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P11086

- PNMT_HUMAN

UniProt

P11086 - PNMT_HUMAN

Protein

Phenylethanolamine N-methyltransferase

Gene

PNMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Converts noradrenaline to adrenaline.

    Catalytic activityi

    S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine.

    Kineticsi

    1. KM=99 µM for phenylethanolamine1 Publication
    2. KM=3.4 µM for S-adenosyl-L-methionine1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351S-adenosyl-L-methionine
    Binding sitei40 – 401S-adenosyl-L-methionine
    Binding sitei85 – 851S-adenosyl-L-methionine
    Binding sitei101 – 1011S-adenosyl-L-methionine
    Binding sitei106 – 1061S-adenosyl-L-methionine
    Binding sitei181 – 1811S-adenosyl-L-methionine; via carbonyl oxygen
    Binding sitei219 – 2191Substrate

    GO - Molecular functioni

    1. phenylethanolamine N-methyltransferase activity Source: ProtInc

    GO - Biological processi

    1. catecholamine biosynthetic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. epinephrine biosynthetic process Source: UniProtKB-UniPathway
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Catecholamine biosynthesis

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06868-MONOMER.
    ReactomeiREACT_15551. Catecholamine biosynthesis.
    UniPathwayiUPA00749; UER00736.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylethanolamine N-methyltransferase (EC:2.1.1.28)
    Short name:
    PNMTase
    Alternative name(s):
    Noradrenaline N-methyltransferase
    Gene namesi
    Name:PNMT
    Synonyms:PENT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9160. PNMT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi35 – 351Y → F: Strongly increases KM for substrate and S-adenosyl-L-methionine. 1 Publication
    Mutagenesisi185 – 1851E → A or Q: Strongly reduced enzyme activity. Increases affinity for S-adenosyl-L-methionine. 1 Publication
    Mutagenesisi185 – 1851E → D: Strongly reduced enzyme activity. Decreases affinity for substrate and S-adenosyl-L-methionine 3-fold. 1 Publication
    Mutagenesisi219 – 2191E → A: Reduced enzyme activity. Decreases affinity for substrate 6-fold. Decreases affinity for S-adenosyl-L-methionine 2-fold. 1 Publication
    Mutagenesisi267 – 2671D → A or N: Strongly reduced enzyme activity. Decreases affinity for substrate 200-fold. Decreases affinity for S-adenosyl-L-methionine 3-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA274.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282Phenylethanolamine N-methyltransferasePRO_0000159709Add
    BLAST

    Proteomic databases

    PRIDEiP11086.

    PTM databases

    PhosphoSiteiP11086.

    Expressioni

    Gene expression databases

    ArrayExpressiP11086.
    BgeeiP11086.
    CleanExiHS_PNMT.
    GenevestigatoriP11086.

    Organism-specific databases

    HPAiCAB017029.
    HPA043412.
    HPA051005.

    Interactioni

    Protein-protein interaction databases

    BioGridi111410. 2 interactions.
    STRINGi9606.ENSP00000269582.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 269
    Helixi27 – 293
    Helixi32 – 409
    Turni42 – 454
    Helixi53 – 6614
    Beta strandi73 – 797
    Helixi85 – 873
    Helixi90 – 934
    Beta strandi95 – 1006
    Helixi104 – 11411
    Helixi124 – 13411
    Helixi140 – 15011
    Beta strandi151 – 1555
    Beta strandi161 – 1633
    Beta strandi173 – 18210
    Helixi184 – 1874
    Helixi191 – 20212
    Beta strandi205 – 21814
    Beta strandi221 – 2244
    Beta strandi227 – 2304
    Helixi236 – 24510
    Beta strandi248 – 25710
    Helixi260 – 2623
    Beta strandi265 – 2673
    Beta strandi271 – 2799

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HNNX-ray2.40A/B1-282[»]
    1N7IX-ray2.80A/B1-282[»]
    1N7JX-ray2.70A/B1-282[»]
    1YZ3X-ray2.40A/B1-282[»]
    2AN3X-ray2.20A/B1-282[»]
    2AN4X-ray2.20A/B1-282[»]
    2AN5X-ray2.50A/B1-282[»]
    2G70X-ray2.40A/B1-282[»]
    2G71X-ray2.20A/B1-282[»]
    2G72X-ray2.00A/B1-282[»]
    2G8NX-ray2.15A/B1-282[»]
    2OBFX-ray2.30A/B1-282[»]
    2ONYX-ray2.60A/B1-282[»]
    2ONZX-ray2.80A/B1-282[»]
    2OPBX-ray2.80A/B1-282[»]
    3HCAX-ray2.40A/B1-282[»]
    3HCBX-ray2.40A/B1-282[»]
    3HCCX-ray2.30A/B1-282[»]
    3HCDX-ray2.39A/B1-282[»]
    3HCEX-ray2.85A/B1-282[»]
    3HCFX-ray2.70A/B1-282[»]
    3KPJX-ray2.50A/B1-282[»]
    3KPUX-ray2.40A/B1-282[»]
    3KPVX-ray2.40A/B1-282[»]
    3KPWX-ray2.40A/B1-282[»]
    3KPYX-ray2.40A/B1-282[»]
    3KQMX-ray2.40A/B1-282[»]
    3KQOX-ray2.40A/B1-282[»]
    3KQPX-ray2.40A/B1-282[»]
    3KQQX-ray2.50A/B1-282[»]
    3KQSX-ray2.00A/B1-282[»]
    3KQTX-ray2.40A/B1-282[»]
    3KQVX-ray2.30A/B1-282[»]
    3KQWX-ray2.49A/B1-282[»]
    3KQYX-ray2.20A/B1-282[»]
    3KR0X-ray2.60A/B1-282[»]
    3KR1X-ray2.30A/B1-282[»]
    3KR2X-ray2.30A/B1-282[»]
    4DM3X-ray2.40A/B1-282[»]
    ProteinModelPortaliP11086.
    SMRiP11086. Positions 14-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11086.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 802S-adenosyl-L-methionine binding
    Regioni158 – 1592S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG78422.
    HOGENOMiHOG000013229.
    HOVERGENiHBG000797.
    InParanoidiP11086.
    KOiK00553.
    OMAiEESWYLA.
    PhylomeDBiP11086.
    TreeFamiTF313114.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025820. NNMT/PNMT/TEMT_CS.
    IPR000940. NNMT_TEMT_trans.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10867. PTHR10867. 1 hit.
    PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000384. PNMTase. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
    PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P11086-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGADRSPNA GAAPDSAPGQ AAVASAYQRF EPRAYLRNNY APPRGDLCNP    50
    NGVGPWKLRC LAQTFATGEV SGRTLIDIGS GPTVYQLLSA CSHFEDITMT 100
    DFLEVNRQEL GRWLQEEPGA FNWSMYSQHA CLIEGKGECW QDKERQLRAR 150
    VKRVLPIDVH QPQPLGAGSP APLPADALVS AFCLEAVSPD LASFQRALDH 200
    ITTLLRPGGH LLLIGALEES WYLAGEARLT VVPVSEEEVR EALVRSGYKV 250
    RDLRTYIMPA HLQTGVDDVK GVFFAWAQKV GL 282
    Length:282
    Mass (Da):30,855
    Last modified:July 1, 1989 - v1
    Checksum:i56F3A9981D9ABF4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1702SP → AQ in AAA60131. (PubMed:2835776)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91N → S.1 Publication
    Corresponds to variant rs11569781 [ dbSNP | Ensembl ].
    VAR_029351
    Natural varianti98 – 981T → A Lower activity levels than wild-type. 1 Publication
    Corresponds to variant rs36060376 [ dbSNP | Ensembl ].
    VAR_036829
    Natural varianti112 – 1121R → C.1 Publication
    Corresponds to variant rs34530498 [ dbSNP | Ensembl ].
    VAR_036830
    Natural varianti175 – 1751A → T.1 Publication
    Corresponds to variant rs34341496 [ dbSNP | Ensembl ].
    VAR_036831
    Natural varianti188 – 1881S → C.
    Corresponds to variant rs5639 [ dbSNP | Ensembl ].
    VAR_037611
    Natural varianti211 – 2111L → H.
    Corresponds to variant rs5640 [ dbSNP | Ensembl ].
    VAR_037612
    Natural varianti217 – 2171L → Q.
    Corresponds to variant rs5641 [ dbSNP | Ensembl ].
    VAR_037613
    Natural varianti254 – 2541R → H.
    Corresponds to variant rs5642 [ dbSNP | Ensembl ].
    VAR_037614
    Natural varianti276 – 2761W → R.
    Corresponds to variant rs5643 [ dbSNP | Ensembl ].
    VAR_024547

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03727 mRNA. Translation: AAA60130.1.
    X52730 Genomic DNA. Translation: CAA36944.1.
    J03280 Genomic DNA. Translation: AAA60131.1.
    BC037246 mRNA. Translation: AAH37246.1.
    CCDSiCCDS11343.1.
    PIRiA28171.
    RefSeqiNP_002677.1. NM_002686.4.
    UniGeneiHs.1892.

    Genome annotation databases

    EnsembliENST00000269582; ENSP00000269582; ENSG00000141744.
    GeneIDi5409.
    KEGGihsa:5409.
    UCSCiuc002hsi.2. human.

    Polymorphism databases

    DMDMi130375.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03727 mRNA. Translation: AAA60130.1 .
    X52730 Genomic DNA. Translation: CAA36944.1 .
    J03280 Genomic DNA. Translation: AAA60131.1 .
    BC037246 mRNA. Translation: AAH37246.1 .
    CCDSi CCDS11343.1.
    PIRi A28171.
    RefSeqi NP_002677.1. NM_002686.4.
    UniGenei Hs.1892.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HNN X-ray 2.40 A/B 1-282 [» ]
    1N7I X-ray 2.80 A/B 1-282 [» ]
    1N7J X-ray 2.70 A/B 1-282 [» ]
    1YZ3 X-ray 2.40 A/B 1-282 [» ]
    2AN3 X-ray 2.20 A/B 1-282 [» ]
    2AN4 X-ray 2.20 A/B 1-282 [» ]
    2AN5 X-ray 2.50 A/B 1-282 [» ]
    2G70 X-ray 2.40 A/B 1-282 [» ]
    2G71 X-ray 2.20 A/B 1-282 [» ]
    2G72 X-ray 2.00 A/B 1-282 [» ]
    2G8N X-ray 2.15 A/B 1-282 [» ]
    2OBF X-ray 2.30 A/B 1-282 [» ]
    2ONY X-ray 2.60 A/B 1-282 [» ]
    2ONZ X-ray 2.80 A/B 1-282 [» ]
    2OPB X-ray 2.80 A/B 1-282 [» ]
    3HCA X-ray 2.40 A/B 1-282 [» ]
    3HCB X-ray 2.40 A/B 1-282 [» ]
    3HCC X-ray 2.30 A/B 1-282 [» ]
    3HCD X-ray 2.39 A/B 1-282 [» ]
    3HCE X-ray 2.85 A/B 1-282 [» ]
    3HCF X-ray 2.70 A/B 1-282 [» ]
    3KPJ X-ray 2.50 A/B 1-282 [» ]
    3KPU X-ray 2.40 A/B 1-282 [» ]
    3KPV X-ray 2.40 A/B 1-282 [» ]
    3KPW X-ray 2.40 A/B 1-282 [» ]
    3KPY X-ray 2.40 A/B 1-282 [» ]
    3KQM X-ray 2.40 A/B 1-282 [» ]
    3KQO X-ray 2.40 A/B 1-282 [» ]
    3KQP X-ray 2.40 A/B 1-282 [» ]
    3KQQ X-ray 2.50 A/B 1-282 [» ]
    3KQS X-ray 2.00 A/B 1-282 [» ]
    3KQT X-ray 2.40 A/B 1-282 [» ]
    3KQV X-ray 2.30 A/B 1-282 [» ]
    3KQW X-ray 2.49 A/B 1-282 [» ]
    3KQY X-ray 2.20 A/B 1-282 [» ]
    3KR0 X-ray 2.60 A/B 1-282 [» ]
    3KR1 X-ray 2.30 A/B 1-282 [» ]
    3KR2 X-ray 2.30 A/B 1-282 [» ]
    4DM3 X-ray 2.40 A/B 1-282 [» ]
    ProteinModelPortali P11086.
    SMRi P11086. Positions 14-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111410. 2 interactions.
    STRINGi 9606.ENSP00000269582.

    Chemistry

    BindingDBi P11086.
    ChEMBLi CHEMBL4617.
    GuidetoPHARMACOLOGYi 2496.

    PTM databases

    PhosphoSitei P11086.

    Polymorphism databases

    DMDMi 130375.

    Proteomic databases

    PRIDEi P11086.

    Protocols and materials databases

    DNASUi 5409.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269582 ; ENSP00000269582 ; ENSG00000141744 .
    GeneIDi 5409.
    KEGGi hsa:5409.
    UCSCi uc002hsi.2. human.

    Organism-specific databases

    CTDi 5409.
    GeneCardsi GC17P037824.
    HGNCi HGNC:9160. PNMT.
    HPAi CAB017029.
    HPA043412.
    HPA051005.
    MIMi 171190. gene.
    neXtProti NX_P11086.
    PharmGKBi PA274.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG78422.
    HOGENOMi HOG000013229.
    HOVERGENi HBG000797.
    InParanoidi P11086.
    KOi K00553.
    OMAi EESWYLA.
    PhylomeDBi P11086.
    TreeFami TF313114.

    Enzyme and pathway databases

    UniPathwayi UPA00749 ; UER00736 .
    BioCyci MetaCyc:HS06868-MONOMER.
    Reactomei REACT_15551. Catecholamine biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P11086.
    GenomeRNAii 5409.
    NextBioi 20943.
    PROi P11086.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11086.
    Bgeei P11086.
    CleanExi HS_PNMT.
    Genevestigatori P11086.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025820. NNMT/PNMT/TEMT_CS.
    IPR000940. NNMT_TEMT_trans.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10867. PTHR10867. 1 hit.
    Pfami PF01234. NNMT_PNMT_TEMT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000384. PNMTase. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS01100. NNMT_PNMT_TEMT. 1 hit.
    PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of cDNA and chromosomal assignment of the gene for human phenylethanolamine N-methyltransferase, the enzyme for epinephrine biosynthesis."
      Kaneda N., Ichinose H., Kobayashi K., Oka K., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T.
      J. Biol. Chem. 263:7672-7677(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure of human phenylethanolamine N-methyltransferase gene: existence of two types of mRNA with different transcription initiation sites."
      Sasaoka T., Kaneda N., Kurosawa Y., Fujita K., Nagatsu T.
      Neurochem. Int. 15:555-565(1989)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    3. "Transgenic mice express the human phenylethanolamine N-methyltransferase gene in adrenal medulla and retina."
      Baetge E.E., Behringer R.R., Messing A., Brinster R.L., Palmiter R.D.
      Proc. Natl. Acad. Sci. U.S.A. 85:3648-3652(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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: Brain, Lung and Testis.
    5. "Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT."
      Martin J.L., Begun J., McLeish M.J., Caine J.M., Grunewald G.L.
      Structure 9:977-985(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND SYNTHETIC INHIBITOR.
    6. "Mode of binding of methyl acceptor substrates to the adrenaline-synthesizing enzyme phenylethanolamine N-methyltransferase: implications for catalysis."
      Gee C.L., Tyndall J.D.A., Grunewald G.L., Wu Q., McLeish M.J., Martin J.L.
      Biochemistry 44:16875-16885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS AND S-ADENOSYL-L-HOMOCYSTEINE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-35; GLU-185; GLU-219 AND ASP-267.
    7. "Comparison of the binding of 3-fluoromethyl-7-sulfonyl-1,2,3,4-tetrahydroisoquinolines with their isosteric sulfonamides to the active site of phenylethanolamine N-methyltransferase."
      Grunewald G.L., Seim M.R., Regier R.C., Martin J.L., Gee C.L., Drinkwater N., Criscione K.R.
      J. Med. Chem. 49:5424-5433(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
    8. "Enzyme adaptation to inhibitor binding: a cryptic binding site in phenylethanolamine N-methyltransferase."
      Gee C.L., Drinkwater N., Tyndall J.D.A., Grunewald G.L., Wu Q., McLeish M.J., Martin J.L.
      J. Med. Chem. 50:4845-4853(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH SYNTHETIC INHIBITOR.
    9. "Human phenylethanolamine N-methyltransferase pharmacogenomics: gene re-sequencing and functional genomics."
      Ji Y., Salavaggione O.E., Wang L., Adjei A.A., Eckloff B., Wieben E.D., Weinshilboum R.M.
      J. Neurochem. 95:1766-1776(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SER-9; ALA-98; CYS-112 AND THR-175, CHARACTERIZATION OF VARIANT ALA-98.

    Entry informationi

    Entry nameiPNMT_HUMAN
    AccessioniPrimary (citable) accession number: P11086
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 145 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 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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