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Q9UNP9

- PPIE_HUMAN

UniProt

Q9UNP9 - PPIE_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase E

Gene

PPIE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. cyclosporin A binding Source: ProtInc
    2. nucleotide binding Source: InterPro
    3. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. RNA binding Source: UniProtKB

    GO - Biological processi

    1. mRNA splicing, via spliceosome Source: UniProtKB
    2. positive regulation of viral genome replication Source: UniProtKB
    3. protein folding Source: UniProtKB-KW
    4. protein peptidyl-prolyl isomerization Source: GOC
    5. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase E (EC:5.2.1.8)
    Short name:
    PPIase E
    Alternative name(s):
    Cyclophilin E
    Cyclophilin-33
    Rotamase E
    Gene namesi
    Name:PPIE
    Synonyms:CYP33
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9258. PPIE.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33583.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301Peptidyl-prolyl cis-trans isomerase EPRO_0000064157Add
    BLAST

    Proteomic databases

    MaxQBiQ9UNP9.
    PaxDbiQ9UNP9.
    PRIDEiQ9UNP9.

    PTM databases

    PhosphoSiteiQ9UNP9.

    Expressioni

    Tissue specificityi

    Found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiQ9UNP9.
    BgeeiQ9UNP9.
    CleanExiHS_PPIE.
    GenevestigatoriQ9UNP9.

    Organism-specific databases

    HPAiHPA020131.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KMT2AQ031644EBI-591818,EBI-591370
    XAB2Q9HCS73EBI-591818,EBI-295232

    Protein-protein interaction databases

    BioGridi115714. 13 interactions.
    IntActiQ9UNP9. 10 interactions.
    MINTiMINT-3082792.
    STRINGi9606.ENSP00000312769.

    Structurei

    Secondary structure

    1
    301
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Helixi19 – 268
    Helixi27 – 293
    Beta strandi32 – 365
    Turni41 – 433
    Beta strandi48 – 569
    Helixi57 – 6711
    Beta strandi70 – 723
    Beta strandi78 – 814
    Beta strandi141 – 1488
    Beta strandi151 – 16010
    Turni162 – 1643
    Helixi166 – 17712
    Turni178 – 1803
    Beta strandi188 – 1936
    Turni194 – 1963
    Beta strandi197 – 2004
    Turni203 – 2053
    Beta strandi206 – 2094
    Beta strandi214 – 2174
    Beta strandi230 – 2367
    Beta strandi248 – 2536
    Helixi256 – 2583
    Turni259 – 2613
    Beta strandi264 – 2707
    Helixi272 – 2798
    Beta strandi292 – 2998

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZMFX-ray1.88A137-301[»]
    2CQBNMR-A1-89[»]
    2KU7NMR-A2-82[»]
    2KYXNMR-A3-83[»]
    2R99X-ray1.61A131-301[»]
    3LPYX-ray2.00A/B5-82[»]
    3MDFX-ray1.85A/B1-83[»]
    3UCHX-ray2.50A129-301[»]
    ProteinModelPortaliQ9UNP9.
    SMRiQ9UNP9. Positions 1-108, 138-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UNP9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 8479RRMPROSITE-ProRule annotationAdd
    BLAST
    Domaini143 – 299157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 634Poly-Ala

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    HOVERGENiHBG001065.
    KOiK09564.
    OMAiAFIEFEL.
    PhylomeDBiQ9UNP9.
    TreeFamiTF313817.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR016304. Cyclophilin-type_PPIase_E.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q9UNP9-1) [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

    MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA    50
    FVEFELAEDA AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD 100
    WLKKFSGKTL EENKEEEGSE PPKAETQEGE PIAKKARSNP QVYMDIKIGN 150
    KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK GFGFKGSSFH RIIPQFMCQG 200
    GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG PNTNGSQFFL 250
    TCDKTDWLDG KHVVFGEVTE GLDVLRQIEA QGSKDGKPKQ KVIIADCGEY 300
    V 301
    Length:301
    Mass (Da):33,431
    Last modified:May 1, 2000 - v1
    Checksum:iF3226149A790BA42
    GO
    Isoform B (identifier: Q9UNP9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         280-301: AQGSKDGKPKQKVIIADCGEYV → KQEESAITSQPRSWKLT

    Show »
    Length:296
    Mass (Da):33,085
    Checksum:iB70A7F239825B54D
    GO
    Isoform 3 (identifier: Q9UNP9-3) [UniParc]FASTAAdd to Basket

    Also known as: Cyclophilin-33B

    The sequence of this isoform differs from the canonical sequence as follows:
         280-301: AQGSKDGKPKQKVIIADCGEYV → VAPDTKASKARGSRKNKDGQERNWGKSQKVESHTI

    Show »
    Length:314
    Mass (Da):34,991
    Checksum:iC5D0CFB2673046D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511K → R in AAZ93379. 1 PublicationCurated
    Sequence conflicti207 – 2071N → D in AAZ93379. 1 PublicationCurated
    Sequence conflicti287 – 2871K → N in AAC00006. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei280 – 30122AQGSK…CGEYV → VAPDTKASKARGSRKNKDGQ ERNWGKSQKVESHTI in isoform 3. 1 PublicationVSP_046370Add
    BLAST
    Alternative sequencei280 – 30122AQGSK…CGEYV → KQEESAITSQPRSWKLT in isoform B. 2 PublicationsVSP_005181Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104012 mRNA. Translation: AAD19906.1.
    AF104013 mRNA. Translation: AAD19907.1.
    AF042385 mRNA. Translation: AAC00006.1.
    AF042386 mRNA. Translation: AAC00007.1.
    DQ160195 mRNA. Translation: AAZ93379.1.
    AK313666 mRNA. Translation: BAG36418.1.
    AL049824, AL033527, AL035404 Genomic DNA. Translation: CAI19347.1.
    AL049824, AL033527, AL035404 Genomic DNA. Translation: CAI19348.1.
    AL049824, AL035404 Genomic DNA. Translation: CAI19350.1.
    AL033527, AL035404, AL049824 Genomic DNA. Translation: CAI19409.1.
    AL033527, AL035404, AL049824 Genomic DNA. Translation: CAI19410.1.
    AL035404, AL033527, AL049824 Genomic DNA. Translation: CAI19576.1.
    AL035404, AL033527, AL049824 Genomic DNA. Translation: CAI19577.1.
    AL035404, AL049824 Genomic DNA. Translation: CAI19579.1.
    CH471059 Genomic DNA. Translation: EAX07255.1.
    BC004898 mRNA. Translation: AAH04898.1.
    BC008451 mRNA. Translation: AAH08451.1.
    BC107736 mRNA. Translation: AAI07737.1.
    CCDSiCCDS442.1. [Q9UNP9-2]
    CCDS443.1. [Q9UNP9-1]
    CCDS53299.1. [Q9UNP9-3]
    PIRiS66681.
    RefSeqiNP_001181936.1. NM_001195007.1. [Q9UNP9-3]
    NP_006103.1. NM_006112.3. [Q9UNP9-1]
    NP_982281.1. NM_203456.2. [Q9UNP9-2]
    XP_006710351.1. XM_006710288.1. [Q9UNP9-3]
    UniGeneiHs.524690.

    Genome annotation databases

    EnsembliENST00000324379; ENSP00000312769; ENSG00000084072. [Q9UNP9-1]
    ENST00000356511; ENSP00000348904; ENSG00000084072. [Q9UNP9-2]
    ENST00000372830; ENSP00000361918; ENSG00000084072. [Q9UNP9-3]
    GeneIDi10450.
    KEGGihsa:10450.
    UCSCiuc001cds.2. human. [Q9UNP9-1]
    uc001cdv.3. human. [Q9UNP9-2]

    Polymorphism databases

    DMDMi13124097.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104012 mRNA. Translation: AAD19906.1 .
    AF104013 mRNA. Translation: AAD19907.1 .
    AF042385 mRNA. Translation: AAC00006.1 .
    AF042386 mRNA. Translation: AAC00007.1 .
    DQ160195 mRNA. Translation: AAZ93379.1 .
    AK313666 mRNA. Translation: BAG36418.1 .
    AL049824 , AL033527 , AL035404 Genomic DNA. Translation: CAI19347.1 .
    AL049824 , AL033527 , AL035404 Genomic DNA. Translation: CAI19348.1 .
    AL049824 , AL035404 Genomic DNA. Translation: CAI19350.1 .
    AL033527 , AL035404 , AL049824 Genomic DNA. Translation: CAI19409.1 .
    AL033527 , AL035404 , AL049824 Genomic DNA. Translation: CAI19410.1 .
    AL035404 , AL033527 , AL049824 Genomic DNA. Translation: CAI19576.1 .
    AL035404 , AL033527 , AL049824 Genomic DNA. Translation: CAI19577.1 .
    AL035404 , AL049824 Genomic DNA. Translation: CAI19579.1 .
    CH471059 Genomic DNA. Translation: EAX07255.1 .
    BC004898 mRNA. Translation: AAH04898.1 .
    BC008451 mRNA. Translation: AAH08451.1 .
    BC107736 mRNA. Translation: AAI07737.1 .
    CCDSi CCDS442.1. [Q9UNP9-2 ]
    CCDS443.1. [Q9UNP9-1 ]
    CCDS53299.1. [Q9UNP9-3 ]
    PIRi S66681.
    RefSeqi NP_001181936.1. NM_001195007.1. [Q9UNP9-3 ]
    NP_006103.1. NM_006112.3. [Q9UNP9-1 ]
    NP_982281.1. NM_203456.2. [Q9UNP9-2 ]
    XP_006710351.1. XM_006710288.1. [Q9UNP9-3 ]
    UniGenei Hs.524690.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZMF X-ray 1.88 A 137-301 [» ]
    2CQB NMR - A 1-89 [» ]
    2KU7 NMR - A 2-82 [» ]
    2KYX NMR - A 3-83 [» ]
    2R99 X-ray 1.61 A 131-301 [» ]
    3LPY X-ray 2.00 A/B 5-82 [» ]
    3MDF X-ray 1.85 A/B 1-83 [» ]
    3UCH X-ray 2.50 A 129-301 [» ]
    ProteinModelPortali Q9UNP9.
    SMRi Q9UNP9. Positions 1-108, 138-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115714. 13 interactions.
    IntActi Q9UNP9. 10 interactions.
    MINTi MINT-3082792.
    STRINGi 9606.ENSP00000312769.

    PTM databases

    PhosphoSitei Q9UNP9.

    Polymorphism databases

    DMDMi 13124097.

    Proteomic databases

    MaxQBi Q9UNP9.
    PaxDbi Q9UNP9.
    PRIDEi Q9UNP9.

    Protocols and materials databases

    DNASUi 10450.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324379 ; ENSP00000312769 ; ENSG00000084072 . [Q9UNP9-1 ]
    ENST00000356511 ; ENSP00000348904 ; ENSG00000084072 . [Q9UNP9-2 ]
    ENST00000372830 ; ENSP00000361918 ; ENSG00000084072 . [Q9UNP9-3 ]
    GeneIDi 10450.
    KEGGi hsa:10450.
    UCSCi uc001cds.2. human. [Q9UNP9-1 ]
    uc001cdv.3. human. [Q9UNP9-2 ]

    Organism-specific databases

    CTDi 10450.
    GeneCardsi GC01P040157.
    HGNCi HGNC:9258. PPIE.
    HPAi HPA020131.
    MIMi 602435. gene.
    neXtProti NX_Q9UNP9.
    PharmGKBi PA33583.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOVERGENi HBG001065.
    KOi K09564.
    OMAi AFIEFEL.
    PhylomeDBi Q9UNP9.
    TreeFami TF313817.

    Miscellaneous databases

    ChiTaRSi PPIE. human.
    EvolutionaryTracei Q9UNP9.
    GeneWikii PPIE_(gene).
    GenomeRNAii 10450.
    NextBioi 39609.
    PROi Q9UNP9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNP9.
    Bgeei Q9UNP9.
    CleanExi HS_PPIE.
    Genevestigatori Q9UNP9.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR016304. Cyclophilin-type_PPIase_E.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001475. PPI_cyclophilin_E. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Co-amplification of a novel cyclophilin-like gene (PPIE) with L-myc in small cell lung cancer cell lines."
      Kim J.-O., Nau M.M., Allikian K.A., Makela T.P., Alitalo K., Johnson B.E., Kelley M.J.
      Oncogene 17:1019-1026(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
    2. Slater C., Thill G., Obar R.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
    3. Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Tang Z., Huang B., Lin L., Yang S.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. "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] (ISOFORM A).
      Tissue: Brain.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 A).
      Tissue: Bone marrow, Colon and Lung.
    8. "A nuclear RNA-binding cyclophilin in human T cells."
      Mi H., Kops O., Zimmermann E., Jaeschke A., Tropschug M.
      FEBS Lett. 398:201-205(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the RNA recognition motif in peptidyl-prolyl cis-trans isomerase E."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-89.

    Entry informationi

    Entry nameiPPIE_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNP9
    Secondary accession number(s): B2R971
    , O43634, O43635, Q32Q72, Q3S611, Q5TGA0, Q5TGA2, Q5TGA3, Q9UIZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 147 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 1
      Human chromosome 1: 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