ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O95050


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name INMT_HUMAN
Primary accession number O95050
Secondary accession numbers Q3KP49 Q9P1Y2 Q9UBY4 Q9UHQ0
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on November 13, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 66)
Name and origin of the protein
Protein name Indolethylamine N-methyltransferase
Synonyms Indolamine N-methyltransferase
EC 2.1.1.49
Aromatic alkylamine N-methyltransferase
Arylamine N-methyltransferase
Amine N-methyltransferase
Gene name
Name: INMT
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT GLY-219.
TISSUE=Placenta, and Skeletal muscle;
DOI=10.1006/geno.1999.5960; PubMed=10552930 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson M.A., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M.;
"Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization.";
Genomics 61:285-297(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-28 AND GLY-219.
TISSUE=Lung, and Spleen;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
Kitano T., Kobayakawa H., Saitou N.;
"Silver project.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[5]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
Structural genomics consortium (SGC);
"The crystal structure of human indolethylamine N-methyltransferase in complex with SAH.";
Submitted (JUN-2005) to the PDB data bank.
Comments
  • FUNCTION: Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential).
  • CATALYTIC ACTIVITY: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
  • SUBUNIT: Monomer (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity).
  • TISSUE SPECIFICITY: 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.
  • SIMILARITY: Belongs to the NNMT/PNMT/TEMT family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF128846; AAF18304.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF128847; AAF18305.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF128848; AAF18306.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006022; AAD04723.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033813; AAH33813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106902; AAI06903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106903; AAI06904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB041362; BAA94451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006765.4; -.
UniGene Hs.632629
3D structure databases
PDB
2A14; X-ray; 1.70 A; A=1-263.[ExPASy / RCSB / EBI]
PDBsum 2A14; -.
ModBase O95050.
Enzyme and pathway databases
BioCyc MetaCyc:ENSG00000011177-MON; -.
Organism-specific databases
HGNC HGNC:6069; INMT.
GenAtlas INMT.
MIM 604854; gene. [NCBI / EBI]
PharmGKB PA403; -.
GeneCards O95050.
Gene expression databases
ArrayExpress O95050; -.
CleanEx HS_INMT; -.
GermOnline ENSG00000011177; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0030748; Molecular function: amine N-methyltransferase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR000940; NNMT_TEMT_trans.
Graphical view of domain structure.
PANTHER PTHR10867; NNMT_TEMT_trans; 1.
Pfam PF01234; NNMT_PNMT_TEMT; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000384; PNMTase; 1.
PROSITE PS01100; NNMT_PNMT_TEMT; 1.
ProtoNet O95050.
Genome annotation databases
Ensembl ENSG00000011177; Homo sapiens. [Contig view]
GeneID 11185; -.
KEGG hsa:11185; -.
Phylogenomic databases
HOGENOM O95050; -.
HOVERGEN O95050; -.
Other
NextBio 42567; -.
SOURCE INMT; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Methyltransferase; Polymorphism; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   263  263     Indolethylamine N-methyltransferase. PRO_0000159712
REGION   85    87  3     S-adenosyl-L-methionine binding. 
REGION   142   143  2     S-adenosyl-L-methionine binding. 
BINDING   20    20        S-adenosyl-L-methionine. 
BINDING   25    25        S-adenosyl-L-methionine. 
BINDING   63    63        S-adenosyl-L-methionine; via carbonyl oxygen. 
BINDING   69    69        S-adenosyl-L-methionine. 
BINDING   90    90        S-adenosyl-L-methionine. 
BINDING   163   163        S-adenosyl-L-methionine; via carbonyl oxygen. 
VARIANT   28    28  1     D -> N (in dbSNP:rs4723010 [NCBI]). VAR_036991 [3D]
VARIANT   205   205  1     M -> V (in dbSNP:rs2302339 [NCBI]). VAR_011616 [3D]
VARIANT   219   219  1     E -> G (in dbSNP:rs2302340 [NCBI]). VAR_011617 [3D]
VARIANT   246   246  1     N -> S (in dbSNP:rs6970210 [NCBI]). VAR_036992 [3D]
VARIANT   254   254  1     F -> C (in dbSNP:rs4720015 [NCBI]). VAR_036993 [3D]
VARIANT   258   258  1     R -> H (in dbSNP:rs6970605 [NCBI]). VAR_036994 [3D]
HELIX   8    14  7      
HELIX   17    24  8      
HELIX   33    49  17      
STRAND   56    63  8      
HELIX   69    71  3      
HELIX   74    76  3      
STRAND   78    86  9      
HELIX   88    99  12      
HELIX   108   117  10      
HELIX   121   123  3      
HELIX   124   134  11      
STRAND   135   140  6      
STRAND   145   147  3      
TURN   148   151  4      
STRAND   157   164  8      
HELIX   166   169  4      
HELIX   173   184  12      
STRAND   187   200  14      
STRAND   203   206  4      
STRAND   209   212  4      
HELIX   218   227  10      
STRAND   230   238  9      
TURN   244   246  3      
STRAND   252   259  8      
Sequence information
Length: 263 AA [This is the length of the unprocessed precursor] Molecular weight: 28891 Da [This is the MW of the unprocessed precursor] CRC64: 12B3AC66597E70A3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKGGFTGGDE YQKHFLPRDY LATYYSFDGS PSPEAEMLKF NLECLHKTFG PGGLQGDTLI 

        70         80         90        100        110        120 
DIGSGPTIYQ VLAACDSFQD ITLSDFTDRN REELEKWLKK EPGAYDWTPA VKFACELEGN 

       130        140        150        160        170        180 
SGRWEEKEEK LRAAVKRVLK CDVHLGNPLA PAVLPLADCV LTLLAMECAC CSLDAYRAAL 

       190        200        210        220        230        240 
CNLASLLKPG GHLVTTVTLR LPSYMVGKRE FSCVALEKEE VEQAVLDAGF DIEQLLHSPQ 

       250        260 
SYSVTNAANN GVCFIVARKK PGP 

O95050 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!