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P19113

- DCHS_HUMAN

UniProt

P19113 - DCHS_HUMAN

Protein

Histidine decarboxylase

Gene

HDC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the biosynthesis of histamine from histidine.1 Publication

    Catalytic activityi

    L-histidine = histamine + CO2.1 Publication

    Cofactori

    Pyridoxal phosphate.1 Publication

    Kineticsi

    1. KM=0.1 mM for histidine1 Publication

    Vmax=1880 nmol/min/mg enzyme1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811Substrate; via amide nitrogen
    Binding sitei194 – 1941Substrate

    GO - Molecular functioni

    1. histidine decarboxylase activity Source: UniProtKB
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. catecholamine biosynthetic process Source: UniProtKB-KW
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. histamine biosynthetic process Source: UniProtKB
    4. histidine catabolic process Source: UniProtKB
    5. histidine metabolic process Source: ProtInc
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Catecholamine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06697-MONOMER.
    BRENDAi4.1.1.22. 2681.
    ReactomeiREACT_1249. Histidine catabolism.
    UniPathwayiUPA00822; UER00786.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine decarboxylase (EC:4.1.1.22)
    Short name:
    HDC
    Gene namesi
    Name:HDC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:4855. HDC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi305 – 3051K → G: Loss of enzyme activity. 1 Publication
    Mutagenesisi334 – 3341Y → F: Loss of enzyme activity. 1 Publication
    Mutagenesisi354 – 3541S → G: Strongly decreases affinity for histidine. Strongly increases affinity for L-DOPA and confers enzyme activity toward L-DOPA. 1 Publication

    Organism-specific databases

    PharmGKBiPA29233.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 662662Histidine decarboxylasePRO_0000146950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei305 – 3051N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP19113.
    PRIDEiP19113.

    PTM databases

    PhosphoSiteiP19113.

    Expressioni

    Gene expression databases

    ArrayExpressiP19113.
    BgeeiP19113.
    CleanExiHS_HDC.
    GenevestigatoriP19113.

    Organism-specific databases

    HPAiHPA038891.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109317. 1 interaction.
    STRINGi9606.ENSP00000267845.

    Structurei

    Secondary structure

    1
    662
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2320
    Helixi25 – 273
    Turni36 – 394
    Helixi40 – 423
    Helixi54 – 6411
    Helixi66 – 683
    Beta strandi79 – 813
    Helixi87 – 9913
    Turni106 – 1083
    Helixi110 – 12718
    Helixi131 – 1333
    Beta strandi143 – 1486
    Helixi150 – 17223
    Helixi178 – 1825
    Beta strandi185 – 1906
    Helixi195 – 20410
    Beta strandi207 – 2115
    Helixi221 – 23313
    Beta strandi237 – 24610
    Turni248 – 2503
    Helixi256 – 26611
    Beta strandi269 – 2735
    Helixi277 – 2826
    Helixi284 – 2907
    Helixi293 – 2953
    Beta strandi297 – 3015
    Helixi303 – 3064
    Beta strandi314 – 3207
    Helixi321 – 3255
    Turni326 – 3283
    Helixi333 – 3353
    Turni338 – 3425
    Helixi346 – 3494
    Beta strandi350 – 3534
    Helixi359 – 39335
    Beta strandi406 – 41510
    Helixi417 – 43014
    Beta strandi432 – 4343
    Beta strandi436 – 4405
    Beta strandi443 – 4497
    Helixi457 – 47519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E1OX-ray1.80A/B/C/D/E/F2-477[»]
    ProteinModelPortaliP19113.
    SMRiP19113. Positions 2-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000121941.
    HOVERGENiHBG000944.
    InParanoidiP19113.
    KOiK01590.
    OMAiPICASEG.
    OrthoDBiEOG75B851.
    PhylomeDBiP19113.
    TreeFamiTF313863.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR010977. Aromatic_deC.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    PRINTSiPR00800. YHDCRBOXLASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19113-1) [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

    MMEPEEYRER GREMVDYICQ YLSTVRERRV TPDVQPGYLR AQLPESAPED    50
    PDSWDSIFGD IERIIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN 100
    CLGFTWASSP ACTELEMNVM DWLAKMLGLP EHFLHHHPSS QGGGVLQSTV 150
    SESTLIALLA ARKNKILEMK TSEPDADESC LNARLVAYAS DQAHSSVEKA 200
    GLISLVKMKF LPVDDNFSLR GEALQKAIEE DKQRGLVPVF VCATLGTTGV 250
    CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL KGIEYADSFT 300
    FNPSKWMMVH FDCTGFWVKD KYKLQQTFSV NPIYLRHANS GVATDFMHWQ 350
    IPLSRRFRSV KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRNDPSFEI 400
    PAKRHLGLVV FRLKGPNCLT ENVLKEIAKA GRLFLIPATI QDKLIIRFTV 450
    TSQFTTRDDI LRDWNLIRDA ATLILSQHCT SQPSPRVGNL ISQIRGARAW 500
    ACGTSLQSVS GAGDDPVQAR KIIKQPQRVG AGPMKRENGL HLETLLDPVD 550
    DCFSEEAPDA TKHKLSSFLF SYLSVQTKKK TVRSLSCNSV PVSAQKPLPT 600
    EASVKNGGSS RVRIFSRFPE DMMMLKKSAF KKLIKFYSVP SFPECSSQCG 650
    LQLPCCPLQA MV 662
    Length:662
    Mass (Da):74,141
    Last modified:February 1, 1996 - v2
    Checksum:iD7611CFAAD60F469
    GO
    Isoform 2 (identifier: P19113-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         348-380: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:629
    Mass (Da):70,059
    Checksum:i72BDB69D63CE7606
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181N → M no nucleotide entry (PubMed:1425659)Curated
    Sequence conflicti148 – 1481S → Q in CAA38196. (PubMed:2216786)Curated
    Sequence conflicti148 – 1481S → Q no nucleotide entry (PubMed:1425659)Curated
    Sequence conflicti500 – 5001W → M no nucleotide entry (PubMed:1425659)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311T → M.1 Publication
    Corresponds to variant rs17740607 [ dbSNP | Ensembl ].
    VAR_048873
    Natural varianti49 – 491E → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036470
    Natural varianti285 – 2851E → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036471
    Natural varianti553 – 5531F → L.
    Corresponds to variant rs16963486 [ dbSNP | Ensembl ].
    VAR_048874
    Natural varianti644 – 6441E → D.
    Corresponds to variant rs2073440 [ dbSNP | Ensembl ].
    VAR_033846

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei348 – 38033Missing in isoform 2. 1 PublicationVSP_056296Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54297 mRNA. Translation: CAA38196.1.
    M60445 mRNA. Translation: AAC41698.1.
    D16583 Genomic DNA. Translation: BAA04015.1.
    AC009753 Genomic DNA. No translation available.
    AC022087 Genomic DNA. No translation available.
    BC130527 mRNA. Translation: AAI30528.1.
    BC144173 mRNA. Translation: AAI44174.1.
    CCDSiCCDS10134.1.
    PIRiA49882.
    RefSeqiNP_002103.2. NM_002112.3.
    UniGeneiHs.1481.

    Genome annotation databases

    EnsembliENST00000267845; ENSP00000267845; ENSG00000140287.
    ENST00000543581; ENSP00000440252; ENSG00000140287.
    GeneIDi3067.
    KEGGihsa:3067.
    UCSCiuc001zxy.3. human.

    Polymorphism databases

    DMDMi1352220.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54297 mRNA. Translation: CAA38196.1 .
    M60445 mRNA. Translation: AAC41698.1 .
    D16583 Genomic DNA. Translation: BAA04015.1 .
    AC009753 Genomic DNA. No translation available.
    AC022087 Genomic DNA. No translation available.
    BC130527 mRNA. Translation: AAI30528.1 .
    BC144173 mRNA. Translation: AAI44174.1 .
    CCDSi CCDS10134.1.
    PIRi A49882.
    RefSeqi NP_002103.2. NM_002112.3.
    UniGenei Hs.1481.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4E1O X-ray 1.80 A/B/C/D/E/F 2-477 [» ]
    ProteinModelPortali P19113.
    SMRi P19113. Positions 2-477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109317. 1 interaction.
    STRINGi 9606.ENSP00000267845.

    Chemistry

    DrugBanki DB00117. L-Histidine.
    DB00114. Pyridoxal Phosphate.
    GuidetoPHARMACOLOGYi 1274.

    PTM databases

    PhosphoSitei P19113.

    Polymorphism databases

    DMDMi 1352220.

    Proteomic databases

    PaxDbi P19113.
    PRIDEi P19113.

    Protocols and materials databases

    DNASUi 3067.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267845 ; ENSP00000267845 ; ENSG00000140287 .
    ENST00000543581 ; ENSP00000440252 ; ENSG00000140287 .
    GeneIDi 3067.
    KEGGi hsa:3067.
    UCSCi uc001zxy.3. human.

    Organism-specific databases

    CTDi 3067.
    GeneCardsi GC15M050534.
    HGNCi HGNC:4855. HDC.
    HPAi HPA038891.
    MIMi 142704. gene.
    neXtProti NX_P19113.
    PharmGKBi PA29233.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000121941.
    HOVERGENi HBG000944.
    InParanoidi P19113.
    KOi K01590.
    OMAi PICASEG.
    OrthoDBi EOG75B851.
    PhylomeDBi P19113.
    TreeFami TF313863.

    Enzyme and pathway databases

    UniPathwayi UPA00822 ; UER00786 .
    BioCyci MetaCyc:HS06697-MONOMER.
    BRENDAi 4.1.1.22. 2681.
    Reactomei REACT_1249. Histidine catabolism.

    Miscellaneous databases

    GeneWikii Histidine_decarboxylase.
    GenomeRNAii 3067.
    NextBioi 12133.
    PROi P19113.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19113.
    Bgeei P19113.
    CleanExi HS_HDC.
    Genevestigatori P19113.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR010977. Aromatic_deC.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    PRINTSi PR00800. YHDCRBOXLASE.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived from human basophilic leukemia cell line, KU-812-F."
      Yamauchi K., Ruriko S., Ohkawara Y., Tanno Y., Maeyama K., Watanabe T., Satoh K., Yoshizawa M., Shibahara S., Takishima T.
      Nucleic Acids Res. 18:5891-5891(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15."
      Zahnow C.A., Yi H.F., McBride O.W., Joseph D.R.
      DNA Seq. 1:395-400(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells."
      Mamune-Sato R., Yamauchi K., Tanno Y., Ohkawara Y., Ohtsu H., Katayose D., Maeyama K., Watanabe T., Shibahara S., Takishima T.
      Eur. J. Biochem. 209:533-539(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Leukemia.
    4. "Structure of the L-histidine decarboxylase gene."
      Yatsunami K., Ohtsu H., Tsuchikawa M., Higuchi T., Ishibashi K., Shida A., Shima Y., Nakagawa S., Yamauchi K., Yamamoto M., Hayashi N., Watanabe T., Ichikawa A.
      J. Biol. Chem. 269:1554-1559(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 2), VARIANT MET-31.
    7. "Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase."
      Komori H., Nitta Y., Ueno H., Higuchi Y.
      J. Biol. Chem. 287:29175-29183(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-477 IN COMPLEX WITH HISTIDINE METHYL ESTER AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-305; TYR-334 AND SER-354.
    8. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-49 AND LYS-285.

    Entry informationi

    Entry nameiDCHS_HUMAN
    AccessioniPrimary (citable) accession number: P19113
    Secondary accession number(s): A1L4G0, B7ZM01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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 15
      Human chromosome 15: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3