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PPIA (human)

Overview PPIA PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Interacts with HIV-1 Capsid protein. Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Note: This description may include information from UniProtKB. Protein type: Cyclophilin; Isomerase; EC 5.2.1.8 Cellular Component: extracellular region; nucleus; cytosol Molecular Function: protein binding; peptidyl-prolyl cis-trans isomerase activity; unfolded protein binding; virion binding; peptide binding Biological Process: platelet activation; uncoating of virus; platelet degranulation; protein peptidyl-prolyl isomerization; viral reproduction; protein folding; RNA-dependent DNA replication; virus-host interaction; entry into host cell; blood coagulation; regulation of viral genome replication; leukocyte migration Reference #:  P62937 (UniProtKB) Alt. Names/Synonyms: Cyclophilin A; Cyclosporin A-binding protein; CYPA; CYPH; MGC117158; MGC12404; MGC23397; Peptidyl-prolyl cis-trans isomerase A; peptidylprolyl isomerase A; peptidylprolyl isomerase A (cyclophilin A); PPIA; PPIase A; Rotamase A; T cell cyclophilin Gene Symbols: PPIA Molecular weight: 18,012 Da Basal Isoelectric point: 7.68  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PPIA 1AK4 - A/B=1-165 (human) 1AWQ - A=1-165 (human) 1AWR - A/B/C/D/E/F=1-165 (human) 1AWS - A=1-165 (human) 1AWT - A/B/C/D/E/F=1-165 (human) 1AWU - A=1-165 (human) 1AWV - A/B/C/D/E/F=1-165 (human) 1BCK - A=1-165 (human) 1CWA - A=1-165 (human) 1CWB - A=1-165 (human) 1CWC - A=1-165 (human) 1CWF - A=1-165 (human) 1CWH - A=1-165 (human) 1CWI - A=1-165 (human) 1CWJ - A=1-165 (human) 1CWK - A=1-165 (human) 1CWL - A=1-165 (human) 1CWM - A=1-165 (human) 1CWO - A=1-165 (human) 1FGL - A=1-165 (human) 1M63 - C/G=1-165 (human) 1M9C - A/B=1-165 (human) 1M9D - A/B=1-165 (human) 1M9E - A/B=1-164 (human) 1M9F - A/B=1-165 (human) 1M9X - A/B/E/F=1-165 (human) 1M9Y - A/B/E/F=1-165 (human) 1MF8 - C=1-165 (human) 1MIK - A=1-165 (human) 1NMK - A/B=1-165 (human) 1OCA - A=1-165 (human) 1RMH - A/B=1-165 (human) 1VBS - A=1-165 (human) 1VBT - A/B=1-165 (human) 1W8L - A=1-165 (human) 1W8M - A=1-165 (human) 1W8V - A=1-165 (human) 1YND - A/B=1-165 (human) 1ZKF - A/B=1-165 (human) 2ALF - A=1-165 (human) 2CPL - A=1-165 (human) 2CYH - A=1-165 (human) 2RMA - A/C/E/G/I/K/M/O/Q/S=1-165 (human) 2RMB - A/C/E/G/I/K/M/O/Q/S=1-165 (human) 2X25 - B=2-165 (human) 2X2A - A/B=1-165 (human) 2X2C - S/Q/O/M/K=1-165 (human) 2X2D - C/B=1-165 (human) 2XGY - B=1-165 (human) 3CYH - A=1-165 (human) 3CYS - A=1-165 (human) 3K0M - A=1-165 (human) 3K0N - A=1-165 (human) 3K0O - A=1-165 (human) 3K0P - A=1-165 (human) 3K0Q - A=1-165 (human) 3K0R - A=1-165 (human) 3ODI - S/A/O/K/E/Q/M/C/I/G=1-165 (human) 3ODL - S/A/O/K/E/Q/M/C/I/G=1-165 (human) 3RDD - A=1-165 (human) 4CYH - A=1-165 (human) 5CYH - A=1-165 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB 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 5CYH  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	10		T5-p	___MVNPtVFFDIAV
0	1		S21-p	GEPLGRVsFELFADk
0	116		K28-u	sFELFADkVPkTAEN
0	4		K28-a	sFELFADkVPkTAEN
0	78		K31-u	LFADkVPkTAENFRA
0	1		K31-a	LFADkVPkTAENFRA
0	27		K44-a	RALSTGEkGFGykGS
0	70		K44-u	RALSTGEkGFGykGS
0	11		Y48-p	TGEkGFGykGSCFHR
0	56		K49-a	GEkGFGykGSCFHRI
0	48		K49-u	GEkGFGykGSCFHRI
0	3		S51	kGFGykGSCFHRIIP
0	1		C52	GFGykGSCFHRIIPG
1	36		K76-a	RHNGTGGksIyGEkF
0	35		K76-u	RHNGTGGksIyGEkF
0	2		S77-p	HNGTGGksIyGEkFE
0	42		Y79-p	GTGGksIyGEkFEDE
1	33		K82-a	GksIyGEkFEDENFI
0	104		K82-u	GksIyGEkFEDENFI
0	1		K91-a	EDENFILkHtGPGIL
0	1		K91-u	EDENFILkHtGPGIL
0	4		T93-p	ENFILkHtGPGILsM
0	2		S99-p	HtGPGILsMANAGPN
0	17		S110-p	AGPNTNGsQFFICTA
0	1		T116	GsQFFICTAkTEWLD
0	18		K118-a	QFFICTAkTEWLDGk
0	13		K118-u	QFFICTAkTEWLDGk
0	58		K125-a	kTEWLDGkHVVFGkV
0	47		K125-u	kTEWLDGkHVVFGkV
0	9		K131-a	GkHVVFGkVkEGMNI
0	36		K131-u	GkHVVFGkVkEGMNI
0	1		K133-a	HVVFGkVkEGMNIVE
0	7		K133-u	HVVFGkVkEGMNIVE
0	2		S147-p	EAMERFGsRNGKTSK
0	1		K155-a	RNGKTSKkItIADCG
0	41		K155-u	RNGKTSKkItIADCG
0	1		T157-p	GKTSKkItIADCGQL

	mouse
T5-p	___MVNPtVFFDITA
S21-p	DEPLGRVsFELFADk
K28-u	sFELFADkVPkTAEN
K28-a	sFELFADkVPkTAEN
K31-u	LFADkVPkTAENFRA
K31	LFADkVPKTAENFRA
K44	RALSTGEKGFGYkGs
K44-u	RALSTGEkGFGYkGs
Y48	TGEkGFGYkGssFHR
K49-a	GEkGFGYkGssFHRI
K49-u	GEkGFGYkGssFHRI
S51-p	kGFGYkGssFHRIIP
S52-p	GFGYkGssFHRIIPG
R76	RHNGTGGRsIyGEkF
R76	RHNGTGGRsIyGEkF
S77-p	HNGTGGRsIyGEkFE
Y79-p	GTGGRsIyGEkFEDE
K82-a	GRsIyGEkFEDENFI
K82-u	GRsIyGEkFEDENFI
K91	EDENFILKHtGPGIL
K91	EDENFILKHtGPGIL
T93-p	ENFILKHtGPGILsM
S99-p	HtGPGILsMANAGPN
S110-p	AGPNTNGsQFFICtA
T116-p	GsQFFICtAKTEWLD
K118	QFFICtAKTEWLDGk
K118	QFFICtAKTEWLDGk
K125-a	KTEWLDGkHVVFGkV
K125-u	KTEWLDGkHVVFGkV
K131-a	GkHVVFGkVkEGMNI
K131-u	GkHVVFGkVkEGMNI
K133	HVVFGkVKEGMNIVE
K133-u	HVVFGkVkEGMNIVE
S147-p	EAMERFGsRNGKTSK
K155	RNGKTSKKITISDCG
K155-u	RNGKTSKkITISDCG
T157	GKTSKkITISDCGQL

	rat
T5	___MVNPTVFFDITA
C21	GEPLGRVCFELFADk
K28-u	CFELFADkVPkTAEN
K28	CFELFADKVPkTAEN
K31-u	LFADkVPkTAENFRA
K31	LFADkVPKTAENFRA
K44	RALSTGEKGFGYkGS
K44-u	RALSTGEkGFGYkGS
Y48	TGEkGFGYkGSSFHR
K49	GEkGFGYKGSSFHRI
K49-u	GEkGFGYkGSSFHRI
S51	kGFGYkGSSFHRIIP
S52	GFGYkGSSFHRIIPG
K76	RHNGTGGKSIyGEkF
K76-u	RHNGTGGkSIyGEkF
S77	HNGTGGkSIyGEkFE
Y79-p	GTGGkSIyGEkFEDE
K82	GkSIyGEKFEDENFI
K82-u	GkSIyGEkFEDENFI
K91	EDENFILKHTGPGIL
K91	EDENFILKHTGPGIL
T93	ENFILKHTGPGILSM
S99	HTGPGILSMANAGPN
S110	AGPNTNGSQFFICTA
T116	GSQFFICTAKTEWLD
K118	QFFICTAKTEWLDGK
K118	QFFICTAKTEWLDGK
K125	KTEWLDGKHVVFGKV
K125	KTEWLDGKHVVFGKV
K131	GKHVVFGKVKEGMSI
K131	GKHVVFGKVKEGMSI
K133	HVVFGKVKEGMSIVE
K133	HVVFGKVKEGMSIVE
S147	EAMERFGSRNGKTSK
K155	RNGKTSKKITISDCG
K155	RNGKTSKKITISDCG
T157	GKTSKKITISDCGQL

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