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Protein

Ribulose-phosphate 3-epimerase

Gene

RPE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Fe(2+), and probably also with Mn(2+), Zn(2+) and Co2+.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Substrate
Metal bindingi35 – 351Divalent metal cation
Active sitei37 – 371Proton acceptorCurated
Metal bindingi37 – 371Divalent metal cation
Metal bindingi70 – 701Divalent metal cation
Binding sitei70 – 701Substrate
Active sitei175 – 1751Proton donorCurated
Metal bindingi175 – 1751Divalent metal cation
Binding sitei177 – 1771Substrate; via amide nitrogen

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ribulose-phosphate 3-epimerase activity Source: UniProtKB

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

BRENDAi5.1.3.1. 2681.
ReactomeiREACT_1859. 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-3-epimerase
Gene namesi
Name:RPE
ORF Names:HUSSY-17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10293. RPE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101S → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi12 – 121L → A: Reduces enzyme activity by half. 1 Publication
Mutagenesisi35 – 351H → A: Alters protein structure. Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi37 – 371D → A: Alters protein structure. Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi39 – 391M → A: Lowers enzyme activity by 10%. 1 Publication
Mutagenesisi70 – 701H → A: Alters protein structure. 1 Publication
Mutagenesisi72 – 721M → A: Reduces enzyme activity by half. 1 Publication
Mutagenesisi141 – 1411M → A: No effect on enzyme activity. 1 Publication
Mutagenesisi175 – 1751D → A: Alters protein structure. 1 Publication

Organism-specific databases

PharmGKBiPA34654.

Polymorphism and mutation databases

DMDMi34924986.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 228227Ribulose-phosphate 3-epimerasePRO_0000171587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96AT9.
PaxDbiQ96AT9.
PRIDEiQ96AT9.

Expressioni

Gene expression databases

BgeeiQ96AT9.
CleanExiHS_RPE.
ExpressionAtlasiQ96AT9. baseline and differential.
GenevisibleiQ96AT9. HS.

Organism-specific databases

HPAiHPA036498.
HPA036499.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-372480,EBI-372480

Protein-protein interaction databases

BioGridi112040. 6 interactions.
IntActiQ96AT9. 2 interactions.
MINTiMINT-1448309.
STRINGi9606.ENSP00000352401.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi16 – 183Combined sources
Helixi19 – 2810Combined sources
Beta strandi34 – 4512Combined sources
Helixi51 – 6111Combined sources
Beta strandi63 – 653Combined sources
Beta strandi67 – 726Combined sources
Helixi76 – 794Combined sources
Helixi80 – 867Combined sources
Beta strandi89 – 946Combined sources
Helixi95 – 973Combined sources
Helixi101 – 11010Combined sources
Beta strandi114 – 1196Combined sources
Helixi125 – 1273Combined sources
Helixi129 – 1346Combined sources
Beta strandi136 – 1438Combined sources
Turni145 – 1473Combined sources
Helixi154 – 1563Combined sources
Helixi157 – 16610Combined sources
Beta strandi171 – 1777Combined sources
Turni180 – 1823Combined sources
Helixi183 – 1897Combined sources
Beta strandi193 – 1975Combined sources
Helixi198 – 2014Combined sources
Helixi206 – 22318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OVPX-ray1.70A/B1-228[»]
3OVQX-ray2.00A/B1-228[»]
3OVRX-ray1.95A/B1-228[»]
3QC3X-ray2.20A/B1-224[»]
ProteinModelPortaliQ96AT9.
SMRiQ96AT9. Positions 4-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96AT9.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0036.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
InParanoidiQ96AT9.
KOiK01783.
OMAiKTIDVCA.
OrthoDBiEOG789CC1.
PhylomeDBiQ96AT9.
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]

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. AlignAdd to basket

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

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

Note: No experimental confirmation available.
Show »
Length:220
Mass (Da):23,924
Checksum:i626FAFD9426AE406
GO
Isoform 3 (identifier: Q96AT9-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:178
Mass (Da):19,537
Checksum:iC2D4353C7FFAEC41
GO
Isoform 4 (identifier: Q96AT9-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:199
Mass (Da):21,739
Checksum:i88D6C3598F28A1E1
GO
Isoform 5 (identifier: Q96AT9-5) [UniParc]FASTAAdd to basket

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

Note: Gene prediction based on EST data.
Show »
Length:160
Mass (Da):17,570
Checksum:i9B6890E5E78B7D35
GO

Sequence cautioni

The sequence BAB71076.1 differs from that shown. Reason: Frameshift at position 69. Curated
The sequence BAC04212.1 differs from that shown. Reason: Frameshift at position 42. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801P → L in BAC04212 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6868Missing in isoform 3 and isoform 5. CuratedVSP_047117Add
BLAST
Alternative sequencei43 – 6826Missing in isoform 2. 1 PublicationVSP_008317Add
BLAST
Alternative sequencei114 – 1141K → KSCSVTQAEVQWHSQGPLQ in isoform 2 and isoform 3. 1 PublicationVSP_008318
Alternative sequencei160 – 18829Missing in isoform 4. 1 PublicationVSP_055265Add
BLAST

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.
CCDSiCCDS2388.1. [Q96AT9-1]
CCDS42810.1. [Q96AT9-3]
CCDS63107.1. [Q96AT9-4]
CCDS63108.1. [Q96AT9-5]
RefSeqiNP_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_008847.1. NM_006916.2. [Q96AT9-3]
NP_954699.1. NM_199229.2. [Q96AT9-1]
XP_006712740.1. XM_006712677.2. [Q96AT9-5]
UniGeneiHs.282260.
Hs.591638.
Hs.734255.

Genome annotation databases

EnsembliENST00000354506; ENSP00000346501; ENSG00000197713. [Q96AT9-4]
ENST00000359429; ENSP00000352401; ENSG00000197713.
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]
GeneIDi6120.
KEGGihsa:6120.
UCSCiuc002vdn.4. human. [Q96AT9-1]
uc002vdo.4. human.
uc010zjf.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

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.
CCDSiCCDS2388.1. [Q96AT9-1]
CCDS42810.1. [Q96AT9-3]
CCDS63107.1. [Q96AT9-4]
CCDS63108.1. [Q96AT9-5]
RefSeqiNP_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_008847.1. NM_006916.2. [Q96AT9-3]
NP_954699.1. NM_199229.2. [Q96AT9-1]
XP_006712740.1. XM_006712677.2. [Q96AT9-5]
UniGeneiHs.282260.
Hs.591638.
Hs.734255.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OVPX-ray1.70A/B1-228[»]
3OVQX-ray2.00A/B1-228[»]
3OVRX-ray1.95A/B1-228[»]
3QC3X-ray2.20A/B1-224[»]
ProteinModelPortaliQ96AT9.
SMRiQ96AT9. Positions 4-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112040. 6 interactions.
IntActiQ96AT9. 2 interactions.
MINTiMINT-1448309.
STRINGi9606.ENSP00000352401.

Polymorphism and mutation databases

DMDMi34924986.

Proteomic databases

MaxQBiQ96AT9.
PaxDbiQ96AT9.
PRIDEiQ96AT9.

Protocols and materials databases

DNASUi6120.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354506; ENSP00000346501; ENSG00000197713. [Q96AT9-4]
ENST00000359429; ENSP00000352401; ENSG00000197713.
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]
GeneIDi6120.
KEGGihsa:6120.
UCSCiuc002vdn.4. human. [Q96AT9-1]
uc002vdo.4. human.
uc010zjf.3. human.

Organism-specific databases

CTDi6120.
GeneCardsiGC02P210867.
H-InvDBHIX0190555.
HGNCiHGNC:10293. RPE.
HPAiHPA036498.
HPA036499.
MIMi180480. gene.
neXtProtiNX_Q96AT9.
PharmGKBiPA34654.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0036.
GeneTreeiENSGT00390000001447.
HOGENOMiHOG000259349.
HOVERGENiHBG044821.
InParanoidiQ96AT9.
KOiK01783.
OMAiKTIDVCA.
OrthoDBiEOG789CC1.
PhylomeDBiQ96AT9.
TreeFamiTF300157.

Enzyme and pathway databases

BRENDAi5.1.3.1. 2681.
ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

EvolutionaryTraceiQ96AT9.
GeneWikiiRPE_(gene).
GenomeRNAii6120.
NextBioi23767.
PROiQ96AT9.
SOURCEiSearch...

Gene expression databases

BgeeiQ96AT9.
CleanExiHS_RPE.
ExpressionAtlasiQ96AT9. baseline and differential.
GenevisibleiQ96AT9. HS.

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

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. 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.

Entry informationi

Entry nameiRPE_HUMAN
AccessioniPrimary (citable) accession number: Q96AT9
Secondary accession number(s): A8K4S0
, B4E016, C9JPQ7, O43767, Q53TV9, Q8N215, Q96N34, Q9BSB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.