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Protein

Deoxyribose-phosphate aldolase

Gene

Dera

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation.By similarity

Catalytic activityi

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde.By similarity

Pathwayi: 2-deoxy-D-ribose 1-phosphate degradation

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoglucomutase-2 (Pgm2)
  2. Deoxyribose-phosphate aldolase (Dera)
This subpathway is part of the pathway 2-deoxy-D-ribose 1-phosphate degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate, the pathway 2-deoxy-D-ribose 1-phosphate degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei218 – 2181Schiff-base intermediate with acetaldehydeBy similarity
Active sitei254 – 2541By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiR-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00002; UER00468.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyribose-phosphate aldolase (EC:4.1.2.4By similarity)
Short name:
DERA
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase
Phosphodeoxyriboaldolase
Short name:
Deoxyriboaldolase
Gene namesi
Name:Dera
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1913762. Dera.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmic granule By similarity
  • Nucleus By similarity

  • Note: Recruited to stress granules but not to processing bodies upon arsenite or clotrimazole treatment or energy deprivation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Deoxyribose-phosphate aldolasePRO_0000057311Add
BLAST

Proteomic databases

EPDiQ91YP3.
MaxQBiQ91YP3.
PaxDbiQ91YP3.
PRIDEiQ91YP3.

PTM databases

iPTMnetiQ91YP3.
PhosphoSiteiQ91YP3.

Expressioni

Gene expression databases

BgeeiQ91YP3.
ExpressionAtlasiQ91YP3. baseline and differential.
GenevisibleiQ91YP3. MM.

Interactioni

Subunit structurei

Interacts with YBX1.By similarity

Protein-protein interaction databases

BioGridi231264. 1 interaction.
MINTiMINT-1869951.
STRINGi10090.ENSMUSP00000084959.

Structurei

3D structure databases

ProteinModelPortaliQ91YP3.
SMRiQ91YP3. Positions 44-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3981. Eukaryota.
COG0274. LUCA.
GeneTreeiENSGT00390000007878.
HOGENOMiHOG000241644.
HOVERGENiHBG030164.
InParanoidiQ91YP3.
KOiK01619.
OMAiKIATVTN.
OrthoDBiEOG7B5WWC.
PhylomeDBiQ91YP3.
TreeFamiTF314251.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PANTHERiPTHR10889. PTHR10889. 1 hit.
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF001357. DeoC. 1 hit.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00126. deoC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91YP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAHCRGTEL DLSWISKVQV NHAAVLRRAQ QIQARRSVKK EWQAAWLLKA
60 70 80 90 100
VTFIDLTTLS GDDTFSNVQR LCYKAKYPIR ADLLKALNMD DKGITTAAVC
110 120 130 140 150
VYPARVCDAV KALKAAGCSI PVASVATGFP AGQTHLKTRL EEIRLAVEDG
160 170 180 190 200
ATEIDVVINR TLVLTGQWEA LYDEVTQFRK ACGEAHLKTI LATGELGSLT
210 220 230 240 250
NVYKASLVAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI RDFFWKTGNK
260 270 280 290 300
VGFKPAGGIR TAKESLAWLS LVKEELGDEW LTPDLFRIGA SSLLSDIERQ
310
IYHHVTGRYA AYHDLPMS
Length:318
Mass (Da):34,975
Last modified:December 1, 2001 - v1
Checksum:i1C7DE27CF423816F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK083298 mRNA. Translation: BAC38850.1.
AK145820 mRNA. Translation: BAE26672.1.
AK150273 mRNA. Translation: BAE29429.1.
AK150712 mRNA. Translation: BAE29790.1.
AK152462 mRNA. Translation: BAE31239.1.
AK169418 mRNA. Translation: BAE41164.1.
BC016218 mRNA. Translation: AAH16218.1.
CCDSiCCDS20666.1.
RefSeqiNP_766321.1. NM_172733.1.
UniGeneiMm.29181.

Genome annotation databases

EnsembliENSMUST00000087675; ENSMUSP00000084959; ENSMUSG00000030225.
GeneIDi232449.
KEGGimmu:232449.
UCSCiuc009enh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK083298 mRNA. Translation: BAC38850.1.
AK145820 mRNA. Translation: BAE26672.1.
AK150273 mRNA. Translation: BAE29429.1.
AK150712 mRNA. Translation: BAE29790.1.
AK152462 mRNA. Translation: BAE31239.1.
AK169418 mRNA. Translation: BAE41164.1.
BC016218 mRNA. Translation: AAH16218.1.
CCDSiCCDS20666.1.
RefSeqiNP_766321.1. NM_172733.1.
UniGeneiMm.29181.

3D structure databases

ProteinModelPortaliQ91YP3.
SMRiQ91YP3. Positions 44-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231264. 1 interaction.
MINTiMINT-1869951.
STRINGi10090.ENSMUSP00000084959.

PTM databases

iPTMnetiQ91YP3.
PhosphoSiteiQ91YP3.

Proteomic databases

EPDiQ91YP3.
MaxQBiQ91YP3.
PaxDbiQ91YP3.
PRIDEiQ91YP3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087675; ENSMUSP00000084959; ENSMUSG00000030225.
GeneIDi232449.
KEGGimmu:232449.
UCSCiuc009enh.1. mouse.

Organism-specific databases

CTDi51071.
MGIiMGI:1913762. Dera.

Phylogenomic databases

eggNOGiKOG3981. Eukaryota.
COG0274. LUCA.
GeneTreeiENSGT00390000007878.
HOGENOMiHOG000241644.
HOVERGENiHBG030164.
InParanoidiQ91YP3.
KOiK01619.
OMAiKIATVTN.
OrthoDBiEOG7B5WWC.
PhylomeDBiQ91YP3.
TreeFamiTF314251.

Enzyme and pathway databases

UniPathwayiUPA00002; UER00468.
ReactomeiR-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

ChiTaRSiDera. mouse.
NextBioi381127.
PROiQ91YP3.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YP3.
ExpressionAtlasiQ91YP3. baseline and differential.
GenevisibleiQ91YP3. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PANTHERiPTHR10889. PTHR10889. 1 hit.
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF001357. DeoC. 1 hit.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00126. deoC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Heart, Liver and Placenta.
  2. "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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiDEOC_MOUSE
AccessioniPrimary (citable) accession number: Q91YP3
Secondary accession number(s): Q3UD33, Q9CZI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.