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Protein

Ribose-5-phosphate isomerase

Gene

Rpia

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

Functioni

Catalytic activityi

D-ribose 5-phosphate = D-ribulose 5-phosphate.

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-5-phosphate isomerase (Rpia)
This subpathway is part of the pathway pentose phosphate pathway, 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-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

GO - Molecular functioni

  • monosaccharide binding Source: Ensembl
  • ribose-5-phosphate isomerase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiR-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00115; UER00412.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-5-phosphate isomerase (EC:5.3.1.6)
Alternative name(s):
Phosphoriboisomerase
Gene namesi
Name:Rpia
Synonyms:Rpi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103254. Rpia.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Ribose-5-phosphate isomerasePRO_0000158522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP47968.
MaxQBiP47968.
PaxDbiP47968.
PeptideAtlasiP47968.
PRIDEiP47968.

PTM databases

iPTMnetiP47968.
PhosphoSiteiP47968.
SwissPalmiP47968.

Expressioni

Tissue specificityi

Found in the spleen, kidney, thymus, heart, brain and lung. Higher levels are found in testis.1 Publication

Gene expression databases

BgeeiP47968.
CleanExiMM_RPIA.
GenevisibleiP47968. MM.

Interactioni

Protein-protein interaction databases

IntActiP47968. 1 interaction.
MINTiMINT-4133120.
STRINGi10090.ENSMUSP00000064158.

Structurei

3D structure databases

ProteinModelPortaliP47968.
SMRiP47968. Positions 72-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3075. Eukaryota.
COG0120. LUCA.
GeneTreeiENSGT00390000004352.
HOGENOMiHOG000276369.
HOVERGENiHBG017746.
InParanoidiP47968.
KOiK01807.
OMAiDEVDRHM.
OrthoDBiEOG7V1FS4.
TreeFamiTF105758.

Family and domain databases

HAMAPiMF_00170. Rib_5P_isom_A.
InterProiIPR004788. Ribose5P_isomerase_typA.
IPR020672. Ribose5P_isomerase_typA_subgr.
[Graphical view]
PANTHERiPTHR11934. PTHR11934. 1 hit.
PfamiPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00021. rpiA. 1 hit.

Sequencei

Sequence statusi: Complete.

P47968-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRPGPFSTL YGRVLAPLPG RAGGAASGGG GNNWGLSGSH VQLPGRAHSE
60 70 80 90 100
TRGDKGGSSA GGPAPSTMSK AEEAKKLASH TAVENHVKNN QVLGIGSGST
110 120 130 140 150
IVHAVQRIAE RVKQENLDLI CIPTSFQARQ LILQYGLTLS DLDQHPEIDL
160 170 180 190 200
AIDGADEVDA ELNLIKGGGG CLTQEKIVAG YASRFIVIAD FRKDSKNLGD
210 220 230 240 250
RWHKGIPIEV IPMAYVPVSR AVAQKFGGEV ELRMAVNKAG PVVTDNGNFI
260 270 280 290 300
LDWKFDRVHK WSEVNTAIKM TPGVVDTGLF INMAERVYFG MQDGSVNVRE

KPF
Length:303
Mass (Da):32,451
Last modified:July 24, 2007 - v2
Checksum:iF8535B80A9D823C8
GO

Sequence cautioni

The sequence AAC42060.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23281.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841E → D in BAE23281 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35034 mRNA. Translation: AAC42060.1. Different initiation.
AK137235 mRNA. Translation: BAE23281.1. Different initiation.
BC053526 mRNA. Translation: AAH53526.2.
CCDSiCCDS39504.1.
PIRiI53951.
RefSeqiNP_033101.2. NM_009075.2.
UniGeneiMm.17905.

Genome annotation databases

EnsembliENSMUST00000066134; ENSMUSP00000064158; ENSMUSG00000053604.
GeneIDi19895.
KEGGimmu:19895.
UCSCiuc009cfy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35034 mRNA. Translation: AAC42060.1. Different initiation.
AK137235 mRNA. Translation: BAE23281.1. Different initiation.
BC053526 mRNA. Translation: AAH53526.2.
CCDSiCCDS39504.1.
PIRiI53951.
RefSeqiNP_033101.2. NM_009075.2.
UniGeneiMm.17905.

3D structure databases

ProteinModelPortaliP47968.
SMRiP47968. Positions 72-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP47968. 1 interaction.
MINTiMINT-4133120.
STRINGi10090.ENSMUSP00000064158.

PTM databases

iPTMnetiP47968.
PhosphoSiteiP47968.
SwissPalmiP47968.

Proteomic databases

EPDiP47968.
MaxQBiP47968.
PaxDbiP47968.
PeptideAtlasiP47968.
PRIDEiP47968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066134; ENSMUSP00000064158; ENSMUSG00000053604.
GeneIDi19895.
KEGGimmu:19895.
UCSCiuc009cfy.1. mouse.

Organism-specific databases

CTDi22934.
MGIiMGI:103254. Rpia.

Phylogenomic databases

eggNOGiKOG3075. Eukaryota.
COG0120. LUCA.
GeneTreeiENSGT00390000004352.
HOGENOMiHOG000276369.
HOVERGENiHBG017746.
InParanoidiP47968.
KOiK01807.
OMAiDEVDRHM.
OrthoDBiEOG7V1FS4.
TreeFamiTF105758.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00412.
ReactomeiR-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

PROiP47968.
SOURCEiSearch...

Gene expression databases

BgeeiP47968.
CleanExiMM_RPIA.
GenevisibleiP47968. MM.

Family and domain databases

HAMAPiMF_00170. Rib_5P_isom_A.
InterProiIPR004788. Ribose5P_isomerase_typA.
IPR020672. Ribose5P_isomerase_typA_subgr.
[Graphical view]
PANTHERiPTHR11934. PTHR11934. 1 hit.
PfamiPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00021. rpiA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ribose 5-phosphate isomerase-encoding gene is located immediately downstream from that encoding murine immunoglobulin kappa."
    Apel T.W., Scherer A., Adachi T., Auch D., Ayane M., Reth M.
    Gene 156:191-197(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Pre-B cell.
  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 48-303.
    Strain: C57BL/6J.
    Tissue: Urinary bladder.
  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] OF 52-303.
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiRPIA_MOUSE
AccessioniPrimary (citable) accession number: P47968
Secondary accession number(s): Q3UVI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 24, 2007
Last modified: July 6, 2016
This is version 118 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

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.