Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96AT9

- RPE_HUMAN

UniProt

Q96AT9 - RPE_HUMAN

Protein

Ribulose-phosphate 3-epimerase

Gene

RPE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

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

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. racemase and epimerase activity, acting on carbohydrates and derivatives Source: InterPro
    5. ribulose-phosphate 3-epimerase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB
    2. pentose-phosphate shunt Source: UniProtKB
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Cobalt, Iron, Manganese, Metal-binding, Zinc

    Enzyme and pathway databases

    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10293. RPE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    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.

    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

    ArrayExpressiQ96AT9.
    BgeeiQ96AT9.
    CleanExiHS_RPE.
    GenevestigatoriQ96AT9.

    Organism-specific databases

    HPAiHPA036498.
    HPA036499.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-372480,EBI-372480

    Protein-protein interaction databases

    BioGridi112040. 4 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 – 105
    Helixi16 – 183
    Helixi19 – 2810
    Beta strandi34 – 4512
    Helixi51 – 6111
    Beta strandi63 – 653
    Beta strandi67 – 726
    Helixi76 – 794
    Helixi80 – 867
    Beta strandi89 – 946
    Helixi95 – 973
    Helixi101 – 11010
    Beta strandi114 – 1196
    Helixi125 – 1273
    Helixi129 – 1346
    Beta strandi136 – 1438
    Turni145 – 1473
    Helixi154 – 1563
    Helixi157 – 16610
    Beta strandi171 – 1777
    Turni180 – 1823
    Helixi183 – 1897
    Beta strandi193 – 1975
    Helixi198 – 2014
    Helixi206 – 22318

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000259349.
    HOVERGENiHBG044821.
    InParanoidiQ96AT9.
    KOiK01783.
    OMAiKPIICPS.
    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. Align

    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

    MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG    50
    HPVVESLRKQ LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN 100
    PGALIKDIRE NGMKVGLAIK PGTSVEYLAP WANQIDMALV MTVEPGFGGQ 150
    KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP DTVHKCAEAG ANMIVSGSAI 200
    MRSEDPRSVI NLLRNVCSEA AQKRSLDR 228
    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.
    The sequence BAC04212.1 differs from that shown. Reason: Frameshift at position 42.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    RefSeqiNP_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]
    UniGeneiHs.282260.
    Hs.591638.
    Hs.734255.

    Genome annotation databases

    EnsembliENST00000359429; 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]
    GeneIDi6120.
    KEGGihsa:6120.
    UCSCiuc002vdn.4. human. [Q96AT9-1]
    uc002vdo.4. human.

    Polymorphism databases

    DMDMi34924986.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 ]
    RefSeqi NP_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 ]
    UniGenei Hs.282260.
    Hs.591638.
    Hs.734255.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 4-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112040. 4 interactions.
    IntActi Q96AT9. 2 interactions.
    MINTi MINT-1448309.
    STRINGi 9606.ENSP00000352401.

    Polymorphism databases

    DMDMi 34924986.

    Proteomic databases

    MaxQBi Q96AT9.
    PaxDbi Q96AT9.
    PRIDEi Q96AT9.

    Protocols and materials databases

    DNASUi 6120.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli 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.4. human. [Q96AT9-1 ]
    uc002vdo.4. human.

    Organism-specific databases

    CTDi 6120.
    GeneCardsi GC02P210867.
    H-InvDB HIX0190555.
    HGNCi HGNC:10293. RPE.
    HPAi HPA036498.
    HPA036499.
    MIMi 180480. gene.
    neXtProti NX_Q96AT9.
    PharmGKBi PA34654.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0036.
    HOGENOMi HOG000259349.
    HOVERGENi HBG044821.
    InParanoidi Q96AT9.
    KOi K01783.
    OMAi KPIICPS.
    OrthoDBi EOG789CC1.
    PhylomeDBi Q96AT9.
    TreeFami TF300157.

    Enzyme and pathway databases

    Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).

    Miscellaneous databases

    EvolutionaryTracei Q96AT9.
    GeneWikii RPE_(gene).
    GenomeRNAii 6120.
    NextBioi 23767.
    PROi Q96AT9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96AT9.
    Bgeei Q96AT9.
    CleanExi HS_RPE.
    Genevestigatori Q96AT9.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR026019. Ribul_P_3_epim.
    IPR000056. Ribul_P_3_epim-like.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    PANTHERi PTHR11749. PTHR11749. 1 hit.
    Pfami PF00834. Ribul_P_3_epim. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001461. RPE. 1 hit.
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR01163. rpe. 1 hit.
    PROSITEi PS01085. RIBUL_P_3_EPIMER_1. 1 hit.
    PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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