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P30405

- PPIF_HUMAN

UniProt

P30405 - PPIF_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Gene

PPIF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Binds cyclosporin A (CsA). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP.

    GO - Molecular functioni

    1. cyclosporin A binding Source: Ensembl
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: Ensembl
    2. cellular response to arsenic-containing substance Source: UniProtKB
    3. cellular response to calcium ion Source: UniProtKB
    4. cellular response to hydrogen peroxide Source: UniProtKB
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of ATPase activity Source: UniProtKB
    7. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    8. negative regulation of oxidative phosphorylation Source: UniProtKB
    9. negative regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
    10. negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
    11. positive regulation of necrotic cell death Source: Ensembl
    12. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    13. protein folding Source: UniProtKB-KW
    14. regulation of mitochondrial membrane permeability Source: UniProtKB
    15. regulation of mitochondrial membrane permeability involved in programmed necrotic cell death Source: UniProtKB
    16. regulation of proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
    17. response to ischemia Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Apoptosis, Necrosis

    Keywords - Ligandi

    Cyclosporin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase F, mitochondrial (EC:5.2.1.8)
    Short name:
    PPIase F
    Alternative name(s):
    Cyclophilin D
    Short name:
    CyP-D
    Short name:
    CypD
    Cyclophilin F
    Mitochondrial cyclophilin
    Short name:
    CyP-M
    Rotamase F
    Gene namesi
    Name:PPIF
    Synonyms:CYP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9259. PPIF.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. membrane Source: ProtInc
    2. mitochondrial inner membrane Source: Ensembl
    3. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi203 – 2031C → S: Blocks Ca(2+)-induced mPTP opening and reduces hydrogen peroxide-induced cell death. 1 Publication

    Organism-specific databases

    PharmGKBiPA33584.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionSequence AnalysisAdd
    BLAST
    Chaini30 – 207178Peptidyl-prolyl cis-trans isomerase F, mitochondrialPRO_0000025489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671N6-acetyllysine; alternateBy similarity
    Modified residuei67 – 671N6-succinyllysine; alternateBy similarity
    Modified residuei86 – 861N6-succinyllysineBy similarity
    Modified residuei167 – 1671N6-acetyllysineBy similarity
    Modified residuei175 – 1751N6-succinyllysineBy similarity
    Modified residuei190 – 1901N6-succinyllysineBy similarity
    Modified residuei203 – 2031S-nitrosocysteineBy similarity

    Post-translational modificationi

    Deacteylated at Lys-167 by SIRT3.By similarity

    Keywords - PTMi

    Acetylation, S-nitrosylation

    Proteomic databases

    MaxQBiP30405.
    PaxDbiP30405.
    PeptideAtlasiP30405.
    PRIDEiP30405.

    2D gel databases

    OGPiP30405.
    UCD-2DPAGEP30405.

    PTM databases

    PhosphoSiteiP30405.

    Expressioni

    Gene expression databases

    ArrayExpressiP30405.
    BgeeiP30405.
    CleanExiHS_PPIF.
    GenevestigatoriP30405.

    Interactioni

    Subunit structurei

    Believed to associate with the mitochondrial permeability transition pore complex (PTPC). Associates with the mitochondrial membrane ATP synthase F1F0 ATP synthase; the association is increased by inorganic phosphate (Pi) and decreased by cyclosporin A (CsA). Interacts with ATP5B; ATP5H and ATP5O. Interacts with SLC25A3; the interaction is impaired by CsA. Interacts with BCL2; the interaction is impaired by CsA. Interacts with TP53; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by CsA. Interacts with C1QBP.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046374EBI-5544229,EBI-366083

    Protein-protein interaction databases

    BioGridi115411. 25 interactions.
    IntActiP30405. 5 interactions.
    MINTiMINT-3011711.
    STRINGi9606.ENSP00000225174.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi47 – 548
    Beta strandi57 – 6610
    Turni68 – 703
    Helixi72 – 8312
    Turni84 – 863
    Beta strandi94 – 996
    Turni100 – 1023
    Beta strandi103 – 1064
    Turni109 – 1113
    Beta strandi112 – 1154
    Beta strandi120 – 1234
    Beta strandi139 – 1424
    Beta strandi144 – 1463
    Beta strandi150 – 1523
    Beta strandi154 – 1596
    Helixi162 – 1643
    Turni165 – 1673
    Beta strandi170 – 1767
    Helixi178 – 1869
    Beta strandi198 – 2058

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BITX-ray1.71X43-207[»]
    2BIUX-ray1.71X43-207[»]
    2Z6WX-ray0.96A/B44-207[»]
    3QYUX-ray1.54A44-207[»]
    3R49X-ray1.77A43-207[»]
    3R4GX-ray1.05A43-207[»]
    3R54X-ray1.35A43-207[»]
    3R56X-ray1.40A43-207[»]
    3R57X-ray1.71A43-207[»]
    3R59X-ray1.10A43-207[»]
    3RCFX-ray1.15A43-207[»]
    3RCGX-ray0.97A43-207[»]
    3RCIX-ray1.44X43-207[»]
    3RCKX-ray1.26X43-207[»]
    3RCLX-ray1.70A43-207[»]
    3RD9X-ray1.40X43-207[»]
    3RDAX-ray1.07X43-207[»]
    3RDBX-ray1.55A43-207[»]
    3RDCX-ray1.94A43-207[»]
    4J58X-ray1.28A44-207[»]
    4J59X-ray1.92A44-207[»]
    4J5AX-ray1.58X44-207[»]
    4J5BX-ray2.01A44-207[»]
    4J5CX-ray1.03X44-207[»]
    4J5DX-ray1.32X44-207[»]
    4J5EX-ray0.99X44-207[»]
    4O8HX-ray0.85A43-207[»]
    4O8IX-ray1.45A43-207[»]
    ProteinModelPortaliP30405.
    SMRiP30405. Positions 44-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30405.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 205157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cyclophilin-type PPIase family.Curated
    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiP30405.
    KOiK09565.
    OMAiAFMCQAG.
    OrthoDBiEOG79GT7W.
    PhylomeDBiP30405.
    TreeFamiTF312801.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30405-1) [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

    MLALRCGSRW LGLLSVPRSV PLRLPAARAC SKGSGDPSSS SSSGNPLVYL    50
    DVDANGKPLG RVVLELKADV VPKTAENFRA LCTGEKGFGY KGSTFHRVIP 100
    SFMCQAGDFT NHNGTGGKSI YGSRFPDENF TLKHVGPGVL SMANAGPNTN 150
    GSQFFICTIK TDWLDGKHVV FGHVKEGMDV VKKIESFGSK SGRTSKKIVI 200
    TDCGQLS 207
    Length:207
    Mass (Da):22,040
    Last modified:April 1, 1993 - v1
    Checksum:iD7C76F1D4049F16A
    GO
    Isoform 2 (identifier: P30405-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-207: VLSMANAGPN...IVITDCGQLS → WMASMLCSVTSKRAWTS

    Show »
    Length:155
    Mass (Da):16,541
    Checksum:iBA0C086F1899B2DF
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 20769VLSMA…CGQLS → WMASMLCSVTSKRAWTS in isoform 2. 2 PublicationsVSP_056286Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80254 mRNA. Translation: AAA58434.1.
    AK296669 mRNA. Translation: BAG59266.1.
    AL133481, AL391665 Genomic DNA. Translation: CAH72725.1.
    AL391665, AL133481 Genomic DNA. Translation: CAI40994.1.
    CH471083 Genomic DNA. Translation: EAW54645.1.
    BC005020 mRNA. Translation: AAH05020.1.
    BC110299 mRNA. Translation: AAI10300.1.
    CCDSiCCDS7358.1.
    PIRiA41581.
    RefSeqiNP_005720.1. NM_005729.3.
    UniGeneiHs.381072.

    Genome annotation databases

    EnsembliENST00000225174; ENSP00000225174; ENSG00000108179.
    ENST00000394579; ENSP00000378080; ENSG00000108179.
    GeneIDi10105.
    KEGGihsa:10105.
    UCSCiuc001kai.3. human.

    Polymorphism databases

    DMDMi231968.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80254 mRNA. Translation: AAA58434.1 .
    AK296669 mRNA. Translation: BAG59266.1 .
    AL133481 , AL391665 Genomic DNA. Translation: CAH72725.1 .
    AL391665 , AL133481 Genomic DNA. Translation: CAI40994.1 .
    CH471083 Genomic DNA. Translation: EAW54645.1 .
    BC005020 mRNA. Translation: AAH05020.1 .
    BC110299 mRNA. Translation: AAI10300.1 .
    CCDSi CCDS7358.1.
    PIRi A41581.
    RefSeqi NP_005720.1. NM_005729.3.
    UniGenei Hs.381072.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BIT X-ray 1.71 X 43-207 [» ]
    2BIU X-ray 1.71 X 43-207 [» ]
    2Z6W X-ray 0.96 A/B 44-207 [» ]
    3QYU X-ray 1.54 A 44-207 [» ]
    3R49 X-ray 1.77 A 43-207 [» ]
    3R4G X-ray 1.05 A 43-207 [» ]
    3R54 X-ray 1.35 A 43-207 [» ]
    3R56 X-ray 1.40 A 43-207 [» ]
    3R57 X-ray 1.71 A 43-207 [» ]
    3R59 X-ray 1.10 A 43-207 [» ]
    3RCF X-ray 1.15 A 43-207 [» ]
    3RCG X-ray 0.97 A 43-207 [» ]
    3RCI X-ray 1.44 X 43-207 [» ]
    3RCK X-ray 1.26 X 43-207 [» ]
    3RCL X-ray 1.70 A 43-207 [» ]
    3RD9 X-ray 1.40 X 43-207 [» ]
    3RDA X-ray 1.07 X 43-207 [» ]
    3RDB X-ray 1.55 A 43-207 [» ]
    3RDC X-ray 1.94 A 43-207 [» ]
    4J58 X-ray 1.28 A 44-207 [» ]
    4J59 X-ray 1.92 A 44-207 [» ]
    4J5A X-ray 1.58 X 44-207 [» ]
    4J5B X-ray 2.01 A 44-207 [» ]
    4J5C X-ray 1.03 X 44-207 [» ]
    4J5D X-ray 1.32 X 44-207 [» ]
    4J5E X-ray 0.99 X 44-207 [» ]
    4O8H X-ray 0.85 A 43-207 [» ]
    4O8I X-ray 1.45 A 43-207 [» ]
    ProteinModelPortali P30405.
    SMRi P30405. Positions 44-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115411. 25 interactions.
    IntActi P30405. 5 interactions.
    MINTi MINT-3011711.
    STRINGi 9606.ENSP00000225174.

    Chemistry

    DrugBanki DB01093. Dimethyl sulfoxide.
    DB00172. L-Proline.

    PTM databases

    PhosphoSitei P30405.

    Polymorphism databases

    DMDMi 231968.

    2D gel databases

    OGPi P30405.
    UCD-2DPAGE P30405.

    Proteomic databases

    MaxQBi P30405.
    PaxDbi P30405.
    PeptideAtlasi P30405.
    PRIDEi P30405.

    Protocols and materials databases

    DNASUi 10105.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225174 ; ENSP00000225174 ; ENSG00000108179 .
    ENST00000394579 ; ENSP00000378080 ; ENSG00000108179 .
    GeneIDi 10105.
    KEGGi hsa:10105.
    UCSCi uc001kai.3. human.

    Organism-specific databases

    CTDi 10105.
    GeneCardsi GC10P081107.
    HGNCi HGNC:9259. PPIF.
    MIMi 604486. gene.
    neXtProti NX_P30405.
    PharmGKBi PA33584.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    InParanoidi P30405.
    KOi K09565.
    OMAi AFMCQAG.
    OrthoDBi EOG79GT7W.
    PhylomeDBi P30405.
    TreeFami TF312801.

    Miscellaneous databases

    ChiTaRSi PPIF. human.
    EvolutionaryTracei P30405.
    GeneWikii PPIF.
    GenomeRNAii 10105.
    NextBioi 38221.
    PROi P30405.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30405.
    Bgeei P30405.
    CleanExi HS_PPIF.
    Genevestigatori P30405.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms."
      Bergsma D.J., Eder C., Gross M., Kersten H., Sylvester D., Appelbaum E., Cusimano D., Livi G.P., McLauglin M.M., Kasyan K., Porter T.G., Silverman C., Dunnington D., Hand A., Prichett W.P., Bossard M.J., Brandt M., Levy M.A.
      J. Biol. Chem. 266:23204-23214(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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 2).
      Tissue: Umbilical cord blood.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Blood and Ovary.
    6. "Import and processing of heart mitochondrial cyclophilin D."
      Johnson N., Khan A., Virji S., Ward J.M., Crompton M.
      Eur. J. Biochem. 263:353-359(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect."
      Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J., Gunter T.E.
      J. Biol. Chem. 284:9692-9699(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BCL2.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Complement 1q-binding protein inhibits the mitochondrial permeability transition pore and protects against oxidative stress-induced death."
      McGee A.M., Baines C.P.
      Biochem. J. 433:119-125(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C1QBP.
    10. "Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore."
      Nguyen T.T., Stevens M.V., Kohr M., Steenbergen C., Sack M.N., Murphy E.
      J. Biol. Chem. 286:40184-40192(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-203.
    11. "p53 opens the mitochondrial permeability transition pore to trigger necrosis."
      Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S., Moll U.M.
      Cell 149:1536-1548(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    12. "Crystal engineering yields crystals of cyclophilin D diffracting to 1.7 A resolution."
      Schlatter D., Thoma R., Kung E., Stihle M., Muller F., Borroni E., Cesura A., Hennig M.
      Acta Crystallogr. D 61:513-519(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 43-207.
    13. "Crystal structure of human cyclophilin D in complex with its inhibitor, cyclosporin A at 0.96-A resolution."
      Kajitani K., Fujihashi M., Kobayashi Y., Shimizu S., Tsujimoto Y., Miki K.
      Proteins 70:1635-1639(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) OF 44-207 IN COMPLEX WITH CYCLOSPORIN A.
    14. "In-plate protein crystallization, in situ ligand soaking and X-ray diffraction."
      le Maire A., Gelin M., Pochet S., Hoh F., Pirocchi M., Guichou J.F., Ferrer J.L., Labesse G.
      Acta Crystallogr. D 67:747-755(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 44-207.

    Entry informationi

    Entry nameiPPIF_HUMAN
    AccessioniPrimary (citable) accession number: P30405
    Secondary accession number(s): Q2YDB7, Q5W131
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 138 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 10
      Human chromosome 10: 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