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Q9H492

- MLP3A_HUMAN

UniProt

Q9H492 - MLP3A_HUMAN

Protein

Microtubule-associated proteins 1A/1B light chain 3A

Gene

MAP1LC3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei120 – 1212Cleavage; by ATG4BBy similarity

    GO - Molecular functioni

    1. phosphatidylethanolamine binding Source: UniProtKB
    2. phospholipid binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. autophagic vacuole assembly Source: UniProtKB
    2. mitochondrion degradation Source: MGI

    Keywords - Biological processi

    Autophagy, Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated proteins 1A/1B light chain 3A
    Alternative name(s):
    Autophagy-related protein LC3 A
    Autophagy-related ubiquitin-like modifier LC3 A
    MAP1 light chain 3-like protein 1
    MAP1A/MAP1B light chain 3 A
    Short name:
    MAP1A/MAP1B LC3 A
    Microtubule-associated protein 1 light chain 3 alpha
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:6838. MAP1LC3A.

    Subcellular locationi

    GO - Cellular componenti

    1. autophagic vacuole Source: UniProtKB
    2. autophagic vacuole membrane Source: UniProtKB-SubCell
    3. cytoplasmic vesicle Source: UniProtKB-KW
    4. cytosol Source: UniProtKB
    5. late endosome Source: Ensembl
    6. microtubule Source: UniProtKB-KW
    7. organelle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1201G → A: No processing of precursor. 1 Publication

    Organism-specific databases

    PharmGKBiPA30582.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 120120Microtubule-associated proteins 1A/1B light chain 3APRO_0000017192Add
    BLAST
    Propeptidei121 – 1211Removed in mature formPRO_0000017193

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine; by PKA1 Publication
    Lipidationi120 – 1201Phosphatidylethanolamine amidated glycine1 Publication

    Post-translational modificationi

    The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094).1 Publication
    The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.1 Publication
    Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity.2 Publications

    Keywords - PTMi

    Lipoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H492.
    PaxDbiQ9H492.
    PRIDEiQ9H492.

    PTM databases

    PhosphoSiteiQ9H492.

    Miscellaneous databases

    PMAP-CutDBQ9H492.

    Expressioni

    Tissue specificityi

    Most abundant in heart, brain, liver, skeletal muscle and testis but absent in thymus and peripheral blood leukocytes.1 Publication

    Gene expression databases

    BgeeiQ9H492.
    CleanExiHS_MAP1LC3A.
    GenevestigatoriQ9H492.

    Organism-specific databases

    HPAiHPA007649.

    Interactioni

    Subunit structurei

    3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins By similarity. Interacts with SQSTM1 By similarity. Interacts with TP53INP1 and TP53INP2. Directly interacts with SQSTM1; this interaction leads to MAP1LC3A recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG13 and ULK1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bnip3lQ9Z2F77EBI-720768,EBI-1774669From a different organism.
    NBR1Q145965EBI-720768,EBI-742698
    SQSTM1Q135017EBI-720768,EBI-307104
    UBQLN4Q9NRR53EBI-720768,EBI-711226

    Protein-protein interaction databases

    BioGridi124137. 99 interactions.
    DIPiDIP-49052N.
    IntActiQ9H492. 380 interactions.
    MINTiMINT-1420598.
    STRINGi9606.ENSP00000363970.

    Structurei

    Secondary structure

    1
    121
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 43
    Helixi7 – 104
    Helixi13 – 2614
    Beta strandi30 – 378
    Beta strandi42 – 443
    Beta strandi51 – 555
    Helixi60 – 7011
    Beta strandi80 – 834
    Turni84 – 863
    Beta strandi91 – 933
    Helixi95 – 1028
    Beta strandi109 – 1168

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ECIX-ray2.65A/B1-121[»]
    3WALX-ray2.00A2-121[»]
    3WANX-ray1.77A/B2-121[»]
    ProteinModelPortaliQ9H492.
    SMRiQ9H492. Positions 2-121.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H492.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATG8 family.Curated

    Phylogenomic databases

    eggNOGiNOG264390.
    HOGENOMiHOG000232034.
    HOVERGENiHBG051706.
    KOiK10435.
    OMAiWAHADEV.
    OrthoDBiEOG7XH6RV.
    PhylomeDBiQ9H492.
    TreeFamiTF312964.

    Family and domain databases

    InterProiIPR004241. Atg8_like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10969. PTHR10969. 1 hit.
    PfamiPF02991. Atg8. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H492-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT    50
    KFLVPDHVNM SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE 100
    QEKDEDGFLY MVYASQETFG F 121
    Length:121
    Mass (Da):14,272
    Last modified:May 10, 2005 - v2
    Checksum:i48C1FBE8F7892AF3
    GO
    Isoform 2 (identifier: Q9H492-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MPSDRPFKQRRSF → MKMRFFSSPCGKAAVDP

    Note: No experimental confirmation available.

    Show »
    Length:125
    Mass (Da):14,493
    Checksum:i097697B5424FC425
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MPSDR…QRRSF → MKMRFFSSPCGKAAVDP in isoform 2. CuratedVSP_013660Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276658 mRNA. Translation: AAK35151.1.
    BT007452 mRNA. Translation: AAP36120.1.
    AL833855 mRNA. Translation: CAD38714.1.
    AL118520 Genomic DNA. Translation: CAC14078.1.
    AL118520 Genomic DNA. Translation: CAI40290.1.
    CH471077 Genomic DNA. Translation: EAW76263.1.
    CH471077 Genomic DNA. Translation: EAW76264.1.
    CH471077 Genomic DNA. Translation: EAW76265.1.
    CH471077 Genomic DNA. Translation: EAW76266.1.
    BC015810 mRNA. Translation: AAH15810.1.
    CCDSiCCDS13237.1. [Q9H492-2]
    CCDS13238.1. [Q9H492-1]
    RefSeqiNP_115903.1. NM_032514.3. [Q9H492-1]
    NP_852610.1. NM_181509.2. [Q9H492-2]
    XP_005260634.1. XM_005260577.1. [Q9H492-1]
    UniGeneiHs.632273.

    Genome annotation databases

    EnsembliENST00000360668; ENSP00000353886; ENSG00000101460. [Q9H492-1]
    ENST00000374837; ENSP00000363970; ENSG00000101460. [Q9H492-2]
    ENST00000397709; ENSP00000380821; ENSG00000101460. [Q9H492-1]
    GeneIDi84557.
    KEGGihsa:84557.
    UCSCiuc002xap.2. human. [Q9H492-2]
    uc002xaq.2. human. [Q9H492-1]

    Polymorphism databases

    DMDMi85701362.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276658 mRNA. Translation: AAK35151.1 .
    BT007452 mRNA. Translation: AAP36120.1 .
    AL833855 mRNA. Translation: CAD38714.1 .
    AL118520 Genomic DNA. Translation: CAC14078.1 .
    AL118520 Genomic DNA. Translation: CAI40290.1 .
    CH471077 Genomic DNA. Translation: EAW76263.1 .
    CH471077 Genomic DNA. Translation: EAW76264.1 .
    CH471077 Genomic DNA. Translation: EAW76265.1 .
    CH471077 Genomic DNA. Translation: EAW76266.1 .
    BC015810 mRNA. Translation: AAH15810.1 .
    CCDSi CCDS13237.1. [Q9H492-2 ]
    CCDS13238.1. [Q9H492-1 ]
    RefSeqi NP_115903.1. NM_032514.3. [Q9H492-1 ]
    NP_852610.1. NM_181509.2. [Q9H492-2 ]
    XP_005260634.1. XM_005260577.1. [Q9H492-1 ]
    UniGenei Hs.632273.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ECI X-ray 2.65 A/B 1-121 [» ]
    3WAL X-ray 2.00 A 2-121 [» ]
    3WAN X-ray 1.77 A/B 2-121 [» ]
    ProteinModelPortali Q9H492.
    SMRi Q9H492. Positions 2-121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124137. 99 interactions.
    DIPi DIP-49052N.
    IntActi Q9H492. 380 interactions.
    MINTi MINT-1420598.
    STRINGi 9606.ENSP00000363970.

    PTM databases

    PhosphoSitei Q9H492.

    Polymorphism databases

    DMDMi 85701362.

    Proteomic databases

    MaxQBi Q9H492.
    PaxDbi Q9H492.
    PRIDEi Q9H492.

    Protocols and materials databases

    DNASUi 84557.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360668 ; ENSP00000353886 ; ENSG00000101460 . [Q9H492-1 ]
    ENST00000374837 ; ENSP00000363970 ; ENSG00000101460 . [Q9H492-2 ]
    ENST00000397709 ; ENSP00000380821 ; ENSG00000101460 . [Q9H492-1 ]
    GeneIDi 84557.
    KEGGi hsa:84557.
    UCSCi uc002xap.2. human. [Q9H492-2 ]
    uc002xaq.2. human. [Q9H492-1 ]

    Organism-specific databases

    CTDi 84557.
    GeneCardsi GC20P033134.
    HGNCi HGNC:6838. MAP1LC3A.
    HPAi HPA007649.
    MIMi 601242. gene.
    neXtProti NX_Q9H492.
    PharmGKBi PA30582.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264390.
    HOGENOMi HOG000232034.
    HOVERGENi HBG051706.
    KOi K10435.
    OMAi WAHADEV.
    OrthoDBi EOG7XH6RV.
    PhylomeDBi Q9H492.
    TreeFami TF312964.

    Miscellaneous databases

    EvolutionaryTracei Q9H492.
    GeneWikii MAP1LC3A.
    GenomeRNAii 84557.
    NextBioi 74441.
    PMAP-CutDB Q9H492.
    PROi Q9H492.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H492.
    CleanExi HS_MAP1LC3A.
    Genevestigatori Q9H492.

    Family and domain databases

    InterProi IPR004241. Atg8_like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10969. PTHR10969. 1 hit.
    Pfami PF02991. Atg8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B."
      He H., Dang Y., Dai F., Guo Z., Wu J., She X., Pei Y., Chen Y., Ling W., Wu C., Zhao S., Liu J.O., Yu L.
      J. Biol. Chem. 278:29278-29287(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-120.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Amygdala.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    7. "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
      Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
      J. Biol. Chem. 276:1701-1706(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG7.
    8. "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p."
      Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
      J. Biol. Chem. 277:13739-13744(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG3.
    9. "HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates."
      Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T., Kominami E.
      J. Biol. Chem. 279:36268-36276(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIPIDATION AT GLY-120, CLEAVAGE BY APG4B.
    10. "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
      Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
      J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
    11. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53INP2.
    12. Cited for: PHOSPHORYLATION AT SER-12 BY PKA, FUNCTION.
    13. "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
      Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
      Cell Death Differ. 19:1525-1535(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
      Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
      J. Biol. Chem. 287:39275-39290(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG13 AND ULK1.
    15. "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription."
      Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.
      PLoS ONE 7:E34034-E34034(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53INP1 AND TP53INP2.
    16. "The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation."
      Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J., Roy C.R.
      Science 338:1072-1076(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DECONJUGATION BY LEGIONELLA RAVZ.

    Entry informationi

    Entry nameiMLP3A_HUMAN
    AccessioniPrimary (citable) accession number: Q9H492
    Secondary accession number(s): E1P5P4, E1P5P5, Q9BXW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3