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P19113

- DCHS_HUMAN

UniProt

P19113 - DCHS_HUMAN

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

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 enzyme

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
Complete GO annotation...

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
Complete GO annotation...

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 decarboxylase
PRO_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

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.

Family & Domainsi

Sequence similaritiesi

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]

Sequencei

Sequence statusi: Complete.

P19113-1 [UniParc]FASTAAdd to Basket

« 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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181N → M no nucleotide entry 1 Publication
Sequence conflicti148 – 1481S → Q in CAA38196. 1 Publication
Sequence conflicti148 – 1481S → Q no nucleotide entry 1 Publication
Sequence conflicti500 – 5001W → M no nucleotide entry 1 Publication

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.
BC130527 mRNA. Translation: AAI30528.1.
CCDSiCCDS10134.1.
PIRiA49882.
RefSeqiNP_002103.2. NM_002112.3.
UniGeneiHs.1481.

Genome annotation databases

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

Polymorphism databases

DMDMi1352220.

Keywords - Coding sequence diversityi

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 .
BC130527 mRNA. Translation: AAI30528.1 .
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 .
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

« Hide 'large scale' publications
  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. 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
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 127 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

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