A1A4I4 (PKN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 62. History...
Names and origin
|Protein names||Recommended name:|
Serine/threonine-protein kinase N1
Protein kinase C-like 1
Protein kinase C-like PKN
Protein kinase PKN-alpha
Protein-kinase C-related kinase 1
Serine-threonine protein kinase N
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||944 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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.
ATP + a protein = ADP + a phosphoprotein.
Kinase activity is activated upon binding to Rho proteins (RHOA, RHOB and RAC1). Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids. Activated by caspase-3 (CASP3) cleavage during apoptosis. Two specific sites, Thr-776 (activation loop of the kinase domain) and Ser-918 (turn motif), need to be phosphorylated for its full activation By similarity.
Interacts with ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with RAC1. Interacts (via REM 1 repeat) with RHOA. Interacts with RHOB. Interacts with ZFAND6. Interacts (via C-terminus) with PDPK1. In case of infection, interacts with S.typhimurium protein SspH1 By similarity.
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 manner By similarity. Localization to endosomes is mediated via its interaction with RHOB By similarity. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis By similarity.
The C1 domain does not bind the diacylglycerol (DAG) By similarity.
Autophosphorylated; preferably on serine. Phosphorylated during mitosis By similarity.
Activated by limited proteolysis with trypsin By similarity.
In case of infection, polyubiquitinated by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its proteasomal degradation By similarity.
Contains 1 AGC-kinase C-terminal domain.
Contains 1 C2 domain.
Contains 1 protein kinase domain.
Contains 3 REM (Hr1) repeats.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 944||943||Serine/threonine-protein kinase N1||PRO_0000394261|
|Repeat||34 – 111||78||REM 1|
|Repeat||124 – 210||87||REM 2|
|Repeat||211 – 292||82||REM 3|
|Domain||326 – 462||137||C2|
|Domain||617 – 876||260||Protein kinase|
|Domain||877 – 944||68||AGC-kinase C-terminal|
|Nucleotide binding||623 – 631||9||ATP By similarity|
|Region||182 – 186||5||Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination By similarity|
|Active site||742||1||Proton acceptor By similarity|
|Binding site||646||1||ATP By similarity|
|Site||109 – 110||2||Cleavage; by caspase-3 By similarity|
|Site||455 – 456||2||Cleavage; by caspase-3 By similarity|
|Site||559 – 560||2||Cleavage; by caspase-3 By similarity|
Amino acid modifications
|Modified residue||2||1||N-acetylalanine By similarity|
|Modified residue||206||1||Phosphoserine By similarity|
|Modified residue||375||1||Phosphoserine By similarity|
|Modified residue||449||1||N6-acetyllysine By similarity|
|Modified residue||534||1||Phosphoserine By similarity|
|Modified residue||538||1||Phosphoserine By similarity|
|Modified residue||776||1||Phosphothreonine; by PDPK1 By similarity|
|Modified residue||780||1||Phosphothreonine By similarity|
|Modified residue||916||1||Phosphothreonine By similarity|
|Modified residue||918||1||Phosphoserine By similarity|
|BC126539 mRNA. Translation: AAI26540.1.|
|RefSeq||NP_001073715.1. NM_001080246.1. |
3D structure databases
|SMR||A1A4I4. Positions 13-98, 123-200. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|Gene3D||1.10.287.160. 3 hits. |
126.96.36.199. 2 hits.
|InterPro||IPR000961. AGC-kinase_C. |
|Pfam||PF02185. HR1. 3 hits. |
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
|SMART||SM00239. C2. 1 hit. |
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
|SUPFAM||SSF46585. SSF46585. 3 hits. |
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
|PROSITE||PS51285. AGC_KINASE_CTER. 1 hit. |
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
|Accession||Primary (citable) accession number: A1A4I4|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families