Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Peptidyl-prolyl cis-trans isomerase A  

UniProtKB / Swiss-Prot ID :  PPIA_HUMAN

Gene Name (Synonyms) : 
PPIA, CYPA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

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

Protein Sequence MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRH...
Predicted Secondary Structure CCCCEEEEEEEECCEECCEEEEEEECCCCCHHHHHHHHHHCCCCCCCCCCCEEEEECCCCEEECCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1none----MVNPT
----CCCCE
6.24HPRD
Link
2N-acetylvaline; partial.---MVNPTV
---CCCCEE
13.61UniProtKB
Link
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFADKVPKT
EECCCCCHH
57.94Phosphositeplus
Link
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFADKVPKT
EECCCCCHH
57.94SysPTM
Link
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).LFADKVPKT
EECCCCCHH
57.94UniProtKB
Link
28N6-acetyllysineLFADKVPKT
EECCCCCHH
57.94HPRD
Link
28N6-acetyllysineLFADKVPKT
EECCCCCHH
57.94Phosphositeplus
Link
28N6-acetyllysine.LFADKVPKT
EECCCCCHH
57.94UniProtKB
Link
31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DKVPKTAEN
CCCCHHHHH
64.45Phosphositeplus
Link
44Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)STGEKGFGY
HCCCCCCCC
61.97Phosphositeplus
Link
44N6-acetyllysineSTGEKGFGY
HCCCCCCCC
61.97HPRD
Link
44N6-acetyllysineSTGEKGFGY
HCCCCCCCC
61.97Phosphositeplus
Link
44N6-acetyllysine.STGEKGFGY
HCCCCCCCC
61.97UniProtKB
Link
48PhosphotyrosineKGFGYKGSC
CCCCCCCCE
15.20Phosphositeplus
Link
49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GFGYKGSCF
CCCCCCCEE
44.73Phosphositeplus
Link
49N6-acetyllysineGFGYKGSCF
CCCCCCCEE
44.73HPRD
Link
49N6-acetyllysineGFGYKGSCF
CCCCCCCEE
44.73Phosphositeplus
Link
49N6-acetyllysine.GFGYKGSCF
CCCCCCCEE
44.73UniProtKB
Link
76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GTGGKSIYG
CCCCCCCCC
34.72Phosphositeplus
Link
76N6-acetyllysineGTGGKSIYG
CCCCCCCCC
34.72HPRD
Link
76N6-acetyllysineGTGGKSIYG
CCCCCCCCC
34.72Phosphositeplus
Link
76N6-acetyllysine.GTGGKSIYG
CCCCCCCCC
34.72UniProtKB
Link
77PhosphoserineTGGKSIYGE
CCCCCCCCC
25.07Phosphositeplus
Link
79PhosphotyrosineGKSIYGEKF
CCCCCCCCC
26.73Phosphositeplus
Link
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IYGEKFEDE
CCCCCCCCC
50.09Phosphositeplus
Link
82N6-acetyllysineIYGEKFEDE
CCCCCCCCC
50.09HPRD
Link
82N6-acetyllysineIYGEKFEDE
CCCCCCCCC
50.09Phosphositeplus
Link
82N6-acetyllysine.IYGEKFEDE
CCCCCCCCC
50.09UniProtKB
Link
93PhosphothreonineILKHTGPGI
CCCCCCCCE
43.41HPRD
Link
93PhosphothreonineILKHTGPGI
CCCCCCCCE
43.41Phosphositeplus
Link
110PhosphoserineNTNGSQFFI
CCCCCEEEE
26.36Phosphositeplus
Link
118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ICTAKTEWL
EECCCCCCC
28.91Phosphositeplus
Link
118N6-acetyllysineICTAKTEWL
EECCCCCCC
28.91HPRD
Link
125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)WLDGKHVVF
CCCCCEEEE
32.66Phosphositeplus
Link
125N6-acetyllysineWLDGKHVVF
CCCCCEEEE
32.66HPRD
Link
125N6-acetyllysineWLDGKHVVF
CCCCCEEEE
32.66Phosphositeplus
Link
125N6-acetyllysineWLDGKHVVF
CCCCCEEEE
32.66SysPTM
Link
125N6-acetyllysine.WLDGKHVVF
CCCCCEEEE
32.66UniProtKB
Link
131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVFGKVKEG
EEEEEEECC
38.37Phosphositeplus
Link
131N6-acetyllysineVVFGKVKEG
EEEEEEECC
38.37HPRD
Link
131N6-acetyllysineVVFGKVKEG
EEEEEEECC
38.37Phosphositeplus
Link
131N6-acetyllysine.VVFGKVKEG
EEEEEEECC
38.37UniProtKB
Link
133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FGKVKEGMN
EEEEECCHH
52.62Phosphositeplus
Link
147PhosphoserineERFGSRNGK
HHCCCCCCC
21.62Phosphositeplus
Link
157PhosphothreonineSKKITIADC
CCCEEEEEE
20.99PhosphoELM
Link
157PhosphothreonineSKKITIADC
CCCEEEEEE
20.99Phosphositeplus
Link
157Phosphothreonine.SKKITIADC
CCCEEEEEE
20.99UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3305423MINT15161933
PRR13_HUMANphysical interactionEBI-759082
intact16189514
PTPRN_HUMANphysical interaction
physical interaction
physical interaction
EBI-728395
EBI-728386
EBI-728
intact16273344
16273344
16273344
BASI_HUMANin vivo
yeast 2-hybrid
HPRD:00457HPRD11943775
PPIA_HUMANin vivoHPRD:00457HPRD12167617
CD99_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00457HPRD15388255
PRS23_HUMANyeast 2-hybridHPRD:00457HPRD16169070
PRR13_HUMANyeast 2-hybridHPRD:00457HPRD16189514
RB_HUMANin vitro
in vivo
HPRD:00457HPRD12210730
S10A8_HUMANyeast 2-hybridHPRD:00457HPRD16169070
SPT5H_HUMANyeast 2-hybridHPRD:00457HPRD16169070
CD4_HUMANENSP00000348240STRING
CXCR4_HUMANENSP00000348240STRING
ABC3G_HUMANENSP00000348240STRING
CCR5_HUMANENSP00000348240STRING
BAF_HUMANENSP00000348240STRING
BASI_HUMANENSP00000348240STRING
WDR92_HUMANENSP00000351238STRING
PP2BA_HUMANENSP00000351238STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00091Cyclosporine
DB00172L-Proline
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-49; LYS-76;LYS-82; LYS-125 AND LYS-131, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures