Protein: Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N) (Q63433)
Organism: Rattus norvegicus (Rat)
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 (By similarity). 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 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15375078}. Nucleus {ECO:0000250|UniProtKB:Q16512}. Endosome {ECO:0000250|UniProtKB:Q16512}. Cell membrane {ECO:0000269|PubMed:15375078}; Peripheral membrane protein {ECO:0000269|PubMed:15375078}. Cleavage furrow {ECO:0000250|UniProtKB:Q16512}. Midbody {ECO:0000250|UniProtKB:Q16512}. Note=Associates with chromatin in a ligand-dependent manner (By similarity). Localization to endosomes is mediated via its interaction with RHOB. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis (By similarity). Association to the cell membrane is dependent on Ser-377 phosphorylation. {ECO:0000250|UniProtKB:Q16512, ECO:0000269|PubMed:15375078}.
Interaction partners:
- Transforming protein RhoA
- RSA-14-44 protein.
- Ras-related C3 botulinum toxin substrate 1
- 3-phosphoinositide-dependent protein kinase 1
- Protein SET
- Serine/threonine-protein kinase N2
- M-phase inducer phosphatase
- Rho-related GTP-binding protein RhoB
- Ras homolog family member C.
- 14-3-3 protein epsilon
Sequence:
MAGDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLKREIRKELKLKEGAENLRRATTDLGRSLAPVELLLRGSARRLDLLHQQLQELHAHVVLPDPTAGSDAPQSLAEGSPVCSSTNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQALQAGQLESQAAPDEAHGDPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLRESLERRLGELPADHPKGRLLREELTAASSAAFSAILPGPFPATHYSTLSKPAPLTGTLEVRVVGCKNLPETIPWSPPPSVGASGTPDSRTPFLSRPARGLYNRSGSLSGRSSLKGEAENSTEVSTVLKLDNTVVGQTAWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPIIERIPRLQRQKKIFSKQQGQTFQRARQMNIDVATWVRLLRRLIPNAVATGSFSPNASPGSEIRSTGDISMEKLNLGADSDSSSQKSPAGLPSTSCSLSSPTHESTTSPELPSETQETPGPGLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFHSSGELFAIKALKKGDIVARDEVESLMCEKRILATVTRAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSTERDAEDVKKQPFFRTLDWDALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFRDFDFVAGGY