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Protein Page:
PPIA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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
Chromosomal Location of Human Ortholog: 7p13
Cellular Component: extracellular space; membrane; extracellular region; nucleus; cytosol
Molecular Function: protein binding; peptidyl-prolyl cis-trans isomerase activity; unfolded protein binding; virion binding; peptide binding
Biological Process: release of virus from host; platelet activation; uncoating of virus; positive regulation of viral genome replication; protein peptidyl-prolyl isomerization; viral reproduction; protein folding; RNA-dependent DNA replication; virus assembly; viral infectious cycle; platelet degranulation; positive regulation of protein secretion; entry into host cell; blood coagulation; leukocyte migration; regulation of viral genome replication
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® Total Proteins
Select Structure to View Below

PPIA

Protein Structure Not Found.


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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
 

Show Multiple Sequence Alignment


 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 11 T5-p ___MVNPtVFFDIAV
0 2 S21-p GEPLGRVsFELFADk
0 116 K28-ub sFELFADkVPkTAEN
0 5 K28-ac sFELFADkVPkTAEN
0 78 K31-ub LFADkVPkTAENFRA
0 2 K31-ac LFADkVPkTAENFRA
1 28 K44-ac RALSTGEkGFGykGS
0 70 K44-ub RALSTGEkGFGykGS
0 11 Y48-p TGEkGFGykGSCFHR
0 57 K49-ac GEkGFGykGSCFHRI
0 48 K49-ub GEkGFGykGSCFHRI
0 1 K49-sc GEkGFGykGSCFHRI
0 3 S51 kGFGykGSCFHRIIP
0 2 C52 GFGykGSCFHRIIPG
0 37 K76-ac RHNGTGGksIyGEkF
0 35 K76-ub RHNGTGGksIyGEkF
0 1 K76-sc RHNGTGGksIyGEkF
0 3 S77-p HNGTGGksIyGEkFE
0 45 Y79-p GTGGksIyGEkFEDE
1 34 K82-ac GksIyGEkFEDENFI
0 104 K82-ub GksIyGEkFEDENFI
0 2 K91-ac EDENFILkHtGPGIL
0 1 K91-ub EDENFILkHtGPGIL
0 5 T93-p ENFILkHtGPGILsM
0 3 S99-p HtGPGILsMANAGPN
0 18 S110-p AGPNTNGsQFFICTA
0 1 T116 GsQFFICTAkTEWLD
0 19 K118-ac QFFICTAkTEWLDGk
0 13 K118-ub QFFICTAkTEWLDGk
1 59 K125-ac kTEWLDGkHVVFGkV
0 47 K125-ub kTEWLDGkHVVFGkV
0 1 K125-sc kTEWLDGkHVVFGkV
0 10 K131-ac GkHVVFGkVkEGMNI
0 36 K131-ub GkHVVFGkVkEGMNI
0 1 K133-ac HVVFGkVkEGMNIVE
0 7 K133-ub HVVFGkVkEGMNIVE
0 1 N137 GkVkEGMNIVEAMER
0 3 S147-p EAMERFGsRNGKTSK
0 1 K155-ac RNGKTSKkItIADCG
0 41 K155-ub RNGKTSKkItIADCG
0 1 T157-p GKTSKkItIADCGQL
  mouse

 
T5-p ___MVNPtVFFDITA
S21-p DEPLGRVsFELFADk
K28-ub sFELFADkVPkTAEN
K28-ac sFELFADkVPkTAEN
K31-ub LFADkVPkTAENFRA
K31-ac LFADkVPkTAENFRA
K44-ac RALSTGEkGFGYkGs
K44-ub RALSTGEkGFGYkGs
Y48 TGEkGFGYkGssFHR
K49-ac GEkGFGYkGssFHRI
K49-ub GEkGFGYkGssFHRI
K49 GEkGFGYKGssFHRI
S51-p kGFGYkGssFHRIIP
S52-p GFGYkGssFHRIIPG
R76 RHNGTGGRsIyGEkF
R76 RHNGTGGRsIyGEkF
R76 RHNGTGGRsIyGEkF
S77-p HNGTGGRsIyGEkFE
Y79-p GTGGRsIyGEkFEDE
K82-ac GRsIyGEkFEDENFI
K82-ub GRsIyGEkFEDENFI
K91 EDENFILKHtGPGIL
K91 EDENFILKHtGPGIL
T93-p ENFILKHtGPGILsM
S99-p HtGPGILsMANAGPN
S110-p AGPNTNGsQFFICtA
T116-p GsQFFICtAKTEWLD
K118 QFFICtAKTEWLDGk
K118 QFFICtAKTEWLDGk
K125-ac KTEWLDGkHVVFGkV
K125-ub KTEWLDGkHVVFGkV
K125 KTEWLDGKHVVFGkV
K131-ac GkHVVFGkVkEGMNI
K131-ub GkHVVFGkVkEGMNI
K133 HVVFGkVKEGMNIVE
K133-ub HVVFGkVkEGMNIVE
N137 GkVkEGMNIVEAMER
S147-p EAMERFGsRNGKTSK
K155 RNGKTSKKITISDCG
K155-ub RNGKTSKkITISDCG
T157 GKTSKkITISDCGQL
  rat

 
T5 ___MVNPTVFFDITA
C21 GEPLGRVCFELFADk
K28-ub CFELFADkVPkTAEN
K28-ac CFELFADkVPkTAEN
K31-ub LFADkVPkTAENFRA
K31 LFADkVPKTAENFRA
K44-ac RALSTGEkGFGYkGS
K44-ub RALSTGEkGFGYkGS
Y48 TGEkGFGYkGSsFHR
K49-ac GEkGFGYkGSsFHRI
K49-ub GEkGFGYkGSsFHRI
K49 GEkGFGYKGSsFHRI
S51 kGFGYkGSsFHRIIP
S52-p GFGYkGSsFHRIIPG
K76-ac RHNGTGGkSIyGEkF
K76-ub RHNGTGGkSIyGEkF
K76 RHNGTGGKSIyGEkF
S77 HNGTGGkSIyGEkFE
Y79-p GTGGkSIyGEkFEDE
K82-ac GkSIyGEkFEDENFI
K82-ub GkSIyGEkFEDENFI
K91 EDENFILKHTGPGIL
K91 EDENFILKHTGPGIL
T93 ENFILKHTGPGILSM
S99 HTGPGILSMANAGPN
S110 AGPNTNGSQFFICTA
T116 GSQFFICTAKTEWLD
K118 QFFICTAKTEWLDGk
K118 QFFICTAKTEWLDGk
K125-ac KTEWLDGkHVVFGkV
K125 KTEWLDGKHVVFGkV
K125 KTEWLDGKHVVFGkV
K131-ac GkHVVFGkVkEGMsI
K131 GkHVVFGKVkEGMsI
K133-ac HVVFGkVkEGMsIVE
K133 HVVFGkVKEGMsIVE
S137-p GkVkEGMsIVEAMER
S147 EAMERFGSRNGKTSK
K155 RNGKTSKKITISDCG
K155 RNGKTSKKITISDCG
T157 GKTSKKITISDCGQL
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