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Q96BT7

- ALKB8_HUMAN

UniProt

Q96BT7 - ALKB8_HUMAN

Protein

Alkylated DNA repair protein alkB homolog 8

Gene

ALKBH8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA. Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys). Required for normal survival after DNA damage. May inhibit apoptosis and promote cell survival and angiogenesis.2 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + carboxymethyluridine(34) in tRNA = S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi238 – 2381Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi240 – 2401Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi292 – 2921Iron; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: InterPro
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB-KW
    5. tRNA (uracil) methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. tRNA methylation Source: UniProtKB

    Keywords - Molecular functioni

    Methyltransferase, Oxidoreductase, Transferase

    Keywords - Ligandi

    Iron, Metal-binding, RNA-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkylated DNA repair protein alkB homolog 8 (EC:1.14.11.-)
    Alternative name(s):
    Probable alpha-ketoglutarate-dependent dioxygenase ABH8
    S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8
    tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8 (EC:2.1.1.229)
    Gene namesi
    Name:ALKBH8
    Synonyms:ABH8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:25189. ALKBH8.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485296.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 664664Alkylated DNA repair protein alkB homolog 8PRO_0000337125Add
    BLAST

    Proteomic databases

    MaxQBiQ96BT7.
    PaxDbiQ96BT7.
    PRIDEiQ96BT7.

    PTM databases

    PhosphoSiteiQ96BT7.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest expression in spleen, followed by pancreas and lung.1 Publication

    Inductioni

    Up-regulated after DNA damage. Induction is mediated via ATM.1 Publication

    Gene expression databases

    ArrayExpressiQ96BT7.
    BgeeiQ96BT7.
    CleanExiHS_ALKBH8.
    GenevestigatoriQ96BT7.

    Organism-specific databases

    HPAiHPA038725.

    Interactioni

    Subunit structurei

    Interacts with TRMT112.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000374219.

    Structurei

    Secondary structure

    1
    664
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 283
    Turni30 – 345
    Beta strandi38 – 403
    Beta strandi43 – 486
    Helixi52 – 543
    Helixi58 – 669
    Beta strandi71 – 755
    Beta strandi81 – 899
    Helixi90 – 9910
    Turni100 – 1023
    Beta strandi104 – 1063
    Beta strandi112 – 1143
    Beta strandi116 – 1194
    Beta strandi121 – 1299
    Beta strandi137 – 1404
    Helixi146 – 1538
    Beta strandi175 – 1773
    Helixi202 – 21413
    Beta strandi222 – 2298
    Beta strandi235 – 2384
    Turni242 – 2443
    Beta strandi249 – 2568
    Beta strandi258 – 2636
    Beta strandi269 – 2746
    Beta strandi278 – 2825
    Helixi285 – 2884
    Beta strandi290 – 2945
    Beta strandi298 – 3047
    Beta strandi307 – 3093
    Beta strandi315 – 3184
    Beta strandi320 – 3245
    Beta strandi328 – 3347
    Turni346 – 3483
    Turni350 – 3556

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQ2NMR-A25-125[»]
    3THPX-ray3.20A25-355[»]
    3THTX-ray3.01A/B/C/D25-355[»]
    ProteinModelPortaliQ96BT7.
    SMRiQ96BT7. Positions 25-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96BT7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 12078RRMAdd
    BLAST
    Domaini220 – 337118Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni227 – 2293Alpha-ketoglutarate bindingBy similarity
    Regioni328 – 3347Alpha-ketoglutarate bindingBy similarity
    Regioni411 – 664254Methyltransferase domainAdd
    BLAST

    Sequence similaritiesi

    Belongs to the alkB family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0500.
    HOGENOMiHOG000007984.
    HOVERGENiHBG067234.
    InParanoidiQ96BT7.
    KOiK10770.
    OMAiPCNCSYP.
    OrthoDBiEOG780RMC.
    PhylomeDBiQ96BT7.
    TreeFamiTF316056.

    Family and domain databases

    Gene3Di2.60.120.590. 1 hit.
    3.40.50.150. 2 hits.
    InterProiIPR027450. AlkB-like.
    IPR015095. AlkB_hom8_N.
    IPR013216. Methyltransf_11.
    IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
    PF09004. DUF1891. 1 hit.
    PF08241. Methyltransf_11. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96BT7-1) [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

    MDSNHQSNYK LSKTEKKFLR KQIKAKHTLL RHEGIETVSY ATQSLVVANG    50
    GLGNGVSRNQ LLPVLEKCGL VDALLMPPNK PYSFARYRTT EESKRAYVTL 100
    NGKEVVDDLG QKITLYLNFV EKVQWKELRP QALPPGLMVV EEIISSEEEK 150
    MLLESVDWTE DTDNQNSQKS LKHRRVKHFG YEFHYENNNV DKDKPLSGGL 200
    PDICESFLEK WLRKGYIKHK PDQMTINQYE PGQGIPAHID THSAFEDEIV 250
    SLSLGSEIVM DFKHPDGIAV PVMLPRRSLL VMTGESRYLW THGITCRKFD 300
    TVQASESLKS GIITSDVGDL TLSKRGLRTS FTFRKVRQTP CNCSYPLVCD 350
    SQRKETPPSF PESDKEASRL EQEYVHQVYE EIAGHFSSTR HTPWPHIVEF 400
    LKALPSGSIV ADIGCGNGKY LGINKELYMI GCDRSQNLVD ICRERQFQAF 450
    VCDALAVPVR SGSCDACISI AVIHHFATAE RRVAALQEIV RLLRPGGKAL 500
    IYVWAMEQEY NKQKSKYLRG NRNSQGKKEE MNSDTSVQRS LVEQMRDMGS 550
    RDSASSVPRI NDSQEGGCNS RQVSNSKLPV HVNRTSFYSQ DVLVPWHLKG 600
    NPDKGKPVEP FGPIGSQDPS PVFHRYYHVF REGELEGACR TVSDVRILQS 650
    YYDQGNWCVI LQKA 664
    Length:664
    Mass (Da):75,208
    Last modified:May 20, 2008 - v2
    Checksum:i4BE595D6757C2A43
    GO
    Isoform 2 (identifier: Q96BT7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         234-238: GIPAH → DCHGF
         239-664: Missing.

    Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:238
    Mass (Da):27,440
    Checksum:i24EF6A3A66DCC2F7
    GO
    Isoform 3 (identifier: Q96BT7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-224: GYIKHKPDQM → AEKNLEVGIH
         225-664: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:224
    Mass (Da):25,742
    Checksum:i6FD66E832509EE87
    GO
    Isoform 4 (identifier: Q96BT7-4) [UniParc]FASTAAdd to Basket

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

    Note: May be due to competing donor splice site. No experimental confirmation available.

    Show »
    Length:667
    Mass (Da):75,558
    Checksum:iBF6DB408A2B1B39C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101K → R in BAC04566. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MFAM in isoform 4. 1 PublicationVSP_039159
    Alternative sequencei215 – 22410GYIKHKPDQM → AEKNLEVGIH in isoform 3. 1 PublicationVSP_033925
    Alternative sequencei225 – 664440Missing in isoform 3. 1 PublicationVSP_033926Add
    BLAST
    Alternative sequencei234 – 2385GIPAH → DCHGF in isoform 2. 1 PublicationVSP_033927
    Alternative sequencei239 – 664426Missing in isoform 2. 1 PublicationVSP_033928Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB218768 mRNA. Translation: BAG16270.1.
    AK095523 mRNA. Translation: BAC04566.1.
    AK293603 mRNA. Translation: BAG57067.1.
    AK304413 mRNA. Translation: BAG65244.1.
    AP001823 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67089.1.
    CH471065 Genomic DNA. Translation: EAW67090.1.
    BC015183 mRNA. Translation: AAH15183.1.
    CCDSiCCDS8337.2. [Q96BT7-1]
    RefSeqiNP_620130.2. NM_138775.2. [Q96BT7-1]
    XP_005271784.1. XM_005271727.1. [Q96BT7-4]
    UniGeneiHs.503763.

    Genome annotation databases

    EnsembliENST00000260318; ENSP00000260318; ENSG00000137760. [Q96BT7-2]
    ENST00000389568; ENSP00000374219; ENSG00000137760. [Q96BT7-1]
    ENST00000417449; ENSP00000397673; ENSG00000137760. [Q96BT7-4]
    ENST00000428149; ENSP00000415885; ENSG00000137760. [Q96BT7-1]
    ENST00000429370; ENSP00000391225; ENSG00000137760. [Q96BT7-3]
    GeneIDi91801.
    KEGGihsa:91801.
    UCSCiuc001pjk.3. human. [Q96BT7-1]

    Polymorphism databases

    DMDMi189027650.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB218768 mRNA. Translation: BAG16270.1 .
    AK095523 mRNA. Translation: BAC04566.1 .
    AK293603 mRNA. Translation: BAG57067.1 .
    AK304413 mRNA. Translation: BAG65244.1 .
    AP001823 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67089.1 .
    CH471065 Genomic DNA. Translation: EAW67090.1 .
    BC015183 mRNA. Translation: AAH15183.1 .
    CCDSi CCDS8337.2. [Q96BT7-1 ]
    RefSeqi NP_620130.2. NM_138775.2. [Q96BT7-1 ]
    XP_005271784.1. XM_005271727.1. [Q96BT7-4 ]
    UniGenei Hs.503763.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQ2 NMR - A 25-125 [» ]
    3THP X-ray 3.20 A 25-355 [» ]
    3THT X-ray 3.01 A/B/C/D 25-355 [» ]
    ProteinModelPortali Q96BT7.
    SMRi Q96BT7. Positions 25-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000374219.

    PTM databases

    PhosphoSitei Q96BT7.

    Polymorphism databases

    DMDMi 189027650.

    Proteomic databases

    MaxQBi Q96BT7.
    PaxDbi Q96BT7.
    PRIDEi Q96BT7.

    Protocols and materials databases

    DNASUi 91801.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260318 ; ENSP00000260318 ; ENSG00000137760 . [Q96BT7-2 ]
    ENST00000389568 ; ENSP00000374219 ; ENSG00000137760 . [Q96BT7-1 ]
    ENST00000417449 ; ENSP00000397673 ; ENSG00000137760 . [Q96BT7-4 ]
    ENST00000428149 ; ENSP00000415885 ; ENSG00000137760 . [Q96BT7-1 ]
    ENST00000429370 ; ENSP00000391225 ; ENSG00000137760 . [Q96BT7-3 ]
    GeneIDi 91801.
    KEGGi hsa:91801.
    UCSCi uc001pjk.3. human. [Q96BT7-1 ]

    Organism-specific databases

    CTDi 91801.
    GeneCardsi GC11M107373.
    HGNCi HGNC:25189. ALKBH8.
    HPAi HPA038725.
    MIMi 613306. gene.
    neXtProti NX_Q96BT7.
    PharmGKBi PA143485296.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0500.
    HOGENOMi HOG000007984.
    HOVERGENi HBG067234.
    InParanoidi Q96BT7.
    KOi K10770.
    OMAi PCNCSYP.
    OrthoDBi EOG780RMC.
    PhylomeDBi Q96BT7.
    TreeFami TF316056.

    Miscellaneous databases

    EvolutionaryTracei Q96BT7.
    GenomeRNAii 91801.
    NextBioi 77461.
    PROi Q96BT7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96BT7.
    Bgeei Q96BT7.
    CleanExi HS_ALKBH8.
    Genevestigatori Q96BT7.

    Family and domain databases

    Gene3Di 2.60.120.590. 1 hit.
    3.40.50.150. 2 hits.
    InterProi IPR027450. AlkB-like.
    IPR015095. AlkB_hom8_N.
    IPR013216. Methyltransf_11.
    IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF13532. 2OG-FeII_Oxy_2. 1 hit.
    PF09004. DUF1891. 1 hit.
    PF08241. Methyltransf_11. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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; 3 AND 4).
      Tissue: Brain and Trachea.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2).
      Tissue: Uterus.
    6. "A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression."
      Shimada K., Nakamura M., Anai S., De Velasco M., Tanaka M., Tsujikawa K., Ouji Y., Konishi N.
      Cancer Res. 69:3157-3164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Human AlkB homolog ABH8 is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival."
      Fu D., Brophy J.A., Chan C.T., Atmore K.A., Begley U., Paules R.S., Dedon P.C., Begley T.J., Samson L.D.
      Mol. Cell. Biol. 30:2449-2459(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TRMT112, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Solution structure of RNA binding domain in hypothetical protein LOC91801."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 25-125.

    Entry informationi

    Entry nameiALKB8_HUMAN
    AccessioniPrimary (citable) accession number: Q96BT7
    Secondary accession number(s): B1Q2M0, B4DEF6, Q8N989
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 114 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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