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Protein Page:
PPIB (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
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; Secreted; Secreted, signal peptide; Isomerase; EC 5.2.1.8; Cyclophilin
Cellular Component: membrane; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome; nucleus
Molecular Function: collagen binding; protein binding; peptidyl-prolyl cis-trans isomerase activity; unfolded protein binding; protein complex binding; peptide binding
Biological Process: extracellular matrix organization and biogenesis; protein peptidyl-prolyl isomerization; protein stabilization; positive regulation of multicellular organism growth
Reference #:  P23284 (UniProtKB)
Alt. Names/Synonyms: Cyclophilin B; cyclophilin-like protein; CYP-S1; CYPB; MGC14109; MGC2224; OI9; Peptidyl-prolyl cis-trans isomerase B; peptidylprolyl isomerase B; peptidylprolyl isomerase B (cyclophilin B); PPIase B; PPIB; Rotamase B; S-cyclophilin; SCYLP
Gene Symbols: PPIB
Molecular weight: 23,743 Da
Basal Isoelectric point: 9.42  Predict pI for various phosphorylation states
Select Structure to View Below

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


 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 1 K67-ub VIFGLFGkTVPKtVD
0 1 K67 VIFGLFGKTVPKtVD
0 1 K71 LFGkTVPKtVDNFVA
0 1 T72-p FGkTVPKtVDNFVAL
0 1 K84 VALATGEKGFGYkNS
0 1 K84 VALATGEKGFGYkNS
0 1 K89 GEKGFGYKNSKFHRV
0 1 K89-sc GEKGFGYkNSKFHRV
0 18 K98-ac SKFHRVIkDFMIQGG
0 1 K98-ub SKFHRVIkDFMIQGG
0 1 K98 SKFHRVIKDFMIQGG
0 1 T108 MIQGGDFTRGDGTGG
0 1 K116-ub RGDGTGGkSIYGERF
0 1 K116 RGDGTGGKSIYGERF
0 1 K129 RFPDENFKLkHYGPG
0 1 K131-ub 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-ub kTAWLDGkHVVFGkV
0 1 K171-ac GkHVVFGkVLEGMEV
0 1 S184-p EVVRKVEstKTDSRD
0 1 T185-p VVRKVEstKTDSRDK
0 2 K209-ac CGKIEVEkPFAIAkE
0 3 K209-ub CGKIEVEkPFAIAkE
0 8 K215 EkPFAIAKE______
0 1 K215-sc EkPFAIAkE______
  mouse

 
K67 VVFGLFGKTVPkTVD
K67-sc VVFGLFGkTVPkTVD
K71-ac LFGkTVPkTVDNFVA
T72 FGkTVPkTVDNFVAL
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-sc RGDGTGGkSIYGERF
K129-ac RFPDENFkLKHYGPG
K131 PDENFkLKHYGPGWV
S139 HYGPGWVSMANAGKD
T147 MANAGKDTNGSQFFI
S150 AGKDTNGSQFFITTV
K158 QFFITTVKTSWLDGk
K158-sc QFFITTVkTSWLDGk
K165-ub kTSWLDGkHVVFGKV
K171 GkHVVFGKVLEGMDV
S184 DVVRKVESTKTDSRD
T185 VVRKVESTKTDSRDK
K209-ac SGKIEVEkPFAIAkE
K209-ub SGKIEVEkPFAIAkE
K215-ac EkPFAIAkE______
K215-sc EkPFAIAkE______
  rat

 
K67 VTFGLFGKTVPKTVD
K67 VTFGLFGKTVPKTVD
K71 LFGKTVPKTVDNFVA
T72 FGKTVPKTVDNFVAL
K84 VALATGEKGFGYKNS
K84 VALATGEKGFGYKNS
K89 GEKGFGYKNSKFHRV
K89 GEKGFGYKNSKFHRV
K98 SKFHRVIKDFMIQGG
K98 SKFHRVIKDFMIQGG
K98 SKFHRVIKDFMIQGG
T108 MIQGGDFTRGDGTGG
K116 RGDGTGGKSIYGERF
K116 RGDGTGGKSIYGERF
K129 RFPDENFKLKHYGPG
K131 PDENFKLKHYGPGWV
S139 HYGPGWVSMANAGKD
T147 MANAGKDTNGSQFFI
S150 AGKDTNGSQFFITTV
K158 QFFITTVKTSWLDGK
K158 QFFITTVKTSWLDGK
K165 KTSWLDGKHVVFGKV
K171 GKHVVFGKVLEGMDV
N184 DVVRKVENTKTDSRD
T185 VVRKVENTKTDSRDK
K209 CGKIEVEKPFAIAKE
K209 CGKIEVEKPFAIAKE
K215 EKPFAIAKE______
K215 EKPFAIAKE______
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