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Protein

Pterin-4-alpha-carbinolamine dehydratase 2

Gene

PCBD2

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

Functioni

Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity).By similarity
Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity.1 Publication

Catalytic activityi

(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O.

GO - Molecular functioni

  1. 4-alpha-hydroxytetrahydrobiopterin dehydratase activity Source: UniProtKB-EC
  2. phenylalanine 4-monooxygenase activity Source: Ensembl

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: UniProtKB
  2. protein heterooligomerization Source: Ensembl
  3. protein homotetramerization Source: Ensembl
  4. tetrahydrobiopterin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS13433-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pterin-4-alpha-carbinolamine dehydratase 2 (EC:4.2.1.96)
Short name:
PHS 2
Alternative name(s):
4-alpha-hydroxy-tetrahydropterin dehydratase 2
DcoH-like protein DCoHm
Dimerization cofactor of hepatocyte nuclear factor 1 from muscle
HNF-1-alpha dimerization cofactor
Gene namesi
Name:PCBD2
Synonyms:DCOH2, DCOHM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:24474. PCBD2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
  2. nucleus Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Pterin-4-alpha-carbinolamine dehydratase 2PRO_0000063057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-acetyllysine; alternateBy similarity
Modified residuei114 – 1141N6-succinyllysine; alternateBy similarity
Modified residuei118 – 1181N6-acetyllysine; alternateBy similarity
Modified residuei118 – 1181N6-succinyllysine; alternateBy similarity
Modified residuei125 – 1251N6-acetyllysine; alternateBy similarity
Modified residuei125 – 1251N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H0N5.
PaxDbiQ9H0N5.
PRIDEiQ9H0N5.

PTM databases

PhosphoSiteiQ9H0N5.

Expressioni

Gene expression databases

BgeeiQ9H0N5.
CleanExiHS_PCBD2.
ExpressionAtlasiQ9H0N5. baseline and differential.
GenevestigatoriQ9H0N5.

Organism-specific databases

HPAiHPA036428.

Interactioni

Subunit structurei

Homotetramer. Interacts with DYRK1B.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DYRK1BQ9Y4632EBI-634289,EBI-634187

Protein-protein interaction databases

BioGridi123893. 32 interactions.
IntActiQ9H0N5. 2 interactions.
MINTiMINT-4539105.
STRINGi9606.ENSP00000254908.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 4913Combined sources
Beta strandi56 – 594Combined sources
Beta strandi61 – 666Combined sources
Helixi70 – 8718Combined sources
Beta strandi92 – 965Combined sources
Beta strandi99 – 1046Combined sources
Turni107 – 1104Combined sources
Helixi114 – 12815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C45X-ray1.45A28-130[»]
ProteinModelPortaliQ9H0N5.
SMRiQ9H0N5. Positions 32-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2154.
GeneTreeiENSGT00390000007221.
HOGENOMiHOG000007680.
HOVERGENiHBG000259.
InParanoidiQ9H0N5.
KOiK01724.
OMAiDAHWLTA.
PhylomeDBiQ9H0N5.
TreeFamiTF300188.

Family and domain databases

Gene3Di3.30.1360.20. 1 hit.
HAMAPiMF_00434. Pterin_4_alpha.
InterProiIPR001533. Trans/pterin_deHydtase.
[Graphical view]
PANTHERiPTHR12599. PTHR12599. 1 hit.
PfamiPF01329. Pterin_4a. 1 hit.
[Graphical view]
SUPFAMiSSF55248. SSF55248. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9H0N5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVLGALGA TRRLLAALRG QSLGLAAMSS GTHRLTAEER NQAILDLKAA
60 70 80 90 100
GWSELSERDA IYKEFSFHNF NQAFGFMSRV ALQAEKMNHH PEWFNVYNKV
110 120 130
QITLTSHDCG ELTKKDVKLA KFIEKAAASV
Length:130
Mass (Da):14,365
Last modified:June 16, 2009 - v4
Checksum:i7B834F95D7ACD1EE
GO

Sequence cautioni

The sequence AAM18136.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361T → I in CAB66655. (PubMed:11230166)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136721 mRNA. Translation: CAB66655.1.
AC006077 Genomic DNA. No translation available.
AC008670 Genomic DNA. No translation available.
BC054021 mRNA. Translation: AAH54021.1.
AF499009 mRNA. Translation: AAM18136.1. Different initiation.
CCDSiCCDS43364.1.
RefSeqiNP_115527.3. NM_032151.4.
UniGeneiHs.710014.

Genome annotation databases

EnsembliENST00000254908; ENSP00000254908; ENSG00000132570.
ENST00000512783; ENSP00000421544; ENSG00000132570.
GeneIDi84105.
KEGGihsa:84105.
UCSCiuc010jdz.3. human.

Polymorphism databases

DMDMi239938927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136721 mRNA. Translation: CAB66655.1.
AC006077 Genomic DNA. No translation available.
AC008670 Genomic DNA. No translation available.
BC054021 mRNA. Translation: AAH54021.1.
AF499009 mRNA. Translation: AAM18136.1. Different initiation.
CCDSiCCDS43364.1.
RefSeqiNP_115527.3. NM_032151.4.
UniGeneiHs.710014.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C45X-ray1.45A28-130[»]
ProteinModelPortaliQ9H0N5.
SMRiQ9H0N5. Positions 32-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123893. 32 interactions.
IntActiQ9H0N5. 2 interactions.
MINTiMINT-4539105.
STRINGi9606.ENSP00000254908.

PTM databases

PhosphoSiteiQ9H0N5.

Polymorphism databases

DMDMi239938927.

Proteomic databases

MaxQBiQ9H0N5.
PaxDbiQ9H0N5.
PRIDEiQ9H0N5.

Protocols and materials databases

DNASUi84105.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254908; ENSP00000254908; ENSG00000132570.
ENST00000512783; ENSP00000421544; ENSG00000132570.
GeneIDi84105.
KEGGihsa:84105.
UCSCiuc010jdz.3. human.

Organism-specific databases

CTDi84105.
GeneCardsiGC05P134241.
H-InvDBHIX0018595.
HGNCiHGNC:24474. PCBD2.
HPAiHPA036428.
MIMi609836. gene.
neXtProtiNX_Q9H0N5.
PharmGKBiPA142671197.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2154.
GeneTreeiENSGT00390000007221.
HOGENOMiHOG000007680.
HOVERGENiHBG000259.
InParanoidiQ9H0N5.
KOiK01724.
OMAiDAHWLTA.
PhylomeDBiQ9H0N5.
TreeFamiTF300188.

Enzyme and pathway databases

BioCyciMetaCyc:HS13433-MONOMER.

Miscellaneous databases

ChiTaRSiPCBD2. human.
GeneWikiiPCBD2.
GenomeRNAii84105.
NextBioi73363.
PROiQ9H0N5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H0N5.
CleanExiHS_PCBD2.
ExpressionAtlasiQ9H0N5. baseline and differential.
GenevestigatoriQ9H0N5.

Family and domain databases

Gene3Di3.30.1360.20. 1 hit.
HAMAPiMF_00434. Pterin_4_alpha.
InterProiIPR001533. Trans/pterin_deHydtase.
[Graphical view]
PANTHERiPTHR12599. PTHR12599. 1 hit.
PfamiPF01329. Pterin_4a. 1 hit.
[Graphical view]
SUPFAMiSSF55248. SSF55248. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
  4. "Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1alpha."
    Lim S., Jin K., Friedman E.
    J. Biol. Chem. 277:25040-25046(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-130, FUNCTION IN HNF-1-ALPHA REGULATION, INTERACTION WITH DYRK1B.
    Tissue: Skeletal muscle.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPHS2_HUMAN
AccessioniPrimary (citable) accession number: Q9H0N5
Secondary accession number(s): Q8TD40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 16, 2009
Last modified: February 4, 2015
This is version 113 of the entry and version 4 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.