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Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

PPID

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. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. May be involved in hepatitis C virus (HCV) replication and release.7 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

Enzyme regulationi

Less sensitive to inhibition by cyclosporin A than is CYP-18.

GO - Molecular functioni

  • cyclosporin A binding Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • heat shock protein binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • Hsp90 protein binding Source: UniProtKB
  • peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cellular response to UV-A Source: UniProtKB
  • chaperone-mediated protein folding Source: UniProtKB
  • lipid particle organization Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of protein secretion Source: UniProtKB
  • positive regulation of viral genome replication Source: UniProtKB
  • protein complex assembly Source: UniProtKB
  • protein folding Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • viral release from host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Apoptosis, Protein transport, Transport

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase D (EC:5.2.1.8)
Short name:
PPIase D
Alternative name(s):
40 kDa peptidyl-prolyl cis-trans isomerase
Cyclophilin-40
Short name:
CYP-40
Cyclophilin-related protein
Rotamase D
Gene namesi
Name:PPID
Synonyms:CYP40, CYPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9257. PPID.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 2271K → A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8. 2 Publications
Mutagenesisi231 – 2311N → A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8. 2 Publications
Mutagenesisi234 – 2341F → A: Impairs interaction with HSP90AB1 and HSPA8. 2 Publications
Mutagenesisi274 – 2741S → L: Impairs interaction with HSP90AB1 and HSPA8. 2 Publications
Mutagenesisi278 – 2781N → A: Abolishes interaction with HSP90AB1. 2 Publications
Mutagenesisi284 – 2841L → A: Impairs interaction with HSP90AB1 and HSPA8. 2 Publications
Mutagenesisi285 – 2851K → A: Impairs interaction with HSP90AB1 and HSPA8. 2 Publications
Mutagenesisi308 – 3081K → A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8. 2 Publications
Mutagenesisi312 – 3121R → A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8. 2 Publications
Mutagenesisi329 – 3291D → A: Impairs interaction with HSP90AB1. 1 Publication

Organism-specific databases

PharmGKBiPA33582.

Chemistry

ChEMBLiCHEMBL1697657.

Polymorphism and mutation databases

BioMutaiPPID.
DMDMi729274.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 370369Peptidyl-prolyl cis-trans isomerase DPRO_0000064153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei171 – 1711N6-acetyllysineBy similarity
Modified residuei198 – 1981PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ08752.
MaxQBiQ08752.
PaxDbiQ08752.
PeptideAtlasiQ08752.
PRIDEiQ08752.

2D gel databases

REPRODUCTION-2DPAGEIPI00003927.

PTM databases

iPTMnetiQ08752.
PhosphoSiteiQ08752.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ08752.
CleanExiHS_PPID.
ExpressionAtlasiQ08752. baseline and differential.
GenevisibleiQ08752. HS.

Organism-specific databases

HPAiHPA019520.
HPA019692.

Interactioni

Subunit structurei

Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone complexes. Found in HSP90 chaperone complexes with kinase clients LCK or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for binding to HSP90AB1 and the interaction is mutually exclusive with the PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not FKBP4 compete for binding to HSPA8 and the interaction is mutually exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and S100A2; the interactions dissociate the PPID:HSP90AA1 interaction. Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3. Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or DYNC1I2).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ILF2Q129054EBI-716596,EBI-357925
MYBP011032EBI-716596,EBI-6502562From a different organism.
RACK1P632444EBI-716596,EBI-296739
RPS3P233964EBI-716596,EBI-351193
XRCC6P129564EBI-716596,EBI-353208

GO - Molecular functioni

  • estrogen receptor binding Source: UniProtKB
  • heat shock protein binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • Hsp90 protein binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111477. 55 interactions.
DIPiDIP-34893N.
IntActiQ08752. 23 interactions.
MINTiMINT-1399772.
STRINGi9606.ENSP00000303754.

Chemistry

BindingDBiQ08752.

Structurei

3D structure databases

ProteinModelPortaliQ08752.
SMRiQ08752. Positions 2-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 183165PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST
Repeati223 – 25634TPR 1Add
BLAST
Repeati273 – 30634TPR 2Add
BLAST
Repeati307 – 34034TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 21531Chaperone activityBy similarityAdd
BLAST
Regioni214 – 370157Interaction with HSP90AB1By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
HOVERGENiHBG053654.
InParanoidiQ08752.
KOiK05864.
OMAiKGIGHTT.
OrthoDBiEOG79GT7W.
PhylomeDBiQ08752.
TreeFamiTF324493.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q08752-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA
60 70 80 90 100
LCTGEKGIGH TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG
110 120 130 140 150
EKFEDENFHY KHDREGLLSM ANAGRNTNGS QFFITTVPTP HLDGKHVVFG
160 170 180 190 200
QVIKGIGVAR ILENVEVKGE KPAKLCVIAE CGELKEGDDG GIFPKDGSGD
210 220 230 240 250
SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE MAIKKYAEVL
260 270 280 290 300
RYVDSSKAVI ETADRAKLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL
310 320 330 340 350
ELDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQGIAPED KAIQAELLKV
360 370
KQKIKAQKDK EKAVYAKMFA
Length:370
Mass (Da):40,764
Last modified:January 23, 2007 - v3
Checksum:i39D4100748B35D48
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491R → C.1 Publication
Corresponds to variant rs2070631 [ dbSNP | Ensembl ].
VAR_021021
Natural varianti196 – 1961D → V.
Corresponds to variant rs2230222 [ dbSNP | Ensembl ].
VAR_051771
Natural varianti302 – 3021L → I.1 Publication
Corresponds to variant rs9410 [ dbSNP | Ensembl ].
VAR_021022
Natural varianti335 – 3351G → E.1 Publication
Corresponds to variant rs17843956 [ dbSNP | Ensembl ].
VAR_021023

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11667 mRNA. Translation: AAA35731.1.
D63861 Genomic DNA. Translation: BAA09923.1.
AY714221 Genomic DNA. Translation: AAT97986.1.
AK313929 mRNA. Translation: BAG36649.1.
CH471056 Genomic DNA. Translation: EAX04853.1.
BC030707 mRNA. Translation: AAH30707.1.
CCDSiCCDS3801.1.
PIRiA45981.
RefSeqiNP_005029.1. NM_005038.2.
UniGeneiHs.183958.

Genome annotation databases

EnsembliENST00000307720; ENSP00000303754; ENSG00000171497.
GeneIDi5481.
KEGGihsa:5481.
UCSCiuc003iqc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Cyclophilin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11667 mRNA. Translation: AAA35731.1.
D63861 Genomic DNA. Translation: BAA09923.1.
AY714221 Genomic DNA. Translation: AAT97986.1.
AK313929 mRNA. Translation: BAG36649.1.
CH471056 Genomic DNA. Translation: EAX04853.1.
BC030707 mRNA. Translation: AAH30707.1.
CCDSiCCDS3801.1.
PIRiA45981.
RefSeqiNP_005029.1. NM_005038.2.
UniGeneiHs.183958.

3D structure databases

ProteinModelPortaliQ08752.
SMRiQ08752. Positions 2-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111477. 55 interactions.
DIPiDIP-34893N.
IntActiQ08752. 23 interactions.
MINTiMINT-1399772.
STRINGi9606.ENSP00000303754.

Chemistry

BindingDBiQ08752.
ChEMBLiCHEMBL1697657.

PTM databases

iPTMnetiQ08752.
PhosphoSiteiQ08752.

Polymorphism and mutation databases

BioMutaiPPID.
DMDMi729274.

2D gel databases

REPRODUCTION-2DPAGEIPI00003927.

Proteomic databases

EPDiQ08752.
MaxQBiQ08752.
PaxDbiQ08752.
PeptideAtlasiQ08752.
PRIDEiQ08752.

Protocols and materials databases

DNASUi5481.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307720; ENSP00000303754; ENSG00000171497.
GeneIDi5481.
KEGGihsa:5481.
UCSCiuc003iqc.4. human.

Organism-specific databases

CTDi5481.
GeneCardsiPPID.
HGNCiHGNC:9257. PPID.
HPAiHPA019520.
HPA019692.
MIMi601753. gene.
neXtProtiNX_Q08752.
PharmGKBiPA33582.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
HOVERGENiHBG053654.
InParanoidiQ08752.
KOiK05864.
OMAiKGIGHTT.
OrthoDBiEOG79GT7W.
PhylomeDBiQ08752.
TreeFamiTF324493.

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.

Miscellaneous databases

ChiTaRSiPPID. human.
GeneWikiiPPID.
GenomeRNAii5481.
PROiQ08752.
SOURCEiSearch...

Gene expression databases

BgeeiQ08752.
CleanExiHS_PPID.
ExpressionAtlasiQ08752. baseline and differential.
GenevisibleiQ08752. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization."
    Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E., Bayney R.M.
    J. Biol. Chem. 268:12303-12310(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Pancreas.
  2. "The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene."
    Yokoi H., Shimizu Y., Anazawa H., Lefebvre C.A., Korneluk R.G., Ikeda J.E.
    Genomics 35:448-455(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. NIEHS SNPs program
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-49; ILE-302 AND GLU-335.
  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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17.
    Tissue: Platelet.
  8. "Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism."
    Leverson J.D., Ness S.A.
    Mol. Cell 1:203-211(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYB.
  9. "Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock."
    Mark P.J., Ward B.K., Kumar P., Lahooti H., Minchin R.F., Ratajczak T.
    Cell Stress Chaperones 6:59-70(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40."
    Pirkl F., Buchner J.
    J. Mol. Biol. 308:795-806(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
  11. "A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90."
    Ward B.K., Allan R.K., Mok D., Temple S.E., Taylor P., Dornan J., Mark P.J., Shaw D.J., Kumar P., Walkinshaw M.D., Ratajczak T.
    J. Biol. Chem. 277:40799-40809(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AB1, MUTAGENESIS OF LYS-227; ASN-231; PHE-234; SER-274; ASN-278; LEU-284; LYS-285; LYS-308; ARG-312 AND ASP-329.
  12. "High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients."
    Scroggins B.T., Prince T., Shao J., Uma S., Huang W., Guo Y., Yun B.G., Hedman K., Matts R.L., Hartson S.D.
    Biochemistry 42:12550-12561(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN HSP90 COMPLEXES.
  13. Cited for: INTERACTION WITH HSPA8, MUTAGENESIS OF LYS-227; ASN-231; PHE-234; SER-274; ASN-278; LEU-284; LYS-285; LYS-308 AND ARG-312.
  14. "Cyclophilin-40 has a cellular role in the aryl hydrocarbon receptor signaling."
    Luu T.C., Bhattacharya P., Chan W.K.
    FEBS Lett. 582:3167-3173(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. Cited for: FUNCTION.
  18. "Identification of cyclophilin-40-interacting proteins reveals potential cellular function of cyclophilin-40."
    Park M.S., Chu F., Xie J., Wang Y., Bhattacharya P., Chan W.K.
    Anal. Biochem. 410:257-265(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ILF2; XRCC6; RACK1 AND RPS3.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion."
    Anderson L.J., Lin K., Compton T., Wiedmann B.
    Virol. J. 8:329-329(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "The heat shock protein-90 co-chaperone, Cyclophilin 40, promotes ALK-positive, anaplastic large cell lymphoma viability and its expression is regulated by the NPM-ALK oncoprotein."
    Pearson J.D., Mohammed Z., Bacani J.T., Lai R., Ingham R.J.
    BMC Cancer 12:229-229(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Cyclophilin 40 alters UVA-induced apoptosis and mitochondrial ROS generation in keratinocytes."
    Jandova J., Janda J., Sligh J.E.
    Exp. Cell Res. 319:750-760(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  24. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPPID_HUMAN
AccessioniPrimary (citable) accession number: Q08752
Secondary accession number(s): B2R9V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 159 of the entry and version 3 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

Caution

This protein should not be confused with mitochondrial peptidyl-prolyl cis-trans isomerase F (PPIF) which is often referred to as cyclophilin D or CypD.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.