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Protein

Ribulose-phosphate 3-epimerase

Gene

Rpe

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.By similarity

Catalytic activityi

D-ribulose 5-phosphate = D-xylulose 5-phosphate.

Cofactori

Fe2+By similarity, Mn2+By similarity, Zn2+By similarity, Co2+By similarityNote: Binds 1 divalent metal cation per subunit. Active with Fe2+, and probably also with Mn2+, Zn2+ and Co2+.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101SubstrateBy similarity
Metal bindingi35 – 351Divalent metal cationBy similarity
Active sitei37 – 371Proton acceptorBy similarity
Metal bindingi37 – 371Divalent metal cationBy similarity
Metal bindingi70 – 701Divalent metal cationBy similarity
Binding sitei70 – 701SubstrateBy similarity
Active sitei175 – 1751Proton donorBy similarity
Metal bindingi175 – 1751Divalent metal cationBy similarity
Binding sitei177 – 1771Substrate; via amide nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Cobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose-phosphate 3-epimerase (EC:5.1.3.1)
Alternative name(s):
Ribulose-5-phosphate-epimerase
Gene namesi
Name:Rpe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1913896. Rpe.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 228227Ribulose-phosphate 3-epimerasePRO_0000171588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8VEE0.
MaxQBiQ8VEE0.
PaxDbiQ8VEE0.
PRIDEiQ8VEE0.

Expressioni

Gene expression databases

BgeeiQ8VEE0.
CleanExiMM_RPE.
ExpressionAtlasiQ8VEE0. baseline and differential.
GenevisibleiQ8VEE0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027157.

Structurei

3D structure databases

ProteinModelPortaliQ8VEE0.
SMRiQ8VEE0. Positions 4-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni146 – 1494Substrate bindingBy similarity
Regioni197 – 1982Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3111. Eukaryota.
COG0036. LUCA.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
InParanoidiQ8VEE0.
KOiK01783.
PhylomeDBiQ8VEE0.
TreeFamiTF300157.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VEE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG
60 70 80 90 100
HPVVESLRKQ LGQDPFFDMH MMVSRPEQWV KPMAVAGANQ YTFHLEATEN
110 120 130 140 150
PGALIKDIRE NGMKVGLAIK PGTTVEYLAP WANQIDMALV MTVEPGFGGQ
160 170 180 190 200
KFMEDMMPKV HWLRTQFPTL DIEVDGGVGP DTVQKCAEAG ANMIVSGSAI
210 220
MRSDDPRAVI NLLRNVCSEA AQKRSLDR
Length:228
Mass (Da):24,945
Last modified:March 1, 2002 - v1
Checksum:i81BBAF45F7EF48A8
GO

Sequence cautioni

The sequence BAC26287.1 differs from that shown.Curated
The sequence BAC26287.1 differs from that shown. Reason: Erroneous termination at position 229. Translated as stop.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007735 mRNA. No translation available.
AK017774 mRNA. Translation: BAB30922.2.
AK088152 mRNA. Translation: BAC40175.1.
AK029088 mRNA. Translation: BAC26287.1. Sequence problems.
BC019126 mRNA. Translation: AAH19126.1.
CCDSiCCDS15022.1.
RefSeqiNP_001297571.1. NM_001310642.1.
NP_001297572.1. NM_001310643.1.
NP_001297573.1. NM_001310644.1.
NP_079959.2. NM_025683.3.
UniGeneiMm.240912.

Genome annotation databases

EnsembliENSMUST00000027157; ENSMUSP00000027157; ENSMUSG00000026005.
GeneIDi66646.
KEGGimmu:66646.
UCSCiuc007bik.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007735 mRNA. No translation available.
AK017774 mRNA. Translation: BAB30922.2.
AK088152 mRNA. Translation: BAC40175.1.
AK029088 mRNA. Translation: BAC26287.1. Sequence problems.
BC019126 mRNA. Translation: AAH19126.1.
CCDSiCCDS15022.1.
RefSeqiNP_001297571.1. NM_001310642.1.
NP_001297572.1. NM_001310643.1.
NP_001297573.1. NM_001310644.1.
NP_079959.2. NM_025683.3.
UniGeneiMm.240912.

3D structure databases

ProteinModelPortaliQ8VEE0.
SMRiQ8VEE0. Positions 4-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027157.

Proteomic databases

EPDiQ8VEE0.
MaxQBiQ8VEE0.
PaxDbiQ8VEE0.
PRIDEiQ8VEE0.

Protocols and materials databases

DNASUi66646.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027157; ENSMUSP00000027157; ENSMUSG00000026005.
GeneIDi66646.
KEGGimmu:66646.
UCSCiuc007bik.1. mouse.

Organism-specific databases

CTDi6120.
MGIiMGI:1913896. Rpe.

Phylogenomic databases

eggNOGiKOG3111. Eukaryota.
COG0036. LUCA.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
InParanoidiQ8VEE0.
KOiK01783.
PhylomeDBiQ8VEE0.
TreeFamiTF300157.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8VEE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VEE0.
CleanExiMM_RPE.
ExpressionAtlasiQ8VEE0. baseline and differential.
GenevisibleiQ8VEE0. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
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 and NOD.
    Tissue: Embryo, Pancreas, Skin and Thymus.
  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].
    Tissue: Bone marrow.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRPE_MOUSE
AccessioniPrimary (citable) accession number: Q8VEE0
Secondary accession number(s): Q8C130, Q9BSB5, Q9CQZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 102 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. 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.