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P62937 (PPIA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase A

Short name=PPIase A
EC=5.2.1.8
Alternative name(s):
Cyclophilin A
Cyclosporin A-binding protein
Rotamase A
Gene names
Name:PPIA
Synonyms:CYPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

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

Enzyme regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

Subunit structure

Interacts with HIV-1 Capsid protein. Ref.13

Subcellular location

Cytoplasm. Secreted. Note: Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation. Ref.14

Post-translational modification

Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition. Ref.11 Ref.32

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Secreted
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA-dependent DNA replication

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

entry into host cell

Traceable author statement. Source: Reactome

establishment of integrated proviral latency

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

lipid particle organization

Inferred from mutant phenotype PubMed 21711559. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of protein secretion

Inferred from mutant phenotype PubMed 21711559. Source: UniProtKB

positive regulation of viral genome replication

Inferred from mutant phenotype PubMed 19932913. Source: UniProtKB

protein folding

Traceable author statement PubMed 2179953PubMed 2644542. Source: UniProtKB

protein peptidyl-prolyl isomerization

Inferred from direct assay PubMed 14993672. Source: UniProtKB

regulation of viral genome replication

Inferred from mutant phenotype PubMed 11250896. Source: UniProtKB

uncoating of virus

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral release from host cell

Traceable author statement PubMed 21711559. Source: UniProtKB

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay PubMed 16780588. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay PubMed 16780588. Source: UniProtKB

   Molecular_functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay PubMed 14993672. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12730686PubMed 16169070PubMed 16273344PubMed 23152499PubMed 23935497. Source: IntAct

unfolded protein binding

Traceable author statement PubMed 2644542. Source: UniProtKB

virion binding

Non-traceable author statement PubMed 11250896. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB82EBI-437708,EBI-6927873From a different organism.
gagQ724976EBI-437708,EBI-1036263From a different organism.
PTPRNQ168493EBI-437708,EBI-728153
SUPT5HO002672EBI-437708,EBI-710464

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165Peptidyl-prolyl cis-trans isomerase A
PRO_0000423240
Initiator methionine11Removed; alternate Ref.8 Ref.9 Ref.10 Ref.11
Chain2 – 165164Peptidyl-prolyl cis-trans isomerase A, N-terminally processed
PRO_0000064115

Regions

Domain7 – 163157PPIase cyclophilin-type

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15 Ref.19 Ref.20
Modified residue21N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed Ref.11 Ref.15
Modified residue281N6-acetyllysine; alternate Ref.16
Modified residue441N6-acetyllysine Ref.16
Modified residue761N6-acetyllysine Ref.16
Modified residue821N6-acetyllysine Ref.16
Modified residue931Phosphothreonine Ref.17
Modified residue1251N6-acetyllysine Ref.16 Ref.32
Modified residue1311N6-acetyllysine Ref.16
Modified residue1331N6-acetyllysine By similarity
Glycosylation1081N-linked (GlcNAc...) Potential
Cross-link28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Experimental info

Mutagenesis1211W → A: 200-fold decrease of sensitivity to CsA. Ref.12
Mutagenesis1211W → F: 75-fold decrease of sensitivity to CsA. Ref.12
Sequence conflict891I → T in AAH05982. Ref.7
Sequence conflict1061N → I in AAH07104. Ref.7
Sequence conflict1651E → D in CAG32988. Ref.4

Secondary structure

....................................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62937 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9B2E637A555E4434

FASTA16518,012
        10         20         30         40         50         60 
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE 

       130        140        150        160 
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE 

« Hide

References

« Hide 'large scale' references
[1]"Complementary DNA for human T-cell cyclophilin."
Haendler B., Hofer-Warbinek R., Hofer E.
EMBO J. 6:947-950(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leukemic T-cell.
[2]"Characterization of the human cyclophilin gene and of related processed pseudogenes."
Haendler B., Hofer E.
Eur. J. Biochem. 190:477-482(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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. expand/collapse author list , 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].
Tissue: Subthalamic nucleus.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]NIEHS SNPs program
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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].
Tissue: Bone marrow, Brain, Cervix, Colon, Lung, Skeletal muscle, Skin and Urinary bladder.
[8]"Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy."
Meier U., Beier-Hellwig K., Klug J., Linder D., Beier H.M.
Hum. Reprod. 10:1305-1310(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30.
[9]"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 2-19.
Tissue: Platelet.
[10]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[11]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[12]"Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue."
Liu J., Chen C.-M., Walsh C.T.
Biochemistry 30:2306-2310(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-121.
[13]"Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B."
Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.
Cell 73:1067-1078(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 CAPSID PROTEIN.
[14]"Cyclophilin A is secreted by a vesicular pathway in vascular smooth muscle cells."
Suzuki J., Jin Z.G., Meoli D.F., Matoba T., Berk B.C.
Circ. Res. 98:811-817(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-76; LYS-82; LYS-125 AND LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy."
Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H., Wuethrich K., Walkinshaw M.D.
Nature 353:276-279(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), STRUCTURE BY NMR.
[22]"Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A resolution."
Ke H., Zydowsky L.D., Liu J., Walsh C.T.
Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[23]"X-ray structure of a decameric cyclophilin-cyclosporin crystal complex."
Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M., Walkinshaw M.D.
Nature 361:91-94(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CYCLOPHILIN.
[24]"X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1-A resolution."
Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.
J. Mol. Biol. 234:1119-1130(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[25]"Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization."
Zhao Y., Ke H.
Biochemistry 35:7356-7361(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[26]"Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein."
Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.
Protein Sci. 6:2297-2307(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
[27]"X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A."
Kallen J., Mikol V., Taylor P., Walkinshaw M.D.
J. Mol. Biol. 283:435-449(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[28]"Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes."
Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.
Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
[29]"Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin."
Jin L., Harrison S.C.
Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
[30]"Solution structure of the cyclosporin A/cyclophilin complex by NMR."
Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T., Holzman T.F., Simmer R.L., Fesik S.W.
Nature 361:88-91(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF COMPLEX WITH CYCLOPHILIN.
[31]"The NMR solution conformation of unligated human cyclophilin A."
Ottiger M., Zerbe O., Guentert P., Wuethrich K.
J. Mol. Biol. 272:64-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[32]"Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization."
Lammers M., Neumann H., Chin J.W., James L.C.
Nat. Chem. Biol. 6:331-337(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) ALONE AND IN COMPLEX WITH CYCLOSPORINE AND HIV-1 CAPSID, ACETYLATION AT LYS-125.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Cyclophilin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00052 mRNA. Translation: CAA68264.1.
X52851 Genomic DNA. Translation: CAA37039.1.
AK290085 mRNA. Translation: BAF82774.1.
CR456707 mRNA. Translation: CAG32988.1.
AB451307 mRNA. Translation: BAG70121.1.
AB451438 mRNA. Translation: BAG70252.1.
AY739283 Genomic DNA. Translation: AAU13906.1.
BC000689 mRNA. Translation: AAH00689.1.
BC003026 mRNA. Translation: AAH03026.2.
BC005320 mRNA. Translation: AAH05320.1.
BC005982 mRNA. Translation: AAH05982.1.
BC007104 mRNA. Translation: AAH07104.1.
BC013915 mRNA. Translation: AAH13915.1.
BC073992 mRNA. Translation: AAH73992.1.
BC106030 mRNA. Translation: AAI06031.1.
BC137057 mRNA. Translation: AAI37058.1.
BC137058 mRNA. Translation: AAI37059.1.
CCDSCCDS5494.1.
PIRCSHUA. A94496.
RefSeqNP_066953.1. NM_021130.3.
UniGeneHs.356331.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AK4X-ray2.36A/B1-165[»]
1AWQX-ray1.58A2-165[»]
1AWRX-ray1.58A/B/C/D/E/F2-165[»]
1AWSX-ray2.55A2-165[»]
1AWTX-ray2.55A/B/C/D/E/F2-165[»]
1AWUX-ray2.34A2-165[»]
1AWVX-ray2.34A/B/C/D/E/F2-165[»]
1BCKX-ray1.80A1-165[»]
1CWAX-ray2.10A1-165[»]
1CWBX-ray2.20A1-165[»]
1CWCX-ray1.86A1-165[»]
1CWFX-ray1.86A1-165[»]
1CWHX-ray1.86A1-165[»]
1CWIX-ray1.90A1-165[»]
1CWJX-ray1.80A1-165[»]
1CWKX-ray1.80A1-165[»]
1CWLX-ray1.80A1-165[»]
1CWMX-ray2.00A1-165[»]
1CWOX-ray1.86A1-165[»]
1FGLX-ray1.80A1-165[»]
1M63X-ray2.80C/G1-165[»]
1M9CX-ray2.00A/B1-165[»]
1M9DX-ray1.90A/B1-165[»]
1M9EX-ray1.72A/B1-164[»]
1M9FX-ray1.73A/B1-165[»]
1M9XX-ray1.70A/B/E/F1-165[»]
1M9YX-ray1.90A/B/E/F1-165[»]
1MF8X-ray3.10C1-165[»]
1MIKX-ray1.76A1-165[»]
1NMKX-ray2.10A/B1-165[»]
1OCANMR-A1-165[»]
1RMHX-ray2.40A/B2-165[»]
1VBSX-ray2.00A1-165[»]
1VBTX-ray2.30A/B1-165[»]
1W8LX-ray1.80A2-165[»]
1W8MX-ray1.65A2-165[»]
1W8VX-ray1.70A2-165[»]
1YNDX-ray1.60A/B1-165[»]
1ZKFX-ray2.55A/B1-165[»]
2ALFX-ray1.90A2-165[»]
2CPLX-ray1.63A1-165[»]
2CYHX-ray1.64A2-165[»]
2RMAX-ray2.10A/C/E/G/I/K/M/O/Q/S1-165[»]
2RMBX-ray2.10A/C/E/G/I/K/M/O/Q/S1-165[»]
2X25X-ray1.20B2-165[»]
2X2AX-ray1.40A/B1-165[»]
2X2CX-ray2.41K/M/O/Q/S1-165[»]
2X2DX-ray1.95B/C1-165[»]
2XGYX-ray1.80B1-165[»]
3CYHX-ray1.90A2-165[»]
3CYSNMR-A1-165[»]
3K0MX-ray1.25A1-165[»]
3K0NX-ray1.39A1-165[»]
3K0OX-ray1.55A1-165[»]
3K0PX-ray1.65A1-165[»]
3K0QX-ray2.32A1-165[»]
3K0RX-ray2.42A1-165[»]
3ODIX-ray2.20A/C/E/G/I/K/M/O/Q/S1-165[»]
3ODLX-ray2.31A/C/E/G/I/K/M/O/Q/S1-165[»]
3RDDX-ray2.14A1-165[»]
4CYHX-ray2.10A2-165[»]
4IPZX-ray1.67A1-165[»]
5CYHX-ray2.10A2-165[»]
ProteinModelPortalP62937.
SMRP62937. Positions 2-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111474. 62 interactions.
DIPDIP-6080N.
IntActP62937. 38 interactions.
MINTMINT-4999116.
STRING9606.ENSP00000419425.

Chemistry

BindingDBP62937.
ChEMBLCHEMBL1949.
DrugBankDB00091. Cyclosporine.
DB00172. L-Proline.
GuidetoPHARMACOLOGY2751.

PTM databases

PhosphoSiteP62937.

Polymorphism databases

DMDM51702775.

2D gel databases

DOSAC-COBS-2DPAGEP62937.
OGPP62937.
REPRODUCTION-2DPAGEIPI00419585.
P62937.
SWISS-2DPAGEP62937.
UCD-2DPAGEP62937.

Proteomic databases

MaxQBP62937.
PaxDbP62937.
PeptideAtlasP62937.
PRIDEP62937.

Protocols and materials databases

DNASU5478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000468812; ENSP00000419425; ENSG00000196262.
GeneID5478.
KEGGhsa:5478.
UCSCuc003tlw.3. human.

Organism-specific databases

CTD5478.
GeneCardsGC07P044803.
HGNCHGNC:9253. PPIA.
HPACAB004655.
MIM123840. gene.
neXtProtNX_P62937.
PharmGKBPA33574.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOVERGENHBG001065.
InParanoidP62937.
KOK03767.
OMAHVERMVT.
PhylomeDBP62937.
TreeFamTF316719.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP62937.
BgeeP62937.
CleanExHS_PPIA.
GenevestigatorP62937.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIA. human.
EvolutionaryTraceP62937.
GeneWikiPeptidylprolyl_isomerase_A.
GenomeRNAi5478.
NextBio21206.
PROP62937.
SOURCESearch...

Entry information

Entry namePPIA_HUMAN
AccessionPrimary (citable) accession number: P62937
Secondary accession number(s): A8K220 expand/collapse secondary AC list , P05092, Q3KQW3, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM