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Q9H244

- P2Y12_HUMAN

UniProt

Q9H244 - P2Y12_HUMAN

Protein

P2Y purinoceptor 12

Gene

P2RY12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei93 – 931ADP
    Binding sitei97 – 971ADP; via carbonyl oxygen
    Binding sitei105 – 1051ADP
    Binding sitei187 – 1871ADP
    Binding sitei191 – 1911ADP
    Binding sitei263 – 2631ADP
    Binding sitei280 – 2801ADP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi156 – 1594ADP
    Nucleotide bindingi175 – 1795ADP
    Nucleotide bindingi256 – 2594ADP

    GO - Molecular functioni

    1. ADP receptor activity Source: UniProtKB
    2. G-protein coupled adenosine receptor activity Source: Ensembl
    3. guanyl-nucleotide exchange factor activity Source: Reactome

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: UniProtKB
    2. blood coagulation Source: Reactome
    3. calcium ion transmembrane transport Source: Ensembl
    4. cell projection organization Source: Ensembl
    5. G-protein coupled purinergic nucleotide receptor signaling pathway Source: GOC
    6. G-protein coupled receptor signaling pathway Source: UniProtKB
    7. hemostasis Source: UniProtKB
    8. negative regulation of cell differentiation Source: Ensembl
    9. negative regulation of norepinephrine secretion Source: Ensembl
    10. platelet activation Source: Reactome
    11. platelet aggregation Source: UniProtKB
    12. positive regulation of GTPase activity Source: GOC
    13. positive regulation of ion transport Source: Ensembl
    14. potassium ion transmembrane transport Source: Ensembl
    15. protein kinase B signaling Source: Ensembl
    16. regulation of calcium ion transport Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_18289. P2Y receptors.
    REACT_19231. G alpha (i) signalling events.
    REACT_20653. ADP signalling through P2Y purinoceptor 12.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    P2Y purinoceptor 12
    Short name:
    P2Y12
    Alternative name(s):
    ADP-glucose receptor
    Short name:
    ADPG-R
    P2T(AC)
    P2Y(AC)
    P2Y(cyc)
    P2Y12 platelet ADP receptor
    Short name:
    P2Y(ADP)
    SP1999
    Gene namesi
    Name:P2RY12
    Synonyms:HORK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18124. P2RY12.

    Subcellular locationi

    Cell membrane 4 Publications; Multi-pass membrane protein 4 Publications

    GO - Cellular componenti

    1. basal plasma membrane Source: Ensembl
    2. caveola Source: Ensembl
    3. external side of plasma membrane Source: Ensembl
    4. integral component of membrane Source: UniProtKB-KW
    5. intrinsic component of membrane Source: UniProtKB
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Bleeding disorder, platelet-type 8 (BDPLT8) [MIM:609821]: A condition characterized by mild to moderate mucocutaneous bleeding, and excessive bleeding after surgery or trauma. The defect is due to severe impairment of platelet response to ADP resulting in defective platelet aggregation.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti256 – 2561R → Q in BDPLT8. 1 Publication
    VAR_025383
    Natural varianti265 – 2651R → W in BDPLT8. 1 Publication
    VAR_025384

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801K → A: Abolishes ADP binding. 1 Publication
    Mutagenesisi83 – 831S → A: No effect on ADP binding. 1 Publication
    Mutagenesisi97 – 971C → A: Abolishes ADP binding. 1 Publication
    Mutagenesisi156 – 1561S → A: Slightly decreases affinity for ADP. 1 Publication
    Mutagenesisi159 – 1591N → A: Slightly decreases affinity for ADP. 1 Publication
    Mutagenesisi175 – 1751C → A: Abolishes ADP binding. 1 Publication
    Mutagenesisi256 – 2561R → A: Decreases affinity for ADP. 1 Publication
    Mutagenesisi280 – 2801K → A: Abolishes ADP binding. 2 Publications
    Mutagenesisi281 – 2811E → A: Abolishes ADP binding. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi609821. phenotype.
    Orphaneti36355. P2Y12 defect.
    240935. Resistance to clopidogrel in myocardial infarction, cerebrovascular accident, oblitering arteriopathy of the lower limbs.
    PharmGKBiPA134971947.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342P2Y purinoceptor 12PRO_0000070036Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi6 – 61N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi17 ↔ 270
    Modified residuei55 – 551PhosphoserineBy similarity
    Modified residuei57 – 571PhosphoserineBy similarity
    Disulfide bondi97 ↔ 175

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9H244.
    PRIDEiQ9H244.

