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 N2  

UniProtKB / Swiss-Prot ID :  PKN2_MOUSE

Gene Name (Synonyms) : 
Pkn2, Prk2, Prkcl2  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm. Nucleus (By similarity). Membrane. Cell projection, lamellipodium (By similarity). Cytoplasm, cytoskeleton (By similarity). Cleavage furrow (By similarity). Midbody (By similarity). Cell junction (By similarity). Note=Colocalizes with PTPN13 i 

Protein Function :  PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associates with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c- fos serum response factor (SRF). 

Protein Sequence MASNPDRGEILLTELQGDSRTLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLR...
Predicted Secondary Structure CCCCCCCCCEEEEEECCCCCCCCCCCCHHHHHHCCCHHHHHHCCHHHHHHHHHHHHHHHHHHHHHHHHHH...
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
&
Experimental PTM Sites
Predicted PTM Sites
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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
3Phosphoserine--MASNPDR
--CCCCCCC
47.82Phosphositeplus
Link-
110PhosphoserineHIVVSDPED
HHCCCCCCC
36.23Phosphositeplus
Link-
305PhosphoserineSPTLSPRQS
CCCCCCCCC
22.10PhosphoELM
Link-
359PhosphoserineLPGWSPSDN
CCCCCCCCC
22.05Phosphositeplus
Link-
366PhosphoserineDNRSSFMSR
CCCCCCCCC
23.02PhosphoELM
Link-
366Phosphoserine.DNRSSFMSR
CCCCCCCCC
23.02UniProtKB
Link-
534PhosphoserineSGTFSPQTP
CCEECCCCC
18.88Phosphositeplus
Link-
537PhosphothreonineFSPQTPVPA
ECCCCCCCC
29.63Phosphositeplus
Link-
581PhosphoserinePPRASSLGE
CCCCCCCCC
27.63SysPTM
Link-
582PhosphoserinePRASSLGET
CCCCCCCCC
39.13PhosphoELM
Link-
582PhosphoserinePRASSLGET
CCCCCCCCC
39.13Phosphositeplus
Link-
582PhosphoserinePRASSLGET
CCCCCCCCC
39.13SysPTM
Link-
582Phosphoserine.PRASSLGET
CCCCCCCCC
39.13UniProtKB
Link-
619PhosphoserineLRPKSKSEY
CCCCCCCCC
44.06Phosphositeplus
Link-
621PhosphoserinePKSKSEYEL
CCCCCCCCC
53.13Phosphositeplus
Link-
809PhosphotyrosineEGMGYGDRT
HHCCCCCEE
13.63Phosphositeplus
Link-
813PhosphothreonineYGDRTSTFC
CCCEEEEEC
36.54Phosphositeplus
Link-
814PhosphoserineGDRTSTFCG
CCEEEEECC
22.00Phosphositeplus
Link-
815PhosphothreonineDRTSTFCGT
CEEEEECCC
23.49Phosphositeplus
Link-
819PhosphothreonineTFCGTPEFL
EECCCHHHC
22.33Phosphositeplus
Link-
957PhosphothreonineAPILTPPRE
CCCCCCCCC
31.78Phosphositeplus
Link-
957PhosphothreonineAPILTPPRE
CCCCCCCCC
31.78SysPTM
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
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures