P70268 · PKN1_MOUSE

  • Protein
    Serine/threonine-protein kinase N1
  • Gene
    Pkn1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

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.

TypeIDPosition(s)Description
Site108-109Cleavage; by caspase-3
Site457-458Cleavage; by caspase-3
Site561-562Cleavage; by caspase-3
Binding site625-633ATP (UniProtKB | ChEBI)
Binding site648ATP (UniProtKB | ChEBI)
Active site744Proton acceptor

GO annotations

AspectTerm
Cellular Componentcleavage furrow
Cellular Componentcytoplasm
Cellular Componentcytoplasmic vesicle
Cellular Componentendosome
Cellular Componentmidbody
Cellular Componentnucleus
Cellular Componentprotein-containing complex
Molecular FunctionATP binding
Molecular Functionchromatin binding
Molecular Functiondiacylglycerol-dependent serine/threonine kinase activity
Molecular Functionhistone binding
Molecular Functionhistone deacetylase binding
Molecular Functionhistone H3T11 kinase activity
Molecular Functionnuclear androgen receptor binding
Molecular Functionnuclear receptor coactivator activity
Molecular Functionprotein kinase activity
Molecular Functionprotein kinase C binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionsmall GTPase binding
Biological ProcessB cell apoptotic process
Biological ProcessB cell homeostasis
Biological Processepithelial cell migration
Biological Processhyperosmotic response
Biological Processnegative regulation of B cell proliferation
Biological Processpost-translational protein modification
Biological Processprotein phosphorylation
Biological Processregulation of cell motility
Biological Processregulation of germinal center formation
Biological Processregulation of immunoglobulin production
Biological Processregulation of transcription by RNA polymerase II
Biological Processrenal system process
Biological Processsignal transduction
Biological Processspleen development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase N1
  • EC number
  • Alternative names
    • Protein kinase C-like 1
    • Protein kinase C-like PKN
    • Protein-kinase C-related kinase 1
    • Serine-threonine protein kinase N

Gene names

    • Name
      Pkn1
    • Synonyms
      Pkn, Prk1, Prkcl1

Organism names

  • Taxonomic identifier
  • Strains
    • 129
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P70268
  • Secondary accessions
    • Q3UEA6
    • Q7TST2
    • Q8BTL8

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Endosome
Cell membrane
; Peripheral membrane protein
Cleavage furrow
Midbody
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

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00000557202-946Serine/threonine-protein kinase N1
Modified residue69Phosphoserine
Modified residue377Phosphoserine
Modified residue451N6-acetyllysine
Modified residue536Phosphoserine
Modified residue540Phosphoserine
Modified residue562Phosphoserine
Modified residue565Phosphoserine
Modified residue612Phosphoserine
Modified residue778Phosphothreonine; by PDPK1
Modified residue782Phosphothreonine
Modified residue918Phosphothreonine
Modified residue920Phosphoserine

Post-translational modification

Autophosphorylated; preferably on serine.
Activated by limited proteolysis with trypsin.

Keywords

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).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain25-100REM-1 1
Domain114-193REM-1 2
Domain202-283REM-1 3
Domain310-473C2
Region345-387Disordered
Region557-607Disordered
Compositional bias558-602Polar residues
Domain619-878Protein kinase
Domain879-946AGC-kinase C-terminal
Region906-925Disordered

Domain

The C1 domain does not bind the diacylglycerol (DAG).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    946
  • Mass (Da)
    104,411
  • Last updated
    2004-11-23 v3
  • Checksum
    FCB4E61AD27C1271
MAGDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLKREIRKELKLKEGAENLRRATTDLGRSLAPVELLLRGSARRLDLLHQQLQELHAHVVLPDPAAGSDATQSLAEGSPICSSTNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSSKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQALQAGELESQAAPDEAQGDPELGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSGAKAPDRKAVSEAQEKLTESNQKLGLLRESLERRLGELPADHPKGRLLREELTAASSSAFSAILPGPFPATHYSTLSKPAPLTGTLEVRVVGCKNLPETIPWSPPPSVGASGTPESRTPFLSRPARGLYSRSGSLSGRSSLRGEAENATEVSTVLKLDNTVVGQTAWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPIIERIPRLQRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPSAVATGTFSPNASPGAEIRHTGDISMEKLNLGADSDSSSQKSPPGLPSTSCSLSSPTHESTTSPELPSETQETPGPGLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRSSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTRAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSTERDAEDVKKQPFFRSLGWDVLLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFRDFDFVAGGY

P70268-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-7: MAGDAVQ → MAADPPLDSELE

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
D6RH37D6RH37_MOUSEPkn1796

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0392231-7in isoform 2
Compositional bias558-602Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp