Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Lactoperoxidase  

UniProtKB / Swiss-Prot ID :  PERL_BOVIN

Gene Name (Synonyms) : 
LPO  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Secreted, extracellular space. 

Protein Function :  LPO is an antimicrobial agent. It is thought to help protect the udder from infection and promote growth in newborn calves. 

Protein Sequence MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQL...
Predicted Secondary Structure CCHHHHHHHHHHHHHHHHCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCHHHH...
Protein Variant
LocationDescription
394A -> S.
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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
Protein Variant
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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
212N-linked (GlcNAc...).VLDQNRSLL
CCCCCCCHH
34.86UniProtKB
Link
315Phosphoserine.GSEPSLASR
CCCHHHHHH
32.30UniProtKB
Link
322N-linked (GlcNAc...).SRLRNLSSP
HHHHHHCCC
49.19UniProtKB
Link
358N-linked (GlcNAc...).CEFINTTAR
CCCCCCCCC
36.38UniProtKB
Link
449N-linked (GlcNAc...).YQGYNNSVD
CCCCCCCCC
40.92UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Inhibition of lactoperoxidase by its own catalytic product: crystalstructure of the hypothiocyanate-inhibited bovine lactoperoxidase at2.3-A resolution.";
Singh A.K., Singh N., Sharma S., Shin K., Takase M., Kaur P.,Srinivasan A., Singh T.P.;
Biophys. J. 96:646-654(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-712 IN COMPLEX WITHHYPOTHIOCYANATE, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 ANDASN-449, PHOSPHORYLATION AT SER-315, COFACTOR, CALCIUM-BINDING SITES,AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"Inhibition of lactoperoxidase by its own catalytic product: crystalstructure of the hypothiocyanate-inhibited bovine lactoperoxidase at2.3-A resolution.";
Singh A.K., Singh N., Sharma S., Shin K., Takase M., Kaur P.,Srinivasan A., Singh T.P.;
Biophys. J. 96:646-654(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-712 IN COMPLEX WITHHYPOTHIOCYANATE, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 ANDASN-449, PHOSPHORYLATION AT SER-315, COFACTOR, CALCIUM-BINDING SITES,AND DISULFIDE BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures