Full text data of PCBD2
PCBD2
(DCOH2, DCOHM)
[Confidence: low (only semi-automatic identification from reviews)]
Pterin-4-alpha-carbinolamine dehydratase 2; PHS 2; 4.2.1.96 (4-alpha-hydroxy-tetrahydropterin dehydratase 2; DcoH-like protein DCoHm; Dimerization cofactor of hepatocyte nuclear factor 1 from muscle; HNF-1-alpha dimerization cofactor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Pterin-4-alpha-carbinolamine dehydratase 2; PHS 2; 4.2.1.96 (4-alpha-hydroxy-tetrahydropterin dehydratase 2; DcoH-like protein DCoHm; Dimerization cofactor of hepatocyte nuclear factor 1 from muscle; HNF-1-alpha dimerization cofactor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H0N5
ID PHS2_HUMAN Reviewed; 130 AA.
AC Q9H0N5; Q8TD40;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-JUN-2009, sequence version 4.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase 2;
DE Short=PHS 2;
DE EC=4.2.1.96;
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase 2;
DE AltName: Full=DcoH-like protein DCoHm;
DE AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1 from muscle;
DE AltName: Full=HNF-1-alpha dimerization cofactor;
GN Name=PCBD2; Synonyms=DCOH2, DCOHM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-130, FUNCTION IN HNF-1-ALPHA
RP REGULATION, AND INTERACTION WITH DYRK1B.
RC TISSUE=Skeletal muscle;
RX PubMed=11980910; DOI=10.1074/jbc.M203257200;
RA Lim S., Jin K., Friedman E.;
RT "Mirk protein kinase is activated by MKK3 and functions as a
RT transcriptional activator of HNF1alpha.";
RL J. Biol. Chem. 277:25040-25046(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to
CC both prevent the formation of 7-pterins and accelerate the
CC formation of quinonoid-BH2 (By similarity).
CC -!- FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-
CC alpha and enhances its transcriptional activity.
CC -!- CATALYTIC ACTIVITY: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-
CC 5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-
CC dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
CC -!- SUBUNIT: Homotetramer. Interacts with DYRK1B.
CC -!- INTERACTION:
CC Q9Y463:DYRK1B; NbExp=2; IntAct=EBI-634289, EBI-634187;
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine
CC dehydratase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM18136.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL136721; CAB66655.1; -; mRNA.
DR EMBL; AC006077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054021; AAH54021.1; -; mRNA.
DR EMBL; AF499009; AAM18136.1; ALT_INIT; mRNA.
DR RefSeq; NP_115527.3; NM_032151.4.
DR UniGene; Hs.710014; -.
DR PDB; 4C45; X-ray; 1.45 A; A=28-130.
DR PDBsum; 4C45; -.
DR ProteinModelPortal; Q9H0N5; -.
DR SMR; Q9H0N5; 35-128.
DR IntAct; Q9H0N5; 2.
DR MINT; MINT-4539105; -.
DR STRING; 9606.ENSP00000254908; -.
DR PhosphoSite; Q9H0N5; -.
DR DMDM; 239938927; -.
DR PaxDb; Q9H0N5; -.
DR PRIDE; Q9H0N5; -.
DR DNASU; 84105; -.
DR Ensembl; ENST00000254908; ENSP00000254908; ENSG00000132570.
DR Ensembl; ENST00000512783; ENSP00000421544; ENSG00000132570.
DR GeneID; 84105; -.
DR KEGG; hsa:84105; -.
DR UCSC; uc010jdz.3; human.
DR CTD; 84105; -.
DR GeneCards; GC05P134241; -.
DR H-InvDB; HIX0018595; -.
DR HGNC; HGNC:24474; PCBD2.
DR HPA; HPA036428; -.
DR MIM; 609836; gene.
DR neXtProt; NX_Q9H0N5; -.
DR PharmGKB; PA142671197; -.
DR eggNOG; COG2154; -.
DR HOGENOM; HOG000007680; -.
DR HOVERGEN; HBG000259; -.
DR InParanoid; Q9H0N5; -.
DR KO; K01724; -.
DR OMA; DAHWLTA; -.
DR PhylomeDB; Q9H0N5; -.
DR BioCyc; MetaCyc:HS13433-MONOMER; -.
DR ChiTaRS; PCBD2; human.
DR GeneWiki; PCBD2; -.
DR GenomeRNAi; 84105; -.
DR NextBio; 73363; -.
DR PRO; PR:Q9H0N5; -.
DR ArrayExpress; Q9H0N5; -.
DR Bgee; Q9H0N5; -.
DR CleanEx; HS_PCBD2; -.
DR Genevestigator; Q9H0N5; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.20; -; 1.
DR InterPro; IPR001533; Trans/pterin_deHydtase.
DR PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Lyase;
KW Reference proteome; Tetrahydrobiopterin biosynthesis.
FT CHAIN 1 130 Pterin-4-alpha-carbinolamine dehydratase
FT 2.
FT /FTId=PRO_0000063057.
FT MOD_RES 114 114 N6-acetyllysine (By similarity).
FT MOD_RES 118 118 N6-acetyllysine (By similarity).
FT MOD_RES 125 125 N6-acetyllysine (By similarity).
FT CONFLICT 36 36 T -> I (in Ref. 1; CAB66655).
FT HELIX 37 49
FT STRAND 56 59
FT STRAND 61 66
FT HELIX 70 87
FT STRAND 92 96
FT STRAND 99 104
FT TURN 107 110
FT HELIX 114 128
SQ SEQUENCE 130 AA; 14365 MW; 7B834F95D7ACD1EE CRC64;
MAAVLGALGA TRRLLAALRG QSLGLAAMSS GTHRLTAEER NQAILDLKAA GWSELSERDA
IYKEFSFHNF NQAFGFMSRV ALQAEKMNHH PEWFNVYNKV QITLTSHDCG ELTKKDVKLA
KFIEKAAASV
//
ID PHS2_HUMAN Reviewed; 130 AA.
AC Q9H0N5; Q8TD40;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-JUN-2009, sequence version 4.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase 2;
DE Short=PHS 2;
DE EC=4.2.1.96;
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase 2;
DE AltName: Full=DcoH-like protein DCoHm;
DE AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1 from muscle;
DE AltName: Full=HNF-1-alpha dimerization cofactor;
GN Name=PCBD2; Synonyms=DCOH2, DCOHM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-130, FUNCTION IN HNF-1-ALPHA
RP REGULATION, AND INTERACTION WITH DYRK1B.
RC TISSUE=Skeletal muscle;
RX PubMed=11980910; DOI=10.1074/jbc.M203257200;
RA Lim S., Jin K., Friedman E.;
RT "Mirk protein kinase is activated by MKK3 and functions as a
RT transcriptional activator of HNF1alpha.";
RL J. Biol. Chem. 277:25040-25046(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to
CC both prevent the formation of 7-pterins and accelerate the
CC formation of quinonoid-BH2 (By similarity).
CC -!- FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-
CC alpha and enhances its transcriptional activity.
CC -!- CATALYTIC ACTIVITY: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-
CC 5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-
CC dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
CC -!- SUBUNIT: Homotetramer. Interacts with DYRK1B.
CC -!- INTERACTION:
CC Q9Y463:DYRK1B; NbExp=2; IntAct=EBI-634289, EBI-634187;
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine
CC dehydratase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM18136.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL136721; CAB66655.1; -; mRNA.
DR EMBL; AC006077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054021; AAH54021.1; -; mRNA.
DR EMBL; AF499009; AAM18136.1; ALT_INIT; mRNA.
DR RefSeq; NP_115527.3; NM_032151.4.
DR UniGene; Hs.710014; -.
DR PDB; 4C45; X-ray; 1.45 A; A=28-130.
DR PDBsum; 4C45; -.
DR ProteinModelPortal; Q9H0N5; -.
DR SMR; Q9H0N5; 35-128.
DR IntAct; Q9H0N5; 2.
DR MINT; MINT-4539105; -.
DR STRING; 9606.ENSP00000254908; -.
DR PhosphoSite; Q9H0N5; -.
DR DMDM; 239938927; -.
DR PaxDb; Q9H0N5; -.
DR PRIDE; Q9H0N5; -.
DR DNASU; 84105; -.
DR Ensembl; ENST00000254908; ENSP00000254908; ENSG00000132570.
DR Ensembl; ENST00000512783; ENSP00000421544; ENSG00000132570.
DR GeneID; 84105; -.
DR KEGG; hsa:84105; -.
DR UCSC; uc010jdz.3; human.
DR CTD; 84105; -.
DR GeneCards; GC05P134241; -.
DR H-InvDB; HIX0018595; -.
DR HGNC; HGNC:24474; PCBD2.
DR HPA; HPA036428; -.
DR MIM; 609836; gene.
DR neXtProt; NX_Q9H0N5; -.
DR PharmGKB; PA142671197; -.
DR eggNOG; COG2154; -.
DR HOGENOM; HOG000007680; -.
DR HOVERGEN; HBG000259; -.
DR InParanoid; Q9H0N5; -.
DR KO; K01724; -.
DR OMA; DAHWLTA; -.
DR PhylomeDB; Q9H0N5; -.
DR BioCyc; MetaCyc:HS13433-MONOMER; -.
DR ChiTaRS; PCBD2; human.
DR GeneWiki; PCBD2; -.
DR GenomeRNAi; 84105; -.
DR NextBio; 73363; -.
DR PRO; PR:Q9H0N5; -.
DR ArrayExpress; Q9H0N5; -.
DR Bgee; Q9H0N5; -.
DR CleanEx; HS_PCBD2; -.
DR Genevestigator; Q9H0N5; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.20; -; 1.
DR InterPro; IPR001533; Trans/pterin_deHydtase.
DR PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Lyase;
KW Reference proteome; Tetrahydrobiopterin biosynthesis.
FT CHAIN 1 130 Pterin-4-alpha-carbinolamine dehydratase
FT 2.
FT /FTId=PRO_0000063057.
FT MOD_RES 114 114 N6-acetyllysine (By similarity).
FT MOD_RES 118 118 N6-acetyllysine (By similarity).
FT MOD_RES 125 125 N6-acetyllysine (By similarity).
FT CONFLICT 36 36 T -> I (in Ref. 1; CAB66655).
FT HELIX 37 49
FT STRAND 56 59
FT STRAND 61 66
FT HELIX 70 87
FT STRAND 92 96
FT STRAND 99 104
FT TURN 107 110
FT HELIX 114 128
SQ SEQUENCE 130 AA; 14365 MW; 7B834F95D7ACD1EE CRC64;
MAAVLGALGA TRRLLAALRG QSLGLAAMSS GTHRLTAEER NQAILDLKAA GWSELSERDA
IYKEFSFHNF NQAFGFMSRV ALQAEKMNHH PEWFNVYNKV QITLTSHDCG ELTKKDVKLA
KFIEKAAASV
//
MIM
609836
*RECORD*
*FIELD* NO
609836
*FIELD* TI
*609836 PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE 2; PCBD2
;;DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA 2; DCOH2;;
read moreDIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1 FROM MUSCLE;
DCOHM
*FIELD* TX
CLONING
Using MIRK (DYRK1B; 604556) as bait in a yeast 2-hybrid screen of a
human skeletal muscle cDNA library, Lim et al. (2002) identified PCBD2,
which they called DCOHM, encoding a deduced 103-amino acid protein. The
DCOHM protein shares 78% sequence identity with DCOH (PCBD1; 126090).
Rose et al. (2004) identified the mouse homolog and determined the
high-resolution crystal structure of Dcoh2. Dcoh1 and Dcoh2 dimers adopt
the same fold, and their structural differences are confined largely to
the protein surfaces and tetramer interface.
GENE FUNCTION
Using coimmunoprecipitation studies and GST pull-down assays, Lim et al.
(2002) confirmed the interaction of MIRK and DCOHM. DCOH stabilizes
HNF1-alpha (142410) as a dimer and enhances its transcriptional
activity. Using a reporter gene construct, Lim et al. (2002) showed that
DCOHM has a similar activity. In GST pull-down assays, Lim et al. (2002)
found that DCOHM, MIRK, and HNF1-alpha form a complex, and that a direct
interaction between MIRK and HNF1-alpha can occur in the absence of
DCOHM. Lim et al. (2002) concluded that MIRK binds to DCOHM in a
DCOHM/HNF1-alpha tetramer, enabling it to bind and phosphorylate
HNF1-alpha.
Rose et al. (2004) compared the properties of mouse Dcoh1 with those of
Dcoh2. Like Dcoh1, Dcoh2 forms a tetramer, displays
pterin-4-alpha-carbinolamine dehydratase activity, and binds Hnf1-alpha
in vitro and in vivo. Deletion mutant experiments demonstrated that
Dcoh2 binds to the N-terminal dimerization domain of Hnf1-alpha. Unlike
the hyperstable Dcoh1 tetramer, Dcoh2 readily disproportionates and
forms a 2:2 complex with Hnf1-alpha in vitro. Rose et al. (2004)
measured the exchange of monomers in preformed Hnf1-alpha dimers and
found that both Dcoh1 and Dcoh2 stabilize Hnf1-alpha dimers.
MAPPING
By sequence analysis, Rose et al. (2004) mapped the DCOHM gene to
chromosome 5q31.2.
*FIELD* RF
1. Lim, S.; Jin, K.; Friedman, E.: Mirk protein kinase is activated
by MKK3 and functions as a transcriptional activator of HNF1-alpha. J.
Biol. Chem. 277: 25040-25046, 2002. Note: Erratum: J. Biol. Chem.
277: 5047 only, 2004.
2. Rose, R. B.; Pullen, K. E.; Bayle, J. H.; Crabtree, G. R.; Alber,
T.: Biochemical and structural basis for partially redundant enzymatic
and transcriptional functions of DCoH and DCoH2. Biochemistry 43:
7345-7355, 2004.
*FIELD* CD
Jennifer L. Goldstein: 1/19/2006
*FIELD* ED
terry: 06/04/2012
wwang: 10/24/2007
carol: 1/20/2006
*RECORD*
*FIELD* NO
609836
*FIELD* TI
*609836 PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE 2; PCBD2
;;DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA 2; DCOH2;;
read moreDIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1 FROM MUSCLE;
DCOHM
*FIELD* TX
CLONING
Using MIRK (DYRK1B; 604556) as bait in a yeast 2-hybrid screen of a
human skeletal muscle cDNA library, Lim et al. (2002) identified PCBD2,
which they called DCOHM, encoding a deduced 103-amino acid protein. The
DCOHM protein shares 78% sequence identity with DCOH (PCBD1; 126090).
Rose et al. (2004) identified the mouse homolog and determined the
high-resolution crystal structure of Dcoh2. Dcoh1 and Dcoh2 dimers adopt
the same fold, and their structural differences are confined largely to
the protein surfaces and tetramer interface.
GENE FUNCTION
Using coimmunoprecipitation studies and GST pull-down assays, Lim et al.
(2002) confirmed the interaction of MIRK and DCOHM. DCOH stabilizes
HNF1-alpha (142410) as a dimer and enhances its transcriptional
activity. Using a reporter gene construct, Lim et al. (2002) showed that
DCOHM has a similar activity. In GST pull-down assays, Lim et al. (2002)
found that DCOHM, MIRK, and HNF1-alpha form a complex, and that a direct
interaction between MIRK and HNF1-alpha can occur in the absence of
DCOHM. Lim et al. (2002) concluded that MIRK binds to DCOHM in a
DCOHM/HNF1-alpha tetramer, enabling it to bind and phosphorylate
HNF1-alpha.
Rose et al. (2004) compared the properties of mouse Dcoh1 with those of
Dcoh2. Like Dcoh1, Dcoh2 forms a tetramer, displays
pterin-4-alpha-carbinolamine dehydratase activity, and binds Hnf1-alpha
in vitro and in vivo. Deletion mutant experiments demonstrated that
Dcoh2 binds to the N-terminal dimerization domain of Hnf1-alpha. Unlike
the hyperstable Dcoh1 tetramer, Dcoh2 readily disproportionates and
forms a 2:2 complex with Hnf1-alpha in vitro. Rose et al. (2004)
measured the exchange of monomers in preformed Hnf1-alpha dimers and
found that both Dcoh1 and Dcoh2 stabilize Hnf1-alpha dimers.
MAPPING
By sequence analysis, Rose et al. (2004) mapped the DCOHM gene to
chromosome 5q31.2.
*FIELD* RF
1. Lim, S.; Jin, K.; Friedman, E.: Mirk protein kinase is activated
by MKK3 and functions as a transcriptional activator of HNF1-alpha. J.
Biol. Chem. 277: 25040-25046, 2002. Note: Erratum: J. Biol. Chem.
277: 5047 only, 2004.
2. Rose, R. B.; Pullen, K. E.; Bayle, J. H.; Crabtree, G. R.; Alber,
T.: Biochemical and structural basis for partially redundant enzymatic
and transcriptional functions of DCoH and DCoH2. Biochemistry 43:
7345-7355, 2004.
*FIELD* CD
Jennifer L. Goldstein: 1/19/2006
*FIELD* ED
terry: 06/04/2012
wwang: 10/24/2007
carol: 1/20/2006