    PTM databases

    PhosphoSiteiQ9H244.

    Expressioni

    Tissue specificityi

    Highly expressed in the platelets, lower levels in the brain. Lowest levels in the lung, appendix, pituitary and adrenal gland. Expressed in the spinal cord and in the fetal brain.3 Publications

    Gene expression databases

    BgeeiQ9H244.
    CleanExiHS_P2RY12.
    GenevestigatoriQ9H244.

    Organism-specific databases

    HPAiHPA013796.
    HPA014518.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000307259.

    Structurei

    Secondary structure

    1
    342
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 5027
    Helixi58 – 7417
    Helixi77 – 859
    Beta strandi86 – 883
    Helixi91 – 988
    Helixi100 – 12728
    Helixi136 – 16126
    Helixi175 – 1784
    Helixi181 – 22646
    Helixi231 – 2333
    Helixi236 – 24813
    Helixi250 – 26415
    Helixi270 – 29324
    Helixi296 – 2994
    Turni302 – 3043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T78model-A1-337[»]
    1VZ1model-A1-337[»]
    1Y9Cmodel-A1-342[»]
    4NTJX-ray2.62A2-342[»]
    4PXZX-ray2.50A2-342[»]
    4PY0X-ray3.10A2-342[»]
    ProteinModelPortaliQ9H244.
    SMRiQ9H244. Positions 16-223, 239-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727ExtracellularAdd
    BLAST
    Topological domaini51 – 6111CytoplasmicAdd
    BLAST
    Topological domaini83 – 9715ExtracellularAdd
    BLAST
    Topological domaini119 – 14224CytoplasmicAdd
    BLAST
    Topological domaini163 – 18523ExtracellularAdd
    BLAST
    Topological domaini208 – 23326CytoplasmicAdd
    BLAST
    Topological domaini260 – 27819ExtracellularAdd
    BLAST
    Topological domaini299 – 34244CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 5023Helical; Name=1Add
    BLAST
    Transmembranei62 – 8221Helical; Name=2Add
    BLAST
    Transmembranei98 – 11821Helical; Name=3Add
    BLAST
    Transmembranei143 – 16220Helical; Name=4Add
    BLAST
    Transmembranei186 – 20722Helical; Name=5Add
    BLAST
    Transmembranei234 – 25926Helical; Name=6Add
    BLAST
    Transmembranei279 – 29820Helical; Name=7Add
    BLAST

    Family & Domainsi

    Domaini

    The transmembrane domain is composed of seven transmembrane helices; most of these are not strictly perpendicular to the plane of the membrane, but are tilted and/or kinked. Agonist binding promotes a conformation change in the extracellular loops that leads to an inward movement of the transmembrane helices. Antagonists such as AZD1283 can bind to an overlapping site, but block the inward movement of the transmembrane helices (PubMed:24670650, PubMed:24784220).2 Publications

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG147554.
    HOGENOMiHOG000273884.
    HOVERGENiHBG108228.
    InParanoidiQ9H244.
    KOiK04298.
    OMAiIKVFIII.
    OrthoDBiEOG7C2R1H.
    PhylomeDBiQ9H244.
    TreeFamiTF330969.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR005394. P2Y12_rcpt.
    [Graphical view]
    PANTHERiPTHR24233:SF0. PTHR24233:SF0. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PR01569. P2Y12PRNCPTR.
    PROSITEiPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H244-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQAVDNLTSA PGNTSLCTRD YKITQVLFPL LYTVLFFVGL ITNGLAMRIF    50
    FQIRSKSNFI IFLKNTVISD LLMILTFPFK ILSDAKLGTG PLRTFVCQVT 100
    SVIFYFTMYI SISFLGLITI DRYQKTTRPF KTSNPKNLLG AKILSVVIWA 150
    FMFLLSLPNM ILTNRQPRDK NVKKCSFLKS EFGLVWHEIV NYICQVIFWI 200
    NFLIVIVCYT LITKELYRSY VRTRGVGKVP RKKVNVKVFI IIAVFFICFV 250
    PFHFARIPYT LSQTRDVFDC TAENTLFYVK ESTLWLTSLN ACLDPFIYFF 300
    LCKSFRNSLI SMLKCPNSAT SLSQDNRKKE QDGGDPNEET PM 342
    Length:342
    Mass (Da):39,439
    Last modified:March 1, 2001 - v1
    Checksum:i8553D2746C89176D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti256 – 2561R → Q in BDPLT8. 1 Publication
    VAR_025383
    Natural varianti265 – 2651R → W in BDPLT8. 1 Publication
    VAR_025384
    Natural varianti330 – 3301E → G.
    Corresponds to variant rs16846673 [ dbSNP | Ensembl ].
    VAR_049431

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF313449 mRNA. Translation: AAG48944.1.
    AF321815 mRNA. Translation: AAK00948.1.
    AB052684 mRNA. Translation: BAB60824.1.
    AF310685 Genomic DNA. Translation: AAL32292.1.
    AJ320495 mRNA. Translation: CAC87144.1.
    AB083596 Genomic DNA. Translation: BAB89309.1.
    AY136754 mRNA. Translation: AAN01280.1.
    CH471052 Genomic DNA. Translation: EAW78803.1.
    CH471052 Genomic DNA. Translation: EAW78804.1.
    BC017898 mRNA. Translation: AAH17898.1.
    CCDSiCCDS3159.1.
    RefSeqiNP_073625.1. NM_022788.4.
    NP_795345.1. NM_176876.2.
    UniGeneiHs.591281.
    Hs.665544.

    Genome annotation databases

    EnsembliENST00000302632; ENSP00000307259; ENSG00000169313.
    GeneIDi64805.
    KEGGihsa:64805.
    UCSCiuc003eyw.1. human.

    Polymorphism databases

    DMDMi21263835.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF313449 mRNA. Translation: AAG48944.1 .
    AF321815 mRNA. Translation: AAK00948.1 .
    AB052684 mRNA. Translation: BAB60824.1 .
    AF310685 Genomic DNA. Translation: AAL32292.1 .
    AJ320495 mRNA. Translation: CAC87144.1 .
    AB083596 Genomic DNA. Translation: BAB89309.1 .
    AY136754 mRNA. Translation: AAN01280.1 .
    CH471052 Genomic DNA. Translation: EAW78803.1 .
    CH471052 Genomic DNA. Translation: EAW78804.1 .
    BC017898 mRNA. Translation: AAH17898.1 .
    CCDSi CCDS3159.1.
    RefSeqi NP_073625.1. NM_022788.4.
    NP_795345.1. NM_176876.2.
    UniGenei Hs.591281.
    Hs.665544.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T78 model - A 1-337 [» ]
    1VZ1 model - A 1-337 [» ]
    1Y9C model - A 1-342 [» ]
    4NTJ X-ray 2.62 A 2-342 [» ]
    4PXZ X-ray 2.50 A 2-342 [» ]
    4PY0 X-ray 3.10 A 2-342 [» ]
    ProteinModelPortali Q9H244.
    SMRi Q9H244. Positions 16-223, 239-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000307259.

    Chemistry

    BindingDBi Q9H244.
    ChEMBLi CHEMBL2001.
    DrugBanki DB00758. Clopidogrel.
    DB01240. Epoprostenol.
    DB00208. Ticlopidine.
    DB00374. Treprostinil.
    GuidetoPHARMACOLOGYi 328.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q9H244.

    Polymorphism databases

    DMDMi 21263835.

    Proteomic databases

    PaxDbi Q9H244.
    PRIDEi Q9H244.

    Protocols and materials databases

    DNASUi 64805.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302632 ; ENSP00000307259 ; ENSG00000169313 .
    GeneIDi 64805.
    KEGGi hsa:64805.
    UCSCi uc003eyw.1. human.

    Organism-specific databases

    CTDi 64805.
    GeneCardsi GC03M151055.
    HGNCi HGNC:18124. P2RY12.
    HPAi HPA013796.
    HPA014518.
    MIMi 600515. gene.
    609821. phenotype.
    neXtProti NX_Q9H244.
    Orphaneti 36355. P2Y12 defect.
    240935. Resistance to clopidogrel in myocardial infarction, cerebrovascular accident, oblitering arteriopathy of the lower limbs.
    PharmGKBi PA134971947.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147554.
    HOGENOMi HOG000273884.
    HOVERGENi HBG108228.
    InParanoidi Q9H244.
    KOi K04298.
    OMAi IKVFIII.
    OrthoDBi EOG7C2R1H.
    PhylomeDBi Q9H244.
    TreeFami TF330969.

    Enzyme and pathway databases

    Reactomei REACT_18289. P2Y receptors.
    REACT_19231. G alpha (i) signalling events.
    REACT_20653. ADP signalling through P2Y purinoceptor 12.

    Miscellaneous databases

    GeneWikii P2Y12.
    GenomeRNAii 64805.
    NextBioi 66896.
    PROi Q9H244.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H244.
    CleanExi HS_P2RY12.
    Genevestigatori Q9H244.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR005394. P2Y12_rcpt.
    [Graphical view ]
    PANTHERi PTHR24233:SF0. PTHR24233:SF0. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR01569. P2Y12PRNCPTR.
    PROSITEi PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN BDPLT8.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Hypothalamus.
    3. "Molecular cloning of the platelet P2T(AC) ADP receptor: pharmacological comparison with another ADP receptor, the P2Y1 receptor."
      Takasaki J., Kamohara M., Saito T., Matsumoto M., Matsumoto S., Ohishi T., Soga T., Matsushime H., Furuichi K.
      Mol. Pharmacol. 60:432-439(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    4. "ADP-glucose activates a G-protein coupled receptor and inhibits smooth muscle contractions."
      Reinscheid R.K., Nothacker H.-P., Wang Z., Zeng J., Ehlert F.J., Civelli O.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning and characterization of a human platelet ADP-receptor."
      Bruess M., von Kugelgen I., Bonisch H.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    6. "Identification of G protein-coupled receptor genes from the human genome sequence."
      Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.
      FEBS Lett. 520:97-101(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    9. "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: Prostate.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH THE AGONIST AZD1283, FUNCTION, DISULFIDE BOND, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-80; SER-156; ASN-159; LYS-280 AND GLU-281.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-342 IN COMPLEX WITH THE ADP ANALOG 2-(METHYLSULFANYL)ADENOSINE 5'-(TRIHYDROGEN DIPHOSPHATE), FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF SER-83; CYS-97; CYS-175; ARG-256 AND LYS-280.
    12. "Molecular bases of defective signal transduction in the platelet P2Y12 receptor of a patient with congenital bleeding."
      Cattaneo M., Zighetti M.L., Lombardi R., Martinez C., Lecchi A., Conley P.B., Ware J., Ruggeri Z.M.
      Proc. Natl. Acad. Sci. U.S.A. 100:1978-1983(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BDPLT8 GLN-256 AND TRP-265, FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiP2Y12_HUMAN
    AccessioniPrimary (citable) accession number: Q9H244
    Secondary accession number(s): D3DNJ5, Q546J7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 128 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. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    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