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ARATH:DSP4

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Species (Taxon ID) Arabidopsis thaliana (Mouse-ear cress). (3702)
Gene Name(s) DSP4 (synonyms: PTPKIS1, SEX4)
Protein Name(s) Phosphoglucan phosphatase DSP4, chloroplastic

AtPTPKIS1 Dual specificity protein phosphatase 4 Protein STARCH-EXCESS 4 AtSEX4

External Links
UniProt Q9FEB5
EMBL AJ302781
AJ302779
AJ302779
AL049711
CP002686
AF439823
AY143878
AY084675
PIR T49097
RefSeq NP_566960.1
UniGene At.24067
PDB 3NME
4PYH
PDBsum 3NME
4PYH
ProteinModelPortal Q9FEB5
SMR Q9FEB5
IntAct Q9FEB5
STRING 3702.AT3G52180.1-P
CAZy CBM48
PRIDE Q9FEB5
EnsemblPlants AT3G52180.1
GeneID 824383
KEGG ath:AT3G52180
TAIR AT3G52180
HOGENOM HOG000005968
InParanoid Q9FEB5
OMA RLMIREY
PhylomeDB Q9FEB5
BioCyc ARA:AT3G52180-MONOMER
MetaCyc:AT3G52180-MONOMER
Proteomes UP000006548
ExpressionAtlas Q9FEB5
Genevestigator Q9FEB5
GO GO:0009507
GO:0009570
GO:0019203
GO:0030247
GO:0008138
GO:0006470
GO:0005983
GO:0005982
Gene3D 3.90.190.10
InterPro IPR030079
IPR000340
IPR014756
IPR029021
IPR000387
PANTHER PTHR10343:SF46
Pfam PF00782
SUPFAM SSF52799
SSF81296
PROSITE PS50056

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005982

starch metabolic process

PMID:19141707[1]

ECO:0000315

P

Figure 1 shows SEX4 incubated with different amounts of prephosphorylated starch granules caused dephosphorylates the starch granule surface. Activity increased with starch added. Activity decreased when leaf extracts from mutants sex4 when compared to wild type extracts.

complete
CACAO 7116

enables

GO:2001066

amylopectin binding

PMID:24799671[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019203

carbohydrate phosphatase activity

PMID:24799671[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0005983

starch catabolic process

PMID:24799671[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0005982

starch metabolic process

PMID:19141707[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0030247

polysaccharide binding

PMID:16623901[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019203

carbohydrate phosphatase activity

PMID:19141707[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009570

chloroplast stroma

PMID:20061580[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009570

chloroplast stroma

PMID:18633119[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:18431481[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:16772378[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:16623901[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0005983

starch catabolic process

PMID:19776162[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0005982

starch metabolic process

PMID:16513634[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:2001070

starch binding

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002927728
TAIR:locus:2085542

F

Seeded From UniProt

complete

involved_in

GO:0046838

phosphorylated carbohydrate dephosphorylation

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002927728
TAIR:locus:2085542

P

Seeded From UniProt

complete

enables

GO:0019203

carbohydrate phosphatase activity

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002927728
TAIR:locus:2085542
UniProtKB:Q9FEB5

F

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002927728
TAIR:locus:2085542
UniProtKB:Q9FEB5

C

Seeded From UniProt

complete

involved_in

GO:0005983

starch catabolic process

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002927728
TAIR:locus:2085542
UniProtKB:Q9FEB5

P

Seeded From UniProt

complete

involved_in

GO:0005982

starch metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030079

P

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020422

P

Seeded From UniProt

complete

involved_in

GO:0007623

circadian rhythm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030079

P

Seeded From UniProt

complete

enables

GO:0008138

protein tyrosine/serine/threonine phosphatase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000340
InterPro:IPR020422

F

Seeded From UniProt

complete

involved_in

GO:0016311

dephosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000340
InterPro:IPR000387

P

Seeded From UniProt

complete

enables

GO:0016791

phosphatase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000387

F

Seeded From UniProt

complete

enables

GO:0019203

carbohydrate phosphatase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030079

F

Seeded From UniProt

complete

involved_in

GO:0005982

starch metabolic process

PMID:16623901[3]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009536

plastid

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0934

C

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0150
UniProtKB-SubCell:SL-0049

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0119

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Kötting, O et al. (2009) STARCH-EXCESS4 is a laforin-like Phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana. Plant Cell 21 334-46 PubMed GONUTS page
  2. 2.0 2.1 2.2 Meekins, DA et al. (2014) Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity. Proc. Natl. Acad. Sci. U.S.A. 111 7272-7 PubMed GONUTS page
  3. 3.0 3.1 3.2 Kerk, D et al. (2006) A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch. Plant J. 46 400-13 PubMed GONUTS page
  4. Ferro, M et al. (2010) AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol. Cell Proteomics 9 1063-84 PubMed GONUTS page
  5. Rutschow, H et al. (2008) Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiol. 148 156-75 PubMed GONUTS page
  6. Zybailov, B et al. (2008) Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 3 e1994 PubMed GONUTS page
  7. Sokolov, LN et al. (2006) A redox-regulated chloroplast protein phosphatase binds to starch diurnally and functions in its accumulation. Proc. Natl. Acad. Sci. U.S.A. 103 9732-7 PubMed GONUTS page
  8. Streb, S et al. (2009) The debate on the pathway of starch synthesis: a closer look at low-starch mutants lacking plastidial phosphoglucomutase supports the chloroplast-localized pathway. Plant Physiol. 151 1769-72 PubMed GONUTS page
  9. Niittylä, T et al. (2006) Similar protein phosphatases control starch metabolism in plants and glycogen metabolism in mammals. J. Biol. Chem. 281 11815-8 PubMed GONUTS page
  10. 10.0 10.1 10.2 10.3 10.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page