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Q9H0N5

- PHS2_HUMAN

UniProt

Q9H0N5 - PHS2_HUMAN

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
  1. 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
    3. protein binding Source: UniProtKB

    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

    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

    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

    ArrayExpressiQ9H0N5.
    BgeeiQ9H0N5.
    CleanExiHS_PCBD2.
    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.
    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

    MAAVLGALGA TRRLLAALRG QSLGLAAMSS GTHRLTAEER NQAILDLKAA    50
    GWSELSERDA IYKEFSFHNF NQAFGFMSRV ALQAEKMNHH PEWFNVYNKV 100
    QITLTSHDCG ELTKKDVKLA KFIEKAAASV 130
    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.
    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

    ArrayExpressi Q9H0N5.
    Bgeei Q9H0N5.
    CleanExi HS_PCBD2.
    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

    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 1, 2014
    This is version 109 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