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Q9UKV5

- AMFR_HUMAN

UniProt

Q9UKV5 - AMFR_HUMAN

Protein

E3 ubiquitin-protein ligase AMFR

Gene

AMFR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri341 – 37939RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. receptor activity Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular component movement Source: ProtInc
    3. endoplasmic reticulum unfolded protein response Source: UniProtKB
    4. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. learning or memory Source: Ensembl
    6. protein oligomerization Source: UniProtKB
    7. protein polyubiquitination Source: UniProtKB
    8. signal transduction Source: ProtInc
    9. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase, Receptor

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase AMFR (EC:6.3.2.-)
    Alternative name(s):
    Autocrine motility factor receptor
    Short name:
    AMF receptor
    RING finger protein 45
    gp78
    Gene namesi
    Name:AMFR
    Synonyms:RNF45
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:463. AMFR.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. dendrite Source: Ensembl
    2. endoplasmic reticulum membrane Source: UniProt
    3. growth cone Source: Ensembl
    4. Hrd1p ubiquitin ligase complex Source: UniProt
    5. integral component of endoplasmic reticulum membrane Source: UniProtKB
    6. integral component of membrane Source: UniProtKB
    7. membrane Source: UniProtKB
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: Ensembl
    10. perinuclear region of cytoplasm Source: ParkinsonsUK-UCL
    11. protein complex Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi356 – 3561C → G: No degradation of HMGCR. 1 Publication

    Organism-specific databases

    PharmGKBiPA24768.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 643643E3 ubiquitin-protein ligase AMFRPRO_0000064579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei516 – 5161Phosphoserine1 Publication
    Modified residuei542 – 5421PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKV5.
    PeptideAtlasiQ9UKV5.
    PRIDEiQ9UKV5.

    PTM databases

    PhosphoSiteiQ9UKV5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UKV5.
    BgeeiQ9UKV5.
    CleanExiHS_AMFR.
    GenevestigatoriQ9UKV5.

    Organism-specific databases

    HPAiCAB026381.
    HPA029018.

    Interactioni

    Subunit structurei

    Interacts with RNF5. Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation By similarity. Interacts with DRL1. Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7. Component of the VCP/p97-AMFR/gp78 complex that enhances VCP/p97 binding to polyubiquitinated proteins for their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway. Interacts (via the VIM) with VCP/p97. Interacts (via its membrane domain) with INSIG1; the interaction initiates the sterol-mediated ubiquitination and degradation of HMGCR by the ERAD pathway.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VCPP550726EBI-1046367,EBI-355164

    Protein-protein interaction databases

    BioGridi106764. 86 interactions.
    DIPiDIP-29060N.
    IntActiQ9UKV5. 16 interactions.
    MINTiMINT-2821880.
    STRINGi9606.ENSP00000290649.

    Structurei

    Secondary structure

    1
    643
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi332 – 3376
    Beta strandi342 – 3443
    Beta strandi351 – 3533
    Beta strandi355 – 3573
    Beta strandi359 – 3613
    Helixi362 – 3698
    Beta strandi376 – 3783
    Helixi456 – 46712
    Helixi473 – 48311
    Helixi486 – 4949
    Helixi575 – 59925
    Helixi625 – 63713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EJSNMR-A452-502[»]
    2LVNNMR-C453-504[»]
    2LVONMR-C453-504[»]
    2LVPNMR-C453-504[»]
    2LVQNMR-D453-504[»]
    2LXHNMR-C313-393[»]
    2LXPNMR-B574-600[»]
    C327-384[»]
    3FSHX-ray2.76C574-601[»]
    3H8KX-ray1.80B573-600[»]
    3TIWX-ray1.80C/D622-640[»]
    4G3OX-ray1.60A456-498[»]
    4LADX-ray2.30B313-393[»]
    B574-600[»]
    ProteinModelPortaliQ9UKV5.
    SMRiQ9UKV5. Positions 327-384, 453-504, 574-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKV5.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei82 – 10221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei122 – 14221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei145 – 16521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei186 – 20621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei215 – 23521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei276 – 29621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei429 – 44921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini456 – 49843CUEPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni614 – 64330VCP/p97-interacting motif (VIM)Add
    BLAST

    Domaini

    The VCP/p97-interacting motif (VIM) is sufficient for binding VCP/p97 to form a complex capable of transferring VCP/p97 from the cytosol to microsomes.

    Sequence similaritiesi

    Contains 1 CUE domain.CuratedPROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.CuratedPROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri341 – 37939RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5243.
    HOGENOMiHOG000037436.
    HOVERGENiHBG044694.
    InParanoidiQ9UKV5.
    KOiK10636.
    OMAiNTACCFL.
    OrthoDBiEOG7QRQT8.
    PhylomeDBiQ9UKV5.
    TreeFamiTF320052.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR003892. CUE.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02845. CUE. 1 hit.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00546. CUE. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS51140. CUE. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UKV5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLLFLERFP WPSLRTYTGL SGLALLGTII SAYRALSQPE AGPGEPDQLT    50
    ASLQPEPPAP ARPSAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK 100
    LIQCIVFGPL RVSERQHLKD KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL 150
    WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM SSHGRVLSLL VAMLLSCCGL 200
    AAVCSITGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH LWDLNHEGTW 250
    EGKGTYVYYT DFVMELTLLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY 300
    LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA 350
    ARKLPCGHLF HNSCLRSWLE QDTSCPTCRM SLNIADNNRV REEHQGENLD 400
    ENLVPVAAAE GRPRLNQHNH FFHFDGSRIA SWLPSFSVEV MHTTNILGIT 450
    QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL QLTRSVEITT DNILEGRIQV 500
    PFPTQRSDSI RPALNSPVER PSSDQEEGET SAQTERVPLD LSPRLEETLD 550
    FGEVEVEPSE VEDFEARGSR FSKSADERQR MLVQRKDELL QQARKRFLNK 600
    SSEDDAASES FLPSEGASSD PVTLRRRMLA AAAERRLQKQ QTS 643
    Length:643
    Mass (Da):72,996
    Last modified:June 1, 2003 - v2
    Checksum:i8782324609C0E62A
    GO

    Sequence cautioni

    The sequence AAA36671.1 differs from that shown. Reason: Several sequencing errors.
    The sequence AAA79362.1 differs from that shown. Reason: Frameshift at positions 355, 388, 411, 487, 537, 583 and 632.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti406 – 4061V → D in AAA79362. (PubMed:7626106)Curated
    Sequence conflicti491 – 4911D → V in AAA79362. (PubMed:7626106)Curated
    Sequence conflicti500 – 5001V → L in AAA79362. (PubMed:7626106)Curated
    Sequence conflicti614 – 6141S → L in AAD56722. (PubMed:10456327)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti605 – 6051D → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035790

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124145 mRNA. Translation: AAD56722.1.
    BC069197 mRNA. Translation: AAH69197.1.
    L35233 mRNA. Translation: AAA79362.1. Frameshift.
    M63175 mRNA. Translation: AAA36671.1. Sequence problems.
    CCDSiCCDS10758.1.
    PIRiA39877.
    RefSeqiNP_001135.3. NM_001144.5.
    UniGeneiHs.295137.

    Genome annotation databases

    EnsembliENST00000290649; ENSP00000290649; ENSG00000159461.
    GeneIDi267.
    KEGGihsa:267.
    UCSCiuc002eiy.4. human.

    Polymorphism databases

    DMDMi34922250.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124145 mRNA. Translation: AAD56722.1 .
    BC069197 mRNA. Translation: AAH69197.1 .
    L35233 mRNA. Translation: AAA79362.1 . Frameshift.
    M63175 mRNA. Translation: AAA36671.1 . Sequence problems.
    CCDSi CCDS10758.1.
    PIRi A39877.
    RefSeqi NP_001135.3. NM_001144.5.
    UniGenei Hs.295137.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EJS NMR - A 452-502 [» ]
    2LVN NMR - C 453-504 [» ]
    2LVO NMR - C 453-504 [» ]
    2LVP NMR - C 453-504 [» ]
    2LVQ NMR - D 453-504 [» ]
    2LXH NMR - C 313-393 [» ]
    2LXP NMR - B 574-600 [» ]
    C 327-384 [» ]
    3FSH X-ray 2.76 C 574-601 [» ]
    3H8K X-ray 1.80 B 573-600 [» ]
    3TIW X-ray 1.80 C/D 622-640 [» ]
    4G3O X-ray 1.60 A 456-498 [» ]
    4LAD X-ray 2.30 B 313-393 [» ]
    B 574-600 [» ]
    ProteinModelPortali Q9UKV5.
    SMRi Q9UKV5. Positions 327-384, 453-504, 574-599.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106764. 86 interactions.
    DIPi DIP-29060N.
    IntActi Q9UKV5. 16 interactions.
    MINTi MINT-2821880.
    STRINGi 9606.ENSP00000290649.

    PTM databases

    PhosphoSitei Q9UKV5.

    Polymorphism databases

    DMDMi 34922250.

    Proteomic databases

    MaxQBi Q9UKV5.
    PeptideAtlasi Q9UKV5.
    PRIDEi Q9UKV5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290649 ; ENSP00000290649 ; ENSG00000159461 .
    GeneIDi 267.
    KEGGi hsa:267.
    UCSCi uc002eiy.4. human.

    Organism-specific databases

    CTDi 267.
    GeneCardsi GC16M056395.
    HGNCi HGNC:463. AMFR.
    HPAi CAB026381.
    HPA029018.
    MIMi 603243. gene.
    neXtProti NX_Q9UKV5.
    PharmGKBi PA24768.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5243.
    HOGENOMi HOG000037436.
    HOVERGENi HBG044694.
    InParanoidi Q9UKV5.
    KOi K10636.
    OMAi NTACCFL.
    OrthoDBi EOG7QRQT8.
    PhylomeDBi Q9UKV5.
    TreeFami TF320052.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi AMFR. human.
    EvolutionaryTracei Q9UKV5.
    GeneWikii AMFR.
    GenomeRNAii 267.
    NextBioi 1049.
    PROi Q9UKV5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKV5.
    Bgeei Q9UKV5.
    CleanExi HS_AMFR.
    Genevestigatori Q9UKV5.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR003892. CUE.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02845. CUE. 1 hit.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00546. CUE. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS51140. CUE. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein."
      Shimizu K., Tani M., Watanabe H., Nagamachi Y., Niinaka Y., Shiroishi T., Ohwada S., Raz A., Yokota J.
      FEBS Lett. 456:295-300(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "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].
      Tissue: Ovary.
    3. "Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor."
      Huang B., Xie Y., Raz A.
      Biochem. Biophys. Res. Commun. 212:727-742(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 358-643.
      Tissue: Placenta.
    4. "Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor."
      Watanabe H., Carmi P., Hogan V., Raz T., Silletti S., Nabi I.R., Raz A.
      J. Biol. Chem. 266:13442-13448(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 520-643.
    5. "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum."
      Fang S., Ferrone M., Yang C., Jensen J.P., Tiwari S., Weissman A.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:14422-14427(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A UBIQUITIN LIGASE, SUBCELLULAR LOCATION, INTERACTION WITH UBE2G2.
    6. "Overexpression of the tumor autocrine motility factor receptor, gp78, a ubiquitin protein ligase (E3), results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in Hep G2 cells."
      Liang J.S., Kim T., Fang S., Yamaguchi J., Weissman A.M., Fisher E.A., Ginsberg H.N.
      J. Biol. Chem. 278:23984-23988(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION OF APOB.
    7. "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase."
      Song B.L., Sever N., DeBose-Boyd R.A.
      Mol. Cell 19:829-840(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSIG1 AND VCP, FUNCTION, MUTAGENESIS OF CYS-356.
    8. "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
      Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
      Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DERL1 AND VCP.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases."
      Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.
      Arch. Biochem. Biophys. 483:66-74(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Solution structure of RSGI RUH-076, a human CUE domain."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 452-502.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-605.

    Entry informationi

    Entry nameiAMFR_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKV5
    Secondary accession number(s): P26442, Q8IZ70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 122 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3