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P50135

- HNMT_HUMAN

UniProt

P50135 - HNMT_HUMAN

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Protein

Histamine N-methyltransferase

Gene

HNMT

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

Functioni

Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.

Catalytic activityi

S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Substrate
Binding sitei60 – 601S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei89 – 891S-adenosyl-L-methionine
Binding sitei94 – 941S-adenosyl-L-methionine
Binding sitei120 – 1201S-adenosyl-L-methionine; via amide nitrogen
Binding sitei142 – 1421S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei283 – 2831Substrate

GO - Molecular functioni

  1. histamine N-methyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. brain development Source: Ensembl
  2. hyperosmotic response Source: Ensembl
  3. respiratory gaseous exchange Source: ProtInc
  4. response to amine Source: Ensembl
  5. response to cocaine Source: Ensembl
  6. response to glucocorticoid Source: Ensembl
  7. response to interleukin-1 Source: Ensembl
  8. response to tumor cell Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS07674-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histamine N-methyltransferase (EC:2.1.1.8)
Short name:
HMT
Gene namesi
Name:HNMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:5028. HNMT.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. neuron projection Source: Ensembl
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Histamine N-methyltransferasePRO_0000084021Add
BLAST

Proteomic databases

MaxQBiP50135.
PaxDbiP50135.
PeptideAtlasiP50135.
PRIDEiP50135.

PTM databases

PhosphoSiteiP50135.

Expressioni

Gene expression databases

BgeeiP50135.
CleanExiHS_HNMT.
GenevestigatoriP50135.

Organism-specific databases

HPAiHPA035481.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi109418. 5 interactions.
IntActiP50135. 1 interaction.
MINTiMINT-5001055.
STRINGi9606.ENSP00000280097.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi12 – 2312Combined sources
Helixi28 – 3811Combined sources
Helixi40 – 434Combined sources
Beta strandi44 – 463Combined sources
Turni47 – 504Combined sources
Beta strandi52 – 609Combined sources
Helixi65 – 7713Combined sources
Beta strandi82 – 887Combined sources
Helixi92 – 10312Combined sources
Beta strandi111 – 1166Combined sources
Helixi120 – 1289Combined sources
Turni129 – 1313Combined sources
Beta strandi136 – 1438Combined sources
Helixi145 – 1473Combined sources
Helixi151 – 16010Combined sources
Beta strandi162 – 17312Combined sources
Beta strandi175 – 1773Combined sources
Helixi178 – 1869Combined sources
Helixi187 – 1893Combined sources
Helixi201 – 21111Combined sources
Beta strandi215 – 2206Combined sources
Beta strandi223 – 2253Combined sources
Helixi227 – 2304Combined sources
Helixi235 – 24511Combined sources
Beta strandi247 – 2493Combined sources
Helixi250 – 2534Combined sources
Helixi256 – 26510Combined sources
Turni269 – 2713Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi278 – 2825Combined sources
Beta strandi285 – 2917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ICZmodel-A1-249[»]
1JQDX-ray2.28A/B1-292[»]
1JQEX-ray1.91A/B1-292[»]
2AOTX-ray1.90A/B1-292[»]
2AOUX-ray2.30A/B1-292[»]
2AOVX-ray2.48A/B1-292[»]
2AOWX-ray2.97A/B1-292[»]
2AOXX-ray3.12A/B1-292[»]
ProteinModelPortaliP50135.
SMRiP50135. Positions 5-292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50135.

