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%5Fsection">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)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  + phosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  = [(1→4)-α-D-glucosyl]_(n-1)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  + α-D-glucose 1-phosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  EC:2.4.1.1
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  • Search reactions for this EC number in Rhea.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  [(1→4)-α-D-glucosyl]_(n)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  phosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  =

  [(1→4)-α-D-glucosyl]_(n-1)

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  α-D-glucose 1-phosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • 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%5Fsection">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: UniProtKB <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
  • Ref.15

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), PHOSPHORYLATION AT SER-15.
  • Ref.14

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
• ATP binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), PHOSPHORYLATION AT SER-15.
• bile acid binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.16

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
• glucose binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.14

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  • Ref.16

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
• glycogen phosphorylase activity Source: MGIInferred from direct assayⁱ
  • "Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1."
    Zhang T., Wang S., Lin Y., Xu W., Ye D., Xiong Y., Zhao S., Guan K.L.
    Cell Metab 15:75-87(2012) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKB <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
  • Ref.14

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
• linear malto-oligosaccharide phosphorylase activity Source: UniProtKB-EC
• purine nucleobase binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.16

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
• 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 Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• SHG alpha-glucan phosphorylase activity Source: UniProtKB-EC
• vitamin binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.16

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

GO - Biological processⁱ

• 5-phosphoribose 1-diphosphate biosynthetic process Source: Ensembl
• glucose homeostasis Source: UniProtKB <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
  • "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: GO_CentralInferred 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 Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• glycogen metabolic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.14

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  • "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]
• necroptotic process Source: Ensembl
• neutrophil degranulation Source: Reactome
• response to bacterium Source: Ensembl

<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

• UniProt annotation
• GO - Cellular component

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation 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%5Fprocessing%5Fsection">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

Organism-specific 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.14

    "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]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Protein-protein interaction databases

Chemistry databases

Miscellaneous 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

Secondary structure

3D structure databases

Miscellaneous 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%5Flength">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>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR 
        60         70         80         90        100
DYYFALAHTV RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM 
       110        120        130        140        150
INLGLQNACD EAIYQLGLDI EELEEIEEDA GLGNGGLGRL AACFLDSMAT 
       160        170        180        190        200
LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA DDWLRYGNPW EKSRPEFMLP 
       210        220        230        240        250
VHFYGKVEHT NTGTKWIDTQ VVLALPYDTP VPGYMNNTVN TMRLWSARAP 
       260        270        280        290        300
NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 
       310        320        330        340        350
VAATLQDIIR RFKASKFGST RGAGTVFDAF PDQVAIQLND THPALAIPEL 
       360        370        380        390        400
MRIFVDIEKL PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH 
       410        420        430        440        450
LEIIYEINQK HLDRIVALFP KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS 
       460        470        480        490        500
HAVNGVAKIH SDIVKTKVFK DFSELEPDKF QNKTNGITPR RWLLLCNPGL 
       510        520        530        540        550
AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ ENKLKFSQFL 
       560        570        580        590        600
ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV 
       610        620        630        640        650
PRTVIIGGKA APGYHMAKMI IKLITSVADV VNNDPMVGSK LKVIFLENYR 
       660        670        680        690        700
VSLAEKVIPA TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 
       710        720        730        740        750
AEEAGEENLF IFGMRIDDVA ALDKKGYEAK EYYEALPELK LVIDQIDNGF 
       760        770        780        790        800
FSPKQPDLFK DIINMLFYHD RFKVFADYEA YVKCQDKVSQ LYMNPKAWNT 
       810        820        830        840 
MVLKNIAASG KFSSDRTIKE YAQNIWNVEP SDLKISLSNE SNKVNGN    

        10         20         30         40         50
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR 
        60         70         80         90        100
DYYFALAHTV RDHLVGRWIR TQQHYYDKCP KLGLDIEELE EIEEDAGLGN 
       110        120        130        140        150
GGLGRLAACF LDSMATLGLA AYGYGIRYEY GIFNQKIRDG WQVEEADDWL 
       160        170        180        190        200
RYGNPWEKSR PEFMLPVHFY GKVEHTNTGT KWIDTQVVLA LPYDTPVPGY 
       210        220        230        240        250
MNNTVNTMRL WSARAPNDFN LRDFNVGDYI QAVLDRNLAE NISRVLYPND 
       260        270        280        290        300
NFFEGKELRL KQEYFVVAAT LQDIIRRFKA SKFGSTRGAG TVFDAFPDQV 
       310        320        330        340        350
AIQLNDTHPA LAIPELMRIF VDIEKLPWSK AWELTQKTFA YTNHTVLPEA 
       360        370        380        390        400
LERWPVDLVE KLLPRHLEII YEINQKHLDR IVALFPKDVD RLRRMSLIEE 
       410        420        430        440        450
EGSKRINMAH LCIVGSHAVN GVAKIHSDIV KTKVFKDFSE LEPDKFQNKT 
       460        470        480        490        500
NGITPRRWLL LCNPGLAELI AEKIGEDYVK DLSQLTKLHS FLGDDVFLRE 
       510        520        530        540        550
LAKVKQENKL KFSQFLETEY KVKINPSSMF DVQVKRIHEY KRQLLNCLHV 
       560        570        580        590        600
ITMYNRIKKD PKKLFVPRTV IIGGKAAPGY HMAKMIIKLI TSVADVVNND 
       610        620        630        640        650
PMVGSKLKVI FLENYRVSLA EKVIPATDLS EQISTAGTEA SGTGNMKFML 
       660        670        680        690        700
NGALTIGTMD GANVEMAEEA GEENLFIFGM RIDDVAALDK KGYEAKEYYE 
       710        720        730        740        750
ALPELKLVID QIDNGFFSPK QPDLFKDIIN MLFYHDRFKV FADYEAYVKC 
       760        770        780        790        800
QDKVSQLYMN PKAWNTMVLK NIAASGKFSS DRTIKEYAQN IWNVEPSDLK 
       810 
ISLSNESNKV NGN                                         

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

• 100% Identity
• 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

Genetic variation databases

Proteomic databases

Protocols and materials 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. Human chromosome 14
   Human chromosome 14: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
6. SIMILARITY comments
   Index of protein domains and families