Q9H0N5 (PHS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.4. Source: UniProtKB protein heterooligomerization Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	4-alpha-hydroxytetrahydrobiopterin dehydratase activity Inferred from electronic annotation. Source: EC phenylalanine 4-monooxygenase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DYRK1B	Q9Y463	2	EBI-634289,EBI-634187

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 130	130	Pterin-4-alpha-carbinolamine dehydratase 2		PRO_0000063057
Experimental info
	Sequence conflict	36	1	T → I in CAB66655. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H0N5 [UniParc]. Last modified June 16, 2009. Version 4. Checksum: 7B834F95D7ACD1EE	FASTA	130	14,365
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00874020.
RefSeq	NP_115527.3. NM_032151.4.
UniGene	Hs.710014.
3D structure databases
ProteinModelPortal	Q9H0N5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H0N5. 2 interactions.
MINT	MINT-4539105.
STRING	9606.ENSP00000254908.
PTM databases
PhosphoSite	Q9H0N5.
Polymorphism databases
DMDM	239938927.
Proteomic databases
PaxDb	Q9H0N5.
PRIDE	Q9H0N5.
Protocols and materials databases
DNASU	84105.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000254908; ENSP00000254908; ENSG00000132570. ENST00000512783; ENSP00000421544; ENSG00000132570.
GeneID	84105.
KEGG	hsa:84105.
UCSC	uc010jdz.3. human.
Organism-specific databases
CTD	84105.
GeneCards	GC05P134241.
H-InvDB	HIX0018595.
HGNC	HGNC:24474. PCBD2.
HPA	HPA036428.
MIM	609836. gene.
neXtProt	NX_Q9H0N5.
PharmGKB	PA142671197.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2154.
HOGENOM	HOG000007680.
HOVERGEN	HBG000259.
InParanoid	Q9H0N5.
KO	K01724.
OMA	DAHWLTA.
OrthoDB	EOG4QNMXP.
PhylomeDB	Q9H0N5.
Gene expression databases
ArrayExpress	Q9H0N5.
Bgee	Q9H0N5.
CleanEx	HS_PCBD2.
Genevestigator	Q9H0N5.
Family and domain databases
Gene3D	3.30.1360.20. 1 hit.
InterPro	IPR001533. Trans/pterin_deHydtase. [Graphical view]
PANTHER	PTHR12599. PTHR12599. 1 hit.
Pfam	PF01329. Pterin_4a. 1 hit. [Graphical view]
SUPFAM	SSF55248. Trans_pterinDh. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PCBD2. human.
GenomeRNAi	84105.
NextBio	73363.
SOURCE	Search...

Entry information

Entry name

PHS2_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 97 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.