Clathrin heavy chain 1

<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>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

• ankyrin 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "A requirement for ankyrin binding to clathrin during coated pit budding."
    Michaely P., Kamal A., Anderson R.G., Bennett V.
    J. Biol. Chem. 274:35908-35913(1999) [PubMed] [Europe PMC] [Abstract]
• clathrin light chain binding Source: RGDInferred from sequence orthologyⁱ
  • "Clathrin structure characterized with monoclonal antibodies. II. Identification of in vivo forms of clathrin."
    Brodsky F.M.
    J. Cell Biol. 101:2055-2062(1985) [PubMed] [Europe PMC] [Abstract]
• disordered domain specific binding Source: RGDInferred from sequence orthologyⁱ
  • "Unusual structural organization of the endocytic proteins AP180 and epsin 1."
    Kalthoff C., Alves J., Urbanke C., Knorr R., Ungewickell E.J.
    J. Biol. Chem. 277:8209-8216(2002) [PubMed] [Europe PMC] [Abstract]
• double-stranded RNA binding Source: RGDInferred from sequence orthologyⁱ
  • "Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation."
    Watanabe A., Tatematsu M., Saeki K., Shibata S., Shime H., Yoshimura A., Obuse C., Seya T., Matsumoto M.
    J. Biol. Chem. 286:10702-10711(2011) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: RGDInferred from direct assayⁱ
  • "A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction."
    Rapoport I., Boll W., Yu A., Bocking T., Kirchhausen T.
    Mol. Biol. Cell 19:405-413(2008) [PubMed] [Europe PMC] [Abstract]
• low-density lipoprotein particle receptor binding Source: RGDInferred from sequence orthologyⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat. Neurosci. 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• peptide binding Source: RGDInferred from direct assayⁱ
  • "Possible involvement of clathrin in neuritogenesis induced by a protease inhibitor (benzyloxycarbonyl-Leu-Leu-Leu-aldehyde) in PC12 cells."
    Saito Y., Tsubuki S., Ito H., Ohmi-Imajo S., Kawashima S.
    J. Biochem. 112:448-455(1992) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus 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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics."
    Wasiak S., Legendre-Guillemin V., Puertollano R., Blondeau F., Girard M., de Heuvel E., Boismenu D., Bell A.W., Bonifacino J.S., McPherson P.S.
    J. Cell Biol. 158:855-862(2002) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: RGDInferred from sequence orthologyⁱ
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J. Neurosci. 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]
• structural molecule activity Source: InterPro
• ubiquitin-specific protease binding Source: RGDInferred from sequence orthologyⁱ
  • "USP2-45 is a circadian clock output effector regulating calcium absorption at the post-translational level."
    Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E., Katanaev V.L., Gachon F., Staub O.
    PLoS ONE 11:E0145155-E0145155(2016) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• amyloid-beta clearance by transcytosis Source: RGDInferred from sequence orthologyⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat. Neurosci. 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• autophagy Source: UniProtKB-KW
• clathrin coat assembly Source: RGDInferred from sequence orthologyⁱ
  • "Unusual structural organization of the endocytic proteins AP180 and epsin 1."
    Kalthoff C., Alves J., Urbanke C., Knorr R., Ungewickell E.J.
    J. Biol. Chem. 277:8209-8216(2002) [PubMed] [Europe PMC] [Abstract]
• clathrin-dependent endocytosis Source: RGDInferred from sequence orthologyⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat. Neurosci. 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• Golgi organization 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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "A role for clathrin in reassembly of the Golgi apparatus."
    Radulescu A.E., Siddhanta A., Shields D.
    Mol. Biol. Cell 18:94-105(2007) [PubMed] [Europe PMC] [Abstract]
• intracellular protein transport Source: InterPro
• mitotic cell cycle Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.3

    "Clathrin is required for the function of the mitotic spindle."
    Royle S.J., Bright N.A., Lagnado L.
    Nature 434:1152-1157(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• negative regulation of hyaluronan biosynthetic process Source: UniProtKB
• negative regulation of protein localization to plasma membrane Source: RGDInferred from sequence orthologyⁱ
  • "Quantitative proteomics identifies a Dab2/integrin module regulating cell migration."
    Teckchandani A., Toida N., Goodchild J., Henderson C., Watts J., Wollscheid B., Cooper J.A.
    J. Cell Biol. 186:99-111(2009) [PubMed] [Europe PMC] [Abstract]
• receptor internalization Source: RGDInferred from sequence orthologyⁱ
  • "Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference."
    Huang F., Khvorova A., Marshall W., Sorkin A.
    J. Biol. Chem. 279:16657-16661(2004) [PubMed] [Europe PMC] [Abstract]
• receptor-mediated endocytosis Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.3

    "Clathrin is required for the function of the mitotic spindle."
    Royle S.J., Bright N.A., Lagnado L.
    Nature 434:1152-1157(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• regulation of mitotic spindle organization Source: RGDInferred from sequence orthologyⁱ
  • "A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging."
    Booth D.G., Hood F.E., Prior I.A., Royle S.J.
    EMBO J. 30:906-919(2011) [PubMed] [Europe PMC] [Abstract]
• retrograde transport, endosome to Golgi Source: RGDInferred from sequence orthologyⁱ
  • "The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step."
    Esk C., Chen C.Y., Johannes L., Brodsky F.M.
    J. Cell Biol. 188:131-144(2010) [PubMed] [Europe PMC] [Abstract]
• synaptic vesicle endocytosis Source: SynGOInferred from direct assayⁱ
  • "Clathrin-mediated endocytosis is the dominant mechanism of vesicle retrieval at hippocampal synapses."
    Granseth B., Odermatt B., Royle S.J., Lagnado L.
    Neuron 51:773-786(2006) [PubMed] [Europe PMC] [Abstract]
• transferrin transport Source: RGDInferred from sequence orthologyⁱ
  • "Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference."
    Huang F., Khvorova A., Marshall W., Sorkin A.
    J. Biol. Chem. 279:16657-16661(2004) [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

<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

Keywords - Cellular componentⁱ

<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

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM 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%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="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

• ankyrin binding Source: RGDInferred from direct assayⁱ
  • "A requirement for ankyrin binding to clathrin during coated pit budding."
    Michaely P., Kamal A., Anderson R.G., Bennett V.
    J. Biol. Chem. 274:35908-35913(1999) [PubMed] [Europe PMC] [Abstract]
• clathrin light chain binding Source: RGDInferred from sequence orthologyⁱ
  • "Clathrin structure characterized with monoclonal antibodies. II. Identification of in vivo forms of clathrin."
    Brodsky F.M.
    J. Cell Biol. 101:2055-2062(1985) [PubMed] [Europe PMC] [Abstract]
• disordered domain specific binding Source: RGDInferred from sequence orthologyⁱ
  • "Unusual structural organization of the endocytic proteins AP180 and epsin 1."
    Kalthoff C., Alves J., Urbanke C., Knorr R., Ungewickell E.J.
    J. Biol. Chem. 277:8209-8216(2002) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: RGDInferred from direct assayⁱ
  • "A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction."
    Rapoport I., Boll W., Yu A., Bocking T., Kirchhausen T.
    Mol. Biol. Cell 19:405-413(2008) [PubMed] [Europe PMC] [Abstract]
• low-density lipoprotein particle receptor binding Source: RGDInferred from sequence orthologyⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat. Neurosci. 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: RGDInferred from physical interactionⁱ
  • "Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics."
    Wasiak S., Legendre-Guillemin V., Puertollano R., Blondeau F., Girard M., de Heuvel E., Boismenu D., Bell A.W., Bonifacino J.S., McPherson P.S.
    J. Cell Biol. 158:855-862(2002) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: RGDInferred from sequence orthologyⁱ
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J. Neurosci. 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-specific protease binding Source: RGDInferred from sequence orthologyⁱ
  • "USP2-45 is a circadian clock output effector regulating calcium absorption at the post-translational level."
    Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E., Katanaev V.L., Gachon F., Staub O.
    PLoS ONE 11:E0145155-E0145155(2016) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction 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

Domains and Repeats

Region

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

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

Keywords - Domainⁱ

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>Sequence (1+)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 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV 
        60         70         80         90        100
VIIDMNDPSN PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK 
       110        120        130        140        150
AHTMTDDVTF WKWISLNTVA LVTDNAVYHW SMEGESQPVK MFDRHSSLAG 
       160        170        180        190        200
CQIINYRTDA KQKWLLLTGI SAQQNRVVGA MQLYSVDRKV SQPIEGHAAS 
       210        220        230        240        250
FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN QPFPKKAVDV 
       260        270        280        290        300
FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG 
       310        320        330        340        350
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR 
       360        370        380        390        400
MAVRNNLAGA EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR 
       410        420        430        440        450
FQSVPAQPGQ TSPLLQYFGI LLDQGQLNKY ESLELCRPVL QQGRKQLLEK 
       460        470        480        490        500
WLKEDKLECS EELGDLVKSV DPTLALSVYL RANVPNKVIQ CFAETGQVQK 
       510        520        530        540        550
IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE EPLADITQIV 
       560        570        580        590        600
DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL 
       610        620        630        640        650
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW 
       660        670        680        690        700
LVNYFGSLSV EDSLECLRAM LSANIRQNLQ IWVQVASKYH EQLSTQSLIE 
       710        720        730        740        750
LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE 
       760        770        780        790        800
SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNSLQKYI 
       810        820        830        840        850
EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF STDELVAEVE 
       860        870        880        890        900
KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY 
       910        920        930        940        950
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR 
       960        970        980        990       1000
KDPELWGSVL LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL 
      1010       1020       1030       1040       1050
PNELIELLEK IVLDNSVFSE HRNLQNLLIL TAIKADRTRV MEYINRLDNY 
      1060       1070       1080       1090       1100
DAPDIANIAI SNELFEEAFA IFRKFDVNTS AVQVLIEHIG NLDRAYEFAE 
      1110       1120       1130       1140       1150
RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV VQAANTSGNW 
      1160       1170       1180       1190       1200
EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ 
      1210       1220       1230       1240       1250
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST 
      1260       1270       1280       1290       1300
RTWKEVCFAC VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI 
      1310       1320       1330       1340       1350
TMLEAALGLE RAHMGMFTEL AILYSKFKPQ KMREHLELFW SRVNIPKVLR 
      1360       1370       1380       1390       1400
AAEQAHLWAE LVFLYDKYEE YDNAIITMMN HPTDAWKEGQ FKDIITKVAN 
      1410       1420       1430       1440       1450
VELYYKAIQF YLEFKPLLLN DLLMVLSPRL AHTRAVNYFS KVKQLPLVKP 
      1460       1470       1480       1490       1500
YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE 
      1510       1520       1530       1540       1550
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA 
      1560       1570       1580       1590       1600
EELLQWFLQE EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI 
      1610       1620       1630       1640       1650
QVMKEYLTKV DKLDASESLR KEEEQATETQ PIVYGQPQLM LTAGPSVAVP 
      1660       1670 
PQAPFGYGYT APPYGQPQPG FGYSM                            

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

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references