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Protein

Phenylethanolamine N-methyltransferase

Gene

PNMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    Pathway: (R)-adrenaline biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-adrenaline from (R)-noradrenaline.
    Proteins known to be involved in this subpathway in this organism are:
    1. Phenylethanolamine N-methyltransferase (PNMT)
    This subpathway is part of the pathway (R)-adrenaline biosynthesis, which is itself part of Catecholamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-adrenaline from (R)-noradrenaline, the pathway (R)-adrenaline biosynthesis and in Catecholamine biosynthesis.

    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

    • phenylethanolamine N-methyltransferase activity Source: ProtInc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Catecholamine biosynthesis

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06868-MONOMER.
    BRENDAi2.1.1.28. 2681.
    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 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9160. PNMT.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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.

    Polymorphism and mutation databases

    DMDMi130375.

    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

    BgeeiP11086.
    CleanExiHS_PNMT.
    ExpressionAtlasiP11086. baseline and differential.
    GenevisibleiP11086. HS.

    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
    Helixi17 – 259Combined sources
    Helixi27 – 293Combined sources
    Helixi32 – 409Combined sources
    Turni42 – 454Combined sources
    Helixi53 – 6614Combined sources
    Beta strandi73 – 797Combined sources
    Helixi85 – 873Combined sources
    Helixi90 – 923Combined sources
    Beta strandi95 – 1006Combined sources
    Helixi104 – 11411Combined sources
    Helixi124 – 13411Combined sources
    Helixi140 – 15011Combined sources
    Beta strandi151 – 1555Combined sources
    Beta strandi161 – 1633Combined sources
    Beta strandi173 – 18210Combined sources
    Turni184 – 1863Combined sources
    Helixi191 – 20212Combined sources
    Beta strandi205 – 21814Combined sources
    Beta strandi221 – 2244Combined sources
    Beta strandi227 – 2304Combined sources
    Helixi236 – 24611Combined sources
    Beta strandi248 – 25710Combined sources
    Helixi260 – 2623Combined sources
    Beta strandi265 – 2673Combined sources
    Beta strandi271 – 2799Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4MIKX-ray1.95A/B1-282[»]
    4MQ4X-ray2.20A/B1-282[»]
    ProteinModelPortaliP11086.
    SMRiP11086. Positions 16-280.
    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.
    GeneTreeiENSGT00390000011708.
    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.
    [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

            10         20         30         40         50
    MSGADRSPNA GAAPDSAPGQ AAVASAYQRF EPRAYLRNNY APPRGDLCNP
    60 70 80 90 100
    NGVGPWKLRC LAQTFATGEV SGRTLIDIGS GPTVYQLLSA CSHFEDITMT
    110 120 130 140 150
    DFLEVNRQEL GRWLQEEPGA FNWSMYSQHA CLIEGKGECW QDKERQLRAR
    160 170 180 190 200
    VKRVLPIDVH QPQPLGAGSP APLPADALVS AFCLEAVSPD LASFQRALDH
    210 220 230 240 250
    ITTLLRPGGH LLLIGALEES WYLAGEARLT VVPVSEEEVR EALVRSGYKV
    260 270 280
    RDLRTYIMPA HLQTGVDDVK GVFFAWAQKV GL
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4MIKX-ray1.95A/B1-282[»]
    4MQ4X-ray2.20A/B1-282[»]
    ProteinModelPortaliP11086.
    SMRiP11086. Positions 16-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111410. 2 interactions.
    STRINGi9606.ENSP00000269582.

    Chemistry

    BindingDBiP11086.
    ChEMBLiCHEMBL4617.
    GuidetoPHARMACOLOGYi2496.

    PTM databases

    PhosphoSiteiP11086.

    Polymorphism and mutation databases

    DMDMi130375.

    Proteomic databases

    PRIDEiP11086.

    Protocols and materials databases

    DNASUi5409.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi5409.
    GeneCardsiGC17P037824.
    HGNCiHGNC:9160. PNMT.
    HPAiCAB017029.
    HPA043412.
    HPA051005.
    MIMi171190. gene.
    neXtProtiNX_P11086.
    PharmGKBiPA274.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG78422.
    GeneTreeiENSGT00390000011708.
    HOGENOMiHOG000013229.
    HOVERGENiHBG000797.
    InParanoidiP11086.
    KOiK00553.
    OMAiEESWYLA.
    PhylomeDBiP11086.
    TreeFamiTF313114.

    Enzyme and pathway databases

    UniPathwayiUPA00749; UER00736.
    BioCyciMetaCyc:HS06868-MONOMER.
    BRENDAi2.1.1.28. 2681.
    ReactomeiREACT_15551. Catecholamine biosynthesis.

    Miscellaneous databases

    EvolutionaryTraceiP11086.
    GenomeRNAii5409.
    NextBioi20943.
    PROiP11086.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP11086.
    CleanExiHS_PNMT.
    ExpressionAtlasiP11086. baseline and differential.
    GenevisibleiP11086. HS.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025820. NNMT/PNMT/TEMT_CS.
    IPR000940. NNMT_TEMT_trans.
    IPR029063. SAM-dependent_MTases.
    [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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 152 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.