O95050 (INMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Indolethylamine N-methyltransferase
Short name=Indolamine N-methyltransferase
EC=2.1.1.49

Alternative name(s):
Aromatic alkylamine N-methyltransferase
Short name=Amine N-methyltransferase
Short name=Arylamine N-methyltransferase

Gene names

Name:

INMT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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 structure	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.
Sequence similarities	Belongs to the NNMT/PNMT/TEMT family.
Biophysicochemical properties	Kinetic parameters: KM=2.9 mM for tryptamine Ref.1

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amine N-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 263

263

Indolethylamine N-methyltransferase

PRO_0000159712

Regions

Region

85 – 87

3

S-adenosyl-L-methionine binding

Region

142 – 143

2

S-adenosyl-L-methionine binding

Sites

Binding site

20

1

S-adenosyl-L-methionine

Binding site

25

1

S-adenosyl-L-methionine

Binding site

63

1

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

69

1

S-adenosyl-L-methionine

Binding site

90

1

S-adenosyl-L-methionine

Binding site

163

1

S-adenosyl-L-methionine; via carbonyl oxygen

Natural variations

Natural variant

28

1

D → N. Ref.3
Corresponds to variant rs4723010 [ dbSNP | Ensembl ].

VAR_036991

Natural variant

205

1

M → V. Ref.1
Corresponds to variant rs2302339 [ dbSNP | Ensembl ].

VAR_011616

Natural variant

214

1

V → M.
Corresponds to variant rs56800285 [ dbSNP | Ensembl ].

VAR_061373

Natural variant

219

1

E → G. Ref.1 Ref.3
Corresponds to variant rs2302340 [ dbSNP | Ensembl ].

VAR_011617

Natural variant

246

1

N → S.
Corresponds to variant rs6970210 [ dbSNP | Ensembl ].

VAR_036992

Natural variant

254

1

F → C.
Corresponds to variant rs4720015 [ dbSNP | Ensembl ].

VAR_036993

Natural variant

258

1

R → H.
Corresponds to variant rs6970605 [ dbSNP | Ensembl ].

VAR_036994

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

263

Helix Strand Turn

Details...

Helix

8 – 14

7

Helix

17 – 24

8

Helix

33 – 49

17

Beta strand

56 – 63

8

Helix

69 – 71

3

Helix

74 – 76

3

Beta strand

78 – 86

9

Helix

88 – 99

12

Helix

108 – 117

10

Helix

121 – 123

3

Helix

124 – 134

11

Beta strand

135 – 140

6

Beta strand

145 – 147

3

Turn

148 – 151

4

Beta strand

157 – 164

8

Helix

166 – 169

4

Helix

173 – 184

12

Beta strand

187 – 200

14

Beta strand

203 – 206

4

Beta strand

209 – 212

4

Helix

218 – 227

10

Beta strand

230 – 238

9

Turn

244 – 246

3

Beta strand

252 – 259

8

Sequences

	Sequence		Length	Mass (Da)
	O95050 [UniParc]. Last modified November 13, 2007. Version 3. Checksum: 12B3AC66597E70A3	FASTA	263	28,891
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10552930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS VAL-205 AND GLY-219, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Placenta and Skeletal muscle.
[2]	"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: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASN-28 AND GLY-219. Tissue: Lung and Spleen.
[4]	"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: 15014171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF128846 mRNA. Translation: AAF18304.1.
AF128847 mRNA. Translation: AAF18305.1.
AF128848 Genomic DNA. Translation: AAF18306.1.
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.

IPI

IPI00028239.

RefSeq

NP_001186148.1. NM_001199219.1.
NP_006765.4. NM_006774.4.

UniGene

Hs.632629.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A14	X-ray	1.70	A	1-263	[»]

ProteinModelPortal

O95050.

SMR

O95050. Positions 5-261.

ModBase

Search...

Protein-protein interaction databases

STRING

O95050.

PTM databases

PhosphoSite

O95050.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000013222; ENSP00000013222; ENSG00000241644.

GeneID

11185.

KEGG

hsa:11185.

UCSC

uc003tbs.1. human.

Organism-specific databases

CTD

11185.

GeneCards

GC07P030737.

HGNC

HGNC:6069. INMT.

MIM

604854. gene.

neXtProt

NX_O95050.

PharmGKB

PA403.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04368.

HOVERGEN

HBG000797.

InParanoid

O95050.

OrthoDB

EOG49079M.

PhylomeDB

O95050.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000011177-MONOMER.

Gene expression databases

ArrayExpress

O95050.

Bgee

O95050.

CleanEx

HS_INMT.

Genevestigator

O95050.

GermOnline

ENSG00000011177. Homo sapiens.

Family and domain databases

InterPro

IPR000940. NNMT_TEMT_trans.
[Graphical view]

KO

K00562.

PANTHER

PTHR10867. NNMT_TEMT_trans. 1 hit.

Pfam

PF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

PIRSF

PIRSF000384. PNMTase. 1 hit.

PROSITE

PS01100. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

42567.

SOURCE

Search...

Entry information

Entry name

INMT_HUMAN

Accession

Primary (citable) accession number: O95050
Secondary accession number(s): Q3KP49 , Q9P1Y2, Q9UBY4, Q9UHQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 13, 2007
Last modified:	November 16, 2011
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.