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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
PTM	Acetylation
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 tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-alpha-hydroxytetrahydrobiopterin dehydratase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction Ref.4. Source: UniProtKB
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
Amino acid modifications
	Modified residue	125	1	N6-acetyllysine Ref.5
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: 11230166] [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: 15372022] [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: 15489334] [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: 11980910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-130, FUNCTION IN HNF-1-ALPHA REGULATION, INTERACTION WITH DYRK1B. Tissue: Skeletal muscle.
[5]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, MASS SPECTROMETRY.
+	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.
SMR	Q9H0N5. Positions 35-128.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H0N5. 2 interactions.
STRING	Q9H0N5.
PTM databases
PhosphoSite	Q9H0N5.
Polymorphism databases
DMDM	239938927.
Proteomic databases
PRIDE	Q9H0N5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000254908; ENSP00000254908; ENSG00000132570.
GeneID	84105.
KEGG	hsa:84105.
UCSC	uc010jdz.1. 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	prNOG20590.
GeneTree	ENSGT00390000007221.
HOGENOM	HBG705804.
HOVERGEN	HBG000259.
InParanoid	Q9H0N5.
OMA	TSHDCGE.
OrthoDB	EOG4QNMXP.
PhylomeDB	Q9H0N5.
Gene expression databases
ArrayExpress	Q9H0N5.
Bgee	Q9H0N5.
CleanEx	HS_PCBD2.
Genevestigator	Q9H0N5.
Family and domain databases
InterPro	IPR001533. Trans/pterin_deHydtase. [Graphical view]
Gene3D	G3DSA:3.30.1360.20. Trans_pterinDh. 1 hit.
KO	K01724.
PANTHER	PTHR12599. Trans_pterinDh. 1 hit.
Pfam	PF01329. Pterin_4a. 1 hit. [Graphical view]
SUPFAM	SSF55248. Trans_pterinDh. 1 hit.
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 83 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.