Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine/threonine-protein kinase N1  

UniProtKB / Swiss-Prot ID :  PKN1_BOVIN

Gene Name (Synonyms) : 
PKN1, PKN, PRK1, PRKCL1  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Cytoplasm (By similarity). Nucleus (By similarity). Endosome (By similarity). Cell membrane; Peripheral membrane protein (By similarity). Cleavage furrow (By similarity). Midbody (By similarity). Note=Associates with chromatin in a ligand-dependent manne 

Protein Function :  PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser- 159', 'Ser-163' and 'Ser-170', and GFAP. Able to phosphorylate RPS6 in vitro (By similarity). 

Protein Sequence MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRNL...
Predicted Secondary Structure  -
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
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Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
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Modification
Substrate Sites
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Secondary Structure
Accessible Surface Area (%)
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Reference
Structural Characterization
Orthologous
Protein Cluster
There are no experimentally verified PTM sites.
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Protein-Protein Interactions
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Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures