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P19113 (DCHS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine decarboxylase

Short name=HDC
EC=4.1.1.22
Gene names
Name:HDC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the biosynthesis of histamine from histidine. Ref.6

Catalytic activity

L-histidine = histamine + CO2. Ref.6

Cofactor

Pyridoxal phosphate. Ref.6

Pathway

Amine and polyamine biosynthesis; histamine biosynthesis; histamine from L-histidine: step 1/1.

Subunit structure

Homodimer. Ref.6

Sequence similarities

Belongs to the group II decarboxylase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.1 mM for histidine Ref.6

Vmax=1880 nmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Histidine decarboxylase
PRO_0000146950

Sites

Binding site811Substrate; via amide nitrogen
Binding site1941Substrate

Amino acid modifications

Modified residue3051N6-(pyridoxal phosphate)lysine

Natural variations

Natural variant311T → M. Ref.5
Corresponds to variant rs17740607 [ dbSNP | Ensembl ].
VAR_048873
Natural variant491E → V in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036470
Natural variant2851E → K in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036471
Natural variant5531F → L.
Corresponds to variant rs16963486 [ dbSNP | Ensembl ].
VAR_048874
Natural variant6441E → D.
Corresponds to variant rs2073440 [ dbSNP | Ensembl ].
VAR_033846

Experimental info

Mutagenesis3051K → G: Loss of enzyme activity. Ref.6
Mutagenesis3341Y → F: Loss of enzyme activity. Ref.6
Mutagenesis3541S → G: Strongly decreases affinity for histidine. Strongly increases affinity for L-DOPA and confers enzyme activity toward L-DOPA. Ref.6
Sequence conflict1181N → M no nucleotide entry Ref.3
Sequence conflict1481S → Q in CAA38196. Ref.1
Sequence conflict1481S → Q no nucleotide entry Ref.3
Sequence conflict5001W → M no nucleotide entry Ref.3

Secondary structure

............................................................................... 662
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19113 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: D7611CFAAD60F469

FASTA66274,141
        10         20         30         40         50         60 
MMEPEEYRER GREMVDYICQ YLSTVRERRV TPDVQPGYLR AQLPESAPED PDSWDSIFGD 

        70         80         90        100        110        120 
IERIIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN CLGFTWASSP ACTELEMNVM 

       130        140        150        160        170        180 
DWLAKMLGLP EHFLHHHPSS QGGGVLQSTV SESTLIALLA ARKNKILEMK TSEPDADESC 

       190        200        210        220        230        240 
LNARLVAYAS DQAHSSVEKA GLISLVKMKF LPVDDNFSLR GEALQKAIEE DKQRGLVPVF 

       250        260        270        280        290        300 
VCATLGTTGV CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL KGIEYADSFT 

       310        320        330        340        350        360 
FNPSKWMMVH FDCTGFWVKD KYKLQQTFSV NPIYLRHANS GVATDFMHWQ IPLSRRFRSV 

       370        380        390        400        410        420 
KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRNDPSFEI PAKRHLGLVV FRLKGPNCLT 

       430        440        450        460        470        480 
ENVLKEIAKA GRLFLIPATI QDKLIIRFTV TSQFTTRDDI LRDWNLIRDA ATLILSQHCT 

       490        500        510        520        530        540 
SQPSPRVGNL ISQIRGARAW ACGTSLQSVS GAGDDPVQAR KIIKQPQRVG AGPMKRENGL 

       550        560        570        580        590        600 
HLETLLDPVD DCFSEEAPDA TKHKLSSFLF SYLSVQTKKK TVRSLSCNSV PVSAQKPLPT 

       610        620        630        640        650        660 
EASVKNGGSS RVRIFSRFPE DMMMLKKSAF KKLIKFYSVP SFPECSSQCG LQLPCCPLQA 


MV 

« Hide

References

« Hide 'large scale' references
[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].
[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].
[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], 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]"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], VARIANT MET-31.
[6]"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.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-49 AND LYS-285.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54297 mRNA. Translation: CAA38196.1.
M60445 mRNA. Translation: AAC41698.1.
D16583 Genomic DNA. Translation: BAA04015.1.
BC130527 mRNA. Translation: AAI30528.1.
PIRA49882.
RefSeqNP_002103.2. NM_002112.3.
UniGeneHs.1481.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4E1OX-ray1.80A/B/C/D/E/F2-477[»]
ProteinModelPortalP19113.
SMRP19113. Positions 2-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109317. 1 interaction.
STRING9606.ENSP00000267845.

Chemistry

DrugBankDB00117. L-Histidine.
DB00114. Pyridoxal Phosphate.
GuidetoPHARMACOLOGY1274.

PTM databases

PhosphoSiteP19113.

Polymorphism databases

DMDM1352220.

Proteomic databases

PaxDbP19113.
PRIDEP19113.

Protocols and materials databases

DNASU3067.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267845; ENSP00000267845; ENSG00000140287.
GeneID3067.
KEGGhsa:3067.
UCSCuc001zxy.3. human.

Organism-specific databases

CTD3067.
GeneCardsGC15M050534.
HGNCHGNC:4855. HDC.
HPAHPA038891.
MIM142704. gene.
neXtProtNX_P19113.
PharmGKBPA29233.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000121941.
HOVERGENHBG000944.
InParanoidP19113.
KOK01590.
OMALHHHPSS.
OrthoDBEOG75B851.
PhylomeDBP19113.
TreeFamTF313863.

Enzyme and pathway databases

BRENDA4.1.1.22. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00822; UER00786.

Gene expression databases

ArrayExpressP19113.
BgeeP19113.
CleanExHS_HDC.
GenevestigatorP19113.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010977. 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]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSPR00800. YHDCRBOXLASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHistidine_decarboxylase.
GenomeRNAi3067.
NextBio12133.
PROP19113.
SOURCESearch...

Entry information

Entry nameDCHS_HUMAN
AccessionPrimary (citable) accession number: P19113
Secondary accession number(s): A1L4G0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM