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P50135

- HNMT_HUMAN

UniProt

P50135 - HNMT_HUMAN

Protein

Histamine N-methyltransferase

Gene

HNMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    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

    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 – 103
    Helixi12 – 2312
    Helixi28 – 3811
    Helixi40 – 434
    Beta strandi44 – 463
    Turni47 – 504
    Beta strandi52 – 609
    Helixi65 – 7713
    Beta strandi82 – 887
    Helixi92 – 10312
    Beta strandi111 – 1166
    Helixi120 – 1289
    Turni129 – 1313
    Beta strandi136 – 1438
    Helixi145 – 1473
    Helixi151 – 16010
    Beta strandi162 – 17312
    Beta strandi175 – 1773
    Helixi178 – 1869
    Helixi187 – 1893
    Helixi201 – 21111
    Beta strandi215 – 2206
    Beta strandi223 – 2253
    Helixi227 – 2304
    Helixi235 – 24511
    Beta strandi247 – 2493
    Helixi250 – 2534
    Helixi256 – 26510
    Turni269 – 2713
    Beta strandi272 – 2754
    Beta strandi278 – 2825
    Beta strandi285 – 2917

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MASSMRSLFS DHGKYVESFR RFLNHSTEHQ CMQEFMDKKL PGIIGRIGDT    50
    KSEIKILSIG GGAGEIDLQI LSKVQAQYPG VCINNEVVEP SAEQIAKYKE 100
    LVAKTSNLEN VKFAWHKETS SEYQSRMLEK KELQKWDFIH MIQMLYYVKD 150
    IPATLKFFHS LLGTNAKMLI IVVSGSSGWD KLWKKYGSRF PQDDLCQYIT 200
    SDDLTQMLDN LGLKYECYDL LSTMDISDCF IDGNENGDLL WDFLTETCNF 250
    NATAPPDLRA ELGKDLQEPE FSAKKEGKVL FNNTLSFIVI EA 292
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    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 1, 2014
    This is version 135 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