PKN1
entrez
5585
canonical
uniprot
Q16512
canonical
ensembl
ENSG00000123143
resolver
ensp
ENSP00000242783
resolver
ensp
ENSP00000343325
resolver
genesymbol
PKN1
resolver
genesymbol_syn
PAK1
resolver
genesymbol_syn
PKN
resolver
genesymbol_syn
PRK1
resolver
genesymbol_syn
PRKCL1
resolver
hgnc
HGNC:9405
resolver
uniprot
A8K7W5
resolver
uniprot
B2R9R4
resolver
uniprot
B3KVN3
resolver
uniprot
Q15143
resolver
uniprot
Q504U4
resolver
uniprot
Q8IUV5
resolver
uniprot
Q9UD44
resolver
uniprot_entry
PKN1_HUMAN
resolver
uniprot_sec
A8K7W5
resolver
uniprot_sec
B2R9R4
resolver
uniprot_sec
B3KVN3
resolver
uniprot_sec
Q15143
resolver
uniprot_sec
Q504U4
resolver
uniprot_sec
Q8IUV5
resolver
uniprot_sec
Q9UD44
resolver
activity_regulation
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-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation. {ECO:0000269|PubMed:8571126, ECO:0000269|PubMed:9751706}.
uniprot
proteins
amino_acid_sequence
MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQAAPDDTQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSTRLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSMGGPGTPDSRPPFLSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGSEARTTGDISVEKLNLGTDSDSSPQKSSRDPPSSPSSLSSPIQESTAPELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
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 (AR)-dependent transcription, by being recruited to AR 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. {ECO:0000269|PubMed:11104762, ECO:0000269|PubMed:12514133, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:24248594, ECO:0000269|PubMed:8557118, ECO:0000269|PubMed:8621664, ECO:0000269|PubMed:9175763}.
uniprot
proteins
mass_dalton
103932
uniprot
proteins
mutagenesis
MUTAGEN 108; /note="D->A: Abolishes cleavage by caspase-3 and formation of AF1 fragment."; /evidence="ECO:0000269|PubMed:9751706"; MUTAGEN 181; /note="R->A: Abolishes interaction with bacterial SspH1."; /evidence="ECO:0000269|PubMed:24248594"; MUTAGEN 181; /note="R->K: Decreases interaction with bacterial SspH1."; /evidence="ECO:0000269|PubMed:24248594"; MUTAGEN 185; /note="R->A: Abolishes interaction with bacterial SspH1."; /evidence="ECO:0000269|PubMed:24248594"; MUTAGEN 451; /note="D->A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment."; /evidence="ECO:0000269|PubMed:9751706"; MUTAGEN 454; /note="D->A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment."; /evidence="ECO:0000269|PubMed:9751706"; MUTAGEN 558; /note="D->A: Abolishes cleavage by caspase-3 and formation of AF3 fragment."; /evidence="ECO:0000269|PubMed:9751706"; MUTAGEN 560; /note="D->A: Abolishes cleavage by caspase-3 and formation of AF3 fragment."; /evidence="ECO:0000269|PubMed:9751706"; MUTAGEN 644; /note="K->E: Abolishes Serine/threonine-protein kinase activity."; /evidence="ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:8135837"; MUTAGEN 644; /note="K->R: Substantial reduction of autophosphorylation."; /evidence="ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:8135837
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated; preferably on serine. Phosphorylated during mitosis. {ECO:0000269|PubMed:10792047, ECO:0000269|PubMed:17332740}.; PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}.; PTM: (Microbial infection) In case of infection, polyubiquitinated by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its proteasomal degradation. {ECO:0000269|PubMed:24248594}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
PKC subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10388627
uniprot
proteins
pubmed
10619026
uniprot
proteins
pubmed
10792047
uniprot
proteins
pubmed
11104762
uniprot
proteins
pubmed
12514133
uniprot
proteins
pubmed
14514689
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16331689
uniprot
proteins
pubmed
16611232
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17332740
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18006505
uniprot
proteins
pubmed
18066052
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20188095
uniprot
proteins
pubmed
20228790
uniprot
proteins
pubmed
21224381
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21754995
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24248594
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
7851406
uniprot
proteins
pubmed
7988719
uniprot
proteins
pubmed
8135837
uniprot
proteins
pubmed
8557118
uniprot
proteins
pubmed
8571126
uniprot
proteins
pubmed
8621664
uniprot
proteins
pubmed
9175763
uniprot
proteins
pubmed
9478917
uniprot
proteins
pubmed
9751706
uniprot
proteins
sequence_length
942
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:9478917}. Nucleus {ECO:0000269|PubMed:12514133}. Endosome {ECO:0000269|PubMed:9478917}. Cell membrane {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63433}. Cleavage furrow {ECO:0000269|PubMed:17332740}. Midbody {ECO:0000269|PubMed:17332740}. 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. {ECO:0000250|UniProtKB:Q63433, ECO:0000269|PubMed:17332740}.
uniprot
proteins