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P52655

- TF2AA_HUMAN

UniProt

P52655 - TF2AA_HUMAN

Protein

Transcription initiation factor IIA subunit 1

Gene

GTF2A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei274 – 2752Cleavage; by TASP1

    GO - Molecular functioni

    1. DNA binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: BHF-UCL
    4. TBP-class protein binding Source: BHF-UCL
    5. transcription coactivator activity Source: ProtInc
    6. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. gene expression Source: Reactome
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription elongation from RNA polymerase II promoter Source: Reactome
    4. transcription from RNA polymerase II promoter Source: BHF-UCL
    5. transcription initiation from RNA polymerase II promoter Source: Reactome
    6. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_6233. Transcription of the HIV genome.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6332. HIV Transcription Initiation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription initiation factor IIA subunit 1
    Alternative name(s):
    General transcription factor IIA subunit 1
    TFIIAL
    Transcription initiation factor TFIIA 42 kDa subunit
    Short name:
    TFIIA-42
    Cleaved into the following 2 chains:
    Alternative name(s):
    TFIIA p35 subunit
    Alternative name(s):
    TFIIA p19 subunit
    Gene namesi
    Name:GTF2A1
    Synonyms:TF2A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:4646. GTF2A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. transcription factor TFIIA complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi270 – 2701V → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication
    Mutagenesisi272 – 2721Q → A: Abolishes cleavage. 1 Publication
    Mutagenesisi273 – 2731V → A: Abolishes cleavage. 1 Publication
    Mutagenesisi274 – 2741D → A: Abolishes cleavage. 1 Publication
    Mutagenesisi275 – 2751G → A: Abolishes cleavage. 1 Publication
    Mutagenesisi276 – 2761T → A: Does not affect cleavage. 1 Publication
    Mutagenesisi277 – 2771G → A: Does not affect cleavage. 1 Publication
    Mutagenesisi278 – 2781D → A: Significant reduction of cleavage. 1 Publication
    Mutagenesisi280 – 2801S → A: Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321. 2 Publications
    Mutagenesisi281 – 2811S → A: Eliminates phosphorylation; when associated with A-280; A-316 and A-321. 1 Publication
    Mutagenesisi282 – 2821E → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication
    Mutagenesisi316 – 3161S → A: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321. 1 Publication
    Mutagenesisi321 – 3211S → A: Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316. 1 Publication

    Organism-specific databases

    PharmGKBiPA29033.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 376375Transcription initiation factor IIA subunit 1PRO_0000022481Add
    BLAST
    Chaini2 – 274273Transcription initiation factor IIA alpha chainPRO_0000042593Add
    BLAST
    Chaini275 – 376102Transcription initiation factor IIA beta chainPRO_0000042594Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei280 – 2801Phosphoserine; by TAF11 Publication
    Modified residuei281 – 2811Phosphoserine; by TAF11 Publication
    Modified residuei316 – 3161Phosphoserine; by TAF12 Publications
    Modified residuei321 – 3211Phosphoserine; by TAF12 Publications

    Post-translational modificationi

    The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. The cleavage promotes proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52655.
    PaxDbiP52655.
    PRIDEiP52655.

    PTM databases

    PhosphoSiteiP52655.

    Miscellaneous databases

    PMAP-CutDBP52655.

    Expressioni

    Gene expression databases

    ArrayExpressiP52655.
    BgeeiP52655.
    GenevestigatoriP52655.

    Organism-specific databases

    HPAiHPA000869.

    Interactioni

    Subunit structurei

    TFIIA is a heterodimer of the large unprocessed subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12). TFIIA forms a complex with TBP.1 Publication

    Protein-protein interaction databases

    BioGridi109212. 47 interactions.
    IntActiP52655. 6 interactions.
    STRINGi9606.ENSP00000298173.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 3223
    Helixi36 – 5015
    Beta strandi334 – 34512
    Beta strandi348 – 36013
    Beta strandi363 – 37513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NVPX-ray2.10B2-58[»]
    C303-376[»]
    ProteinModelPortaliP52655.
    SMRiP52655. Positions 9-51, 330-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52655.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 8010Poly-Gln
    Compositional biasi81 – 877Poly-His

    Sequence similaritiesi

    Belongs to the TFIIA subunit 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5149.
    HOGENOMiHOG000015236.
    HOVERGENiHBG052771.
    InParanoidiP52655.
    KOiK03122.
    OMAiHMSATGM.
    OrthoDBiEOG7KWSJM.
    PhylomeDBiP52655.
    TreeFamiTF350445.

    Family and domain databases

    Gene3Di1.10.287.100. 1 hit.
    2.30.18.10. 1 hit.
    InterProiIPR009083. TFIIA_a-hlx.
    IPR004855. TFIIA_asu/bsu.
    IPR013028. TFIIA_asu_N.
    IPR009088. TFIIA_b-brl.
    [Graphical view]
    PANTHERiPTHR12694. PTHR12694. 1 hit.
    PfamiPF03153. TFIIA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47396. SSF47396. 1 hit.
    SSF50784. SSF50784. 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 initiation. Align

    Isoform 42 kDa (identifier: P52655-1) [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

    MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL    50
    MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA 100
    QTQQVLIPAS QQATAPQVIV PDSKLIQHMN ASNMSAAATA ATLALPAGVT 150
    PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ SVVLQQQVIP QMQPGGVQAP 200
    VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV AAPTPAQAQI 250
    TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE 300
    KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK 350
    FHLKDGIMNL NGRDYIFSKA IGDAEW 376
    Length:376
    Mass (Da):41,514
    Last modified:October 1, 1996 - v1
    Checksum:i4BAE1853E7E89218
    GO
    Isoform 37 kDa (identifier: P52655-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.

    Show »
    Length:337
    Mass (Da):37,152
    Checksum:i81D62BCC81399DE6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301L → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035667
    Natural varianti109 – 1091A → P.
    Corresponds to variant rs17111579 [ dbSNP | Ensembl ].
    VAR_054043

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939Missing in isoform 37 kDa. CuratedVSP_018798Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75383 mRNA. Translation: CAA53151.1.
    X75383 mRNA. Translation: CAA53152.1.
    X77225 mRNA. Translation: CAA54442.1.
    D14887 mRNA. Translation: BAA03604.1.
    D14886 mRNA. Translation: BAA03603.1.
    AC010582 Genomic DNA. Translation: AAF26776.1.
    BC107155 mRNA. Translation: AAI07156.1.
    BC107156 mRNA. Translation: AAI07157.1.
    CCDSiCCDS9873.1. [P52655-1]
    CCDS9874.1. [P52655-2]
    PIRiA49077.
    RefSeqiNP_001265869.1. NM_001278940.1.
    NP_056943.1. NM_015859.3. [P52655-1]
    NP_963889.1. NM_201595.2. [P52655-2]
    UniGeneiHs.592334.

    Genome annotation databases

    GeneIDi2957.
    KEGGihsa:2957.
    UCSCiuc001xve.2. human. [P52655-1]

    Polymorphism databases

    DMDMi1711663.

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75383 mRNA. Translation: CAA53151.1 .
    X75383 mRNA. Translation: CAA53152.1 .
    X77225 mRNA. Translation: CAA54442.1 .
    D14887 mRNA. Translation: BAA03604.1 .
    D14886 mRNA. Translation: BAA03603.1 .
    AC010582 Genomic DNA. Translation: AAF26776.1 .
    BC107155 mRNA. Translation: AAI07156.1 .
    BC107156 mRNA. Translation: AAI07157.1 .
    CCDSi CCDS9873.1. [P52655-1 ]
    CCDS9874.1. [P52655-2 ]
    PIRi A49077.
    RefSeqi NP_001265869.1. NM_001278940.1.
    NP_056943.1. NM_015859.3. [P52655-1 ]
    NP_963889.1. NM_201595.2. [P52655-2 ]
    UniGenei Hs.592334.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NVP X-ray 2.10 B 2-58 [» ]
    C 303-376 [» ]
    ProteinModelPortali P52655.
    SMRi P52655. Positions 9-51, 330-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109212. 47 interactions.
    IntActi P52655. 6 interactions.
    STRINGi 9606.ENSP00000298173.

    PTM databases

    PhosphoSitei P52655.

    Polymorphism databases

    DMDMi 1711663.

    Proteomic databases

    MaxQBi P52655.
    PaxDbi P52655.
    PRIDEi P52655.

    Protocols and materials databases

    DNASUi 2957.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2957.
    KEGGi hsa:2957.
    UCSCi uc001xve.2. human. [P52655-1 ]

    Organism-specific databases

    CTDi 2957.
    GeneCardsi GC14M081646.
    HGNCi HGNC:4646. GTF2A1.
    HPAi HPA000869.
    MIMi 600520. gene.
    neXtProti NX_P52655.
    PharmGKBi PA29033.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5149.
    HOGENOMi HOG000015236.
    HOVERGENi HBG052771.
    InParanoidi P52655.
    KOi K03122.
    OMAi HMSATGM.
    OrthoDBi EOG7KWSJM.
    PhylomeDBi P52655.
    TreeFami TF350445.

    Enzyme and pathway databases

    Reactomei REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_6233. Transcription of the HIV genome.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6332. HIV Transcription Initiation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

    Miscellaneous databases

    ChiTaRSi GTF2A1. human.
    EvolutionaryTracei P52655.
    GeneWikii GTF2A1.
    GenomeRNAii 2957.
    NextBioi 11720.
    PMAP-CutDB P52655.
    PROi P52655.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52655.
    Bgeei P52655.
    Genevestigatori P52655.

    Family and domain databases

    Gene3Di 1.10.287.100. 1 hit.
    2.30.18.10. 1 hit.
    InterProi IPR009083. TFIIA_a-hlx.
    IPR004855. TFIIA_asu/bsu.
    IPR013028. TFIIA_asu_N.
    IPR009088. TFIIA_b-brl.
    [Graphical view ]
    PANTHERi PTHR12694. PTHR12694. 1 hit.
    Pfami PF03153. TFIIA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47396. SSF47396. 1 hit.
    SSF50784. SSF50784. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a cDNA encoding the largest subunit of TFIIA reveals functions important for activated transcription."
      Ma D., Watanabe H., Mermelstein F., Admon A., Oguri K., Sun X., Wada T., Imai T., Shiroya T., Reinberg D., Handa H.
      Genes Dev. 7:2246-2257(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of human TFIIA."
      Dejong J., Roeder R.G.
      Genes Dev. 7:2220-2234(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    3. Watanabe H., Oguri K., Wada T., Imai T., Shiroya T., Handa H.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      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].
    6. "TAC, a TBP-sans-TAFs complex containing the unprocessed TFIIAalphabeta precursor and the TFIIAgamma subunit."
      Mitsiou D.J., Stunnenberg H.G.
      Mol. Cell 6:527-537(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH GTF2A2 AND TBP.
    7. "Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity."
      Solow S., Salunek M., Ryan R., Lieberman P.M.
      J. Biol. Chem. 276:15886-15892(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-280; SER-281; SER-316 AND SER-321, MUTAGENESIS OF SER-280; SER-281; SER-316 AND SER-321.
    8. "Cleavage and proteasome-mediated degradation of the basal transcription factor TFIIA."
      Hoiby T., Mitsiou D.J., Zhou H., Erdjument-Bromage H., Tempst P., Stunnenberg H.G.
      EMBO J. 23:3083-3091(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 278-289, MUTAGENESIS OF VAL-270; GLN-272; VAL-273; ASP-274; GLY-275; THR-276; GLY-277; ASP-278; SER-280 AND GLU-282.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: FUNCTION OF THE GTF2A1 PRECURSOR, CLEAVAGE BY TASP1.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-30.

    Entry informationi

    Entry nameiTF2AA_HUMAN
    AccessioniPrimary (citable) accession number: P52655
    Secondary accession number(s): Q3KNQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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