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. HNMT family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG39680.
GeneTreeiENSGT00390000002862.
HOGENOMiHOG000231790.
HOVERGENiHBG051914.
InParanoidiP50135.
KOiK00546.
OMAiMDISDCF.
OrthoDBiEOG7Z69CQ.
PhylomeDBiP50135.
TreeFamiTF331080.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016673. Histamine_N-methyltransferase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PIRSFiPIRSF016616. HHMT. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51597. SAM_HNMT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50135-1) [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

        10         20         30         40         50
MASSMRSLFS DHGKYVESFR RFLNHSTEHQ CMQEFMDKKL PGIIGRIGDT
60 70 80 90 100
KSEIKILSIG GGAGEIDLQI LSKVQAQYPG VCINNEVVEP SAEQIAKYKE
110 120 130 140 150
LVAKTSNLEN VKFAWHKETS SEYQSRMLEK KELQKWDFIH MIQMLYYVKD
160 170 180 190 200
IPATLKFFHS LLGTNAKMLI IVVSGSSGWD KLWKKYGSRF PQDDLCQYIT
210 220 230 240 250
SDDLTQMLDN LGLKYECYDL LSTMDISDCF IDGNENGDLL WDFLTETCNF
260 270 280 290
NATAPPDLRA ELGKDLQEPE FSAKKEGKVL FNNTLSFIVI EA
Length:292
Mass (Da):33,295
Last modified:October 1, 1996 - v1
Checksum:i9CCADD1EE0CCB653
GO
Isoform 2 (identifier: P50135-2) [UniParc]FASTAAdd to Basket

Also known as: HNMT-S

The sequence of this isoform differs from the canonical sequence as follows:
     64-292: GEIDLQILSK...NTLSFIVIEA → DCLIRGSSRV...PSFLVSFILF

Note: Has no histamine-methylating activity.

Show »
Length:126
Mass (Da):14,207
Checksum:iD3215E15F10E7EB3
GO
Isoform 3 (identifier: P50135-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-51: IGDTK → YQNCC
     52-292: Missing.

Note: No experimental confirmation available.

Show »
Length:51
Mass (Da):6,046
Checksum:i722B5977BDD19382
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991I → V in BAA03752. (PubMed:7943261)Curated
Sequence conflicti234 – 2341N → D in AAH20677. (PubMed:15489334)Curated

Polymorphismi

Variant Ile-105 has a reduced activity and seems to be linked with a predisposition to asthma.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051T → I.2 Publications
Corresponds to variant rs1801105 [ dbSNP | Ensembl ].
VAR_010252

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei47 – 515IGDTK → YQNCC in isoform 3. 1 PublicationVSP_043482
Alternative sequencei52 – 292241Missing in isoform 3. 1 PublicationVSP_043483Add
BLAST
Alternative sequencei64 – 292229GEIDL…IVIEA → DCLIRGSSRVLKRNSCFILC STRQKDKPGMRIHDERSSEL PFGAARLESKSAFPSFLVSF ILF in isoform 2. 1 PublicationVSP_042027Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16224 mRNA. Translation: BAA03752.1.
U08092 mRNA. Translation: AAA17423.1.
U44111
, U44106, U44107, U44108, U44109, U44110 Genomic DNA. Translation: AAB18137.1.
AF523358 mRNA. Translation: AAN33016.1.
AF523359 mRNA. Translation: AAN33017.1.
AF523360 mRNA. Translation: AAN33018.1.
AF523356 mRNA. Translation: AAN33014.1.
AF523357 mRNA. Translation: AAN33015.1.
AK313804 mRNA. Translation: BAG36540.1.
AC093674 Genomic DNA. Translation: AAY24212.1.
CH471058 Genomic DNA. Translation: EAX11612.1.
CH471058 Genomic DNA. Translation: EAX11613.1.
CH471058 Genomic DNA. Translation: EAX11614.1.
BC005907 mRNA. Translation: AAH05907.1.
BC020677 mRNA. Translation: AAH20677.1.
AH012839 Genomic DNA. Translation: AAP42155.1.
CCDSiCCDS2181.1. [P50135-1]
CCDS33296.1. [P50135-2]
CCDS33297.1. [P50135-3]
PIRiG01409.
RefSeqiNP_001019245.1. NM_001024074.2. [P50135-3]
NP_001019246.1. NM_001024075.1. [P50135-2]
NP_008826.1. NM_006895.2. [P50135-1]
UniGeneiHs.42151.

