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O14717

- TRDMT_HUMAN

UniProt

O14717 - TRDMT_HUMAN

Protein

tRNA (cytosine(38)-C(5))-methyltransferase

Gene

TRDMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp).1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + cytosine(38) in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(38) in tRNA.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei79 – 791PROSITE-ProRule annotation

    GO - Molecular functioni

    1. DNA (cytosine-5-)-methyltransferase activity Source: ProtInc
    2. DNA binding Source: InterPro
    3. RNA binding Source: UniProtKB-KW
    4. tRNA methyltransferase activity Source: MGI

    GO - Biological processi

    1. C-5 methylation of cytosine Source: GOC
    2. response to amphetamine Source: Ensembl
    3. tRNA methylation Source: MGI

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    RNA-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03011-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA (cytosine(38)-C(5))-methyltransferase (EC:2.1.1.204)
    Alternative name(s):
    DNA (cytosine-5)-methyltransferase-like protein 2
    Short name:
    Dnmt2
    DNA methyltransferase homolog HsaIIP
    Short name:
    DNA MTase homolog HsaIIP
    Short name:
    M.HsaIIP
    PuMet
    Gene namesi
    Name:TRDMT1
    Synonyms:DNMT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2977. TRDMT1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162406922.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391tRNA (cytosine(38)-C(5))-methyltransferasePRO_0000088040Add
    BLAST

    Proteomic databases

    MaxQBiO14717.
    PaxDbiO14717.
    PRIDEiO14717.

    PTM databases

    PhosphoSiteiO14717.

    Expressioni

    Tissue specificityi

    Ubiquitous. Higher expression in testis, ovary and thymus and at much lower levels in spleen, prostate, colon, small intestine, and peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiO14717.
    BgeeiO14717.
    CleanExiHS_TRDMT1.
    GenevestigatoriO14717.

    Organism-specific databases

    HPAiCAB009468.
    HPA036946.

    Interactioni

    Protein-protein interaction databases

    BioGridi108124. 14 interactions.
    IntActiO14717. 13 interactions.
    STRINGi9606.ENSP00000367030.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi15 – 239
    Beta strandi26 – 338
    Helixi37 – 4610
    Helixi57 – 593
    Helixi62 – 687
    Beta strandi71 – 755
    Helixi98 – 1058
    Helixi106 – 1083
    Beta strandi114 – 1218
    Helixi124 – 1263
    Helixi128 – 13912
    Beta strandi142 – 1498
    Helixi151 – 1544
    Beta strandi162 – 17211
    Beta strandi182 – 1854
    Helixi253 – 2564
    Helixi263 – 2664
    Helixi270 – 2767
    Helixi277 – 2793
    Turni295 – 2995
    Beta strandi307 – 3093
    Helixi316 – 3216
    Turni322 – 3254
    Helixi328 – 3369
    Helixi345 – 3517
    Helixi366 – 37510
    Helixi379 – 39012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G55X-ray1.80A2-391[»]
    ProteinModelPortaliO14717.
    SMRiO14717. Positions 2-189, 248-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14717.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 391388SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0270.
    HOVERGENiHBG051385.
    InParanoidiO14717.
    KOiK15336.
    OMAiFGVPYSR.
    PhylomeDBiO14717.
    TreeFamiTF300024.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR018117. C5_DNA_meth_AS.
    IPR001525. C5_MeTfrase.
    IPR025813. DNA/tRNA_C5-MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10629. PTHR10629. 1 hit.
    PfamiPF00145. DNA_methylase. 1 hit.
    [Graphical view]
    PRINTSiPR00105. C5METTRFRASE.
    SUPFAMiSSF53335. SSF53335. 2 hits.
    TIGRFAMsiTIGR00675. dcm. 1 hit.
    PROSITEiPS00095. C5_MTASE_2. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform A (identifier: O14717-1) [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

    MEPLRVLELY SGVGGMHHAL RESCIPAQVV AAIDVNTVAN EVYKYNFPHT    50
    QLLAKTIEGI TLEEFDRLSF DMILMSPPCQ PFTRIGRQGD MTDSRTNSFL 100
    HILDILPRLQ KLPKYILLEN VKGFEVSSTR DLLIQTIENC GFQYQEFLLS 150
    PTSLGIPNSR LRYFLIAKLQ SEPLPFQAPG QVLMEFPKIE SVHPQKYAMD 200
    VENKIQEKNV EPNISFDGSI QCSGKDAILF KLETAEEIHR KNQQDSDLSV 250
    KMLKDFLEDD TDVNQYLLPP KSLLRYALLL DIVQPTCRRS VCFTKGYGSY 300
    IEGTGSVLQT AEDVQVENIY KSLTNLSQEE QITKLLILKL RYFTPKEIAN 350
    LLGFPPEFGF PEKITVKQRY RLLGNSLNVH VVAKLIKILY E 391
    Length:391
    Mass (Da):44,597
    Last modified:January 1, 1998 - v1
    Checksum:iBCA549E4EB2E6950
    GO
    Isoform B (identifier: O14717-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-107: Missing.

    Show »
    Length:367
    Mass (Da):41,858
    Checksum:i3801D5651DBC2614
    GO
    Isoform C (identifier: O14717-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-129: Missing.

    Show »
    Length:345
    Mass (Da):39,313
    Checksum:i65939D1BE01D958B
    GO
    Isoform D (identifier: O14717-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         59-63: GITLE → DWPAG
         64-391: Missing.

    Show »
    Length:63
    Mass (Da):6,965
    Checksum:i3DBEA06674461233
    GO
    Isoform E (identifier: O14717-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         59-71: GITLEEFDRLSFD → ITKITKVYSFGKC
         72-391: Missing.

    Show »
    Length:71
    Mass (Da):7,908
    Checksum:i862BC392F37BFA8C
    GO
    Isoform F (identifier: O14717-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         59-107: GITLEEFDRL...SFLHILDILP → RPLDTNNRKL...SVRAITLSSP
         108-391: Missing.

    Show »
    Length:107
    Mass (Da):12,087
    Checksum:iBDD5DD4DC6D6BD3E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti148 – 1481L → I in AAC39764. (PubMed:9592134)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011H → Y.1 Publication
    Corresponds to variant rs11254413 [ dbSNP | Ensembl ].
    VAR_051961

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei59 – 10749GITLE…LDILP → RPLDTNNRKLWLSVPRVYII SNLSWHSKFKATIFSYCKAS VRAITLSSP in isoform F. 1 PublicationVSP_005634Add
    BLAST
    Alternative sequencei59 – 7113GITLE…RLSFD → ITKITKVYSFGKC in isoform E. 1 PublicationVSP_005632Add
    BLAST
    Alternative sequencei59 – 635GITLE → DWPAG in isoform D. 1 PublicationVSP_005630
    Alternative sequencei64 – 391328Missing in isoform D. 1 PublicationVSP_005631Add
    BLAST
    Alternative sequencei72 – 391320Missing in isoform E. 1 PublicationVSP_005633Add
    BLAST
    Alternative sequencei84 – 12946Missing in isoform C. 1 PublicationVSP_005629Add
    BLAST
    Alternative sequencei84 – 10724Missing in isoform B. 1 PublicationVSP_005628Add
    BLAST
    Alternative sequencei108 – 391284Missing in isoform F. 1 PublicationVSP_005635Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012128 mRNA. Translation: AAC51939.1.
    AJ223333 mRNA. Translation: CAA11272.1.
    AF045888 mRNA. Translation: AAC39764.1.
    EF444974 Genomic DNA. Translation: ACA05980.1.
    EF444974 Genomic DNA. Translation: ACA05984.1.
    EF444974 Genomic DNA. Translation: ACA05985.1.
    EF444974 Genomic DNA. Translation: ACA05986.1.
    AL133415, AC067747 Genomic DNA. Translation: CAB87964.1.
    CH471072 Genomic DNA. Translation: EAW86218.1.
    CH471072 Genomic DNA. Translation: EAW86219.1.
    BC047733 mRNA. Translation: AAH47733.1.
    AF329940 mRNA. Translation: AAK68034.1.
    AF329941 mRNA. Translation: AAK68035.1.
    AF329942 mRNA. Translation: AAK68036.1.
    AF329943 mRNA. Translation: AAK68037.1.
    AF329944 mRNA. Translation: AAK68033.1.
    CCDSiCCDS7114.1. [O14717-1]
    RefSeqiNP_004403.1. NM_004412.5. [O14717-1]
    XP_005252432.1. XM_005252375.2. [O14717-3]
    UniGeneiHs.351665.

    Genome annotation databases

    EnsembliENST00000377799; ENSP00000367030; ENSG00000107614. [O14717-1]
    ENST00000424636; ENSP00000389497; ENSG00000107614.
    ENST00000495022; ENSP00000417594; ENSG00000107614. [O14717-4]
    GeneIDi1787.
    KEGGihsa:1787.
    UCSCiuc001iop.3. human. [O14717-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012128 mRNA. Translation: AAC51939.1 .
    AJ223333 mRNA. Translation: CAA11272.1 .
    AF045888 mRNA. Translation: AAC39764.1 .
    EF444974 Genomic DNA. Translation: ACA05980.1 .
    EF444974 Genomic DNA. Translation: ACA05984.1 .
    EF444974 Genomic DNA. Translation: ACA05985.1 .
    EF444974 Genomic DNA. Translation: ACA05986.1 .
    AL133415 , AC067747 Genomic DNA. Translation: CAB87964.1 .
    CH471072 Genomic DNA. Translation: EAW86218.1 .
    CH471072 Genomic DNA. Translation: EAW86219.1 .
    BC047733 mRNA. Translation: AAH47733.1 .
    AF329940 mRNA. Translation: AAK68034.1 .
    AF329941 mRNA. Translation: AAK68035.1 .
    AF329942 mRNA. Translation: AAK68036.1 .
    AF329943 mRNA. Translation: AAK68037.1 .
    AF329944 mRNA. Translation: AAK68033.1 .
    CCDSi CCDS7114.1. [O14717-1 ]
    RefSeqi NP_004403.1. NM_004412.5. [O14717-1 ]
    XP_005252432.1. XM_005252375.2. [O14717-3 ]
    UniGenei Hs.351665.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G55 X-ray 1.80 A 2-391 [» ]
    ProteinModelPortali O14717.
    SMRi O14717. Positions 2-189, 248-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108124. 14 interactions.
    IntActi O14717. 13 interactions.
    STRINGi 9606.ENSP00000367030.

    PTM databases

    PhosphoSitei O14717.

    Proteomic databases

    MaxQBi O14717.
    PaxDbi O14717.
    PRIDEi O14717.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377799 ; ENSP00000367030 ; ENSG00000107614 . [O14717-1 ]
    ENST00000424636 ; ENSP00000389497 ; ENSG00000107614 .
    ENST00000495022 ; ENSP00000417594 ; ENSG00000107614 . [O14717-4 ]
    GeneIDi 1787.
    KEGGi hsa:1787.
    UCSCi uc001iop.3. human. [O14717-1 ]

    Organism-specific databases

    CTDi 1787.
    GeneCardsi GC10M017098.
    HGNCi HGNC:2977. TRDMT1.
    HPAi CAB009468.
    HPA036946.
    MIMi 602478. gene.
    neXtProti NX_O14717.
    PharmGKBi PA162406922.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0270.
    HOVERGENi HBG051385.
    InParanoidi O14717.
    KOi K15336.
    OMAi FGVPYSR.
    PhylomeDBi O14717.
    TreeFami TF300024.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03011-MONOMER.

    Miscellaneous databases

    ChiTaRSi TRDMT1. human.
    EvolutionaryTracei O14717.
    GeneWikii TRDMT1.
    GenomeRNAii 1787.
    NextBioi 7271.
    PROi O14717.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14717.
    Bgeei O14717.
    CleanExi HS_TRDMT1.
    Genevestigatori O14717.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR018117. C5_DNA_meth_AS.
    IPR001525. C5_MeTfrase.
    IPR025813. DNA/tRNA_C5-MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10629. PTHR10629. 1 hit.
    Pfami PF00145. DNA_methylase. 1 hit.
    [Graphical view ]
    PRINTSi PR00105. C5METTRFRASE.
    SUPFAMi SSF53335. SSF53335. 2 hits.
    TIGRFAMsi TIGR00675. dcm. 1 hit.
    PROSITEi PS00095. C5_MTASE_2. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast."
      Yoder J.A., Bestor T.H.
      Hum. Mol. Genet. 7:279-284(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    2. "Cloning and analysis of a novel human putative DNA methyltransferase."
      Van den Wyngaert I., Sprengel J., Kass S.U., Luyten W.H.M.L.
      FEBS Lett. 426:283-289(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    3. "Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells."
      Okano M., Xie S., Li E.
      Nucleic Acids Res. 26:2536-2540(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
      Tissue: Heart.
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 A), VARIANT TYR-101.
      Tissue: Uterus.
    8. "Five novel alternatively spliced transcripts of DNA (cytosine-5) methyltransferase 2 in human peripheral blood leukocytes."
      Franchina M., Hooper J., Kay P.H.
      Int. J. Biochem. Cell Biol. 33:1104-1115(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-179 (ISOFORMS A; B; C; D; E AND F).
      Tissue: Peripheral blood leukocyte.
    9. Cited for: FUNCTION, CATALYTIC ACTIVITY.
    10. "Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA."
      Dong A., Yoder J.A., Zhang X., Zhou L., Bestor T.H., Cheng X.
      Nucleic Acids Res. 29:439-448(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiTRDMT_HUMAN
    AccessioniPrimary (citable) accession number: O14717
    Secondary accession number(s): B0YJ02
    , B0YJ03, B0YJ07, B0YJ08, O43669, Q86WW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 124 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 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3