Glycogen phosphorylase, liver form

<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

<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

• [(1→4)-α-D-glucosyl]_(n)

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  • Search chemical reactions in Rhea for this molecule.

  + phosphate

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  • See the description of this molecule in ChEBI.

  = [(1→4)-α-D-glucosyl]_(n-1)

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  + α-D-glucose 1-phosphate

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  EC:2.4.1.1
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  • See the description of this EC number in ENZYME.
  Source: Rhea

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  • See the description of this reaction in Rhea.

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  [(1→4)-α-D-glucosyl]_(n)

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  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  phosphate

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  • See the description of this molecule in ChEBI.

  zoom

  =

  [(1→4)-α-D-glucosyl]_(n-1)

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  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  α-D-glucose 1-phosphate

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  • See the description of this molecule in ChEBI.

  zoom

<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

<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

Sites

<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

• AMP binding Source: RGDInferred from sequence orthologyⁱ
  • "Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core."
    Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N., Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., Pandit J.
    Mol. Cell 6:139-148(2000) [PubMed] [Europe PMC] [Abstract]
  • "Human liver glycogen phosphorylase inhibitors bind at a new allosteric site."
    Rath V.L., Ammirati M., Danley D.E., Ekstrom J.L., Gibbs E.M., Hynes T.R., Mathiowetz A.M., McPherson R.K., Olson T.V., Treadway J.L., Hoover D.J.
    Chem. Biol. 7:677-682(2000) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: RGDInferred from sequence orthologyⁱ
  • "Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core."
    Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N., Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., Pandit J.
    Mol. Cell 6:139-148(2000) [PubMed] [Europe PMC] [Abstract]
• bile acid binding Source: RGDInferred from sequence orthologyⁱ
  • "Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase."
    Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J., Danley D.E., Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J., Day Y.S., Myszka D.G., Rath V.L.
    Chem. Biol. 9:915-924(2002) [PubMed] [Europe PMC] [Abstract]
• carbohydrate binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Regulation of rat hepatocyte function by P2Y receptors: focus on control of glycogen phosphorylase and cyclic AMP by 2-methylthioadenosine 5'-diphosphate."
    Dixon C.J., Hall J.F., Webb T.E., Boarder M.R.
    J. Pharmacol. Exp. Ther. 311:334-341(2004) [PubMed] [Europe PMC] [Abstract]
  • "Glycogen-binding protein components of rat tissues."
    Satoh K., Sato K.
    Biochem. Biophys. Res. Commun. 96:28-33(1980) [PubMed] [Europe PMC] [Abstract]
• drug binding Source: RGDInferred from direct assayⁱ
  • "Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors."
    Birch A.M., Kenny P.W., Oikonomakos N.G., Otterbein L., Schofield P., Whittamore P.R., Whalley D.P.
    Bioorg. Med. Chem. Lett. 17:394-399(2007) [PubMed] [Europe PMC] [Abstract]
• glycogen phosphorylase activity Source: RGDInferred from direct assayⁱ
  • "Glycogen synthesis by rat hepatocytes."
    Katz J., Golden S., Wals P.A.
    Biochem. J. 180:389-402(1979) [PubMed] [Europe PMC] [Abstract]
  • "Defect in glucokinase translocation in Zucker diabetic fatty rats."
    Fujimoto Y., Donahue E.P., Shiota M.
    Am. J. Physiol. Endocrinol. Metab. 287:E414-23(2004) [PubMed] [Europe PMC] [Abstract]
  • "Regulation of rat hepatocyte function by P2Y receptors: focus on control of glycogen phosphorylase and cyclic AMP by 2-methylthioadenosine 5'-diphosphate."
    Dixon C.J., Hall J.F., Webb T.E., Boarder M.R.
    J. Pharmacol. Exp. Ther. 311:334-341(2004) [PubMed] [Europe PMC] [Abstract]
  • "Glycogen phosphorylase isoenzymes from hepatoma 3924A and from a non-tumorigenic liver cell line. Comparison with the liver and brain enzymes."
    Mayer D., Seelmann-Eggebert G., Letsch I.
    Biochem. J. 282:665-673(1992) [PubMed] [Europe PMC] [Abstract]
  • "Response of glucose metabolism enzymes in an acute porphyria model. Role of reactive oxygen species."
    Lelli S.M., San Martin de Viale L.C., Mazzetti M.B.
    Toxicology 216:49-58(2005) [PubMed] [Europe PMC] [Abstract]
  • "Glucose has to be phosphorylated to activate glycogen synthase, but not to inactivate glycogen phosphorylase in hepatocytes."
    Carabaza A., Ciudad C.J., Baque S., Guinovart J.J.
    FEBS Lett. 296:211-214(1992) [PubMed] [Europe PMC] [Abstract]
  • "Rapid activation of glycogen phosphorylase by steroid hormones in cultured rat hepatocytes."
    Gomez-Munoz A., Hales P., Brindley D.N., Sancho M.J.
    Biochem. J. 262:417-423(1989) [PubMed] [Europe PMC] [Abstract]
  • "Effects of the specific cAMP antagonist, (Rp)-adenosine cyclic 3',5'-phosphorothioate, on the cAMP-dependent protein kinase-induced activity of hepatic glycogen phosphorylase and glycogen synthase."
    Rothermel J.D., Perillo N.L., Marks J.S., Botelho L.H.
    J. Biol. Chem. 259:15294-15300(1984) [PubMed] [Europe PMC] [Abstract]
  • "Glycogen-binding protein components of rat tissues."
    Satoh K., Sato K.
    Biochem. Biophys. Res. Commun. 96:28-33(1980) [PubMed] [Europe PMC] [Abstract]
  • "Electron microscopical study of a cytosolic enzyme in unfixed cryostat sections: demonstration of glycogen phosphorylase activity in rat liver and heart tissue."
    Schellens J.P., Vreeling-Sindelarova H., Van den Munckhof R.J., Frederiks W.M.
    Histochem. J. 27:609-614(1995) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Glycogen phosphorylase isoenzymes from hepatoma 3924A and from a non-tumorigenic liver cell line. Comparison with the liver and brain enzymes."
    Mayer D., Seelmann-Eggebert G., Letsch I.
    Biochem. J. 282:665-673(1992) [PubMed] [Europe PMC] [Abstract]
• linear malto-oligosaccharide phosphorylase activity Source: UniProtKB-EC
• protein homodimerization activity Source: RGD <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors."
    Birch A.M., Kenny P.W., Oikonomakos N.G., Otterbein L., Schofield P., Whittamore P.R., Whalley D.P.
    Bioorg. Med. Chem. Lett. 17:394-399(2007) [PubMed] [Europe PMC] [Abstract]
• purine nucleobase binding Source: RGDInferred from sequence orthologyⁱ
  • "Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase."
    Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J., Danley D.E., Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J., Day Y.S., Myszka D.G., Rath V.L.
    Chem. Biol. 9:915-924(2002) [PubMed] [Europe PMC] [Abstract]
• pyridoxal phosphate binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• SHG alpha-glucan phosphorylase activity Source: UniProtKB-EC
• vitamin binding Source: RGDInferred from sequence orthologyⁱ
  • "Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase."
    Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J., Danley D.E., Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J., Day Y.S., Myszka D.G., Rath V.L.
    Chem. Biol. 9:915-924(2002) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• 5-phosphoribose 1-diphosphate biosynthetic process Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Modulation of glycogen phosphorylase activity affects 5-phosphoribosyl-1-pyrophosphate availability in rat hepatocyte cultures."
    Boer P., Sperling O.
    Nucleosides Nucleotides Nucleic Acids 23:1235-1239(2004) [PubMed] [Europe PMC] [Abstract]
• glucose homeostasis Source: RGDInferred from sequence orthologyⁱ
  • "High frequency of missense mutations in glycogen storage disease type VI."
    Beauchamp N.J., Taybert J., Champion M.P., Layet V., Heinz-Erian P., Dalton A., Tanner M.S., Pronicka E., Sharrard M.J.
    J. Inherit. Metab. Dis. 30:722-734(2007) [PubMed] [Europe PMC] [Abstract]
• glycogen catabolic process Source: RGDInferred from direct assayⁱ
  • "Glycogen synthesis by rat hepatocytes."
    Katz J., Golden S., Wals P.A.
    Biochem. J. 180:389-402(1979) [PubMed] [Europe PMC] [Abstract]
  • "Regulation of rat hepatocyte function by P2Y receptors: focus on control of glycogen phosphorylase and cyclic AMP by 2-methylthioadenosine 5'-diphosphate."
    Dixon C.J., Hall J.F., Webb T.E., Boarder M.R.
    J. Pharmacol. Exp. Ther. 311:334-341(2004) [PubMed] [Europe PMC] [Abstract]
  • "Glycogen-binding protein components of rat tissues."
    Satoh K., Sato K.
    Biochem. Biophys. Res. Commun. 96:28-33(1980) [PubMed] [Europe PMC] [Abstract]
• glycogen metabolic process Source: RGDInferred from direct assayⁱ
  • "Glycogen phosphorylase isoenzymes from hepatoma 3924A and from a non-tumorigenic liver cell line. Comparison with the liver and brain enzymes."
    Mayer D., Seelmann-Eggebert G., Letsch I.
    Biochem. J. 282:665-673(1992) [PubMed] [Europe PMC] [Abstract]
  • "Response of glucose metabolism enzymes in an acute porphyria model. Role of reactive oxygen species."
    Lelli S.M., San Martin de Viale L.C., Mazzetti M.B.
    Toxicology 216:49-58(2005) [PubMed] [Europe PMC] [Abstract]
  • "Glucose has to be phosphorylated to activate glycogen synthase, but not to inactivate glycogen phosphorylase in hepatocytes."
    Carabaza A., Ciudad C.J., Baque S., Guinovart J.J.
    FEBS Lett. 296:211-214(1992) [PubMed] [Europe PMC] [Abstract]
  • "Rapid activation of glycogen phosphorylase by steroid hormones in cultured rat hepatocytes."
    Gomez-Munoz A., Hales P., Brindley D.N., Sancho M.J.
    Biochem. J. 262:417-423(1989) [PubMed] [Europe PMC] [Abstract]
  • "Effects of the specific cAMP antagonist, (Rp)-adenosine cyclic 3',5'-phosphorothioate, on the cAMP-dependent protein kinase-induced activity of hepatic glycogen phosphorylase and glycogen synthase."
    Rothermel J.D., Perillo N.L., Marks J.S., Botelho L.H.
    J. Biol. Chem. 259:15294-15300(1984) [PubMed] [Europe PMC] [Abstract]
  • "Electron microscopical study of a cytosolic enzyme in unfixed cryostat sections: demonstration of glycogen phosphorylase activity in rat liver and heart tissue."
    Schellens J.P., Vreeling-Sindelarova H., Van den Munckhof R.J., Frederiks W.M.
    Histochem. J. 27:609-614(1995) [PubMed] [Europe PMC] [Abstract]
• necroptotic process Source: RGDInferred from sequence orthologyⁱ
  • "RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis."
    Zhang D.W., Shao J., Lin J., Zhang N., Lu B.J., Lin S.C., Dong M.Q., Han J.
    Science 325:332-336(2009) [PubMed] [Europe PMC] [Abstract]
• response to bacterium Source: RGDInferred from sequence orthologyⁱ
  • "Impact of lactobacilli on orally acquired listeriosis."
    Archambaud C., Nahori M.A., Soubigou G., Becavin C., Laval L., Lechat P., Smokvina T., Langella P., Lecuit M., Cossart P.
    Proc. Natl. Acad. Sci. U.S.A. 109:16684-16689(2012) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

<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

Chemistry databases

<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

Amino acid modifications

<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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

<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

GO - Molecular functionⁱ

• identical protein binding Source: RGDInferred from physical interactionⁱ
  • "Glycogen phosphorylase isoenzymes from hepatoma 3924A and from a non-tumorigenic liver cell line. Comparison with the liver and brain enzymes."
    Mayer D., Seelmann-Eggebert G., Letsch I.
    Biochem. J. 282:665-673(1992) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: RGDInferred by curatorⁱ
  • "Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors."
    Birch A.M., Kenny P.W., Oikonomakos N.G., Otterbein L., Schofield P., Whittamore P.R., Whalley D.P.
    Bioorg. Med. Chem. Lett. 17:394-399(2007) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<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

<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

<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

Family and domain databases

<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.

        10         20         30         40         50
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR 
        60         70         80         90        100
DYYFALAHTV RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM 
       110        120        130        140        150
INLGLQNACD EAIYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT 
       160        170        180        190        200
LGLAAYGYGI RYEYGIFNQK IREGWQVEEA DDWLRHGNPW EKARPEFMLP 
       210        220        230        240        250
VHFYGRVEHT QAGTKWVDTQ VVLALPYDTP VPGYMNNTVN TMRLWSARAP 
       260        270        280        290        300
NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 
       310        320        330        340        350
VAATLQDVIR RFKASKFGSK DGVGTVFDAF PDQVAIQLND THPALAIPEL 
       360        370        380        390        400
MRIFVDIEKL PWSKAWEITK KTFAYTNHTV LPEALERWPV DLVEKLLPRH 
       410        420        430        440        450
LQIIYEINQK HLDRIVALFP KDIDRMRRMS LIEEEGGKRI NMAHLCIVGC 
       460        470        480        490        500
HAVNGVAKIH SDIVKTQVFK DFSELEPDKF QNKTNGITPR RWLLLCNPGL 
       510        520        530        540        550
ADLIAEKIGE DYVKDLSQLT KLHSFVGDDI FLREIAKVKQ ENKLKFSQFL 
       560        570        580        590        600
EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV 
       610        620        630        640        650
PRTVIIGGKA APGYHMAKMI IKLVTSVAEV VNNDPMVGSK LKVIFLENYR 
       660        670        680        690        700
VSLAEKVIPA TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 
       710        720        730        740        750
AEEAGEENLF IFGMRVDDVA ALDKKGYEAK EYYEALPELK LVIDQIDNGF 
       760        770        780        790        800
FSPNQPDLFK DIINMLFYHD RFKVFADYEA YVKCQEKVSQ LYMNQKAWNT 
       810        820        830        840        850
MVLRNIAASG KFSSDRTIRE YAKDIWNMEP SDLKISLSKE SSNGVNANGK 

Experimental Info

Sequence databases

Genome annotation databases

<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

• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

1. SIMILARITY comments
   Index of protein domains and families