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O95050

- INMT_HUMAN

UniProt

O95050 - INMT_HUMAN

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Protein
Indolethylamine N-methyltransferase
Gene
INMT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA403.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Indolethylamine N-methyltransferase
PRO_0000159712Add
BLAST

Amino acid modifications

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

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.

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

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.
VSP_045922

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751C → F in AK313832. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 119 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

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