HUMAN:PPIA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PPIA (synonyms: CYPA)
Protein Name(s)	Peptidyl-prolyl cis-trans isomerase A PPIase A Cyclophilin A Cyclosporin A-binding protein Rotamase A Peptidyl-prolyl cis-trans isomerase A, N-terminally processed
External Links
UniProt	P62937
EMBL	Y00052 X52851 AK290085 AK293003 CR456707 AB451307 AB451438 AY739283 AC004854 AC013436 BC000689 BC003026 BC005320 BC005982 BC007104 BC013915 BC073992 BC093076 BC106030 BC137057 BC137058
CCDS	CCDS5494.1 CCDS75592.1
PIR	A94496
RefSeq	NP_001287910.1 NP_066953.1
UniGene	Hs.356331
PDB	1AK4 1AWQ 1AWR 1AWS 1AWT 1AWU 1AWV 1BCK 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1FGL 1M63 1M9C 1M9D 1M9E 1M9F 1M9X 1M9Y 1MF8 1MIK 1NMK 1OCA 1RMH 1VBS 1VBT 1W8L 1W8M 1W8V 1YND 1ZKF 2ALF 2CPL 2CYH 2RMA 2RMB 2X25 2X2A 2X2C 2X2D 2XGY 3CYH 3CYS 3K0M 3K0N 3K0O 3K0P 3K0Q 3K0R 3ODI 3ODL 3RDD 4CYH 4IPZ 5CYH
PDBsum	1AK4 1AWQ 1AWR 1AWS 1AWT 1AWU 1AWV 1BCK 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1FGL 1M63 1M9C 1M9D 1M9E 1M9F 1M9X 1M9Y 1MF8 1MIK 1NMK 1OCA 1RMH 1VBS 1VBT 1W8L 1W8M 1W8V 1YND 1ZKF 2ALF 2CPL 2CYH 2RMA 2RMB 2X25 2X2A 2X2C 2X2D 2XGY 3CYH 3CYS 3K0M 3K0N 3K0O 3K0P 3K0Q 3K0R 3ODI 3ODL 3RDD 4CYH 4IPZ 5CYH
ProteinModelPortal	P62937
SMR	P62937
BioGrid	111474
DIP	DIP-6080N
IntAct	P62937
MINT	MINT-4999116
STRING	9606.ENSP00000419425
BindingDB	P62937
ChEMBL	CHEMBL1949
DrugBank	DB00091 DB00172
GuidetoPHARMACOLOGY	2751
PhosphoSite	P62937
DMDM	51702775
DOSAC-COBS-2DPAGE	P62937
OGP	P62937
REPRODUCTION-2DPAGE	IPI00419585 P62937
SWISS-2DPAGE	P62937
UCD-2DPAGE	P62937
MaxQB	P62937
PaxDb	P62937
PeptideAtlas	P62937
PRIDE	P62937
DNASU	5478
Ensembl	ENST00000355968 ENST00000468812 ENST00000489459 ENST00000620047
GeneID	5478
KEGG	hsa:5478
UCSC	uc003tlw.3
CTD	5478
GeneCards	GC07P044841
HGNC	HGNC:9253
HPA	CAB004655
MIM	123840
neXtProt	NX_P62937
PharmGKB	PA33574
eggNOG	COG0652
GeneTree	ENSGT00760000119119
HOVERGEN	HBG001065
InParanoid	P62937
KO	K03767
OMA	MRSAFFQ
PhylomeDB	P62937
TreeFam	TF316719
Reactome	REACT_12560 REACT_6266 REACT_6359 REACT_6818 REACT_6903 REACT_6918 REACT_6965 REACT_9037 REACT_9055 REACT_9406
ChiTaRS	PPIA
EvolutionaryTrace	P62937
GeneWiki	Peptidylprolyl_isomerase_A
GenomeRNAi	5478
NextBio	21206
PRO	PR:P62937
Proteomes	UP000005640
Bgee	P62937
CleanEx	HS_PPIA
ExpressionAtlas	P62937
Genevestigator	P62937
GO	GO:0005829 GO:0005576 GO:0005615 GO:0070062 GO:0005925 GO:0016020 GO:0005634 GO:0042277 GO:0003755 GO:0044822 GO:0051082 GO:0046790 GO:0007596 GO:0030260 GO:0075713 GO:0050900 GO:0034389 GO:0030168 GO:0002576 GO:0050714 GO:0045070 GO:0006457 GO:0000413 GO:0045069 GO:0006278 GO:0019061 GO:0019058 GO:0016032 GO:0019076 GO:0019068
Gene3D	2.40.100.10
InterPro	IPR029000 IPR024936 IPR020892 IPR002130
Pfam	PF00160
PIRSF	PIRSF001467
PRINTS	PR00153
SUPFAM	SSF50891
PROSITE	PS00170 PS50072

