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Entry version 172 (18 Sep 2019)
Sequence version 1 (01 Jun 1998)
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Protein

Phototropin-1

Gene

PHOT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Phosphorylates BLUS1, a kinase involved in stomatal opening. Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.9 Publications

Miscellaneous

Undergoes a photocycle characterized by fluorescence and absorption changes induced by blue light. Half-time of photoproduct formation is 14 seconds and 70 seconds for dark regeneration.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMNCuratedNote: Binds 2 FMN per subunit.Curated

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Absorptioni

Abs(max)=450 nm1 PublicationExhibits a smaller absorbance peak at 350 nm. The broad fluorescence emission spectrum peaks at 490 nm.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei251FMN1 Publication1
Binding sitei266FMN1 Publication1
Binding sitei276FMN1 Publication1
Binding sitei297FMN1 Publication1
Binding sitei529FMNBy similarity1
Binding sitei544FMNBy similarity1
Binding sitei554FMNBy similarity1
Binding sitei575FMNBy similarity1
Binding sitei692ATPPROSITE-ProRule annotationCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei788Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi233 – 238FMN1 Publication6
Nucleotide bindingi511 – 516FMNBy similarity6
Nucleotide bindingi669 – 677ATPPROSITE-ProRule annotationCurated9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Photoreceptor protein, Receptor, Serine/threonine-protein kinase, Transferase
Biological processSensory transduction
LigandATP-binding, Chromophore, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 399

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phototropin-1 (EC:2.7.11.1)
Alternative name(s):
Non-phototropic hypocotyl protein 1
Root phototropism protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PHOT1
Synonyms:JK224, NPH1, RPT1
Ordered Locus Names:At3g45780
ORF Names:T6D9_110
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT3G45780

The Arabidopsis Information Resource

More...
TAIRi
locus:2102674 AT3G45780

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Enhanced drought tolerance, when associated with PHOT2 disruption.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi234C → A: No effect on the kinase activity regulation. 1 Publication1
Mutagenesisi512C → A: Loss of light-sensing and light-dependent autophosphorylation. 2 Publications1
Mutagenesisi774Missing in nph1-1; loss of phototropism. 1 Publication1
Mutagenesisi936R → K in nph1-2; partial phototropism. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000865221 – 996Phototropin-1Add BLAST996

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei23PhosphoserineBy similarity1
Modified residuei58Phosphoserine1 Publication1
Modified residuei185Phosphoserine1 Publication1
Modified residuei234S-4a-FMN cysteine1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi261Interchain
Modified residuei350PhosphoserineCombined sources1 Publication1
Modified residuei376PhosphoserineCombined sources1
Modified residuei410Phosphoserine1 Publication1
Modified residuei450PhosphoserineCombined sources1
Modified residuei512S-4a-FMN cysteine1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated in response to blue light irradiation.Curated4 Publications
2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O48963

PRoteomics IDEntifications database

More...
PRIDEi
O48963

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O48963

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O48963 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O48963 AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked.

Interacts with PKS1, PKS2, RPT2, RPT3, PHOT2 and BLUS1 (PubMed:10542152, PubMed:15031408, PubMed:16777956, PubMed:18585389, PubMed:20071603, PubMed:23811955). Subunit of a complex made of CAR6, PHOT1 and RPT3/NPH3 (PubMed:21367967).

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
9041, 12 interactors

Database of interacting proteins

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DIPi
DIP-38655N

Protein interaction database and analysis system

More...
IntActi
O48963, 11 interactors

Molecular INTeraction database

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MINTi
O48963

STRING: functional protein association networks

More...
STRINGi
3702.AT3G45780.2

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1996
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O48963

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O48963

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini184 – 257PAS 1PROSITE-ProRule annotationAdd BLAST74
Domaini258 – 312PAC 1PROSITE-ProRule annotationAdd BLAST55
Domaini462 – 535PAS 2PROSITE-ProRule annotationAdd BLAST74
Domaini536 – 590PAC 2PROSITE-ProRule annotationAdd BLAST55
Domaini663 – 952Protein kinasePROSITE-ProRule annotationCuratedAdd BLAST290

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni806 – 862Activation loopBy similarityAdd BLAST57

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The activation loop within the kinase domain is the target of phosphorylation (By similarity). The PAS (PER-ARNT-SIM) domains are required for the binding of FMN chromophores.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IH6N Eukaryota
COG2202 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000265679

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O48963

KEGG Orthology (KO)

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KOi
K20715

Identification of Orthologs from Complete Genome Data

More...
OMAi
NMFTLAP

Database of Orthologous Groups

More...
OrthoDBi
529293at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O48963

Family and domain databases

Conserved Domains Database

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CDDi
cd00130 PAS, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001610 PAC
IPR000014 PAS
IPR000700 PAS-assoc_C
IPR035965 PAS-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13426 PAS_9, 2 hits
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00086 PAC, 2 hits
SM00091 PAS, 2 hits
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55785 SSF55785, 2 hits
SSF56112 SSF56112, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00229 sensory_box, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50113 PAC, 2 hits
PS50112 PAS, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

O48963-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEPTEKPSTK PSSRTLPRDT RGSLEVFNPS TQLTRPDNPV FRPEPPAWQN
60 70 80 90 100
LSDPRGTSPQ PRPQQEPAPS NPVRSDQEIA VTTSWMALKD PSPETISKKT
110 120 130 140 150
ITAEKPQKSA VAAEQRAAEW GLVLKTDTKT GKPQGVGVRN SGGTENDPNG
160 170 180 190 200
KKTTSQRNSQ NSCRSSGEMS DGDVPGGRSG IPRVSEDLKD ALSTFQQTFV
210 220 230 240 250
VSDATKPDYP IMYASAGFFN MTGYTSKEVV GRNCRFLQGS GTDADELAKI
260 270 280 290 300
RETLAAGNNY CGRILNYKKD GTSFWNLLTI APIKDESGKV LKFIGMQVEV
310 320 330 340 350
SKHTEGAKEK ALRPNGLPES LIRYDARQKD MATNSVTELV EAVKRPRALS
360 370 380 390 400
ESTNLHPFMT KSESDELPKK PARRMSENVV PSGRRNSGGG RRNSMQRINE
410 420 430 440 450
IPEKKSRKSS LSFMGIKKKS ESLDESIDDG FIEYGEEDDE ISDRDERPES
460 470 480 490 500
VDDKVRQKEM RKGIDLATTL ERIEKNFVIT DPRLPDNPII FASDSFLELT
510 520 530 540 550
EYSREEILGR NCRFLQGPET DLTTVKKIRN AIDNQTEVTV QLINYTKSGK
560 570 580 590 600
KFWNIFHLQP MRDQKGEVQY FIGVQLDGSK HVEPVRNVIE ETAVKEGEDL
610 620 630 640 650
VKKTAVNIDE AVRELPDANM TPEDLWANHS KVVHCKPHRK DSPPWIAIQK
660 670 680 690 700
VLESGEPIGL KHFKPVKPLG SGDTGSVHLV ELVGTDQLFA MKAMDKAVML
710 720 730 740 750
NRNKVHRARA EREILDLLDH PFLPALYASF QTKTHICLIT DYYPGGELFM
760 770 780 790 800
LLDRQPRKVL KEDAVRFYAA QVVVALEYLH CQGIIYRDLK PENVLIQGNG
810 820 830 840 850
DISLSDFDLS CLTSCKPQLL IPSIDEKKKK KQQKSQQTPI FMAEPMRASN
860 870 880 890 900
SFVGTEEYIA PEIISGAGHT SAVDWWALGI LMYEMLYGYT PFRGKTRQKT
910 920 930 940 950
FTNVLQKDLK FPASIPASLQ VKQLIFRLLQ RDPKKRLGCF EGANEVKQHS
960 970 980 990
FFKGINWALI RCTNPPELET PIFSGEAENG EKVVDPELED LQTNVF
Length:996
Mass (Da):111,689
Last modified:June 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC9B68812F1B3A04E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF030864 mRNA Translation: AAC01753.1
AL157735 Genomic DNA Translation: CAB75791.1
CP002686 Genomic DNA Translation: AEE78072.1
CP002686 Genomic DNA Translation: AEE78073.1
AF360218 mRNA Translation: AAK25928.1
AY040062 mRNA Translation: AAK64120.1

Protein sequence database of the Protein Information Resource

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PIRi
T47518

NCBI Reference Sequences

More...
RefSeqi
NP_001030814.1, NM_001035737.2
NP_190164.1, NM_114447.4

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT3G45780.1; AT3G45780.1; AT3G45780
AT3G45780.2; AT3G45780.2; AT3G45780

Database of genes from NCBI RefSeq genomes

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GeneIDi
823721

Gramene; a comparative resource for plants

More...
Gramenei
AT3G45780.1; AT3G45780.1; AT3G45780
AT3G45780.2; AT3G45780.2; AT3G45780

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT3G45780

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030864 mRNA Translation: AAC01753.1
AL157735 Genomic DNA Translation: CAB75791.1
CP002686 Genomic DNA Translation: AEE78072.1
CP002686 Genomic DNA Translation: AEE78073.1
AF360218 mRNA Translation: AAK25928.1
AY040062 mRNA Translation: AAK64120.1
PIRiT47518
RefSeqiNP_001030814.1, NM_001035737.2
NP_190164.1, NM_114447.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z6CX-ray2.10A/B180-308[»]
4HHDX-ray2.75A/B452-615[»]
SMRiO48963
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi9041, 12 interactors
DIPiDIP-38655N
IntActiO48963, 11 interactors
MINTiO48963
STRINGi3702.AT3G45780.2

PTM databases

iPTMnetiO48963

Proteomic databases

PaxDbiO48963
PRIDEiO48963

Genome annotation databases

EnsemblPlantsiAT3G45780.1; AT3G45780.1; AT3G45780
AT3G45780.2; AT3G45780.2; AT3G45780
GeneIDi823721
GrameneiAT3G45780.1; AT3G45780.1; AT3G45780
AT3G45780.2; AT3G45780.2; AT3G45780
KEGGiath:AT3G45780

Organism-specific databases

AraportiAT3G45780
TAIRilocus:2102674 AT3G45780

Phylogenomic databases

eggNOGiENOG410IH6N Eukaryota
COG2202 LUCA
HOGENOMiHOG000265679
InParanoidiO48963
KOiK20715
OMAiNMFTLAP
OrthoDBi529293at2759
PhylomeDBiO48963

Enzyme and pathway databases

BRENDAi2.7.11.1 399

Miscellaneous databases

EvolutionaryTraceiO48963

Protein Ontology

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PROi
PR:O48963

Gene expression databases

ExpressionAtlasiO48963 baseline and differential
GenevisibleiO48963 AT

Family and domain databases

CDDicd00130 PAS, 2 hits
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001610 PAC
IPR000014 PAS
IPR000700 PAS-assoc_C
IPR035965 PAS-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF13426 PAS_9, 2 hits
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00086 PAC, 2 hits
SM00091 PAS, 2 hits
SM00220 S_TKc, 1 hit
SUPFAMiSSF55785 SSF55785, 2 hits
SSF56112 SSF56112, 1 hit
TIGRFAMsiTIGR00229 sensory_box, 2 hits
PROSITEiView protein in PROSITE
PS50113 PAC, 2 hits
PS50112 PAS, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPHOT1_ARATH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O48963
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 1, 1998
Last modified: September 18, 2019
This is version 172 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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