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Protein

ATP-dependent 6-phosphofructokinase subunit alpha

Gene

PFK1

Organism
Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
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

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Involved in the modulation of glucose-induced microautophagy of peroxisomes independent of its ability to metabolize glucose intermediates.UniRule annotation1 Publication

<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

Mg2+UniRule annotation

<p>This subsection of the ‘Function’ 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

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (PAS_chr3_0456)
  3. ATP-dependent 6-phosphofructokinase subunit alpha (PFK1), ATP-dependent 6-phosphofructokinase subunit gamma (PFK3), ATP-dependent 6-phosphofructokinase subunit beta (PFK2)
  4. no protein annotated in this organism
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei220ATP; via amide nitrogenUniRule annotation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi314Magnesium; catalyticUniRule annotation1
<p>This subsection of the ‘Function’ 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 sitei361Proton acceptorUniRule annotation1
Binding sitei396Substrate; shared with subunit betaUniRule annotation1
Binding sitei460SubstrateUniRule annotation1
Binding sitei487Substrate; shared with subunit betaUniRule annotation1
Binding sitei670Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei765Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation1
Binding sitei832Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei858Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation1
Binding sitei963Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi283 – 284ATPUniRule annotation2
Nucleotide bindingi313 – 316ATPUniRule annotation4

<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 functionAllosteric enzyme, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00109;UER00182

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
Q92448 Curated

MoonProt database of moonlighting proteins

More...
MoonProti
Q92448

<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:
ATP-dependent 6-phosphofructokinase subunit alphaUniRule annotation (EC:2.7.1.11UniRule annotation)
Alternative name(s):
ATP-dependent 6-phosphofructokinase 1UniRule annotation
Short name:
ATP-PFK 1UniRule annotation
Short name:
Phosphofructokinase 1UniRule annotation
Glucose-induced selective autophagy 1 protein
Phosphohexokinase 1UniRule annotation
<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:PFK1
Synonyms:GSA1
Ordered Locus Names:PAS_chr2-1_0402
<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>OrganismiKomagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
<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 identifieri644223 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeKomagataella
<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
  • UP000000314 <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 2

<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 Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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

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>Mutagenesisi361D → S: Abolishes catalytic activity, but not the ability to modulate glucose-induced microautophagy of peroxisomes. 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_00001120421 – 989ATP-dependent 6-phosphofructokinase subunit alphaAdd BLAST989

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q92448

<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

Heterododecamer of 4 alpha, 4 beta and 4 gamma chains. The gamma chain bridges the N-terminal halves of the alpha and beta subunits (By similarity).By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
644223.XP_002491303.1

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q92448

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

More...
SMRi
Q92448

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

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>Regioni1 – 585N-terminal catalytic PFK domain 1Add BLAST585
Regioni359 – 361Substrate bindingUniRule annotation3
Regioni403 – 405Substrate bindingUniRule annotation3
Regioni493 – 496Substrate bindingUniRule annotation4
Regioni586 – 599Interdomain linkerAdd BLAST14
Regioni600 – 989C-terminal regulatory PFK domain 2Add BLAST390
Regioni727 – 731Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni772 – 774Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni864 – 867Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2440 Eukaryota
COG0205 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000200154

KEGG Orthology (KO)

More...
KOi
K00850

Identification of Orthologs from Complete Genome Data

More...
OMAi
KQYDELC

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_03184 Phosphofructokinase_I_E, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009161 6-Pfructokinase_euk
IPR022953 ATP_PFK
IPR015912 Phosphofructokinase_CS
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00365 PFK, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000533 ATP_PFK_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00476 PHFRCTKINASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53784 SSF53784, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02478 6PF1K_euk, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 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>.<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.

Q92448-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEPSISALS FTSFVTNDDK LFEETFNFYT KLGFHATRSY VKDNRSDFEL
60 70 80 90 100
TGISTDSIKE IWLESFPLSE VVETSAGREL RKPLQESVGY QSEALLGYSP
110 120 130 140 150
YQSDGVVIKL RLSNHDLQKN KDLPGEVTFF TASIDKLRAK LIEIGAEIIP
160 170 180 190 200
SEIDLVEFST KDPMGDVISF SSYPSLSSKK ITSPDFFLHP KKEVRSQESI
210 220 230 240 250
VEQVKSEEGK KKIAIITSGG DAPGMNAAVR AVTRAGIFYG CKVYACYEGY
260 270 280 290 300
TGLVKGGDML KELQWQDVRG LLSIGGTIIG TARSKEFRER WGRLQACYNM
310 320 330 340 350
VSNGIDALVV CGGDGSLTGA DLFRNEWPEL IKELLGEGKI TKEQYETHRN
360 370 380 390 400
LTIVGLVGSI DNDMCGTDST IGAYSSLERI IELVDYIDAT AASHSRAFVV
410 420 430 440 450
EVMGRHCGWL GLMSGIATGA DYIFIPERPP SETNWKDDLK KVCLRHREKG
460 470 480 490 500
RRKTTVIVAE GAIDDQLNPI TSEEVKDVLV EIGLDTRITR LGHVQRGGAP
510 520 530 540 550
CAFDRFLATV QGVDAVRAVL ESTPAIPSPV ISILENKIVR QPLVESVAQT
560 570 580 590 600
KTVSDAIEAK DFDKALKLRD QEFATSYESF LSVSKYDDGS YLVPESSRLN
610 620 630 640 650
IAIIHVGAPT SALNPATRVA TLNSLAKGHR VFAIRNGFAG LIRHGAVREL
660 670 680 690 700
NWIDVEDWHN TGGSEIGTNR SLPSDDMGTV AYYFQQYKFD GLIIIGGFEA
710 720 730 740 750
FTALYQLDAA RAQYPIFNIP MCCLPATVSN NVPGTEYSLG SDTCLNTLSG
760 770 780 790 800
YCDAVKQSAS ASRRRTFVVE VQGGYSGYLA SYAGLITGAL AVYTPENPIN
810 820 830 840 850
LQTVQEDIEL LTRTYEEDDG KNRSGKIFIH NEKASKVYTT DLIAAIIGEA
860 870 880 890 900
GKGRFESRTA VPGHVQQGKS PSSIDRVNAC RLAIKCCNFI EDANFQVKHN
910 920 930 940 950
ANLSADERHL RFFYDDGVKT SAVSGKSSVI DDNTSVVIGI QGSEVTFTPV
960 970 980
KQLWEKETHH KWRKGKNVHW EQLNIVSDLL SGRLSIRTT
Length:989
Mass (Da):108,817
Last modified:July 9, 2014 - v2
<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:i6708A34ED94C9DD4
GO

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 conflicti178S → SK in AAB97871 (PubMed:9296392).Curated1
Sequence conflicti570D → E in AAB97871 (PubMed:9296392).Curated1
Sequence conflicti914Y → C in AAB97871 (PubMed:9296392).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U73376 Genomic DNA Translation: AAB97871.1
FN392320 Genomic DNA Translation: CAY69023.1

NCBI Reference Sequences

More...
RefSeqi
XP_002491303.1, XM_002491258.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CAY69023; CAY69023; PAS_chr2-1_0402

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8198870

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ppa:PAS_chr2-1_0402

<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
U73376 Genomic DNA Translation: AAB97871.1
FN392320 Genomic DNA Translation: CAY69023.1
RefSeqiXP_002491303.1, XM_002491258.1

3D structure databases

ProteinModelPortaliQ92448
SMRiQ92448
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi644223.XP_002491303.1

Protein family/group databases

MoonDBiQ92448 Curated
MoonProtiQ92448

Proteomic databases

PRIDEiQ92448

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAY69023; CAY69023; PAS_chr2-1_0402
GeneIDi8198870
KEGGippa:PAS_chr2-1_0402

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
HOGENOMiHOG000200154
KOiK00850
OMAiKQYDELC

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00182

Family and domain databases

HAMAPiMF_03184 Phosphofructokinase_I_E, 1 hit
InterProiView protein in InterPro
IPR009161 6-Pfructokinase_euk
IPR022953 ATP_PFK
IPR015912 Phosphofructokinase_CS
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf
PfamiView protein in Pfam
PF00365 PFK, 2 hits
PIRSFiPIRSF000533 ATP_PFK_euk, 1 hit
PRINTSiPR00476 PHFRCTKINASE
SUPFAMiSSF53784 SSF53784, 2 hits
TIGRFAMsiTIGR02478 6PF1K_euk, 1 hit
PROSITEiView protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiPFKA1_KOMPG
<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: Q92448
Secondary accession number(s): C4R0J9
<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 1, 1997
Last sequence update: July 9, 2014
Last modified: December 5, 2018
This is version 101 of the entry and version 2 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 programFungal 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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