Genome annotation databases

EnsembliENST00000280096; ENSP00000280096; ENSG00000150540. [P50135-3]
ENST00000280097; ENSP00000280097; ENSG00000150540. [P50135-1]
ENST00000329366; ENSP00000333259; ENSG00000150540. [P50135-2]
ENST00000410115; ENSP00000386940; ENSG00000150540. [P50135-1]
ENST00000475675; ENSP00000419415; ENSG00000150540. [P50135-3]
GeneIDi3176.
KEGGihsa:3176.
UCSCiuc002tvd.3. human. [P50135-3]
uc002tve.3. human. [P50135-2]
uc002tvf.3. human. [P50135-1]

Polymorphism databases

DMDMi1708272.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16224 mRNA. Translation: BAA03752.1 .
U08092 mRNA. Translation: AAA17423.1 .
U44111
, U44106 , U44107 , U44108 , U44109 , U44110 Genomic DNA. Translation: AAB18137.1 .
AF523358 mRNA. Translation: AAN33016.1 .
AF523359 mRNA. Translation: AAN33017.1 .
AF523360 mRNA. Translation: AAN33018.1 .
AF523356 mRNA. Translation: AAN33014.1 .
AF523357 mRNA. Translation: AAN33015.1 .
AK313804 mRNA. Translation: BAG36540.1 .
AC093674 Genomic DNA. Translation: AAY24212.1 .
CH471058 Genomic DNA. Translation: EAX11612.1 .
CH471058 Genomic DNA. Translation: EAX11613.1 .
CH471058 Genomic DNA. Translation: EAX11614.1 .
BC005907 mRNA. Translation: AAH05907.1 .
BC020677 mRNA. Translation: AAH20677.1 .
AH012839 Genomic DNA. Translation: AAP42155.1 .
CCDSi CCDS2181.1. [P50135-1 ]
CCDS33296.1. [P50135-2 ]
CCDS33297.1. [P50135-3 ]
PIRi G01409.
RefSeqi NP_001019245.1. NM_001024074.2. [P50135-3 ]
NP_001019246.1. NM_001024075.1. [P50135-2 ]
NP_008826.1. NM_006895.2. [P50135-1 ]
UniGenei Hs.42151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ICZ model - A 1-249 [» ]
1JQD X-ray 2.28 A/B 1-292 [» ]
1JQE X-ray 1.91 A/B 1-292 [» ]
2AOT X-ray 1.90 A/B 1-292 [» ]
2AOU X-ray 2.30 A/B 1-292 [» ]
2AOV X-ray 2.48 A/B 1-292 [» ]
2AOW X-ray 2.97 A/B 1-292 [» ]
2AOX X-ray 3.12 A/B 1-292 [» ]
ProteinModelPortali P50135.
SMRi P50135. Positions 5-292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109418. 5 interactions.
IntActi P50135. 1 interaction.
MINTi MINT-5001055.
STRINGi 9606.ENSP00000280097.

Chemistry

BindingDBi P50135.
ChEMBLi CHEMBL2190.
DrugBanki DB00613. Amodiaquine.
DB00878. Chlorhexidine.
DB00667. Histamine Phosphate.
DB01103. Quinacrine.

PTM databases

PhosphoSitei P50135.

Polymorphism databases

DMDMi 1708272.

Proteomic databases

MaxQBi P50135.
PaxDbi P50135.
PeptideAtlasi P50135.
PRIDEi P50135.

Protocols and materials databases

DNASUi 3176.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000280096 ; ENSP00000280096 ; ENSG00000150540 . [P50135-3 ]
ENST00000280097 ; ENSP00000280097 ; ENSG00000150540 . [P50135-1 ]
ENST00000329366 ; ENSP00000333259 ; ENSG00000150540 . [P50135-2 ]
ENST00000410115 ; ENSP00000386940 ; ENSG00000150540 . [P50135-1 ]
ENST00000475675 ; ENSP00000419415 ; ENSG00000150540 . [P50135-3 ]
GeneIDi 3176.
KEGGi hsa:3176.
UCSCi uc002tvd.3. human. [P50135-3 ]
uc002tve.3. human. [P50135-2 ]
uc002tvf.3. human. [P50135-1 ]

Organism-specific databases

CTDi 3176.
GeneCardsi GC02P138744.
HGNCi HGNC:5028. HNMT.
HPAi HPA035481.
MIMi 605238. gene.
neXtProti NX_P50135.
PharmGKBi PA190.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39680.
GeneTreei ENSGT00390000002862.
HOGENOMi HOG000231790.
HOVERGENi HBG051914.
InParanoidi P50135.
KOi K00546.
OMAi MDISDCF.
OrthoDBi EOG7Z69CQ.
PhylomeDBi P50135.
TreeFami TF331080.

Enzyme and pathway databases

BioCyci MetaCyc:HS07674-MONOMER.

Miscellaneous databases

EvolutionaryTracei P50135.
GenomeRNAii 3176.
NextBioi 12602.
PROi P50135.
SOURCEi Search...

Gene expression databases

Bgeei P50135.
CleanExi HS_HNMT.
Genevestigatori P50135.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR016673. Histamine_N-methyltransferase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PIRSFi PIRSF016616. HHMT. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51597. SAM_HNMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and function of human histamine N-methyltransferase: critical enzyme in histamine metabolism in airway."
    Yamauchi K., Sekizawa K., Suzuki H., Nakazawa H., Ohkawara Y., Katayose D., Ohtsu H., Tamura G., Shibahara S., Takemura M.
    Am. J. Physiol. 267:L342-L349(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  2. "Human histamine N-methyltransferase pharmacogenetics: cloning and expression of kidney cDNA."
    Girard B., Otterness D.M., Wood T.C., Honchel R., Wieben E.D., Weinshilboum R.M.
    Mol. Pharmacol. 45:461-468(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Human histamine N-methyltransferase gene: structural characterization and chromosomal location."
    Aksoy S., Raftogianis R., Weinshilboum R.M.
    Biochem. Biophys. Res. Commun. 219:548-554(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Further characterization of the histamine N-methyltransferase gene: a new mRNA species and several 3'-UTR Variants from human brain."
    Barnes W.G., Grinde E., Crawford D.R., Herrick-Davis K., Hough L.B.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Characterization of a new mRNA species from the human histamine N-methyltransferase gene."
    Barnes W.G., Grinde E., Crawford D.R., Herrick-Davis K., Hough L.B.
    Genomics 83:168-171(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    Tissue: Brain.
  6. "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 1).
    Tissue: Cerebellum.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 3).
    Tissue: Liver and Prostate.
  10. "Homo sapiens histamine N-methyltransferase (HNMT) gene, consensus of Coriell PDR 90."
    Thomae B., Wieben E., Eckloff B., Weinshilboum R.M.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-221.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons."
    Horton J.R., Sawada K., Nishibori M., Zhang X., Cheng X.
    Structure 9:837-849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND INHIBITOR.
  13. "Human histamine N-methyltransferase pharmacogenetics: common genetic polymorphisms that alter activity."
    Preuss C.V., Wood T.C., Szumlanski C.L., Raftogianis R.B., Otterness D.M., Girard B., Scott M.C., Weinshilboum R.M.
    Mol. Pharmacol. 53:708-717(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ILE-105.
  14. "Histamine N-methyltransferase pharmacogenetics: association of a common functional polymorphism with asthma."
    Yan L., Galinsky R.E., Bernstein J.A., Liggett S.B., Weinshilboum R.M.
    Pharmacogenetics 10:261-266(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ILE-105.

Entry informationi

Entry nameiHNMT_HUMAN
AccessioniPrimary (citable) accession number: P50135
Secondary accession number(s): B2R9J3
, Q546Z6, Q7Z7I2, Q8IU56, Q8WW98, Q9BRW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 136 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 2
    Human chromosome 2: 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