Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phosphorylase b kinase regulatory subunit beta  

UniProtKB / Swiss-Prot ID :  KPBB_RABIT

Gene Name (Synonyms) : 
PHKB  

Species :  Oryctolagus cuniculus (Rabbit). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (Potential). 

Protein Function :  Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation. 

Protein Sequence MAGATGLMAEVSWKVLERRARTKRSGSVYEPLKSINLPRPDNETLWDKLDYYYKIVKSTLLLYQSPTTGL...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHHCCCCCHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCC...
Protein Variant
LocationDescription
28V -> I.
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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
2N-acetylalanine.---MAGATG
---CCCCCC
27.86UniProtKB
Link-
12PhosphoserineMAEVSWKVL
HHHHHHHHH
16.82PhosphoELM
Link-
12PhosphoserineMAEVSWKVL
HHHHHHHHH
16.82Phosphositeplus
Link-
12Phosphoserine; by autocatalysis.MAEVSWKVL
HHHHHHHHH
16.82UniProtKB
Link-
27PhosphoserineKRSGSVYEP
CCCCCHHHH
23.83Phosphositeplus
Link-
27Phosphoserine (PKA_group)KRSGSVYEP
CCCCCHHHH
23.83PhosphoELM
Link-
27Phosphoserine; by PKA.KRSGSVYEP
CCCCCHHHH
23.83UniProtKB
Link-
700PhosphoserineVKRQSSTSN
CCEEECCCC
39.35Phosphositeplus
Link-
701PhosphoserineKRQSSTSNA
CEEECCCCH
27.76PhosphoELM
Link-
701Phosphoserine; by PKA.KRQSSTSNA
CEEECCCCH
27.76UniProtKB
Link-
1090S-farnesyl cysteine.NEDSCLVS
CCCCCCCC
7.23UniProtKB
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
Acetylation
ReferencePubMed
"The alpha and beta subunits of phosphorylase kinase are homologous:cDNA cloning and primary structure of the beta subunit.";
Kilimann M.W., Zander N.F., Kuhn C.C., Crabb J.W., Meyer H.E.,Heilmeyer L.M.G. Jr.;
Proc. Natl. Acad. Sci. U.S.A. 85:9381-9385(1988).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
Phosphorylation
ReferencePubMed
"The alpha and beta subunits of phosphorylase kinase are homologous:cDNA cloning and primary structure of the beta subunit.";
Kilimann M.W., Zander N.F., Kuhn C.C., Crabb J.W., Meyer H.E.,Heilmeyer L.M.G. Jr.;
Proc. Natl. Acad. Sci. U.S.A. 85:9381-9385(1988).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
"Localization of phosphoserine residues in the alpha subunit of rabbitskeletal muscle phosphorylase kinase.";
Meyer H.E., Meyer G.F., Dirks H., Heilmeyer L.M.G. Jr.;
Eur. J. Biochem. 188:367-376(1990).
Cited for: PROTEIN SEQUENCE OF 2-18; 25-33; 688-709 AND 1072-1093, ANDPHOSPHORYLATION AT SER-12; SER-27 AND SER-701.
Prenylation
ReferencePubMed
"Farnesylcysteine, a constituent of the alpha and beta subunits ofrabbit skeletal muscle phosphorylase kinase: localization byconversion to S-ethylcysteine and by tandem mass spectrometry.";
Heilmeyer L.M. Jr., Serwe M., Weber C., Metzger J.,Hoffmann-Posorske E., Meyer H.E.;
Proc. Natl. Acad. Sci. U.S.A. 89:9554-9558(1992).
Cited for: PROTEIN SEQUENCE OF 1073-1093, ISOPRENYLATION AT CYS-1090, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures