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Q96AT9 (RPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose-phosphate 3-epimerase

EC=5.1.3.1
Alternative name(s):
Ribulose-5-phosphate-3-epimerase
Gene names
Name:RPE
ORF Names:HUSSY-17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. Ref.8

Catalytic activity

D-ribulose 5-phosphate = D-xylulose 5-phosphate. Ref.8

Cofactor

Binds 1 divalent metal cation per subunit. Active with Fe2+, and probably also with Mn2+, Zn2+ and Co2+. Ref.8

Subunit structure

Homodimer.

Sequence similarities

Belongs to the ribulose-phosphate 3-epimerase family.

Sequence caution

The sequence BAB71076.1 differs from that shown. Reason: Frameshift at position 69.

The sequence BAC04212.1 differs from that shown. Reason: Frameshift at position 42.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-372480,EBI-372480

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96AT9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96AT9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-68: Missing.
     114-114: K → KSCSVTQAEVQWHSQGPLQ
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96AT9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
     114-114: K → KSCSVTQAEVQWHSQGPLQ
Note: Gene prediction based on EST data.
Isoform 4 (identifier: Q96AT9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     160-188: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 228227Ribulose-phosphate 3-epimerase
PRO_0000171587

Regions

Region146 – 1494Substrate binding
Region197 – 1982Substrate binding

Sites

Active site371Proton acceptor Probable
Active site1751Proton donor Probable
Metal binding351Divalent metal cation
Metal binding371Divalent metal cation
Metal binding701Divalent metal cation
Metal binding1751Divalent metal cation
Binding site101Substrate
Binding site701Substrate
Binding site1771Substrate; via amide nitrogen

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Natural variations

Alternative sequence1 – 6868Missing in isoform 3.
VSP_047117
Alternative sequence43 – 6826Missing in isoform 2.
VSP_008317
Alternative sequence1141K → KSCSVTQAEVQWHSQGPLQ in isoform 2 and isoform 3.
VSP_008318
Alternative sequence160 – 18829Missing in isoform 4.
VSP_055265

Experimental info

Mutagenesis101S → A: Nearly abolishes enzyme activity. Ref.8
Mutagenesis121L → A: Reduces enzyme activity by half. Ref.8
Mutagenesis351H → A: Alters protein structure. Nearly abolishes enzyme activity. Ref.8
Mutagenesis371D → A: Alters protein structure. Nearly abolishes enzyme activity. Ref.8
Mutagenesis391M → A: Lowers enzyme activity by 10%. Ref.8
Mutagenesis701H → A: Alters protein structure. Ref.8
Mutagenesis721M → A: Reduces enzyme activity by half. Ref.8
Mutagenesis1411M → A: No effect on enzyme activity. Ref.8
Mutagenesis1751D → A: Alters protein structure. Ref.8
Sequence conflict1801P → L in BAC04212. Ref.1

Secondary structure

............................................. 228
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 447130018AC52331

FASTA22824,928
        10         20         30         40         50         60 
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ 

        70         80         90        100        110        120 
LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN PGALIKDIRE NGMKVGLAIK 

       130        140        150        160        170        180 
PGTSVEYLAP WANQIDMALV MTVEPGFGGQ KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP 

       190        200        210        220 
DTVHKCAEAG ANMIVSGSAI MRSEDPRSVI NLLRNVCSEA AQKRSLDR 

« Hide

Isoform 2 [UniParc].

Checksum: 626FAFD9426AE406
Show »

FASTA22023,924
Isoform 3 [UniParc].

Checksum: C2D4353C7FFAEC41
Show »

FASTA17819,537
Isoform 4 [UniParc].

Checksum: 88D6C3598F28A1E1
Show »

FASTA19921,739

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Tissue: Thymus.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Bone marrow, Placenta and Skin.
[5]"Characterization of 16 novel human genes showing high similarity to yeast sequences."
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-228 (ISOFORM 1).
Tissue: Spleen.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE."
Liang W., Ouyang S., Shaw N., Joachimiak A., Zhang R., Liu Z.J.
FASEB J. 25:497-504(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH IRON ION; D-RIBULOSE 5-PHOSPHATE AND D-XYLULOSE 5-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF SER-10; LEU-12; HIS-35; ASP-37; MET-39; HIS-70; MET-72; MET-141 AND ASP-175.
[9]"Crystal structure of a D-ribulose-5-phosphate-3-epimerase (NP_954699) from Homo sapiens at 2.20 A resolution."
Joint center for structural genomics (JCSG)
Submitted (MAR-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-224 IN COMPLEX WITH ZINC AND IRON IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK056028 mRNA. Translation: BAB71076.1. Frameshift.
AK093658 mRNA. Translation: BAC04212.1. Frameshift.
AK291035 mRNA. Translation: BAF83724.1.
AK303184 mRNA. Translation: BAG64278.1.
AC007038 Genomic DNA. Translation: AAX93087.1.
CH471063 Genomic DNA. Translation: EAW70473.1.
CH471063 Genomic DNA. Translation: EAW70474.1.
BC005148 mRNA. Translation: AAH05148.2.
BC016764 mRNA. Translation: AAH16764.1.
BC072401 mRNA. Translation: AAH72401.1.
AJ224326 mRNA. Translation: CAA11895.1.
CCDSCCDS2388.1. [Q96AT9-1]
CCDS42810.1. [Q96AT9-3]
RefSeqNP_001265211.1. NM_001278282.1. [Q96AT9-3]
NP_001265212.1. NM_001278283.1. [Q96AT9-3]
NP_001265214.1. NM_001278285.1.
NP_001265215.1. NM_001278286.1.
NP_001265217.1. NM_001278288.1.
NP_001265218.1. NM_001278289.1.
NP_008847.1. NM_006916.2. [Q96AT9-3]
NP_954699.1. NM_199229.2. [Q96AT9-1]
UniGeneHs.282260.
Hs.591638.
Hs.734255.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OVPX-ray1.70A/B1-228[»]
3OVQX-ray2.00A/B1-228[»]
3OVRX-ray1.95A/B1-228[»]
3QC3X-ray2.20A/B1-224[»]
ProteinModelPortalQ96AT9.
SMRQ96AT9. Positions 4-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112040. 3 interactions.
IntActQ96AT9. 2 interactions.
MINTMINT-1448309.
STRING9606.ENSP00000352401.

Polymorphism databases

DMDM34924986.

Proteomic databases

MaxQBQ96AT9.
PaxDbQ96AT9.
PRIDEQ96AT9.

Protocols and materials databases

DNASU6120.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359429; ENSP00000352401; ENSG00000197713. [Q96AT9-1]
ENST00000429921; ENSP00000401838; ENSG00000197713. [Q96AT9-3]
ENST00000436630; ENSP00000403808; ENSG00000197713. [Q96AT9-3]
ENST00000454822; ENSP00000394455; ENSG00000197713. [Q96AT9-3]
ENST00000540255; ENSP00000439206; ENSG00000197713.
GeneID6120.
KEGGhsa:6120.
UCSCuc002vdn.4. human. [Q96AT9-1]
uc002vdo.4. human.

Organism-specific databases

CTD6120.
GeneCardsGC02P210867.
H-InvDBHIX0190555.
HGNCHGNC:10293. RPE.
HPAHPA036498.
HPA036499.
MIM180480. gene.
neXtProtNX_Q96AT9.
PharmGKBPA34654.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0036.
HOGENOMHOG000259349.
HOVERGENHBG044821.
InParanoidQ96AT9.
KOK01783.
OMAKPIICPS.
OrthoDBEOG789CC1.
PhylomeDBQ96AT9.
TreeFamTF300157.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ96AT9.
BgeeQ96AT9.
CleanExHS_RPE.
GenevestigatorQ96AT9.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERPTHR11749. PTHR11749. 1 hit.
PfamPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFPIRSF001461. RPE. 1 hit.
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01163. rpe. 1 hit.
PROSITEPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96AT9.
GeneWikiRPE_(gene).
GenomeRNAi6120.
NextBio23767.
PROQ96AT9.
SOURCESearch...

Entry information

Entry nameRPE_HUMAN
AccessionPrimary (citable) accession number: Q96AT9
Secondary accession number(s): A8K4S0 expand/collapse secondary AC list , B4E016, O43767, Q53TV9, Q8N215, Q96N34, Q9BSB5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM