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Q9H0N5 (PHS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pterin-4-alpha-carbinolamine dehydratase 2

Short name=PHS 2
EC=4.2.1.96
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 names
Name:PCBD2
Synonyms:DCOH2, DCOHM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 By similarity. Ref.4

Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. Ref.4

Catalytic activity

(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. HAMAP-Rule MF_00434

Subunit structure

Homotetramer. Interacts with DYRK1B. Ref.4

Sequence similarities

Belongs to the pterin-4-alpha-carbinolamine dehydratase family.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DYRK1BQ9Y4632EBI-634289,EBI-634187

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 130130Pterin-4-alpha-carbinolamine dehydratase 2 HAMAP-Rule MF_00434
PRO_0000063057

Amino acid modifications

Modified residue1141N6-acetyllysine; alternate By similarity
Modified residue1141N6-succinyllysine; alternate By similarity
Modified residue1181N6-acetyllysine; alternate By similarity
Modified residue1181N6-succinyllysine; alternate By similarity
Modified residue1251N6-acetyllysine; alternate By similarity
Modified residue1251N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict361T → I in CAB66655. Ref.1

Secondary structure

................. 130
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H0N5 [UniParc].

Last modified June 16, 2009. Version 4.
Checksum: 7B834F95D7ACD1EE

FASTA13014,365
        10         20         30         40         50         60 
MAAVLGALGA TRRLLAALRG QSLGLAAMSS GTHRLTAEER NQAILDLKAA GWSELSERDA 

        70         80         90        100        110        120 
IYKEFSFHNF NQAFGFMSRV ALQAEKMNHH PEWFNVYNKV QITLTSHDCG ELTKKDVKLA 

       130 
KFIEKAAASV 

« Hide

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_115527.3. NM_032151.4.
UniGeneHs.710014.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4C45X-ray1.45A28-130[»]
ProteinModelPortalQ9H0N5.
SMRQ9H0N5. Positions 32-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123893. 31 interactions.
IntActQ9H0N5. 2 interactions.
MINTMINT-4539105.
STRING9606.ENSP00000254908.

PTM databases

PhosphoSiteQ9H0N5.

Polymorphism databases

DMDM239938927.

Proteomic databases

PaxDbQ9H0N5.
PRIDEQ9H0N5.

Protocols and materials databases

DNASU84105.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254908; ENSP00000254908; ENSG00000132570.
ENST00000512783; ENSP00000421544; ENSG00000132570.
GeneID84105.
KEGGhsa:84105.
UCSCuc010jdz.3. human.

Organism-specific databases

CTD84105.
GeneCardsGC05P134241.
H-InvDBHIX0018595.
HGNCHGNC:24474. PCBD2.
HPAHPA036428.
MIM609836. gene.
neXtProtNX_Q9H0N5.
PharmGKBPA142671197.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2154.
HOGENOMHOG000007680.
HOVERGENHBG000259.
InParanoidQ9H0N5.
KOK01724.
OMADAHWLTA.
PhylomeDBQ9H0N5.
TreeFamTF300188.

Enzyme and pathway databases

BioCycMetaCyc:HS13433-MONOMER.

Gene expression databases

ArrayExpressQ9H0N5.
BgeeQ9H0N5.
CleanExHS_PCBD2.
GenevestigatorQ9H0N5.

Family and domain databases

Gene3D3.30.1360.20. 1 hit.
HAMAPMF_00434. Pterin_4_alpha.
InterProIPR001533. Trans/pterin_deHydtase.
[Graphical view]
PANTHERPTHR12599. PTHR12599. 1 hit.
PfamPF01329. Pterin_4a. 1 hit.
[Graphical view]
SUPFAMSSF55248. SSF55248. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPCBD2. human.
GeneWikiPCBD2.
GenomeRNAi84105.
NextBio73363.
PROQ9H0N5.
SOURCESearch...

Entry information

Entry namePHS2_HUMAN
AccessionPrimary (citable) accession number: Q9H0N5
Secondary accession number(s): Q8TD40
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 105 of the entry and version 4 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

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM