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

Overview
PPIB PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Defects in PPIB are the cause of osteogenesis imperfecta type 9 (OI9). OI9 is a connective tissue disorder characterized by bone fragility, low bone mass and bowing of limbs due to multiple fractures. Short limb dwarfism and blue sclerae are observed in some but not all patients. Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Note: This description may include information from UniProtKB.
Protein type: Chaperone; RNA-binding; Cyclophilin; Secreted; Isomerase; Secreted, signal peptide; EC 5.2.1.8
Chromosomal Location of Human Ortholog: 15q21-q22
Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; focal adhesion; melanosome; membrane; nucleus; perinuclear region of cytoplasm; smooth endoplasmic reticulum
Molecular Function: collagen binding; peptide binding; peptidyl-prolyl cis-trans isomerase activity; protein binding; protein complex binding; unfolded protein binding
Biological Process: positive regulation of multicellular organism growth; protein peptidyl-prolyl isomerization; protein stabilization
Disease: Osteogenesis Imperfecta, Type Ix
Reference #:  P23284 (UniProtKB)
Gene Symbols: PPIB
Molecular weight: 23,743 Da
Basal Isoelectric point: 9.42  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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PPIB

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


 LTP 

LTP: 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.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y47‑p PKVTVKVyFDLRIGD
0 1 K67 VIFGLFGKTVPKtVD
0 2 K67‑ub VIFGLFGkTVPKtVD
0 1 K67 VIFGLFGKTVPKtVD
0 2 K71 LFGkTVPKtVDNFVA
0 1 T72‑p FGkTVPKtVDNFVAL
0 1 T81‑p DNFVALAtGEKGFGY
0 1 K84 VALAtGEKGFGYkNS
0 1 K84 VALAtGEKGFGYkNS
0 1 K89 GEKGFGYKNSKFHRV
0 1 K89‑sc GEKGFGYkNSKFHRV
0 19 K98‑ac SKFHRVIkDFMIQGG
0 1 K98‑ub SKFHRVIkDFMIQGG
0 1 K98 SKFHRVIKDFMIQGG
0 1 T108 MIQGGDFTRGDGTGG
0 1 K116 RGDGTGGKSIYGERF
0 1 K116‑ub RGDGTGGkSIYGERF
0 1 K116 RGDGTGGKSIYGERF
0 1 K129 RFPDENFKLkHYGPG
0 1 K131‑ub PDENFKLkHYGPGWV
0 1 K131‑ac PDENFKLkHYGPGWV
0 2 S139‑p HYGPGWVsMANAGKD
0 1 T147‑p MANAGKDtNGsQFFI
0 1 S150‑p AGKDtNGsQFFITTV
0 1 K158‑ub QFFITTVkTAWLDGk
0 1 K158 QFFITTVKTAWLDGk
0 2 K165‑ac kTAWLDGkHVVFGkV
0 2 K165‑ub kTAWLDGkHVVFGkV
0 2 K171‑ac GkHVVFGkVLEGMEV
0 2 S184‑p EVVRKVEstKtDsRD
0 2 T185‑p VVRKVEstKtDsRDK
0 1 T187‑p RKVEstKtDsRDKPL
0 1 S189‑p VEstKtDsRDKPLKD
0 3 K209‑ac CGKIEVEkPFAIAkE
0 3 K209‑ub CGKIEVEkPFAIAkE
0 8 K215 EkPFAIAKE______
0 1 K215‑sc EkPFAIAkE______
  mouse

 
Y47 PKVTVKVYFDLQIGD
K67 VVFGLFGKTVPkTVD
K67 VVFGLFGKTVPkTVD
K67‑sc VVFGLFGkTVPkTVD
K71‑ac LFGkTVPkTVDNFVA
T72 FGkTVPkTVDNFVAL
T81 DNFVALATGEkGFGY
K84‑ac VALATGEkGFGYkNS
K84‑ub VALATGEkGFGYkNS
K89‑ac GEkGFGYkNSKFHRV
K89‑sc GEkGFGYkNSKFHRV
K98 SKFHRVIKDFMIQGG
K98 SKFHRVIKDFMIQGG
K98‑sc SKFHRVIkDFMIQGG
T108‑p MIQGGDFtRGDGTGG
K116 RGDGTGGKSIYGERF
K116 RGDGTGGKSIYGERF
K116‑sc RGDGTGGkSIYGERF
K129‑ac RFPDENFkLKHYGPG
K131 PDENFkLKHYGPGWV
K131 PDENFkLKHYGPGWV
S139 HYGPGWVSMANAGKD
T147 MANAGKDTNGSQFFI
S150 AGKDTNGSQFFITTV
K158 QFFITTVKTSWLDGk
K158‑sc QFFITTVkTSWLDGk
K165 kTSWLDGKHVVFGKV
K165‑ub kTSWLDGkHVVFGKV
K171 GkHVVFGKVLEGMDV
S184 DVVRKVESTKtDSRD
T185 VVRKVESTKtDSRDK
T187‑p RKVESTKtDSRDKPL
S189 VESTKtDSRDKPLKD
K209‑ac SGKIEVEkPFAIAkE
K209‑ub SGKIEVEkPFAIAkE
K215‑ac EkPFAIAkE______
K215‑sc EkPFAIAkE______
  rat

 
Y47 PKVTVKVYFDFQIGD
K67‑ac VTFGLFGkTVPkTVD
K67 VTFGLFGKTVPkTVD
K67 VTFGLFGKTVPkTVD
K71‑ac LFGkTVPkTVDNFVA
T72 FGkTVPkTVDNFVAL
T81 DNFVALATGEKGFGY
K84 VALATGEKGFGYKNS
K84 VALATGEKGFGYKNS
K89 GEKGFGYKNSKFHRV
K89 GEKGFGYKNSKFHRV
K98 SKFHRVIKDFMIQGG
K98 SKFHRVIKDFMIQGG
K98 SKFHRVIKDFMIQGG
T108 MIQGGDFTRGDGTGG
K116‑ac RGDGTGGkSIYGERF
K116 RGDGTGGKSIYGERF
K116 RGDGTGGKSIYGERF
K129 RFPDENFKLKHYGPG
K131 PDENFKLKHYGPGWV
K131 PDENFKLKHYGPGWV
S139 HYGPGWVSMANAGKD
T147 MANAGKDTNGSQFFI
S150 AGKDTNGSQFFITTV
K158 QFFITTVKTSWLDGk
K158 QFFITTVKTSWLDGk
K165‑ac KTSWLDGkHVVFGKV
K165 KTSWLDGKHVVFGKV
K171 GkHVVFGKVLEGMDV
N184 DVVRKVENTKTDSRD
T185 VVRKVENTKTDSRDK
T187 RKVENTKTDSRDKPL
S189 VENTKTDSRDKPLKD
K209 CGKIEVEKPFAIAKE
K209 CGKIEVEKPFAIAKE
K215 EKPFAIAKE______
K215 EKPFAIAKE______
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