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Q96B02

- UBE2W_HUMAN

UniProt

Q96B02 - UBE2W_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 W

Gene

UBE2W

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

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Transfers ubiquitin in complex with RING/U-box type E3s that do not have active site cysteine residues to form thioester bonds with ubiquitin, and preferentially ubiquitinates the N-terminus of substrates, such as ATXN3, STUB1 and SUMO2.5 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. ubiquitin protein ligase binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to misfolded protein Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. protein K11-linked ubiquitination Source: UniProtKB
    6. protein monoubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ96B02.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 W (EC:6.3.2.19)
    Alternative name(s):
    N-terminus-conjugating E2
    Ubiquitin carrier protein W
    Ubiquitin-conjugating enzyme 16
    Short name:
    UBC-16
    Ubiquitin-protein ligase W
    Gene namesi
    Name:UBE2W
    Synonyms:UBC16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:25616. UBE2W.

    Subcellular locationi

    Nucleus 1 Publication
    Note: In the nucleus, colocalizes with FANCL.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831H → N: Impaired substrate ubiquitination of both Tau and ATXN3. 1 Publication
    Mutagenesisi91 – 911C → A: Loss of predominant nuclear localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670657.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Ubiquitin-conjugating enzyme E2 WPRO_0000232689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Ubiquitinated in vitro in the presence of FANCL By similarity. Autoubiquitinated at Met-1.By similarity1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ96B02.
    PRIDEiQ96B02.

    PTM databases

    PhosphoSiteiQ96B02.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest expression in brain, liver, pancreas and heart.1 Publication

    Gene expression databases

    ArrayExpressiQ96B02.
    BgeeiQ96B02.
    CleanExiHS_UBE2W.
    GenevestigatoriQ96B02.

    Organism-specific databases

    HPAiHPA045161.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with FANCL. Interacts with STUB1/CHIP By similarity.By similarity

    Protein-protein interaction databases

    BioGridi120572. 69 interactions.
    IntActiQ96B02. 67 interactions.
    MINTiMINT-1428082.
    STRINGi9606.ENSP00000397453.

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1712
    Beta strandi35 – 428
    Turni48 – 514
    Beta strandi53 – 608
    Turni62 – 665
    Beta strandi70 – 767
    Helixi93 – 953
    Turni96 – 983
    Helixi105 – 11511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A7LX-ray1.82A/B1-117[»]
    ProteinModelPortaliQ96B02.
    SMRiQ96B02. Positions 1-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96B02.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233453.
    HOVERGENiHBG063308.
    KOiK10688.
    PhylomeDBiQ96B02.
    TreeFamiTF314582.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96B02-1) [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

    MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE    50
    GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS 100
    PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT 150
    C 151
    Length:151
    Mass (Da):17,331
    Last modified:December 1, 2001 - v1
    Checksum:i276B585BBC4CEB71
    GO
    Isoform 2 (identifier: Q96B02-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         5-5: Q → QTTGRRVEVWFP

    Show »
    Length:162
    Mass (Da):18,660
    Checksum:iF41B440840AD0625
    GO
    Isoform 3 (identifier: Q96B02-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLSPRGVTRARQLLPLRLWPRRSWGDGSIM

    Note: No experimental confirmation available.

    Show »
    Length:180
    Mass (Da):20,689
    Checksum:i3E0F0920D2F1AD9F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261N → S in BAB13883. (PubMed:14702039)Curated
    Sequence conflicti45 – 451P → S in BAA91954. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MLSPRGVTRARQLLPLRLWP RRSWGDGSIM in isoform 3. 1 PublicationVSP_042974
    Alternative sequencei5 – 51Q → QTTGRRVEVWFP in isoform 2. 2 PublicationsVSP_017943

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY948289 mRNA. Translation: AAY24555.1.
    AK001873 mRNA. Translation: BAA91954.1.
    AK021735 mRNA. Translation: BAB13883.1.
    AK024050 mRNA. Translation: BAB14800.1.
    AK295792 mRNA. Translation: BAG58613.1.
    CR457275 mRNA. Translation: CAG33556.1.
    CH471068 Genomic DNA. Translation: EAW87009.1.
    CH471068 Genomic DNA. Translation: EAW87011.1.
    AC022826 Genomic DNA. No translation available.
    BC016326 mRNA. Translation: AAH16326.1.
    CCDSiCCDS47874.2. [Q96B02-3]
    RefSeqiNP_001001481.2. NM_001001481.2.
    NP_001257944.1. NM_001271015.1.
    NP_060769.4. NM_018299.4. [Q96B02-3]
    UniGeneiHs.128841.

    Genome annotation databases

    EnsembliENST00000517608; ENSP00000428813; ENSG00000104343. [Q96B02-3]
    ENST00000602593; ENSP00000473561; ENSG00000104343. [Q96B02-1]
    ENST00000602969; ENSP00000473516; ENSG00000104343. [Q96B02-2]
    GeneIDi55284.
    KEGGihsa:55284.
    UCSCiuc003xzt.3. human. [Q96B02-3]
    uc003xzu.4. human. [Q96B02-2]

    Polymorphism databases

    DMDMi74751754.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY948289 mRNA. Translation: AAY24555.1 .
    AK001873 mRNA. Translation: BAA91954.1 .
    AK021735 mRNA. Translation: BAB13883.1 .
    AK024050 mRNA. Translation: BAB14800.1 .
    AK295792 mRNA. Translation: BAG58613.1 .
    CR457275 mRNA. Translation: CAG33556.1 .
    CH471068 Genomic DNA. Translation: EAW87009.1 .
    CH471068 Genomic DNA. Translation: EAW87011.1 .
    AC022826 Genomic DNA. No translation available.
    BC016326 mRNA. Translation: AAH16326.1 .
    CCDSi CCDS47874.2. [Q96B02-3 ]
    RefSeqi NP_001001481.2. NM_001001481.2.
    NP_001257944.1. NM_001271015.1.
    NP_060769.4. NM_018299.4. [Q96B02-3 ]
    UniGenei Hs.128841.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A7L X-ray 1.82 A/B 1-117 [» ]
    ProteinModelPortali Q96B02.
    SMRi Q96B02. Positions 1-117.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120572. 69 interactions.
    IntActi Q96B02. 67 interactions.
    MINTi MINT-1428082.
    STRINGi 9606.ENSP00000397453.

    PTM databases

    PhosphoSitei Q96B02.

    Polymorphism databases

    DMDMi 74751754.

    Proteomic databases

    MaxQBi Q96B02.
    PRIDEi Q96B02.

    Protocols and materials databases

    DNASUi 55284.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000517608 ; ENSP00000428813 ; ENSG00000104343 . [Q96B02-3 ]
    ENST00000602593 ; ENSP00000473561 ; ENSG00000104343 . [Q96B02-1 ]
    ENST00000602969 ; ENSP00000473516 ; ENSG00000104343 . [Q96B02-2 ]
    GeneIDi 55284.
    KEGGi hsa:55284.
    UCSCi uc003xzt.3. human. [Q96B02-3 ]
    uc003xzu.4. human. [Q96B02-2 ]

    Organism-specific databases

    CTDi 55284.
    GeneCardsi GC08M074692.
    HGNCi HGNC:25616. UBE2W.
    HPAi HPA045161.
    MIMi 614277. gene.
    neXtProti NX_Q96B02.
    PharmGKBi PA142670657.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233453.
    HOVERGENi HBG063308.
    KOi K10688.
    PhylomeDBi Q96B02.
    TreeFami TF314582.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q96B02.

    Miscellaneous databases

    ChiTaRSi UBE2W. human.
    EvolutionaryTracei Q96B02.
    GenomeRNAii 55284.
    NextBioi 59442.
    PROi Q96B02.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96B02.
    Bgeei Q96B02.
    CleanExi HS_UBE2W.
    Genevestigatori Q96B02.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization and subcellular localization of a gene encoding a human Ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis thaliana UBC-16 gene product."
      Yin G., Ji C., Wu T., Shen Z., Xu X., Xie Y., Mao Y.
      Front. Biosci. 11:1500-1507(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-91.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Embryo, Hippocampus and Placenta.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Urinary bladder.
    7. "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
      Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
      Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FANCL.
    8. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
      David Y., Ziv T., Admon A., Navon A.
      J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2."
      Zhang Y., Zhou X., Zhao L., Li C., Zhu H., Xu L., Shan L., Liao X., Guo Z., Huang P.
      Mol. Cells 31:113-122(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini."
      Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.
      Biochem. J. 453:137-145(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION AT MET-1, SUBSTRATE SPECIFICITY.
    11. "The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates."
      Scaglione K.M., Basrur V., Ashraf N.S., Konen J.R., Elenitoba-Johnson K.S., Todi S.V., Paulson H.L.
      J. Biol. Chem. 288:18784-18788(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE SPECIFICITY, MUTAGENESIS OF HIS-83.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-117, SUBUNIT.

    Entry informationi

    Entry nameiUBE2W_HUMAN
    AccessioniPrimary (citable) accession number: Q96B02
    Secondary accession number(s): B4DIV1
    , Q1XBE0, Q9H823, Q9HAG6, Q9NV07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 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 8
      Human chromosome 8: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3