Q7X9V2 · PIE1_ARATH

Function

function

Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant H2A.F/Z leading to transcriptional regulation of selected genes (e.g. FLC) by chromatin remodeling. Probable DNA-dependent ATPase. Not involved in the repression of FLC in gametophytes, but required for the reactivation of FLC in early embryos and for the maintenance of full activation of FLC in late embryos.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site561-568ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplant-type cell wall
Cellular ComponentSWI/SNF complex
Cellular ComponentSwr1 complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent chromatin remodeler activity
Molecular FunctionDNA binding
Molecular Functionhelicase activity
Biological Processcell differentiation
Biological Processflower development
Biological Processresponse to cadmium ion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
  • EC number
  • Alternative names
    • Independent early flowering 1 protein
    • Protein CHROMATIN REMODELING 13
      (AtCHR13)

Gene names

    • Name
      PIE1
    • Synonyms
      CHR13
    • ORF names
      MBK21.19
    • Ordered locus names
      At3g12810

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q7X9V2
  • Secondary accessions
    • Q9LTV5

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Early flowering. Loss of H2A.Z from chromatin.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 149 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004237291-2055Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in ovules, but not in stamens.

Induction

Not regulated by vernalization.

Gene expression databases

Interaction

Subunit

Component of the SWR1 chromatin-remodeling complex composed of at least ARP6/ESD1/SUF3, PIE1, SWC6, SWC2 and H2AZs (HTA8, HTA9, HTA11). Interacts (via c-terminus) with SWC6 and ARP6 and (via N-terminus) with H2AZs.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q7X9V2ARP6 Q8LGE34EBI-1537462, EBI-1537316
BINARY Q7X9V2SWC6 Q9FHW24EBI-1537462, EBI-1537353

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif, domain, coiled coil.

TypeIDPosition(s)Description
Region1-47Disordered
Compositional bias21-47Basic and acidic residues
Motif29-36Nuclear localization signal 1
Domain35-107HSA
Coiled coil78-147
Region183-332Disordered
Compositional bias212-229Acidic residues
Coiled coil229-250
Compositional bias230-247Basic and acidic residues
Compositional bias254-282Basic and acidic residues
Compositional bias283-303Polar residues
Compositional bias317-332Polar residues
Region340-359Disordered
Coiled coil392-416
Region432-461Disordered
Domain548-713Helicase ATP-binding
Motif664-667DEAH box
Domain1076-1229Helicase C-terminal
Region1293-1313Disordered
Compositional bias1297-1313Acidic residues
Coiled coil1419-1492
Motif1506-1513Nuclear localization signal 2
Motif1570-1577Nuclear localization signal 3
Region1577-1597Disordered
Domain1673-1727Myb-like
Region1843-1864Disordered
Compositional bias1951-1968Polar residues
Region1951-1977Disordered
Coiled coil2006-2029

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,055
  • Mass (Da)
    234,048
  • Last updated
    2003-10-01 v1
  • Checksum
    ED38EC3C67D7F776
MASKGGKSKPDIVMASKSGKSKPDNESRAKRQKTLEAPKEPRRPKTHWDHVLEEMAWLSKDFESERKWKLAQAKKVALRASKGMLDQASREERKLKEEEQRLRKVALNISKDMKKFWMKVEKLVLYKHQLVRNEKKKKAMDKQLEFLLGQTERYSTMLAENLVEPYKQGQNTPSKPLLTIESKSDEERAEQIPPEINSSAGLESGSPELDEDYDLKSEDETEDDEDTIEEDEKHFTKRERQEELEALQNEVDLPVEELLRRYTSGRVSRETSPVKDENEDNLTSVSRVTSPVKDENQDNLASVGQDHGEDKNNLAASEETEGNPSVRRSNDSYGHLAISETHSHDLEPGMTTASVKSRKEDHTYDFNDEQEDVDFVLANGEEKDDEATLAVEEELAKADNEDHVEEIALLQKESEMPIEVLLARYKEDFGGKDISEDESESSFAVSEDSIVDSDENRQQADLDDDNVDLTECKLDPEPCSENVEGTFHEVAEDNDKDSSDKIADAAAAARSAQPTGFTYSTTKVRTKLPFLLKHSLREYQHIGLDWLVTMYEKKLNGILADEMGLGKTIMTIALLAHLACDKGIWGPHLIVVPTSVMLNWETEFLKWCPAFKILTYFGSAKERKLKRQGWMKLNSFHVCITTYRLVIQDSKMFKRKKWKYLILDEAHLIKNWKSQRWQTLLNFNSKRRILLTGTPLQNDLMELWSLMHFLMPHVFQSHQEFKDWFCNPIAGMVEGQEKINKEVIDRLHNVLRPFLLRRLKRDVEKQLPSKHEHVIFCRLSKRQRNLYEDFIASTETQATLTSGSFFGMISIIMQLRKVCNHPDLFEGRPIVSSFDMAGIDVQLSSTICSLLLESPFSKVDLEALGFLFTHLDFSMTSWEGDEIKAISTPSELIKQRVNLKDDLEAIPLSPKNRKNLQGTNIFEEIRKAVFEERIQESKDRAAAIAWWNSLRCQRKPTYSTSLRTLLTIKGPLDDLKANCSSYMYSSILADIVLSPIERFQKMIELVEAFTFAIPAARVPSPTCWCSKSDSPVFLSPSYKEKVTDLLSPLLSPIRPAIVRRQVYFPDRRLIQFDCGKLQELAMLLRKLKFGGHRALIFTQMTKMLDVLEAFINLYGYTYMRLDGSTPPEERQTLMQRFNTNPKIFLFILSTRSGGVGINLVGADTVIFYDSDWNPAMDQQAQDRCHRIGQTREVHIYRLISESTIEENILKKANQKRVLDNLVIQNGEYNTEFFKKLDPMELFSGHKALTTKDEKETSKHCGADIPLSNADVEAALKQAEDEADYMALKRVEQEEAVDNQEFTEEPVERPEDDELVNEDDIKADEPADQGLVAAGPAKEEMSLLHSDIRDERAVITTSSQEDDTDVLDDVKQMAAAAADAGQAISSFENQLRPIDRYAIRFLELWDPIIVEAAMENEAGFEEKEWELDHIEKYKEEMEAEIDDGEEPLVYEKWDADFATEAYRQQVEVLAQHQLMEDLENEAREREAAEVAEMVLTQNESAHVLKPKKKKKAKKAKYKSLKKGSLAAESKHVKSVVKIEDSTDDDNEEFGYVSSSDSDMVTPLSRMHMKGKKRDLIVDTDEEKTSKKKAKKHKKSLPNSDIKYKQTSALLDELEPSKPSDSMVVDNELKLTNRGKTVGKKFITSMPIKRVLMIKPEKLKKGNLWSRDCVPSPDSWLPQEDAILCAMVHEYGPNWNFVSGTLYGMTAGGAYRGRYRHPAYCCERYRELIQRHILSASDSAVNEKNLNTGSGKALLKVTEENIRTLLNVAAEQPDTEMLLQKHFSCLLSSIWRTSTRTGNDQMLSLNSPIFNRQFMGSVNHTQDLARKPWQGMKVTSLSRKLLESALQDSGPSQPDNTISRSRLQETQPINKLGLELTLEFPRGNDDSLNQFPPMISLSIDGSDSLNYVNEPPGEDVLKGSRVAAENRYRNAANACIEDSFGWASNTFPANDLKSRTGTKAQSLGKHKLSASDSAKSTKSKHRKLLAEQLEGAWVRPNDPNLKFDFTPGDREEEEEQEVDEKANSAEIEMISCSQWYDPFFTSGLDDCSLASDISEIE

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1I9LQH7A0A1I9LQH7_ARATHPIE12051

Sequence caution

The sequence BAB02425.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias21-47Basic and acidic residues
Compositional bias212-229Acidic residues
Compositional bias230-247Basic and acidic residues
Compositional bias254-282Basic and acidic residues
Compositional bias283-303Polar residues
Compositional bias317-332Polar residues
Compositional bias1297-1313Acidic residues
Compositional bias1951-1968Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY279398
EMBL· GenBank· DDBJ
AAP40633.1
EMBL· GenBank· DDBJ
mRNA
AB024033
EMBL· GenBank· DDBJ
BAB02425.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002686
EMBL· GenBank· DDBJ
AEE75248.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp