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Entry version 119 (11 Dec 2019)
Sequence version 1 (01 Oct 2000)
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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

Gene

FKFBP

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

Synthesis and degradation of fructose 2,6-bisphosphate. Regulates carbon partitioning between sucrose versus starch during the diurnal cycle.3 Publications

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

6-phosphofructo-2-kinase activity is activated by pyruvate. 6-phosphofructo-2-kinase activity is inhibited by PPi, phosphoenolpyruvate and 2-phosphoglycerate. Fructose-2,6-bisphosphatase activity is inhibited by pyruvate, fructose 1,6-bisphosphate and 6-phosphogluconate.1 Publication

<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>Kineticsi

  1. KM=0.5 mM for fructose-6-phosphate for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  2. KM=0.19 mM for ATP for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  3. KM=0.028 mM for fructose-2,6-bisphosphate for the fructose-2,6-bisphosphatase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  1. Vmax=180 nmol/min/mg enzyme with fructose-6-phosphate as substrate for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  2. Vmax=270 nmol/min/mg enzyme with fructose-2,6-bisphosphate as substrate for the fructose-2,6-bisphosphatase activity (at pH 6.0 and 25 degrees Celsius)1 Publication

Temperature dependencei

Inactivated by mild heat treatment (42 degrees Celsius during 10 minutes).1 Publication

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 sitei382Fructose 6-phosphateBy similarity1
Binding sitei406Fructose 6-phosphateBy similarity1
<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 sitei431Sequence analysis1
Binding sitei433Fructose 6-phosphateBy similarity1
Binding sitei439Fructose 6-phosphateBy similarity1
Active sitei460Sequence analysis1
Binding sitei496Fructose 6-phosphateBy similarity1
Binding sitei500Fructose 6-phosphateBy similarity1
Binding sitei557Fructose 2,6-bisphosphateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei557Transition state stabilizerBy similarity1
Active sitei558Tele-phosphohistidine intermediateBy similarity1
Binding sitei564Fructose 2,6-bisphosphateBy similarity1
Sitei564Transition state stabilizerBy similarity1
Binding sitei570Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei630Proton donor/acceptorBy similarity1
Binding sitei641Fructose 2,6-bisphosphateBy similarity1
Binding sitei655Fructose 2,6-bisphosphateBy similarity1
Binding sitei659Fructose 2,6-bisphosphateBy similarity1
Binding sitei670Fructose 2,6-bisphosphateBy similarity1
Sitei696Transition state stabilizerBy similarity1
Binding sitei697Fructose 2,6-bisphosphateBy similarity1
Binding sitei701Fructose 2,6-bisphosphateBy similarity1

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 bindingi349 – 357ATPBy similarity9
Nucleotide bindingi469 – 474ATPBy similarity6
Nucleotide bindingi652 – 655ATPBy similarity4
Nucleotide bindingi697 – 701ATPBy similarity5

<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 functionHydrolase, Kinase, Multifunctional enzyme, Transferase
Biological processCarbohydrate metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT1G07110-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.1.105 399
3.1.3.46 399

<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:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Short name:
6PF-2-K/Fru-2,6-P2ase
Short name:
AtF2KP
Short name:
PFK/FBPase
Including the following 2 domains:
6-phosphofructo-2-kinase (EC:2.7.1.105)
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
<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:FKFBP
Synonyms:F2KP
Ordered Locus Names:At1g07110
ORF Names:F10K1.19
<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)
<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 1

Organism-specific databases

Arabidopsis Information Portal

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Araporti
AT1G07110

The Arabidopsis Information Resource

More...
TAIRi
locus:2007367 AT1G07110

<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

Cytoplasm, Membrane

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<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_00004153192 – 7446-phosphofructo-2-kinase/fructose-2,6-bisphosphataseAdd BLAST743

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
<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 residuei220Phosphoserine; by CPK3Combined sources1 Publication1
Modified residuei276PhosphoserineCombined sources1
Modified residuei295PhosphoserineCombined sources1
Modified residuei303Phosphoserine; by CPK3Combined sources1 Publication1

<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

Phosphorylation at Ser-220 and Ser-303 by CPK3 promotes 14-3-3 proteins binding.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q9MB58

PRoteomics IDEntifications database

More...
PRIDEi
Q9MB58

Protein Mass spectra EXtraction

More...
ProMEXi
Q9MB58

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9MB58

<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
Q9MB58 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9MB58 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

Interacts with 14-3-3 proteins; these interactions may regulate both nitrate assimilation and sucrose/starch partitioning in leaves during the diurnal cycle.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
3702.AT1G07110.1

<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

3D structure databases

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

More...
SMRi
Q9MB58

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini17 – 122CBM20PROSITE-ProRule annotationAdd BLAST106

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>Regioni301 – 5496-phosphofructo-2-kinaseAdd BLAST249
Regioni550 – 744Fructose-2,6-bisphosphataseAdd BLAST195

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi320 – 331Poly-AlaAdd BLAST12

<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

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0234 Eukaryota
COG0406 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000181112

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9MB58

KEGG Orthology (KO)

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KOi
K01103

Identification of Orthologs from Complete Genome Data

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OMAi
WRAFQEN

Database of Orthologous Groups

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OrthoDBi
198523at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9MB58

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07067 HP_PGM_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
3.40.50.1240, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR013783 Ig-like_fold
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10606 PTHR10606, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00991 6PFRUCTKNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01065 CBM_2, 1 hit
SM00855 PGAM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49452 SSF49452, 1 hit
SSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51166 CBM20, 1 hit
PS00175 PG_MUTASE, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MB58-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSGASKNTE EDDDGSNGGG GQLYVSLKME NSKVEGELTP HVYGSLPLIG
60 70 80 90 100
SWDPSKALPM QRESALMSEL SFVVPPDHET LDFKFLLKPK NRNTPCIVEE
110 120 130 140 150
GENRLLTGGS LQGDARLALF RLEGDVIVEF RVFINADRVS PIDLATSWRA
160 170 180 190 200
YRENLQPSTV RGIPDVSINP DPKSAECPLE SLELDLAHYE VPAPAPSANS
210 220 230 240 250
YLVYAADNAE NPRSLSASGS FRNDSTPKAA QRNSEDSGVT VDGSPSAKEM
260 270 280 290 300
TIVVPDSSNI YSAFGEAESK SVETLSPFQQ KDGQKGLFVD RGVGSPRLVK
310 320 330 340 350
SLSASSFLID TKQIKNSMPA AAGAVAAAAV ADQMLGPKED RHLAIVLVGL
360 370 380 390 400
PARGKTFTAA KLTRYLRWLG HDTKHFNVGK YRRLKHGVNM SADFFRADNP
410 420 430 440 450
EGVEARTEVA ALAMEDMIAW MQEGGQVGIF DATNSTRVRR NMLMKMAEGK
460 470 480 490 500
CKIIFLETLC NDERIIERNI RLKIQQSPDY SEEMDFEAGV RDFRDRLANY
510 520 530 540 550
EKVYEPVEEG SYIKMIDMVS GNGGQIQVNN ISGYLPGRIV FFLVNTHLTP
560 570 580 590 600
RPILLTRHGE SMDNVRGRIG GDSVISDSGK LYAKKLASFV EKRLKSEKAA
610 620 630 640 650
SIWTSTLQRT NLTASSIVGF PKVQWRALDE INAGVCDGMT YEEVKKNMPE
660 670 680 690 700
EYESRKKDKL RYRYPRGESY LDVIQRLEPV IIELERQRAP VVVISHQAVL
710 720 730 740
RALYAYFADR PLKEIPQIEM PLHTIIEIQM GVSGVQEKRY KLMD
Length:744
Mass (Da):82,559
Last modified:October 1, 2000 - 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:i61EA630DFA01F38A
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAF76986 differs from that shown. Reason: Frameshift.Curated
The sequence AAF82210 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti629D → A in AAF04293 (PubMed:10899575).Curated1

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
AF190739 mRNA Translation: AAF04293.2
AF242859 Genomic DNA Translation: AAF76986.1 Frameshift.
AB035288 mRNA Translation: BAA96353.1
AC067971 Genomic DNA Translation: AAF82210.1 Sequence problems.
CP002684 Genomic DNA Translation: AEE28077.1
AY128346 mRNA Translation: AAM91549.1

Protein sequence database of the Protein Information Resource

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PIRi
H86205

NCBI Reference Sequences

More...
RefSeqi
NP_172191.1, NM_100584.5

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT1G07110.1; AT1G07110.1; AT1G07110

Database of genes from NCBI RefSeq genomes

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GeneIDi
837221

Gramene; a comparative resource for plants

More...
Gramenei
AT1G07110.1; AT1G07110.1; AT1G07110

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G07110

<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
AF190739 mRNA Translation: AAF04293.2
AF242859 Genomic DNA Translation: AAF76986.1 Frameshift.
AB035288 mRNA Translation: BAA96353.1
AC067971 Genomic DNA Translation: AAF82210.1 Sequence problems.
CP002684 Genomic DNA Translation: AEE28077.1
AY128346 mRNA Translation: AAM91549.1
PIRiH86205
RefSeqiNP_172191.1, NM_100584.5

3D structure databases

SMRiQ9MB58
ModBaseiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G07110.1

PTM databases

iPTMnetiQ9MB58

Proteomic databases

PaxDbiQ9MB58
PRIDEiQ9MB58
ProMEXiQ9MB58

Genome annotation databases

EnsemblPlantsiAT1G07110.1; AT1G07110.1; AT1G07110
GeneIDi837221
GrameneiAT1G07110.1; AT1G07110.1; AT1G07110
KEGGiath:AT1G07110

Organism-specific databases

AraportiAT1G07110
TAIRilocus:2007367 AT1G07110

Phylogenomic databases

eggNOGiKOG0234 Eukaryota
COG0406 LUCA
HOGENOMiHOG000181112
InParanoidiQ9MB58
KOiK01103
OMAiWRAFQEN
OrthoDBi198523at2759
PhylomeDBiQ9MB58

Enzyme and pathway databases

BioCyciARA:AT1G07110-MONOMER
BRENDAi2.7.1.105 399
3.1.3.46 399

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9MB58

Gene expression databases

ExpressionAtlasiQ9MB58 baseline and differential
GenevisibleiQ9MB58 AT

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di2.60.40.10, 1 hit
3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR013783 Ig-like_fold
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS
PANTHERiPTHR10606 PTHR10606, 1 hit
PfamiView protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit
PRINTSiPR00991 6PFRUCTKNASE
SMARTiView protein in SMART
SM01065 CBM_2, 1 hit
SM00855 PGAM, 1 hit
SUPFAMiSSF49452 SSF49452, 1 hit
SSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit
PS00175 PG_MUTASE, 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 nameiF26_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: Q9MB58
Secondary accession number(s): Q8L7N6
, Q9LL39, Q9LMK3, Q9SP17
<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: January 25, 2012
Last sequence update: October 1, 2000
Last modified: December 11, 2019
This is version 119 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

Reference proteome

Documents

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