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P30405 - PPIF_HUMAN

UniProt

P30405 - PPIF_HUMAN

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Protein

Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Gene

PPIF

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

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: GO_Central

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. necroptotic process Source: Ensembl
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of ATPase activity Source: UniProtKB
  8. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  9. negative regulation of oxidative phosphorylation Source: UniProtKB
  10. negative regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
  11. negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
  12. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  13. protein folding Source: InterPro
  14. protein peptidyl-prolyl isomerization Source: GO_Central
  15. regulation of mitochondrial membrane permeability Source: UniProtKB
  16. regulation of mitochondrial membrane permeability involved in programmed necrotic cell death Source: UniProtKB
  17. regulation of necrotic cell death Source: Ensembl
  18. regulation of proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
  19. response to ischemia Source: UniProtKB
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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: GO_Central
Complete GO annotation...

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

BgeeiP30405.
CleanExiHS_PPIF.
ExpressionAtlasiP30405. baseline and differential.
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. 27 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 – 548Combined sources
Beta strandi57 – 6610Combined sources
Turni68 – 703Combined sources
Helixi72 – 8312Combined sources
Turni84 – 863Combined sources
Beta strandi94 – 996Combined sources
Turni100 – 1023Combined sources
Beta strandi103 – 1064Combined sources
Turni109 – 1113Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1596Combined sources
Helixi162 – 1643Combined sources
Turni165 – 1673Combined sources
Beta strandi170 – 1767Combined sources
Helixi178 – 1869Combined sources
Beta strandi198 – 2058Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP30405.
KOiK09565.
OMAiDVGADNQ.
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

        10         20         30         40         50
MLALRCGSRW LGLLSVPRSV PLRLPAARAC SKGSGDPSSS SSSGNPLVYL 
        60         70         80         90        100
DVDANGKPLG RVVLELKADV VPKTAENFRA LCTGEKGFGY KGSTFHRVIP 
       110        120        130        140        150
SFMCQAGDFT NHNGTGGKSI YGSRFPDENF TLKHVGPGVL SMANAGPNTN 
       160        170        180        190        200
GSQFFICTIK TDWLDGKHVV FGHVKEGMDV VKKIESFGSK SGRTSKKIVI 

TDCGQLS
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:
EMBLi
GenBanki
DDBJi
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. [P30405-1]
PIRiA41581.
RefSeqiNP_005720.1. NM_005729.3. [P30405-1]
UniGeneiHs.381072.

Genome annotation databases

EnsembliENST00000225174; ENSP00000225174; ENSG00000108179. [P30405-1]
ENST00000394579; ENSP00000378080; ENSG00000108179. [P30405-2]
GeneIDi10105.
KEGGihsa:10105.
UCSCiuc001kai.3. human. [P30405-1]
uc001kaj.3. human.

Polymorphism databases

DMDMi231968.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P30405-1]
PIRiA41581.
RefSeqiNP_005720.1. NM_005729.3. [P30405-1]
UniGeneiHs.381072.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi115411. 27 interactions.
IntActiP30405. 5 interactions.
MINTiMINT-3011711.
STRINGi9606.ENSP00000225174.

Chemistry

DrugBankiDB00091. Cyclosporine.
DB00172. L-Proline.

PTM databases

PhosphoSiteiP30405.

Polymorphism databases

DMDMi231968.

2D gel databases

OGPiP30405.
UCD-2DPAGEP30405.

Proteomic databases

MaxQBiP30405.
PaxDbiP30405.
PeptideAtlasiP30405.
PRIDEiP30405.

Protocols and materials databases

DNASUi10105.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225174; ENSP00000225174; ENSG00000108179. [P30405-1]
ENST00000394579; ENSP00000378080; ENSG00000108179. [P30405-2]
GeneIDi10105.
KEGGihsa:10105.
UCSCiuc001kai.3. human. [P30405-1]
uc001kaj.3. human.

Organism-specific databases

CTDi10105.
GeneCardsiGC10P081107.
HGNCiHGNC:9259. PPIF.
MIMi604486. gene.
neXtProtiNX_P30405.
PharmGKBiPA33584.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP30405.
KOiK09565.
OMAiDVGADNQ.
OrthoDBiEOG79GT7W.
PhylomeDBiP30405.
TreeFamiTF312801.

Miscellaneous databases

ChiTaRSiPPIF. human.
EvolutionaryTraceiP30405.
GeneWikiiPPIF.
GenomeRNAii10105.
NextBioi38221.
PROiP30405.
SOURCEiSearch...

Gene expression databases

BgeeiP30405.
CleanExiHS_PPIF.
ExpressionAtlasiP30405. baseline and differential.
GenevestigatoriP30405.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 142 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

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.