post-translational modificationi

Both Ser-5 and Thr-32 must be phosphorylated for binding to GRF/14-3-3.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO23617.
PRIDEiO23617.

Expressioni

Tissue specificityi

Low expression in leaves, stems, flower buds, flowers and siliques.1 Publication

Inductioni

90-fold induction by sucrose after 24 hours and by heat stress.2 Publications

Gene expression databases

ArrayExpressiO23617.
GenevestigatoriO23617.

Interactioni

Subunit structurei

Binds to the phosphopeptide-binding site of GRF/14-3-3 and to MBF1c.2 Publications

Protein-protein interaction databases

BioGridi12791. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliO23617.
SMRiO23617. Positions 144-546, 589-645.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 546487Glycosyltransferase
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 20 family.
In the C-terminal section; belongs to the trehalose phosphatase family.

Phylogenomic databases

eggNOGiCOG0380.
HOGENOMiHOG000191476.
InParanoidiO23617.
KOiK16055.
OMAiSHRNSAG.
PhylomeDBiO23617.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.

Sequencei

Sequence statusi: Complete.

O23617-1 [UniParc]FASTAAdd to Basket

« Hide

MVSRSYSNLL DLASGNFHSF SREKKRFPRV ATVTGVLSEL DDDNNSNSVC    50
SDAPSSVTQD RIIIVGNQLP IKSHRNSAGK LSFSWDNDSL LLQLKDGMRE 100
DMEVVYIGCL KEQIDTVEQD DVSQRLLENF KCVPAYIPPE LFTKYYHGFC 150
KQHLWPLFHY MLPLTPDLGG RFDRSLWQAY LSVNKIFADK VMEVISPDDD 200
FVWVHDYHLM VLPTFLRKRF NRVKLGFFLH SPFPSSEIYR TLPVRNELLR 250
ALLNADLIGF HTFDYARHFL SCCSRMLGLS YQSKRGTIGL EYYGRTVSIK 300
ILPVGIHISQ LQSILNLPET QTKVAELRDQ FLDQKVLLGV DDMDIFKGIS 350
LKLLAMEQLL TQHPEKRGRV VLVQIANPAR GRGKDVQEVQ SETEATVKRI 400
NEMFGRPGYQ PVVLIDTPLQ FFERIAYYVI AECCLVTAVR DGMNLIPYEY 450
IICRQGNPKL NETIGLDPSA AKKSMLVVSE FIGCSPSLSG AIRVNPWNID 500
AVTEAMDYAL IVSEAEKQMR HEKHHKYVST HDVAYWARSF IQDLERACGD 550
HVRKRCWGIG FGLGFRVVAL DPSFKKLSIE HIVSAYKRTK NRAILLDYDG 600
TMVQPGSIRT TPTRETIEIL NNLSSDPKNI VYLVSGKDRR TLTEWFSSCD 650
DLGLGAEHGY FIRPNDGTDW ETSSLVSGFE WKQIAEPVMR LYTETTDGST 700
IETKETALVW NYQFADPDFG SCQAKELMEH LESVLTNDPV SVKTGQQLVE 750
VKPQGVNKGL VAERLLTTMQ EKGKLLDFIL CVGDDRSDED MFEVIMSAKD 800
GPALSPVAEI FACTVGQKPS KAKYYLDDTA EIIRMLDGLA ATNTTISDQT 850
DSTATVPTKD LF 862
Length:862
Mass (Da):97,454
Last modified:March 18, 2008 - v2
Checksum:iADA155DB26DCB470
GO

Sequence cautioni

The sequence CAB10557.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB78780.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z97344 Genomic DNA. Translation: CAB10557.1. Sequence problems.
AL161547 Genomic DNA. Translation: CAB78780.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83948.1.
BT005967 mRNA. Translation: AAO64902.1.
AK118703 mRNA. Translation: BAC43297.1.
PIRiH71447.
RefSeqiNP_567538.1. NM_117886.2.
UniGeneiAt.4501.

Genome annotation databases

EnsemblPlantsiAT4G17770.1; AT4G17770.1; AT4G17770.
GeneIDi827498.
KEGGiath:AT4G17770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z97344 Genomic DNA. Translation: CAB10557.1 . Sequence problems.
AL161547 Genomic DNA. Translation: CAB78780.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE83948.1 .
BT005967 mRNA. Translation: AAO64902.1 .
AK118703 mRNA. Translation: BAC43297.1 .
PIRi H71447.
RefSeqi NP_567538.1. NM_117886.2.
UniGenei At.4501.

3D structure databases

ProteinModelPortali O23617.
SMRi O23617. Positions 144-546, 589-645.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 12791. 2 interactions.

Protein family/group databases

CAZyi GT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbi O23617.
PRIDEi O23617.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G17770.1 ; AT4G17770.1 ; AT4G17770 .
GeneIDi 827498.
KEGGi ath:AT4G17770.

Organism-specific databases

TAIRi AT4G17770.

Phylogenomic databases

eggNOGi COG0380.
HOGENOMi HOG000191476.
InParanoidi O23617.
KOi K16055.
OMAi SHRNSAG.
PhylomeDBi O23617.

Gene expression databases

ArrayExpressi O23617.
Genevestigatori O23617.

Family and domain databases

Gene3Di 3.40.50.1000. 2 hits.
InterProi IPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view ]
Pfami PF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana."
    Leyman B., Van Dijck P., Thevelein J.M.
    Trends Plant Sci. 6:510-513(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  7. "Trehalose mediated growth inhibition of Arabidopsis seedlings is due to trehalose-6-phosphate accumulation."
    Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M., Smeekens S.C.M.
    Plant Physiol. 135:879-890(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SUCROSE.
  8. "Arabidopsis trehalose-6-phosphate synthase 1 is essential for normal vegetative growth and transition to flowering."
    van Dijken A.J.H., Schluepmann H., Smeekens S.C.M.
    Plant Physiol. 135:969-977(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose."
    Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J., Wong B.H.C., Mackintosh C.
    Plant J. 47:211-223(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-5 AND THR-32, MUTAGENESIS OF SER-5 AND THR-32, INTERACTION WITH GRF/14-3-3, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "The transcriptional co-activator MBF1c is a key regulator of thermotolerance in Arabidopsis thaliana."
    Suzuki N., Bajad S., Shuman J., Shulaev V., Mittler R.
    J. Biol. Chem. 283:9269-9275(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBF1C, INDUCTION BY HEAT.
  11. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPS5_ARATH
AccessioniPrimary (citable) accession number: O23617
Secondary accession number(s): Q8GWQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: June 11, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

2-deoxyglucose, but not phenformin, enhances the phosphorylation of TPS5.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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