RPE

Functionⁱ

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.1 Publication

Catalytic activityⁱ

D-ribulose 5-phosphate = D-xylulose 5-phosphate.1 Publication

Cofactorⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	10	Substrate	1
Metal bindingⁱ	35	Divalent metal cation	1
Active siteⁱ	37	Proton acceptorCurated	1
Metal bindingⁱ	37	Divalent metal cation	1
Metal bindingⁱ	70	Divalent metal cation	1
Binding siteⁱ	70	Substrate	1
Active siteⁱ	175	Proton donorCurated	1
Metal bindingⁱ	175	Divalent metal cation	1
Binding siteⁱ	177	Substrate; via amide nitrogen	1

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
metal ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20923965
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 20923965
ribulose-phosphate 3-epimerase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20923965

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carbohydrate metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 20923965
cellular carbohydrate metabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
pentose catabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
pentose-phosphate shunt
Source: UniProtKB
Inferred from direct assayⁱ
- 20923965
pentose-phosphate shunt, non-oxidative branch
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase
Biological process	Carbohydrate metabolism
Ligand	Cobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	5.1.3.1 2681
Reactomeⁱ	R-HSA-71336 Pentose phosphate pathway

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ribulose-phosphate 3-epimerase (EC:5.1.3.1) Alternative name(s): Ribulose-5-phosphate-3-epimerase
Gene namesⁱ	Name:RPE ORF Names:HUSSY-17
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000197713.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10293 RPE
MIMⁱ	180480 gene
neXtProtⁱ	NX_Q96AT9

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	S → A: Nearly abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	12	L → A: Reduces enzyme activity by half. 1 Publication	1
Mutagenesisⁱ	35	H → A: Alters protein structure. Nearly abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	37	D → A: Alters protein structure. Nearly abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	39	M → A: Lowers enzyme activity by 10%. 1 Publication	1
Mutagenesisⁱ	70	H → A: Alters protein structure. 1 Publication	1
Mutagenesisⁱ	72	M → A: Reduces enzyme activity by half. 1 Publication	1
Mutagenesisⁱ	141	M → A: No effect on enzyme activity. 1 Publication	1
Mutagenesisⁱ	175	D → A: Alters protein structure. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6120
Open Targets More...OpenTargetsⁱ	ENSG00000197713
PharmGKBⁱ	PA34654

Polymorphism and mutation databases

DMDMⁱ	34924986

DMDMⁱ

34924986

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000171587	2 – 228	Ribulose-phosphate 3-epimeraseAdd BLAST		227

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylalanineCombined sources		1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q96AT9
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q96AT9
PaxDbⁱ	Q96AT9
PeptideAtlas More...PeptideAtlasⁱ	Q96AT9
PRIDEⁱ	Q96AT9
ProteomicsDBⁱ	75997 75998 [Q96AT9-2]
TopDownProteomicsⁱ	Q96AT9-1 [Q96AT9-1] Q96AT9-2 [Q96AT9-2]

PTM databases

iPTMnetⁱ	Q96AT9
PhosphoSitePlusⁱ	Q96AT9

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000197713 Expressed in 215 organ(s), highest expression level in adrenal tissue
CleanExⁱ	HS_RPE
ExpressionAtlasⁱ	Q96AT9 baseline and differential
Genevisibleⁱ	Q96AT9 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA036498 HPA036499

HPAⁱ

HPA036498
HPA036499

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-372480,EBI-372480

With

Entry

#Exp.

IntAct

Notes

itself

5

EBI-372480,EBI-372480

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	112040, 51 interactors
IntActⁱ	Q96AT9, 4 interactors
STRINGⁱ	9606.ENSP00000352401

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	6 – 10	Combined sources	5
Helixⁱ	16 – 18	Combined sources	3
Helixⁱ	19 – 28	Combined sources	10
Beta strandⁱ	34 – 45	Combined sources	12
Helixⁱ	51 – 61	Combined sources	11
Beta strandⁱ	63 – 65	Combined sources	3
Beta strandⁱ	67 – 72	Combined sources	6
Helixⁱ	76 – 79	Combined sources	4
Helixⁱ	80 – 86	Combined sources	7
Beta strandⁱ	89 – 94	Combined sources	6
Helixⁱ	95 – 97	Combined sources	3
Helixⁱ	101 – 110	Combined sources	10
Beta strandⁱ	114 – 119	Combined sources	6
Helixⁱ	125 – 127	Combined sources	3
Helixⁱ	129 – 134	Combined sources	6
Beta strandⁱ	136 – 143	Combined sources	8
Turnⁱ	145 – 147	Combined sources	3
Helixⁱ	154 – 156	Combined sources	3
Helixⁱ	157 – 166	Combined sources	10
Beta strandⁱ	171 – 177	Combined sources	7
Turnⁱ	180 – 182	Combined sources	3
Helixⁱ	183 – 189	Combined sources	7
Beta strandⁱ	193 – 197	Combined sources	5
Helixⁱ	198 – 201	Combined sources	4
Helixⁱ	206 – 223	Combined sources	18

Show more details

3D structure databases

ProteinModelPortalⁱ	Q96AT9
SMRⁱ	Q96AT9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q96AT9

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	146 – 149	Substrate binding		4
Regionⁱ	197 – 198	Substrate binding		2

Sequence similaritiesⁱ

Belongs to the ribulose-phosphate 3-epimerase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3111 Eukaryota COG0036 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000001447
HOGENOMⁱ	HOG000259349
HOVERGENⁱ	HBG044821
InParanoidⁱ	Q96AT9
KEGG Orthology (KO) More...KOⁱ	K01783
OMAⁱ	CHLMIED
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0JMQ
PhylomeDBⁱ	Q96AT9
TreeFamⁱ	TF300157

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00429 RPE, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR026019 Ribul_P_3_epim IPR000056 Ribul_P_3_epim-like IPR011060 RibuloseP-bd_barrel
PANTHERⁱ	PTHR11749 PTHR11749, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00834 Ribul_P_3_epim, 1 hit
PIRSFⁱ	PIRSF001461 RPE, 1 hit
SUPFAMⁱ	SSF51366 SSF51366, 1 hit
TIGRFAMsⁱ	TIGR01163 rpe, 1 hit
PROSITEⁱ	View protein in PROSITE PS01085 RIBUL_P_3_EPIMER_1, 1 hit PS01086 RIBUL_P_3_EPIMER_2, 1 hit

Sequences (5+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 5 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 5 described isoforms and 9 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q96AT9-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG 
        60         70         80         90        100
HPVVESLRKQ LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN 
       110        120        130        140        150
PGALIKDIRE NGMKVGLAIK PGTSVEYLAP WANQIDMALV MTVEPGFGGQ 
       160        170        180        190        200
KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP DTVHKCAEAG ANMIVSGSAI 
       210        220 
MRSEDPRSVI NLLRNVCSEA AQKRSLDR

Length:228

Mass (Da):24,928

Last modified:December 1, 2001 - v1

Checksum:ⁱ447130018AC52331

GO

Isoform 2 (identifier: Q96AT9-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
43-68: Missing.
114-114: K → KSCSVTQAEVQWHSQGPLQ

« Hide

        10         20         30         40         50
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHMHMMVSKP 
        60         70         80         90        100
EQWVKPMAVA GANQYTFHLE ATENPGALIK DIRENGMKSC SVTQAEVQWH 
       110        120        130        140        150
SQGPLQVGLA IKPGTSVEYL APWANQIDMA LVMTVEPGFG GQKFMEDMMP 
       160        170        180        190        200
KVHWLRTQFP SLDIEVDGGV GPDTVHKCAE AGANMIVSGS AIMRSEDPRS 
       210        220
VINLLRNVCS EAAQKRSLDR

Note: No experimental confirmation available.

Show »

Length:220

Mass (Da):23,924

Checksum:ⁱ626FAFD9426AE406

GO

Isoform 3 (identifier: Q96AT9-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-68: Missing.
114-114: K → KSCSVTQAEVQWHSQGPLQ

« Hide

        10         20         30         40         50
MHMMVSKPEQ WVKPMAVAGA NQYTFHLEAT ENPGALIKDI RENGMKSCSV 
        60         70         80         90        100
TQAEVQWHSQ GPLQVGLAIK PGTSVEYLAP WANQIDMALV MTVEPGFGGQ 
       110        120        130        140        150
KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP DTVHKCAEAG ANMIVSGSAI 
       160        170 
MRSEDPRSVI NLLRNVCSEA AQKRSLDR

Note: Gene prediction based on EST data.

Show »

Length:178

Mass (Da):19,537

Checksum:ⁱC2D4353C7FFAEC41

GO

Isoform 4 (identifier: Q96AT9-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
160-188: Missing.

« Hide

        10         20         30         40         50
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG 
        60         70         80         90        100
HPVVESLRKQ LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN 
       110        120        130        140        150
PGALIKDIRE NGMKVGLAIK PGTSVEYLAP WANQIDMALV MTVEPGFGGQ 
       160        170        180        190 
KFMEDMMPKA GANMIVSGSA IMRSEDPRSV INLLRNVCSE AAQKRSLDR

Note: No experimental confirmation available.

Show »

Length:199

Mass (Da):21,739

Checksum:ⁱ88D6C3598F28A1E1

GO

Isoform 5 (identifier: Q96AT9-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-68: Missing.

« Hide

        10         20         30         40         50
MHMMVSKPEQ WVKPMAVAGA NQYTFHLEAT ENPGALIKDI RENGMKVGLA 
        60         70         80         90        100
IKPGTSVEYL APWANQIDMA LVMTVEPGFG GQKFMEDMMP KVHWLRTQFP 
       110        120        130        140        150
SLDIEVDGGV GPDTVHKCAE AGANMIVSGS AIMRSEDPRS VINLLRNVCS 
       160
EAAQKRSLDR

Note: Gene prediction based on EST data.

Show »

Length:160

Mass (Da):17,570

Checksum:ⁱ9B6890E5E78B7D35

GO

Computationally mapped potential isoform sequencesⁱ

There are 9 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9IZU8	C9IZU8_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase, EC 5.1.3.1	RPE	225	Annotation score:
C9J9T0	C9J9T0_HUMAN	Ribulose-5-phosphate-3-epimerase, i... Ribulose-5-phosphate-3-epimerase, isoform CRA_a (Ribulose-phosphate 3-epimerase)	RPE hCG_2012337	191	Annotation score:
C9IYE8	C9IYE8_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	141	Annotation score:
C9JCL8	C9JCL8_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	107	Annotation score:
C9J6A7	C9J6A7_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	159	Annotation score:
C9J8S0	C9J8S0_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	157	Annotation score:
E7ESZ6	E7ESZ6_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	147	Annotation score:
E9PBG9	E9PBG9_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	94	Annotation score:
F8WBT4	F8WBT4_HUMAN	Ribulose-phosphate 3-epimerase Ribulose-phosphate 3-epimerase	RPE	60	Annotation score:

Sequence cautionⁱ

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

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	180	P → L in BAC04212 (PubMed:14702039).Curated		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_047117	1 – 68	Missing in isoform 3 and isoform 5. CuratedAdd BLAST	68
Alternative sequenceⁱVSP_008317	43 – 68	Missing in isoform 2. 1 PublicationAdd BLAST	26
Alternative sequenceⁱVSP_008318	114	K → KSCSVTQAEVQWHSQGPLQ in isoform 2 and isoform 3. 1 Publication	1
Alternative sequenceⁱVSP_055265	160 – 188	Missing in isoform 4. 1 PublicationAdd BLAST	29

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2388.1 [Q96AT9-1] CCDS42810.1 [Q96AT9-3] CCDS63107.1 [Q96AT9-4] CCDS63108.1 [Q96AT9-5]
NCBI Reference Sequences More...RefSeqⁱ	NP_001265211.1, NM_001278282.1 [Q96AT9-3] NP_001265212.1, NM_001278283.1 [Q96AT9-3] NP_001265214.1, NM_001278285.1 [Q96AT9-4] NP_001265215.1, NM_001278286.1 [Q96AT9-5] NP_001265217.1, NM_001278288.1 [Q96AT9-5] NP_001265218.1, NM_001278289.1 NP_001305855.1, NM_001318926.1 NP_001305856.1, NM_001318927.1 NP_001305857.1, NM_001318928.1 NP_001305858.1, NM_001318929.1 NP_001305859.1, NM_001318930.1 [Q96AT9-5] NP_001305860.1, NM_001318931.1 [Q96AT9-5] NP_008847.1, NM_006916.2 [Q96AT9-3] NP_954699.1, NM_199229.2 [Q96AT9-1] XP_006712740.1, XM_006712677.3 [Q96AT9-5]
UniGeneⁱ	Hs.282260 Hs.591638 Hs.734255

Genome annotation databases

Keywords - Coding sequence diversityⁱ

Alternative splicing

Protein	Similar proteins		Species	Score	Length	Source
Q96AT9	Ribulose-phosphate 3-epimerase		PANTR		228	UniRef100_Q96AT9
Ribulose-phosphate 3-epimerase		MACMU		228
Ribulose-phosphate 3-epimerase		PONAB		228
Ribulose-phosphate 3-epimerase		CERAT		228
Ribulose-phosphate 3-epimerase		RHIRO		228
+5
Q96AT9-3	RPE isoform 3		PANTR		178	UniRef100_K7C4Z4
Uncharacterized protein		PANPA		178
RPE2-1 (Fragment)		HUMAN		46
Ribulose-phosphate 3-epimerase (Fragment)		HUMAN		94
RPE isoform 7 (Fragment)		PANTR		94
+1
Q96AT9-4	RPE isoform 2		PANTR		199	UniRef100_A0A2I3TT16
Uncharacterized protein		MACMU		199
Uncharacterized protein		COLAP		199
RPE isoform 1		PONAB		199
Uncharacterized protein		CERAT		199
+8
Q96AT9-5	Ribulose-phosphate 3-epimerase		MACMU		236	UniRef100_A0A1D5R167
RPE isoform 10		PANTR		160
RPE isoform 6		PONAB		160
Ribulose-phosphate 3-epimerase (Fragment)		HUMAN		159
RPE isoform 10 (Fragment)		PONAB		159
+1

Protein	Similar proteins		Species	Score	Length	Source
Q96AT9	Ribulose-phosphate 3-epimerase		PANTR		228	UniRef90_Q96AT9
Ribulose-phosphate 3-epimerase		MACMU		228
Ribulose-phosphate 3-epimerase		PONAB		228
Ribulose-phosphate 3-epimerase		CERAT		228
Ribulose-phosphate 3-epimerase		RHIRO		228
+67
Q96AT9-2	ribulose-phosphate 3-epimerase isoform X5		BALAS		216	UniRef90_Q96AT9-2
Uncharacterized protein		COLAP		181
Uncharacterized protein		RHIRO		181
Uncharacterized protein		RHIBE		181
Uncharacterized protein		MACMU		180
+31
Q96AT9-3	Ribulose-phosphate 3-epimerase		ERIEU		243	UniRef90_A0A1S3WD13
RPE isoform 3		PANTR		178
Uncharacterized protein		PANPA		178
RPE2-1 (Fragment)		HUMAN		46
UPI000B510171		AOTNA		248
+6
Q96AT9-4	Ribulose-5-phosphate-3-epimerase		RAT		199	UniRef90_Q3MIF0
RPE isoform 2		PANTR		199
Uncharacterized protein		MACMU		199
Uncharacterized protein		COLAP		199
RPE isoform 1		PONAB		199
+40
Q96AT9-5	Ribulose-phosphate 3-epimerase		MOUSE		235	UniRef90_B2KGF0
Ribulose-phosphate 3-epimerase		NEOLE		240
Ribulose-phosphate 3-epimerase		MACMU		236
RPE isoform 10		PANTR		160
RPE isoform 6		PONAB		160
+27

Protein	Similar proteins		Species	Score	Length	Source
Q96AT9	Ribulose-phosphate 3-epimerase		PANTR		228	UniRef50_Q96AT9
Ribulose-phosphate 3-epimerase		MACMU		228
Ribulose-phosphate 3-epimerase		PONAB		228
Ribulose-phosphate 3-epimerase		CERAT		228
Ribulose-phosphate 3-epimerase		RHIRO		228
+118
Q96AT9-2	ribulose-phosphate 3-epimerase isoform X5		BALAS		216	UniRef50_Q96AT9-2
Uncharacterized protein		COLAP		181
Uncharacterized protein		RHIRO		181
Uncharacterized protein		RHIBE		181
Uncharacterized protein		MANLE		180
+76
Q96AT9-3	Ribulose-phosphate 3-epimerase		ERIEU		243	UniRef50_A0A1S3WD13
RPE isoform 3		PANTR		178
Uncharacterized protein		PANPA		178
RPE2-1 (Fragment)		HUMAN		46
Uncharacterized protein		Macrostomum lignano		223
+17
Q96AT9-4	Ribulose-5-phosphate-3-epimerase		RAT		199	UniRef50_Q3MIF0
ribulose-phosphate 3-epimerase isoform X4		Florida manatee		199
Uncharacterized protein		FELCA		199
ribulose-phosphate 3-epimerase isoform X2		ODORO		199
ribulose-phosphate 3-epimerase isoform X3		Enhydra lutris kenyoni		199
+41
Q96AT9-5	Ribulose-phosphate 3-epimerase		MOUSE		235	UniRef50_B2KGF0
Ribulose-phosphate 3-epimerase		NEOLE		240
Ribulose-phosphate 3-epimerase		MACMU		236
RPE isoform 10		PANTR		160
RPE isoform 6		PONAB		160
+70

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
CCDSⁱ	CCDS2388.1 [Q96AT9-1] CCDS42810.1 [Q96AT9-3] CCDS63107.1 [Q96AT9-4] CCDS63108.1 [Q96AT9-5]
RefSeqⁱ	NP_001265211.1, NM_001278282.1 [Q96AT9-3] NP_001265212.1, NM_001278283.1 [Q96AT9-3] NP_001265214.1, NM_001278285.1 [Q96AT9-4] NP_001265215.1, NM_001278286.1 [Q96AT9-5] NP_001265217.1, NM_001278288.1 [Q96AT9-5] NP_001265218.1, NM_001278289.1 NP_001305855.1, NM_001318926.1 NP_001305856.1, NM_001318927.1 NP_001305857.1, NM_001318928.1 NP_001305858.1, NM_001318929.1 NP_001305859.1, NM_001318930.1 [Q96AT9-5] NP_001305860.1, NM_001318931.1 [Q96AT9-5] NP_008847.1, NM_006916.2 [Q96AT9-3] NP_954699.1, NM_199229.2 [Q96AT9-1] XP_006712740.1, XM_006712677.3 [Q96AT9-5]
UniGeneⁱ	Hs.282260 Hs.591638 Hs.734255

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3OVP	X-ray	1.70	A/B	1-228	[»]
	3OVQ	X-ray	2.00	A/B	1-228	[»]
	3OVR	X-ray	1.95	A/B	1-228	[»]
	3QC3	X-ray	2.20	A/B	1-224	[»]
ProteinModelPortalⁱ	Q96AT9
SMRⁱ	Q96AT9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	112040, 51 interactors
IntActⁱ	Q96AT9, 4 interactors
STRINGⁱ	9606.ENSP00000352401

PTM databases

iPTMnetⁱ	Q96AT9
PhosphoSitePlusⁱ	Q96AT9

Polymorphism and mutation databases

DMDMⁱ	34924986

DMDMⁱ

34924986

Proteomic databases

EPDⁱ	Q96AT9
MaxQBⁱ	Q96AT9
PaxDbⁱ	Q96AT9
PeptideAtlasⁱ	Q96AT9
PRIDEⁱ	Q96AT9
ProteomicsDBⁱ	75997 75998 [Q96AT9-2]
TopDownProteomicsⁱ	Q96AT9-1 [Q96AT9-1] Q96AT9-2 [Q96AT9-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	6120
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000354506; ENSP00000346501; ENSG00000197713 [Q96AT9-4] ENST00000359429; ENSP00000352401; ENSG00000197713 [Q96AT9-1] ENST00000411934; ENSP00000389411; ENSG00000197713 [Q96AT9-5] ENST00000429921; ENSP00000401838; ENSG00000197713 [Q96AT9-3] ENST00000436630; ENSP00000403808; ENSG00000197713 [Q96AT9-3] ENST00000438204; ENSP00000402061; ENSG00000197713 [Q96AT9-5] ENST00000454822; ENSP00000394455; ENSG00000197713 [Q96AT9-3]
GeneIDⁱ	6120
KEGGⁱ	hsa:6120
UCSCⁱ	uc002vdn.5 human [Q96AT9-1]

Organism-specific databases

CTDⁱ	6120
DisGeNETⁱ	6120
EuPathDBⁱ	HostDB:ENSG00000197713.14
GeneCardsⁱ	RPE
H-InvDBⁱ	HIX0190555
HGNCⁱ	HGNC:10293 RPE
HPAⁱ	HPA036498 HPA036499
MIMⁱ	180480 gene
neXtProtⁱ	NX_Q96AT9
OpenTargetsⁱ	ENSG00000197713
PharmGKBⁱ	PA34654
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3111 Eukaryota COG0036 LUCA
GeneTreeⁱ	ENSGT00390000001447
HOGENOMⁱ	HOG000259349
HOVERGENⁱ	HBG044821
InParanoidⁱ	Q96AT9
KOⁱ	K01783
OMAⁱ	CHLMIED
OrthoDBⁱ	EOG091G0JMQ
PhylomeDBⁱ	Q96AT9
TreeFamⁱ	TF300157

Enzyme and pathway databases

BRENDAⁱ	5.1.3.1 2681
Reactomeⁱ	R-HSA-71336 Pentose phosphate pathway

Miscellaneous databases

EvolutionaryTraceⁱ	Q96AT9
GeneWikiⁱ	RPE_(gene)
GenomeRNAiⁱ	6120
Protein Ontology More...PROⁱ	PR:Q96AT9
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000197713 Expressed in 215 organ(s), highest expression level in adrenal tissue
CleanExⁱ	HS_RPE
ExpressionAtlasⁱ	Q96AT9 baseline and differential
Genevisibleⁱ	Q96AT9 HS

Family and domain databases

CDDⁱ	cd00429 RPE, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR026019 Ribul_P_3_epim IPR000056 Ribul_P_3_epim-like IPR011060 RibuloseP-bd_barrel
PANTHERⁱ	PTHR11749 PTHR11749, 1 hit
Pfamⁱ	View protein in Pfam PF00834 Ribul_P_3_epim, 1 hit
PIRSFⁱ	PIRSF001461 RPE, 1 hit
SUPFAMⁱ	SSF51366 SSF51366, 1 hit
TIGRFAMsⁱ	TIGR01163 rpe, 1 hit
PROSITEⁱ	View protein in PROSITE PS01085 RIBUL_P_3_EPIMER_1, 1 hit PS01086 RIBUL_P_3_EPIMER_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RPE_HUMAN
Accessionⁱ	Q96AT9Primary (citable) accession number: Q96AT9 Secondary accession number(s): A8K4S0 Q9BSB5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
	Last sequence update:	December 1, 2001
	Last modified:	September 12, 2018
	This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - Q96AT9 (RPE_HUMAN)

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Ribulose-phosphate 3-epimerase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

Extracellular region or secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