EKS-HOS-00223

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-HOS-00223

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
AGC/PKN	544.3	2.1E-163	621	880	260

Status

Reviewed

Ensembl Protein

ENSP00000343325

UniProt Accession

Q16512; A8K7W5; B2R9R4; B3KVN3; Q15143; Q504U4; Q8IUV5; Q9UD44;

Protein Name

Serine/threonine-protein kinase N1

Protein Synonyms/Alias

Protease-activated kinase 1; PAK-1; 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;

Gene Name

PKN1

Gene Synonyms/Alias

PKN1; PAK1, PKN, PRK1, PRKCL1;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSG00000123143	ENSP00000467422	ENST00000585619
ENSG00000123143	ENSP00000468497	ENST00000592960
ENSG00000123143	ENSP00000466819	ENST00000586237
ENSG00000123143	ENSP00000465867	ENST00000591461
ENSG00000123143	ENSP00000343325	ENST00000342216
ENSG00000123143	ENSP00000466367	ENST00000590097
ENSG00000123143	ENSP00000465842	ENST00000586557
ENSG00000123143	ENSP00000242783	ENST00000242783

Organism

Homo sapiens

Functional Description

PKC-related serine/threonine-protein kinase involved invarious 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' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.

Protein Length

948

Protein Sequence
(FASTA)

MAEANNPSEQ ELESEPRSWS LLEQLGLAGA DLAAPGVQQQ LELERERLRR EIRKELKLKE 60

GAENLRRATT DLGRSLGPVE LLLRGSSRRL DLLHQQLQEL HAHVVLPDPA ATHDGPQSPG 120

AGGPTCSATN LSRVAGLEKQ LAIELKVKQG AENMIQTYSN GSTKDRKLLL TAQQMLQDSK 180

TKIDIIRMQL RRALQAGQLE NQAAPDDTQG SPDLGAVELR IEELRHHFRV EHAVAEGAKN 240

VLRLLSAAKA PDRKAVSEAQ EKLTESNQKL GLLREALERR LGELPADHPK GRLLREELAA 300

ASSAAFSTRL AGPFPATHYS TLCKPAPLTG TLEVRVVGCR DLPETIPWNP TPSMGGPGTP 360

DSRPPFLSRP ARGLYSRSGS LSGRSSLKAE AENTSEVSTV LKLDNTVVGQ TSWKPCGPNA 420

WDQSFTLELE RARELELAVF WRDQRGLCAL KFLKLEDFLD NERHEVQLDM EPQGCLVAEV 480

TFRNPVIERI PRLRRQKKIF SKQQGKAFQR ARQMNIDVAT WVRLLRRLIP NATGTGTFSP 540

GASPGSEART TGDISVEKLN LGTDSDSSPQ KSSRDPPSSP SSLSSPIQES TAPELPSETQ 600

ETPGPALCSP LRKSPLTLED FKFLAVLGRG HFGKVLLSEF RPSGELFAIK ALKKGDIVAR 660

DEVESLMCEK RILAAVTSAG HPFLVNLFGC FQTPEHVCFV MEYSAGGDLM LHIHSDVFSE 720

PRAIFYSACV VLGLQFLHEH KIVYRDLKLD NLLLDTEGYV KIADFGLCKE GMGYGDRTST 780

FCGTPEFLAP EVLTDTSYTR AVDWWGLGVL LYEMLVGESP FPGDDEEEVF DSIVNDEVRY 840

PRFLSAEAIG IMRRLLRRNP ERRLGSSERD AEDVKKQPFF RTLGWEALLA RRLPPPFVPT 900

LSGRTDVSNF DEEFTGEAPT LSPPRDARPL TAAEQAAFLD FDFVAGGC 948

Nucleotide Sequence
(FASTA)

