P62937 (PPIA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Secreted
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Acetylation Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA-dependent DNA replication Traceable author statement. Source: Reactome entry into host cell 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 uncoating of virus Traceable author statement. Source: Reactome viral release from host cell Traceable author statement PubMed 21711559. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay PubMed 16780588. Source: UniProtKB extracellular region Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 16780588. Source: UniProtKB
Molecular_function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay PubMed 14993672. Source: UniProtKB 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
gag	Q72497	6	EBI-437708,EBI-1036263	From a different organism.
PTPRN	Q16849	3	EBI-437708,EBI-728153
SUPT5H	O00267	2	EBI-437708,EBI-710464

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9 Ref.10 Ref.11

Chain

2 – 165

164

Peptidyl-prolyl cis-trans isomerase A

PRO_0000064115

Regions

Domain

7 – 163

157

PPIase cyclophilin-type

Amino acid modifications

Modified residue

2

1

N-acetylvaline; partial Ref.11

Modified residue

21

1

Phosphoserine By similarity

Modified residue

28

1

N6-acetyllysine; alternate Ref.16

Modified residue

44

1

N6-acetyllysine Ref.16

Modified residue

76

1

N6-acetyllysine Ref.16

Modified residue

82

1

N6-acetyllysine Ref.16

Modified residue

93

1

Phosphothreonine Ref.17

Modified residue

125

1

N6-acetyllysine Ref.16 Ref.30

Modified residue

131

1

N6-acetyllysine Ref.16

Glycosylation

108

1

N-linked (GlcNAc...) Potential

Cross-link

28

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.15

Experimental info

Mutagenesis

121

1

W → A: 200-fold decrease of sensitivity to CsA. Ref.12

Mutagenesis

121

1

W → F: 75-fold decrease of sensitivity to CsA. Ref.12

Sequence conflict

89

1

I → T in AAH05982. Ref.7

Sequence conflict

106

1

N → I in AAH07104. Ref.7

Sequence conflict

165

1

E → D in CAG32988. Ref.4

Secondary structure

1

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165

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

15 – 24

10

Turn

26 – 28

3

Helix

30 – 41

12

Turn

42 – 44

3

Beta strand

52 – 57

6

Turn

58 – 60

3

Beta strand

61 – 64

4

Turn

67 – 69

3

Beta strand

70 – 73

4

Beta strand

78 – 81

4

Beta strand

97 – 100

4

Beta strand

102 – 104

3

Beta strand

108 – 110

3

Beta strand

112 – 117

6

Helix

120 – 122

3

Turn

123 – 125

3

Beta strand

128 – 134

7

Helix

136 – 143

8

Helix

148 – 150

3

Turn

153 – 155

3

Beta strand

156 – 164

9

Sequences

	Sequence		Length	Mass (Da)
	P62937 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9B2E637A555E4434	FASTA	165	18,012
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, 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]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-28, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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]	"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.
[20]	"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).
[21]	"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.
[22]	"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).
[23]	"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).
[24]	"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).
[25]	"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).
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.

IPI

IPI00419585.

PIR

CSHUA. A94496.

RefSeq

NP_066953.1. NM_021130.3.

UniGene

Hs.356331.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AK4	X-ray	2.36	A/B	2-164	[»]
1AWQ	X-ray	1.58	A	2-165	[»]
1AWR	X-ray	1.58	A/B/C/D/E/F	2-165	[»]
1AWS	X-ray	2.55	A	2-165	[»]
1AWT	X-ray	2.55	A/B/C/D/E/F	2-165	[»]
1AWU	X-ray	2.34	A	2-165	[»]
1AWV	X-ray	2.34	A/B/C/D/E/F	2-165	[»]
1BCK	X-ray	1.80	A	1-165	[»]
1CWA	X-ray	2.10	A	1-165	[»]
1CWB	X-ray	2.20	A	1-165	[»]
1CWC	X-ray	1.86	A	1-165	[»]
1CWF	X-ray	1.86	A	1-165	[»]
1CWH	X-ray	1.86	A	1-165	[»]
1CWI	X-ray	1.90	A	1-165	[»]
1CWJ	X-ray	1.80	A	1-165	[»]
1CWK	X-ray	1.80	A	1-165	[»]
1CWL	X-ray	1.80	A	1-165	[»]
1CWM	X-ray	2.00	A	1-165	[»]
1CWO	X-ray	1.86	A	2-164	[»]
1FGL	X-ray	1.80	A	2-164	[»]
1M63	X-ray	2.80	C/G	1-165	[»]
1M9C	X-ray	2.00	A/B	1-164	[»]
1M9D	X-ray	1.90	A/B	1-164	[»]
1M9E	X-ray	1.72	A/B	1-163	[»]
1M9F	X-ray	1.73	A/B	1-164	[»]
1M9X	X-ray	1.70	A/B/E/F	1-164	[»]
1M9Y	X-ray	1.90	A/B/E/F	1-164	[»]
1MF8	X-ray	3.10	C	1-165	[»]
1MIK	X-ray	1.76	A	1-165	[»]
1NMK	X-ray	2.10	A/B	1-165	[»]
1OCA	NMR	-	A	1-165	[»]
1RMH	X-ray	2.40	A/B	2-165	[»]
1VBS	X-ray	2.00	A	1-165	[»]
1VBT	X-ray	2.30	A/B	1-165	[»]
1W8L	X-ray	1.80	A	2-164	[»]
1W8M	X-ray	1.65	A	2-164	[»]
1W8V	X-ray	1.70	A	2-164	[»]
1YND	X-ray	1.60	A/B	1-165	[»]
1ZKF	X-ray	2.55	A/B	1-165	[»]
2ALF	X-ray	1.90	A	2-164	[»]
2CPL	X-ray	1.63	A	2-164	[»]
2CYH	X-ray	1.64	A	2-165	[»]
2RMA	X-ray	2.10	A/C/E/G/I/K/M/O/Q/S	2-164	[»]
2RMB	X-ray	2.10	A/C/E/G/I/K/M/O/Q/S	2-164	[»]
2X25	X-ray	1.20	B	2-165	[»]
2X2A	X-ray	1.40	A/B	1-165	[»]
2X2C	X-ray	2.41	K/M/O/Q/S	1-165	[»]
2X2D	X-ray	1.95	B/C	1-165	[»]
2XGY	X-ray	1.80	B	1-165	[»]
3CYH	X-ray	1.90	A	2-165	[»]
3CYS	NMR	-	A	1-165	[»]
3K0M	X-ray	1.25	A	1-165	[»]
3K0N	X-ray	1.39	A	1-165	[»]
3K0O	X-ray	1.55	A	1-165	[»]
3K0P	X-ray	1.65	A	1-165	[»]
3K0Q	X-ray	2.32	A	1-165	[»]
3K0R	X-ray	2.42	A	1-165	[»]
3ODI	X-ray	2.20	A/C/E/G/I/K/M/O/Q/S	1-165	[»]
3ODL	X-ray	2.31	A/C/E/G/I/K/M/O/Q/S	1-165	[»]
3RDD	X-ray	2.14	A	1-165	[»]
4CYH	X-ray	2.10	A	2-165	[»]
5CYH	X-ray	2.10	A	2-165	[»]

ProteinModelPortal

P62937.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6080N.

IntAct

P62937. 33 interactions.

MINT

MINT-4999116.

STRING

9606.ENSP00000419425.

PTM databases

PhosphoSite

P62937.

Polymorphism databases

DMDM

51702775.

2D gel databases

DOSAC-COBS-2DPAGE

P62937.

OGP

P62937.

REPRODUCTION-2DPAGE

IPI00419585.
P62937.

SWISS-2DPAGE

P62937.

UCD-2DPAGE

P62937.

Proteomic databases

PaxDb

P62937.

PeptideAtlas

P62937.

PRIDE

P62937.

Protocols and materials databases

DNASU

5478.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000468812; ENSP00000419425; ENSG00000196262.

GeneID

5478.

KEGG

hsa:5478.

UCSC

uc003tlw.3. human.

Organism-specific databases

CTD

5478.

GeneCards

GC07P044803.

HGNC

HGNC:9253. PPIA.

HPA

CAB004655.

MIM

123840. gene.

neXtProt

NX_P62937.

PharmGKB

PA33574.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0652.

HOVERGEN

HBG001065.

InParanoid

P62937.

KO

K03767.

OMA

IVIQLFP.

OrthoDB

EOG4DJJXN.

PhylomeDB

P62937.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P62937.

Bgee

P62937.

CleanEx

HS_PPIA.

Genevestigator

P62937.

GermOnline

ENSG00000196262. Homo sapiens.
ENSG00000198618. Homo sapiens.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62937.

ChEMBL

CHEMBL1949.

ChiTaRS

PPIA. human.

DrugBank

DB00091. Cyclosporine.
DB00172. L-Proline.

EvolutionaryTrace

P62937.

GenomeRNAi

5478.

NextBio

21206.

SOURCE

Search...

Entry information

Entry name

PPIA_HUMAN

Accession

Primary (citable) accession number: P62937
Secondary accession number(s): A8K220 , 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:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.