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Q9H0N5

- PHS2_HUMAN

UniProt

Q9H0N5 - PHS2_HUMAN

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Protein

Pterin-4-alpha-carbinolamine dehydratase 2

Gene

PCBD2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 31 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 – 4913
Beta strandi56 – 594
Beta strandi61 – 666
Helixi70 – 8718
Beta strandi92 – 965
Beta strandi99 – 1046
Turni107 – 1104
Helixi114 – 12815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiTSHDCGE.
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.

Experimental Info

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS43364.1.
RefSeqi NP_115527.3. NM_032151.4.
UniGenei Hs.710014.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4C45 X-ray 1.45 A 28-130 [» ]
ProteinModelPortali Q9H0N5.
SMRi Q9H0N5. Positions 32-130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123893. 31 interactions.
IntActi Q9H0N5. 2 interactions.
MINTi MINT-4539105.
STRINGi 9606.ENSP00000254908.

PTM databases

PhosphoSitei Q9H0N5.

Polymorphism databases

DMDMi 239938927.

Proteomic databases

MaxQBi Q9H0N5.
PaxDbi Q9H0N5.
PRIDEi Q9H0N5.

Protocols and materials databases

DNASUi 84105.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254908 ; ENSP00000254908 ; ENSG00000132570 .
ENST00000512783 ; ENSP00000421544 ; ENSG00000132570 .
GeneIDi 84105.
KEGGi hsa:84105.
UCSCi uc010jdz.3. human.

Organism-specific databases

CTDi 84105.
GeneCardsi GC05P134241.
H-InvDB HIX0018595.
HGNCi HGNC:24474. PCBD2.
HPAi HPA036428.
MIMi 609836. gene.
neXtProti NX_Q9H0N5.
PharmGKBi PA142671197.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2154.
GeneTreei ENSGT00390000007221.
HOGENOMi HOG000007680.
HOVERGENi HBG000259.
InParanoidi Q9H0N5.
KOi K01724.
OMAi TSHDCGE.
PhylomeDBi Q9H0N5.
TreeFami TF300188.

Enzyme and pathway databases

BioCyci MetaCyc:HS13433-MONOMER.

Miscellaneous databases

ChiTaRSi PCBD2. human.
GeneWikii PCBD2.
GenomeRNAii 84105.
NextBioi 73363.
PROi Q9H0N5.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0N5.
CleanExi HS_PCBD2.
ExpressionAtlasi Q9H0N5. baseline and differential.
Genevestigatori Q9H0N5.

Family and domain databases

Gene3Di 3.30.1360.20. 1 hit.
HAMAPi MF_00434. Pterin_4_alpha.
InterProi IPR001533. Trans/pterin_deHydtase.
[Graphical view ]
PANTHERi PTHR12599. PTHR12599. 1 hit.
Pfami PF01329. Pterin_4a. 1 hit.
[Graphical view ]
SUPFAMi SSF55248. SSF55248. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 110 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