P70268 · PKN1_MOUSE
- ProteinSerine/threonine-protein kinase N1
- GenePkn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids946 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. 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' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Activity regulation
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-778 (activation loop of the kinase domain) and Ser-920 (turn motif), need to be phosphorylated for its full activation.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 108-109 | Cleavage; by caspase-3 | ||||
Sequence: DA | ||||||
Site | 457-458 | Cleavage; by caspase-3 | ||||
Sequence: DN | ||||||
Site | 561-562 | Cleavage; by caspase-3 | ||||
Sequence: DS | ||||||
Binding site | 625-633 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGRGHFGKV | ||||||
Binding site | 648 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 744 | Proton acceptor | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase N1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP70268
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. 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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000055720 | 2-946 | Serine/threonine-protein kinase N1 | |||
Sequence: AGDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLKREIRKELKLKEGAENLRRATTDLGRSLAPVELLLRGSARRLDLLHQQLQELHAHVVLPDPAAGSDATQSLAEGSPICSSTNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSSKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQALQAGELESQAAPDEAQGDPELGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSGAKAPDRKAVSEAQEKLTESNQKLGLLRESLERRLGELPADHPKGRLLREELTAASSSAFSAILPGPFPATHYSTLSKPAPLTGTLEVRVVGCKNLPETIPWSPPPSVGASGTPESRTPFLSRPARGLYSRSGSLSGRSSLRGEAENATEVSTVLKLDNTVVGQTAWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPIIERIPRLQRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPSAVATGTFSPNASPGAEIRHTGDISMEKLNLGADSDSSSQKSPPGLPSTSCSLSSPTHESTTSPELPSETQETPGPGLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRSSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTRAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSTERDAEDVKKQPFFRSLGWDVLLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFRDFDFVAGGY | ||||||
Modified residue | 69 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 377 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 451 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 536 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 540 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 562 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 565 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 612 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 778 | Phosphothreonine; by PDPK1 | ||||
Sequence: T | ||||||
Modified residue | 782 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 918 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 920 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated; preferably on serine.
Activated by limited proteolysis with trypsin.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with ZFAND6 (PubMed:11054541).
Interacts with ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with RAC1 (By similarity).
Interacts (via REM 1 repeat) with RHOA (PubMed:8571127).
Interacts with RHOB. Interacts (via C-terminus) with PDPK1. Interacts with CCNT2; enhances MYOD1-dependent transcription. Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity).
Interacts with ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with RAC1 (By similarity).
Interacts (via REM 1 repeat) with RHOA (PubMed:8571127).
Interacts with RHOB. Interacts (via C-terminus) with PDPK1. Interacts with CCNT2; enhances MYOD1-dependent transcription. Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-100 | REM-1 1 | ||||
Sequence: DLAAPGVQQQLELERERLKREIRKELKLKEGAENLRRATTDLGRSLAPVELLLRGSARRLDLLHQQLQELHAHVVL | ||||||
Domain | 114-193 | REM-1 2 | ||||
Sequence: AEGSPICSSTNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSSKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQALQA | ||||||
Domain | 202-283 | REM-1 3 | ||||
Sequence: PDEAQGDPELGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSGAKAPDRKAVSEAQEKLTESNQKLGLLRESLERRLGELPA | ||||||
Domain | 310-473 | C2 | ||||
Sequence: PFPATHYSTLSKPAPLTGTLEVRVVGCKNLPETIPWSPPPSVGASGTPESRTPFLSRPARGLYSRSGSLSGRSSLRGEAENATEVSTVLKLDNTVVGQTAWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCL | ||||||
Region | 345-387 | Disordered | ||||
Sequence: WSPPPSVGASGTPESRTPFLSRPARGLYSRSGSLSGRSSLRGE | ||||||
Region | 557-607 | Disordered | ||||
Sequence: NLGADSDSSSQKSPPGLPSTSCSLSSPTHESTTSPELPSETQETPGPGLCS | ||||||
Compositional bias | 558-602 | Polar residues | ||||
Sequence: LGADSDSSSQKSPPGLPSTSCSLSSPTHESTTSPELPSETQETPG | ||||||
Domain | 619-878 | Protein kinase | ||||
Sequence: FKFLAVLGRGHFGKVLLSEFRSSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTRAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSTERDAEDVKKQPFF | ||||||
Domain | 879-946 | AGC-kinase C-terminal | ||||
Sequence: RSLGWDVLLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFRDFDFVAGGY | ||||||
Region | 906-925 | Disordered | ||||
Sequence: SNFDEEFTGEAPTLSPPRDA |
Domain
The C1 domain does not bind the diacylglycerol (DAG).
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P70268-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length946
- Mass (Da)104,411
- Last updated2004-11-23 v3
- ChecksumFCB4E61AD27C1271
P70268-2
- Name2
- Differences from canonical
- 1-7: MAGDAVQ → MAADPPLDSELE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6RH37 | D6RH37_MOUSE | Pkn1 | 796 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039223 | 1-7 | in isoform 2 | |||
Sequence: MAGDAVQ → MAADPPLDSELE | ||||||
Compositional bias | 558-602 | Polar residues | ||||
Sequence: LGADSDSSSQKSPPGLPSTSCSLSSPTHESTTSPELPSETQETPG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK089431 EMBL· GenBank· DDBJ | BAC40880.2 EMBL· GenBank· DDBJ | mRNA | ||
AK149649 EMBL· GenBank· DDBJ | BAE29005.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052923 EMBL· GenBank· DDBJ | AAH52923.1 EMBL· GenBank· DDBJ | mRNA | ||
Y07611 EMBL· GenBank· DDBJ | CAA68883.1 EMBL· GenBank· DDBJ | Genomic DNA |