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Protein

Pterin-4-alpha-carbinolamine dehydratase 2

Gene

Pcbd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: MGI
  • protein heterooligomerization Source: MGI
  • protein homotetramerization Source: MGI
  • tetrahydrobiopterin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Enzyme and pathway databases

BRENDAi4.2.1.96. 3474.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1919812. Pcbd2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 136136Pterin-4-alpha-carbinolamine dehydratase 2PRO_0000063058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201N6-acetyllysine; alternateCombined sources
Modified residuei120 – 1201N6-succinyllysine; alternateCombined sources
Modified residuei124 – 1241N6-acetyllysine; alternateCombined sources
Modified residuei124 – 1241N6-succinyllysine; alternateCombined sources
Modified residuei131 – 1311N6-acetyllysine; alternateCombined sources
Modified residuei131 – 1311N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CZL5.
MaxQBiQ9CZL5.
PaxDbiQ9CZL5.
PeptideAtlasiQ9CZL5.
PRIDEiQ9CZL5.

PTM databases

iPTMnetiQ9CZL5.
PhosphoSiteiQ9CZL5.

Expressioni

Gene expression databases

BgeeiQ9CZL5.
GenevisibleiQ9CZL5. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with DYRK1B (By similarity).By similarity

Protein-protein interaction databases

BioGridi215439. 2 interactions.
IntActiQ9CZL5. 2 interactions.
MINTiMINT-4092896.
STRINGi10090.ENSMUSP00000021958.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5513Combined sources
Beta strandi62 – 654Combined sources
Beta strandi67 – 726Combined sources
Helixi76 – 9318Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi105 – 1106Combined sources
Turni113 – 1164Combined sources
Helixi120 – 13314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RU0X-ray1.60A/B36-136[»]
4WILX-ray1.36A/B34-136[»]
ProteinModelPortaliQ9CZL5.
SMRiQ9CZL5. Positions 37-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CZL5.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 119Poly-Ala

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4073. Eukaryota.
COG2154. LUCA.
GeneTreeiENSGT00390000007221.
HOGENOMiHOG000007680.
HOVERGENiHBG000259.
InParanoidiQ9CZL5.
KOiK01724.
OMAiMSADAHW.
OrthoDBiEOG7034K1.
PhylomeDBiQ9CZL5.
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.

Q9CZL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAAAAVAVA AVGARSAGRW LAALRSPGAS RAAMSSDAQW LTAEERDQLI
60 70 80 90 100
PGLKAAGWSE LSERDAIYKE FSFKNFNQAF GFMSRVALQA EKMNHHPEWF
110 120 130
NVYNKVQITL TSHDCGGLTK RDVKLAQFIE KAAASL
Length:136
Mass (Da):14,830
Last modified:June 16, 2009 - v2
Checksum:i5E447CDD57CF7496
GO

Sequence cautioni

The sequence AAH28642.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB28260.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC028642 mRNA. Translation: AAH28642.1. Different initiation.
AK012465 mRNA. Translation: BAB28260.1. Different initiation.
CCDSiCCDS26554.1.
RefSeqiNP_082557.1. NM_028281.1.
UniGeneiMm.28145.

Genome annotation databases

EnsembliENSMUST00000021958; ENSMUSP00000021958; ENSMUSG00000021496.
GeneIDi72562.
KEGGimmu:72562.
UCSCiuc007qrz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC028642 mRNA. Translation: AAH28642.1. Different initiation.
AK012465 mRNA. Translation: BAB28260.1. Different initiation.
CCDSiCCDS26554.1.
RefSeqiNP_082557.1. NM_028281.1.
UniGeneiMm.28145.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RU0X-ray1.60A/B36-136[»]
4WILX-ray1.36A/B34-136[»]
ProteinModelPortaliQ9CZL5.
SMRiQ9CZL5. Positions 37-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215439. 2 interactions.
IntActiQ9CZL5. 2 interactions.
MINTiMINT-4092896.
STRINGi10090.ENSMUSP00000021958.

PTM databases

iPTMnetiQ9CZL5.
PhosphoSiteiQ9CZL5.

Proteomic databases

EPDiQ9CZL5.
MaxQBiQ9CZL5.
PaxDbiQ9CZL5.
PeptideAtlasiQ9CZL5.
PRIDEiQ9CZL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021958; ENSMUSP00000021958; ENSMUSG00000021496.
GeneIDi72562.
KEGGimmu:72562.
UCSCiuc007qrz.1. mouse.

Organism-specific databases

CTDi84105.
MGIiMGI:1919812. Pcbd2.

Phylogenomic databases

eggNOGiKOG4073. Eukaryota.
COG2154. LUCA.
GeneTreeiENSGT00390000007221.
HOGENOMiHOG000007680.
HOVERGENiHBG000259.
InParanoidiQ9CZL5.
KOiK01724.
OMAiMSADAHW.
OrthoDBiEOG7034K1.
PhylomeDBiQ9CZL5.
TreeFamiTF300188.

Enzyme and pathway databases

BRENDAi4.2.1.96. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9CZL5.
PROiQ9CZL5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZL5.
GenevisibleiQ9CZL5. MM.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-136.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-124 AND LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-124 AND LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2."
    Rose R.B., Pullen K.E., Bayle J.H., Crabtree G.R., Alber T.
    Biochemistry 43:7345-7355(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 34-136, SUBUNIT, FUNCTION AS A PHS.

Entry informationi

Entry nameiPHS2_MOUSE
AccessioniPrimary (citable) accession number: Q9CZL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 16, 2009
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.