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O95050

- INMT_HUMAN

UniProt

O95050 - INMT_HUMAN

Protein

Indolethylamine N-methyltransferase

Gene

INMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds By similarity. Catalyzes the N-methylation of tryptamine and structurally related compounds.By similarity1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.1 Publication
    S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium.1 Publication

    Kineticsi

    1. KM=2.9 mM for tryptamine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201S-adenosyl-L-methionine
    Binding sitei25 – 251S-adenosyl-L-methionine
    Binding sitei63 – 631S-adenosyl-L-methionine; via carbonyl oxygen
    Binding sitei69 – 691S-adenosyl-L-methionine
    Binding sitei90 – 901S-adenosyl-L-methionine
    Binding sitei163 – 1631S-adenosyl-L-methionine; via carbonyl oxygen

    GO - Molecular functioni

    1. amine N-methyltransferase activity Source: UniProtKB
    2. thioether S-methyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. amine metabolic process Source: UniProtKB
    2. methylation Source: UniProtKB
    3. response to toxic substance Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Detoxification

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00305-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Indolethylamine N-methyltransferase (EC:2.1.1.49, EC:2.1.1.96)
    Short name:
    Indolamine N-methyltransferase
    Alternative name(s):
    Aromatic alkylamine N-methyltransferase
    Short name:
    Amine N-methyltransferase
    Short name:
    Arylamine N-methyltransferase
    Thioether S-methyltransferase
    Short name:
    TEMT
    Gene namesi
    Name:INMT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6069. INMT.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA403.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 263263Indolethylamine N-methyltransferasePRO_0000159712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131N6-succinyllysineBy similarity
    Modified residuei96 – 961N6-succinyllysineBy similarity

    Proteomic databases

    PaxDbiO95050.
    PRIDEiO95050.

    PTM databases

    PhosphoSiteiO95050.

    Expressioni

    Tissue specificityi

    Widely expressed. The highest levels were in thyroid, adrenal gland, adult and fetal lung. Intermediate levels in heart, placenta, skeletal muscle, testis, small intestine, pancreas, stomach, spinal cord, lymph node and trachea. Very low levels in adult and fetal kidney and liver, in adult spleen, thymus, ovary, colon and bone marrow. Not expressed in peripheral blood leukocytes and brain.1 Publication

    Gene expression databases

    ArrayExpressiO95050.
    BgeeiO95050.
    CleanExiHS_INMT.
    GenevestigatoriO95050.

    Organism-specific databases

    HPAiHPA055180.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000013222.

    Structurei

    Secondary structure

    1
    263
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 147
    Helixi17 – 248
    Helixi33 – 4917
    Beta strandi56 – 638
    Helixi69 – 713
    Helixi74 – 763
    Beta strandi78 – 869
    Helixi88 – 9912
    Helixi108 – 11710
    Helixi121 – 1233
    Helixi124 – 13411
    Beta strandi135 – 1406
    Beta strandi145 – 1473
    Turni148 – 1514
    Beta strandi157 – 1648
    Helixi166 – 1694
    Helixi173 – 18412
    Beta strandi187 – 20014
    Beta strandi203 – 2064
    Beta strandi209 – 2124
    Helixi218 – 22710
    Beta strandi230 – 2389
    Turni244 – 2463
    Beta strandi252 – 2598

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A14X-ray1.70A1-263[»]
    ProteinModelPortaliO95050.
    SMRiO95050. Positions 5-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95050.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 873S-adenosyl-L-methionine binding
    Regioni142 – 1432S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG71857.
    HOGENOMiHOG000013229.
    HOVERGENiHBG000797.
    InParanoidiO95050.
    KOiK00562.
    OMAiAMECACC.
    OrthoDBiEOG7673B9.
    PhylomeDBiO95050.
    TreeFamiTF313114.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025817. Amine_MeTrfase.
    IPR025820. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95050-1) [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

    MKGGFTGGDE YQKHFLPRDY LATYYSFDGS PSPEAEMLKF NLECLHKTFG    50
    PGGLQGDTLI DIGSGPTIYQ VLAACDSFQD ITLSDFTDRN REELEKWLKK 100
    EPGAYDWTPA VKFACELEGN SGRWEEKEEK LRAAVKRVLK CDVHLGNPLA 150
    PAVLPLADCV LTLLAMECAC CSLDAYRAAL CNLASLLKPG GHLVTTVTLR 200
    LPSYMVGKRE FSCVALEKEE VEQAVLDAGF DIEQLLHSPQ SYSVTNAANN 250
    GVCFIVARKK PGP 263
    Length:263
    Mass (Da):28,891
    Last modified:November 13, 2007 - v3
    Checksum:i12B3AC66597E70A3
    GO
    Isoform 2 (identifier: O95050-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-52: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:262
    Mass (Da):28,834
    Checksum:i0DEF8C52DEFE814B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751C → F in AK313832. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281D → N.1 Publication
    Corresponds to variant rs4723010 [ dbSNP | Ensembl ].
    VAR_036991
    Natural varianti205 – 2051M → V.1 Publication
    Corresponds to variant rs2302339 [ dbSNP | Ensembl ].
    VAR_011616
    Natural varianti214 – 2141V → M.
    Corresponds to variant rs56800285 [ dbSNP | Ensembl ].
    VAR_061373
    Natural varianti219 – 2191E → G.3 Publications
    Corresponds to variant rs2302340 [ dbSNP | Ensembl ].
    VAR_011617
    Natural varianti246 – 2461N → S.
    Corresponds to variant rs6970210 [ dbSNP | Ensembl ].
    VAR_036992
    Natural varianti254 – 2541F → C.1 Publication
    Corresponds to variant rs4720015 [ dbSNP | Ensembl ].
    VAR_036993
    Natural varianti258 – 2581R → H.
    Corresponds to variant rs6970605 [ dbSNP | Ensembl ].
    VAR_036994

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei52 – 521Missing in isoform 2. 1 PublicationVSP_045922

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF128846 mRNA. Translation: AAF18304.1.
    AF128847 mRNA. Translation: AAF18305.1.
    AF128848 Genomic DNA. Translation: AAF18306.1.
    AK313832 mRNA. No translation available.
    AC004976 Genomic DNA. No translation available.
    AC006022 Genomic DNA. Translation: AAD04723.1.
    BC033813 mRNA. Translation: AAH33813.1.
    BC106902 mRNA. Translation: AAI06903.1.
    BC106903 mRNA. Translation: AAI06904.1.
    AB041362 Genomic DNA. Translation: BAA94451.1.
    CCDSiCCDS5430.1. [O95050-1]
    CCDS56479.1. [O95050-2]
    RefSeqiNP_001186148.1. NM_001199219.1. [O95050-2]
    NP_006765.4. NM_006774.4. [O95050-1]
    UniGeneiHs.632629.

    Genome annotation databases

    EnsembliENST00000013222; ENSP00000013222; ENSG00000241644. [O95050-1]
    ENST00000409539; ENSP00000386961; ENSG00000241644. [O95050-2]
    GeneIDi11185.
    KEGGihsa:11185.
    UCSCiuc003tbs.1. human. [O95050-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF128846 mRNA. Translation: AAF18304.1 .
    AF128847 mRNA. Translation: AAF18305.1 .
    AF128848 Genomic DNA. Translation: AAF18306.1 .
    AK313832 mRNA. No translation available.
    AC004976 Genomic DNA. No translation available.
    AC006022 Genomic DNA. Translation: AAD04723.1 .
    BC033813 mRNA. Translation: AAH33813.1 .
    BC106902 mRNA. Translation: AAI06903.1 .
    BC106903 mRNA. Translation: AAI06904.1 .
    AB041362 Genomic DNA. Translation: BAA94451.1 .
    CCDSi CCDS5430.1. [O95050-1 ]
    CCDS56479.1. [O95050-2 ]
    RefSeqi NP_001186148.1. NM_001199219.1. [O95050-2 ]
    NP_006765.4. NM_006774.4. [O95050-1 ]
    UniGenei Hs.632629.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A14 X-ray 1.70 A 1-263 [» ]
    ProteinModelPortali O95050.
    SMRi O95050. Positions 5-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000013222.

    Chemistry

    BindingDBi O95050.
    ChEMBLi CHEMBL2131.

    PTM databases

    PhosphoSitei O95050.

    Proteomic databases

    PaxDbi O95050.
    PRIDEi O95050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000013222 ; ENSP00000013222 ; ENSG00000241644 . [O95050-1 ]
    ENST00000409539 ; ENSP00000386961 ; ENSG00000241644 . [O95050-2 ]
    GeneIDi 11185.
    KEGGi hsa:11185.
    UCSCi uc003tbs.1. human. [O95050-1 ]

    Organism-specific databases

    CTDi 11185.
    GeneCardsi GC07P030737.
    HGNCi HGNC:6069. INMT.
    HPAi HPA055180.
    MIMi 604854. gene.
    neXtProti NX_O95050.
    PharmGKBi PA403.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71857.
    HOGENOMi HOG000013229.
    HOVERGENi HBG000797.
    InParanoidi O95050.
    KOi K00562.
    OMAi AMECACC.
    OrthoDBi EOG7673B9.
    PhylomeDBi O95050.
    TreeFami TF313114.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00305-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O95050.
    GenomeRNAii 11185.
    NextBioi 42567.
    PROi O95050.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95050.
    Bgeei O95050.
    CleanExi HS_INMT.
    Genevestigatori O95050.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025817. Amine_MeTrfase.
    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. "Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization."
      Thompson M.A., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M.
      Genomics 61:285-297(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS VAL-205 AND GLY-219, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Placenta and Skeletal muscle.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS GLY-219 AND CYS-254.
      Tissue: Lung.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] (ISOFORM 1), VARIANTS ASN-28 AND GLY-219.
      Tissue: Lung and Spleen.
    5. "Human-specific amino acid changes found in 103 protein-coding genes."
      Kitano T., Liu Y.-H., Ueda S., Saitou N.
      Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
    6. "The crystal structure of human indolethylamine N-methyltransferase in complex with SAH."
      Structural genomics consortium (SGC)
      Submitted (JUN-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

    Entry informationi

    Entry nameiINMT_HUMAN
    AccessioniPrimary (citable) accession number: O95050
    Secondary accession number(s): B8ZZ69
    , Q3KP49, Q9P1Y2, Q9UBY4, Q9UHQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 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 7
      Human chromosome 7: 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