ATGGCGGAGG CCAATAACCC CTCGGAGCAG GAGCTGGAGA GTGAGCCTCG CAGCTGGTCC 60

CTGCTAGAGC AGCTGGGCCT GGCCGGGGCA GACCTGGCGG CCCCCGGGGT ACAGCAGCAG 120

CTGGAGCTGG AGCGGGAGCG GCTGCGGCGG GAAATCCGCA AGGAGCTGAA GCTGAAGGAG 180

GGTGCTGAGA ACCTGCGGCG GGCCACCACT GACCTGGGCC GCAGCCTGGG CCCCGTAGAG 240

CTGCTGCTGC GGGGCTCCTC GCGCCGCCTC GACCTGCTGC ACCAGCAGCT GCAGGAGCTG 300

CACGCCCACG TGGTGCTTCC CGACCCGGCG GCCACCCACG ATGGCCCCCA GTCCCCTGGT 360

GCGGGTGGCC CCACCTGCTC GGCCACCAAC CTGAGCCGCG TGGCGGGCCT GGAGAAGCAG 420

TTGGCCATTG AGCTGAAGGT GAAGCAGGGG GCGGAGAACA TGATCCAGAC CTACAGCAAT 480

GGCAGCACCA AGGACCGGAA GCTGCTGCTG ACAGCCCAGC AGATGTTGCA GGACAGTAAG 540

ACCAAGATTG ACATCATCCG CATGCAACTC CGCCGGGCGC TGCAGGCCGG CCAGCTGGAG 600

AACCAGGCAG CCCCGGATGA CACCCAAGGG AGTCCTGACC TGGGGGCTGT GGAGCTGCGC 660

ATCGAAGAGC TGCGGCACCA CTTCCGAGTG GAGCACGCGG TGGCCGAGGG TGCCAAGAAC 720

GTACTGCGCC TGCTCAGCGC TGCCAAGGCC CCGGACCGCA AGGCAGTCAG CGAGGCCCAG 780

GAGAAATTAA CAGAATCCAA CCAGAAGCTG GGGCTGCTGC GGGAGGCTCT GGAGCGGAGA 840

CTTGGGGAGC TGCCCGCCGA CCACCCCAAG GGGCGGCTGC TGCGAGAAGA GCTCGCTGCG 900

GCCTCCTCCG CTGCCTTCAG CACCCGCCTG GCCGGGCCCT TTCCCGCCAC GCACTACAGC 960

ACCCTGTGCA AGCCCGCGCC GCTCACAGGG ACCCTGGAGG TACGAGTGGT GGGCTGCAGA 1020

GACCTCCCAG AGACCATCCC GTGGAACCCT ACCCCCTCAA TGGGGGGACC TGGGACCCCA 1080

GACAGCCGCC CCCCCTTCCT GAGCCGCCCA GCCCGGGGCC TTTACAGCCG AAGCGGAAGC 1140

CTCAGTGGCC GGAGCAGCCT CAAAGCAGAA GCCGAGAACA CCAGTGAAGT CAGCACTGTG 1200

CTTAAGCTGG ATAACACAGT GGTGGGGCAG ACGTCTTGGA AGCCATGTGG CCCCAATGCC 1260

TGGGACCAGA GCTTCACTCT GGAGCTGGAA AGGGCACGGG AACTGGAGTT GGCTGTGTTC 1320

TGGCGGGACC AGCGGGGCCT GTGTGCCCTC AAATTCCTGA AGTTGGAGGA TTTCTTGGAC 1380

AATGAGAGGC ATGAGGTGCA GCTGGACATG GAACCCCAGG GCTGCCTGGT GGCTGAGGTC 1440

ACCTTCCGCA ACCCTGTCAT TGAGAGGATT CCTCGGCTCC GACGGCAGAA GAAAATTTTC 1500

TCCAAGCAGC AAGGGAAGGC GTTCCAGCGT GCTAGGCAGA TGAACATCGA TGTCGCCACG 1560

TGGGTGCGGC TGCTCCGGAG GCTCATCCCC AATGCCACGG GCACAGGCAC CTTTAGCCCT 1620

GGGGCTTCTC CAGGATCCGA GGCCCGGACC ACGGGTGACA TATCGGTGGA GAAGCTGAAC 1680

CTCGGCACTG ACTCGGACAG CTCACCTCAG AAGAGCTCGC GGGATCCTCC TTCCAGCCCA 1740

TCGAGCCTGA GCTCCCCCAT CCAGGAATCC ACTGCTCCCG AGCTGCCTTC GGAGACCCAG 1800

GAGACCCCAG GCCCCGCCCT GTGCAGCCCT CTGAGGAAGT CACCTCTGAC CCTCGAAGAT 1860

TTCAAGTTCC TGGCGGTGCT GGGCCGGGGT CATTTTGGGA AGGTGCTCCT CTCCGAATTC 1920

CGGCCCAGTG GGGAGCTGTT CGCCATCAAG GCTCTGAAGA AAGGGGACAT TGTGGCCCGA 1980

GACGAGGTGG AGAGCCTGAT GTGTGAGAAG CGGATATTGG CGGCAGTGAC CAGTGCGGGA 2040

CACCCCTTCC TGGTGAACCT CTTCGGCTGT TTCCAGACAC CGGAGCACGT GTGCTTCGTG 2100

ATGGAGTACT CGGCCGGTGG GGACCTGATG CTGCACATCC ACAGCGACGT GTTCTCTGAG 2160

CCCCGTGCCA TCTTTTATTC CGCCTGCGTG GTGCTGGGCC TACAGTTTCT TCACGAACAC 2220

AAGATCGTCT ACAGGGACCT GAAGTTGGAC AATTTGCTCC TGGACACCGA GGGCTACGTC 2280

AAGATCGCAG ACTTTGGCCT CTGCAAGGAG GGGATGGGCT ATGGGGACCG GACCAGCACA 2340

TTCTGTGGGA CCCCGGAGTT CCTGGCCCCT GAGGTGCTGA CGGACACGTC GTACACGCGA 2400

GCTGTGGACT GGTGGGGACT GGGTGTGCTG CTCTACGAGA TGCTGGTTGG CGAGTCCCCA 2460

TTCCCAGGGG ATGATGAGGA GGAGGTCTTC GACAGCATCG TCAACGACGA GGTTCGCTAC 2520

CCCCGCTTCC TGTCGGCCGA AGCCATCGGC ATCATGAGAA GGCTGCTTCG GAGGAACCCA 2580

GAGCGGAGGC TGGGATCTAG CGAGAGAGAT GCAGAAGATG TGAAGAAACA GCCCTTCTTC 2640

AGGACTCTGG GCTGGGAAGC CCTGTTGGCC CGGCGCCTGC CACCGCCCTT TGTGCCCACG 2700

CTGTCCGGCC GCACCGACGT CAGCAACTTC GACGAGGAGT TCACCGGGGA GGCCCCCACA 2760

CTGAGCCCGC CCCGCGACGC GCGGCCCCTC ACAGCCGCGG AGCAGGCAGC CTTCCTGGAC 2820

TTCGACTTCG TGGCCGGGGG CTGCTAG 2847

Domain Profile

S: 1     frllavlgrghfgkvllseykstgelyaikalkkgdilardevesllcekrileavssvr  60

         f++lavlgrghfgkvllse++++gel+aikalkkgdi+ardevesl+cekril+av+s++

Q: 621   FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAG  680

         89**********************************************************

S: 61    hpflvnllacfqtkehvcfvmeyaaggdlmlhihedvfsepravfyaacvvlglqflhek  120

         hpflvnl++cfqt ehvcfvmey+aggdlmlhih+dvfsepra+fy+acvvlglqflhe+

Q: 681   HPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEH  740

         ************************************************************

S: 121   kivyrdlkldnllldtegyvkiadfglckeglgygdrtstfcgtpeflapevltetsytr  180

         kivyrdlkldnllldtegyvkiadfglckeg+gygdrtstfcgtpeflapevlt+tsytr

Q: 741   KIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTR  800

         ************************************************************

S: 181   avdwwglgvllyemlvgespfpgddeeevfdsivndevryprflsveaieilrrllrknp  240

         avdwwglgvllyemlvgespfpgddeeevfdsivndevryprfls+eai+i+rrllr+np

Q: 801   AVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNP  860

         ************************************************************

S: 241   ekrlgaserdaedvkkqpff  260

         e+rlg+serdaedvkkqpff

Q: 861   ERRLGSSERDAEDVKKQPFF  880

         *******************9

Domain Sequence
(FASTA)

FKFLAVLGRG HFGKVLLSEF RPSGELFAIK ALKKGDIVAR DEVESLMCEK RILAAVTSAG 60

HPFLVNLFGC FQTPEHVCFV MEYSAGGDLM LHIHSDVFSE PRAIFYSACV VLGLQFLHEH 120

KIVYRDLKLD NLLLDTEGYV KIADFGLCKE GMGYGDRTST FCGTPEFLAP EVLTDTSYTR 180

AVDWWGLGVL LYEMLVGESP FPGDDEEEVF DSIVNDEVRY PRFLSAEAIG IMRRLLRRNP 240

ERRLGSSERD AEDVKKQPFF 260

Keyword

3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell membrane; Chromatin regulator; Complete proteome; Cytoplasm; Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase.

Sequence Source

Ensembl

Orthology

Ortholog group

Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Felis catus"; ?>Gadus morhua"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pongo abelii"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Xiphophorus maculatus"; ?>

Gene Ontology

GO:0032154	; C:cleavage furrow
GO:0016023	; C:cytoplasmic membrane-bounded vesicle
GO:0005768	; C:endosome
GO:0030496	; C:midbody
GO:0005634	; C:nucleus
GO:0005886	; C:plasma membrane
GO:0050681	; F:androgen receptor binding
GO:0005524	; F:ATP binding
GO:0003682	; F:chromatin binding
GO:0017049	; F:GTP-Rho binding
GO:0042393	; F:histone binding
GO:0042826	; F:histone deacetylase binding
GO:0035402	; F:histone kinase activity (H3-T11 specific)
GO:0030374	; F:ligand-dependent nuclear receptor transcription coactivator activity
GO:0004697	; F:protein kinase C activity
GO:0048365	; F:Rac GTPase binding
GO:0007257	; P:activation of JUN kinase activity
GO:0010631	; P:epithelial cell migration
GO:0006972	; P:hyperosmotic response
GO:2000145	; P:regulation of cell motility
GO:0006357	; P:regulation of transcription from RNA polymerase II promoter
GO:0006351	; P:transcription, DNA-dependent

KEGG

hsa:5585

;

InterPros

IPR000961	; AGC-kinase_C.
IPR000008	; C2_Ca-dep.
IPR008973	; C2_Ca/lipid-bd_dom_CaLB.
IPR011072	; HR1_rho-bd.
IPR011009	; Kinase-like_dom.
IPR017892	; Pkinase_C.
IPR000719	; Prot_kinase_cat_dom.
IPR017441	; Protein_kinase_ATP_BS.
IPR002290	; Ser/Thr_dual-sp_kinase_dom.
IPR008271	; Ser/Thr_kinase_AS.

Pfam

PF02185	; HR1; 3.
PF00069	; Pkinase; 1.
PF00433	; Pkinase_C; 1.

SMARTs

SM00239	; C2; 1.
SM00742	; Hr1; 3.
SM00133	; S_TK_X; 1.
SM00220	; S_TKc; 1.

Prosites

PS51285	; AGC_KINASE_CTER; 1.
PS50004	; C2; FALSE_NEG.
PS00107	; PROTEIN_KINASE_ATP; 1.
PS50011	; PROTEIN_KINASE_DOM; 1.
PS00108	; PROTEIN_KINASE_ST; 1.

Prints

Created Date

20-Feb-2013