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0016018	cyclosporin A binding	PMID:12218175^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:12218175^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:20364129^[2]	ECO:0000314			F		Figure 5 shows that through acetylation, the Cyclophilin A can be regulated by selecting for the cis-trans peptidyl-prolyl bond.	complete CACAO 9308
part_of	GO:0070062	extracellular exosome	PMID:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016018	cyclosporin A binding	PMID:20676357^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:20676357^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	PMID:20676357^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
enables	GO:0016018	cyclosporin A binding	PMID:12357034^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050714	positive regulation of protein secretion	PMID:21711559^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046790	virion binding	PMID:11250896^[14]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045070	positive regulation of viral genome replication	PMID:19932913^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045069	regulation of viral genome replication	PMID:11250896^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034389	lipid droplet organization	PMID:21711559^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16780588^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16780588^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:14993672^[19]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	PMID:14993672^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002594282 SGD:S000003793 SGD:S000004206	F		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002594282 SGD:S000003793 SGD:S000004206	P		Seeded From UniProt	complete
enables	GO:0016018	cyclosporin A binding	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0002936 PANTHER:PTN002594282 RGD:1303174 RGD:3372 RGD:628670 SGD:S000002562 UniProtKB:O43447 UniProtKB:P21568 UniProtKB:P21569 UniProtKB:P23284 UniProtKB:P30405 UniProtKB:P30414 UniProtKB:P45877 UniProtKB:P62937 UniProtKB:Q08752 UniProtKB:Q13427 UniProtKB:Q76NN7 UniProtKB:Q9UNP9	F		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0039581 MGI:MGI:97751 PANTHER:PTN002594282 PomBase:SPAC1B3.03c PomBase:SPBC1709.04c PomBase:SPBC28F2.03 PomBase:SPBP8B7.25 RGD:1303174 RGD:620315 RGD:628670 SGD:S000001099 SGD:S000002562 SGD:S000003793 SGD:S000004206 SGD:S000004543 TAIR:locus:2045663 TAIR:locus:2179822 UniProtKB:O43447 UniProtKB:P21568 UniProtKB:P21569 UniProtKB:P23284 UniProtKB:P24367 UniProtKB:P30405 UniProtKB:P30414 UniProtKB:P34791 UniProtKB:P45877 UniProtKB:P62937 UniProtKB:Q08752 UniProtKB:Q13427 UniProtKB:Q76NN7 UniProtKB:Q9UNP9 WB:WBGene00000879 WB:WBGene00000881 WB:WBGene00000884	F		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0039581 MGI:MGI:97751 PANTHER:PTN002594282 PomBase:SPAC1B3.03c PomBase:SPBC1709.04c PomBase:SPBC28F2.03 PomBase:SPBP8B7.25 RGD:1303174 RGD:620315 RGD:628670 SGD:S000001099 SGD:S000002562 SGD:S000003793 SGD:S000004206 SGD:S000004543 TAIR:locus:2045663 TAIR:locus:2179822 UniProtKB:O43447 UniProtKB:P21568 UniProtKB:P21569 UniProtKB:P23284 UniProtKB:P24367 UniProtKB:P30405 UniProtKB:P30414 UniProtKB:P34791 UniProtKB:P45877 UniProtKB:P62937 UniProtKB:Q08752 UniProtKB:Q13427 UniProtKB:Q76NN7 UniProtKB:Q8IXY8 UniProtKB:Q9UNP9 WB:WBGene00000879 WB:WBGene00000881 WB:WBGene00000884	F		Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002130	P		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002130 InterPro:IPR020892 InterPro:IPR024936	F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020892	P		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:5.2.1.8	F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:2644542^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045069	regulation of viral genome replication	PMID:7590732^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019076	viral release from host cell	PMID:21711559^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:2179953^[23] PMID:2644542^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0075713	establishment of integrated proviral latency	Reactome:R-HSA-162592	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	Reactome:R-HSA-8950328	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0050900	leukocyte migration	Reactome:R-HSA-202733	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035722	interleukin-12-mediated signaling pathway	Reactome:R-HSA-9020591	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030260	entry into host cell	Reactome:R-HSA-173107	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019068	virion assembly	Reactome:R-HSA-175474	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019064	fusion of virus membrane with host plasma membrane	Reactome:R-HSA-164524	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019061	uncoating of virus	Reactome:R-HSA-173771 Reactome:R-HSA-162585	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019058	viral life cycle	Reactome:R-HSA-162588	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006278	RNA-dependent DNA biosynthetic process	Reactome:R-HSA-182876 Reactome:R-HSA-164527 Reactome:R-HSA-164525 Reactome:R-HSA-164516	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8951690 Reactome:R-HSA-3159227 Reactome:R-HSA-3149454 Reactome:R-HSA-182876 Reactome:R-HSA-182859 Reactome:R-HSA-182795 Reactome:R-HSA-180634 Reactome:R-HSA-180632 Reactome:R-HSA-173771 Reactome:R-HSA-173769 Reactome:R-HSA-173642 Reactome:R-HSA-173115 Reactome:R-HSA-173111 Reactome:R-HSA-164528 Reactome:R-HSA-164527 Reactome:R-HSA-164524 Reactome:R-HSA-164520 Reactome:R-HSA-164519 Reactome:R-HSA-164513 Reactome:R-HSA-164512 Reactome:R-HSA-164505 Reactome:R-HSA-164504 Reactome:R-HSA-164503	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798748 Reactome:R-HSA-3159227 Reactome:R-HSA-3139027 Reactome:R-HSA-204485 Reactome:R-HSA-164524 Reactome:R-HSA-164521 Reactome:R-HSA-164515 Reactome:R-HSA-164510 Reactome:R-HSA-164509 Reactome:R-HSA-164508 Reactome:R-HSA-164507 Reactome:R-HSA-164500	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0697	F		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Huai, Q et al. (2002) Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc. Natl. Acad. Sci. U.S.A. 99 12037-42 PubMed GONUTS page
↑ Lammers, M et al. (2010) Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization. Nat. Chem. Biol. 6 331-7 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Davis, TL et al. (2010) Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biol. 8 e1000439 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ Jin, L & Harrison, SC (2002) Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc. Natl. Acad. Sci. U.S.A. 99 13522-6 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Anderson, LJ et al. (2011) Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion. Virol. J. 8 329 PubMed GONUTS page
↑ ^14.0 ^14.1 Braaten, D & Luban, J (2001) Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells. EMBO J. 20 1300-9 PubMed GONUTS page
↑ Gaither, LA et al. (2010) Multiple cyclophilins involved in different cellular pathways mediate HCV replication. Virology 397 43-55 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^18.0 ^18.1 Hu, YH et al. (2006) Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins. BMC Genomics 7 155 PubMed GONUTS page
↑ ^19.0 ^19.1 Kontopidis, G et al. (2004) Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes. Acta Crystallogr. D Biol. Crystallogr. 60 479-85 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^21.0 ^21.1 Takahashi, N et al. (1989) Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337 473-5 PubMed GONUTS page
↑ Willenbrink, W et al. (1995) Cyclophilin A, the major intracellular receptor for the immunosuppressant cyclosporin A, maps to chromosome 7p11.2-p13: four pseudogenes map to chromosomes 3, 10, 14, and 18. Genomics 28 101-4 PubMed GONUTS page
↑ Liu, J et al. (1990) Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 87 2304-8 PubMed GONUTS page

[PMID:12218175-1] 1.0 ^1.1 Huai, Q et al. (2002) Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc. Natl. Acad. Sci. U.S.A. 99 12037-42 PubMed GONUTS page

[PMID:20364129-2] Lammers, M et al. (2010) Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization. Nat. Chem. Biol. 6 331-7 PubMed GONUTS page

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19190083-4] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:21423176-5] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:19946888-6] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:20676357-7] 7.0 ^7.1 ^7.2 Davis, TL et al. (2010) Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biol. 8 e1000439 PubMed GONUTS page

[PMID:19199708-8] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:19056867-9] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-10] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

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