EKS-HOS-00222

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-HOS-00222

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
AGC/PKN	556.7	3.5E-167	331	590	260

Status

Reviewed

Ensembl Protein

ENSP00000439643

UniProt Accession

Q16513; B4DQ21; B4DTP5; B4DVG1; D3DT24; Q08AF4; Q9H1W4;

Protein Name

Serine/threonine-protein kinase N2

Protein Synonyms/Alias

PKN gamma; Protein kinase C-like 2; Protein-kinase C-related kinase 2;

Gene Name

PKN2

Gene Synonyms/Alias

PKN2; PRK2, PRKCL2;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSG00000065243	ENSP00000359536	ENST00000370505
ENSG00000065243	ENSP00000359544	ENST00000370513
ENSG00000065243	ENSP00000401125	ENST00000436111
ENSG00000065243	ENSP00000389076	ENST00000449189
ENSG00000065243	ENSP00000317851	ENST00000316005
ENSG00000065243	ENSP00000359552	ENST00000370521
ENSG00000065243	ENSP00000439643	ENST00000544045

Organism

Homo sapiens

Functional Description

PKC-related serine/threonine-protein kinase and Rho/Raceffector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c- fos serum response factor (SRF). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication.

Protein Length

658

Protein Sequence
(FASTA)

MNSTLEVRLM GCQDILENVP GRSKATSVAL PGWSPSETRS SFMSRTSKSK SGSSRNLLKT 60

DDLSNDVCAV LKLDNTVVGQ TSWKPISNQS WDQKFTLELD RSRELEISVY WRDWRSLCAV 120

KFLRLEDFLD NQRHGMCLYL EPQGTLFAEV TFFNPVIERR PKLQRQKKIF SKQQGKTFLR 180

APQMNINIAT WGRLVRRAIP TVNHSGTFSP QAPVPTTVPV VDVRIPQLAP PASDSTVTKL 240

DFDLEPEPPP APPRASSLGE IDESSELRVL DIPGQDSETV FDIQNDRNSI LPKSQSEYKP 300

DTPQSGLEYS GIQELEDRRS QQRFQFNLQD FRCCAVLGRG HFGKVLLAEY KNTNEMFAIK 360

ALKKGDIVAR DEVDSLMCEK RIFETVNSVR HPFLVNLFAC FQTKEHVCFV MEYAAGGDLM 420

MHIHTDVFSE PRAVFYAACV VLGLQYLHEH KIVYRDLKLD NLLLDTEGFV KIADFGLCKE 480

GMGYGDRTST FCGTPEFLAP EVLTETSYTR AVDWWGLGVL IYEMLVGESP FPGDDEEEVF 540

DSIVNDEVRY PRFLSTEAIS IMRRLLRRNP ERRLGASEKD AEDVKKHPFF RLIDWSALMD 600

KKVKPPFIPT IRGREDVSNF DDEFTSEAPI LTPPREPRIL SEEEQEMFRD FDYIADWC 658

Nucleotide Sequence
(FASTA)

ATGAATAGTA CTTTGGAAGT TCGTCTTATG GGCTGCCAAG ATATCCTAGA GAATGTCCCT 60

GGACGGTCAA AAGCAACATC AGTTGCACTG CCTGGTTGGA GTCCAAGTGA AACCAGATCA 120

TCTTTCATGA GCAGAACGAG TAAAAGTAAA AGCGGAAGTA GTCGAAATCT TCTAAAAACC 180

GATGACTTGT CCAATGATGT CTGTGCTGTT TTGAAGCTCG ATAATACTGT GGTTGGCCAA 240

ACTAGCTGGA AACCCATTTC CAATCAGTCA TGGGACCAGA AGTTTACACT GGAACTGGAC 300

AGGTCACGTG AACTGGAAAT TTCAGTTTAT TGGCGTGATT GGCGGTCTCT GTGTGCTGTA 360

AAATTTCTGA GGTTAGAAGA TTTTTTAGAC AACCAACGGC ATGGCATGTG TCTCTATTTG 420

GAACCACAGG GTACTTTATT TGCAGAGGTT ACCTTTTTTA ATCCAGTTAT TGAAAGAAGA 480

CCAAAACTTC AAAGACAAAA GAAAATTTTT TCAAAGCAAC AAGGCAAAAC ATTTCTCAGA 540

GCTCCTCAAA TGAATATTAA TATTGCCACT TGGGGAAGGC TAGTAAGAAG AGCTATTCCT 600

ACAGTAAATC ATTCTGGCAC CTTCAGCCCT CAAGCTCCTG TGCCTACTAC AGTGCCAGTG 660

GTTGATGTAC GCATCCCTCA ACTAGCACCT CCAGCTAGTG ATTCTACAGT AACCAAATTG 720

GACTTTGATC TTGAGCCTGA ACCTCCTCCA GCCCCACCAC GAGCTTCTTC TCTTGGAGAA 780

ATAGATGAAT CTTCTGAATT AAGAGTTTTG GATATACCAG GACAGGATTC AGAGACTGTT 840

TTTGATATTC AGAATGACAG AAATAGTATA CTTCCAAAAT CTCAATCTGA ATACAAGCCT 900

GATACTCCTC AGTCAGGCCT AGAATATAGT GGTATTCAAG AACTTGAGGA CAGAAGATCT 960

CAGCAAAGGT TTCAGTTTAA TCTACAAGAT TTCAGGTGTT GTGCTGTCTT GGGAAGAGGA 1020

CATTTTGGAA AGGTGCTTTT AGCTGAATAT AAAAACACAA ATGAGATGTT TGCTATAAAA 1080

GCCTTAAAGA AAGGAGATAT TGTGGCTCGA GATGAAGTAG ACAGCCTGAT GTGTGAAAAA 1140

AGAATTTTTG AAACTGTGAA TAGTGTAAGG CATCCCTTTT TGGTGAACCT TTTTGCATGT 1200

TTCCAAACCA AAGAGCATGT TTGCTTTGTA ATGGAATATG CTGCCGGTGG GGACCTAATG 1260

ATGCACATTC ATACTGATGT CTTTTCTGAA CCAAGAGCTG TATTTTATGC TGCTTGTGTA 1320

GTTCTTGGGT TGCAGTATTT ACATGAACAC AAAATTGTTT ATAGAGATTT GAAATTGGAT 1380

AACTTATTGC TAGATACAGA GGGCTTTGTG AAAATTGCTG ATTTTGGTCT TTGCAAAGAA 1440

GGAATGGGAT ATGGAGATAG AACAAGCACA TTTTGTGGCA CTCCTGAATT TCTTGCCCCA 1500

GAAGTATTAA CAGAAACTTC TTATACAAGG GCTGTAGATT GGTGGGGCCT TGGCGTGCTT 1560

ATATATGAAA TGCTTGTTGG TGAGTCTCCC TTTCCTGGTG ATGATGAAGA GGAAGTTTTT 1620

GACAGTATTG TAAATGATGA AGTAAGGTAT CCAAGGTTCT TATCTACAGA AGCCATTTCT 1680

ATAATGAGAA GGCTGTTAAG AAGAAATCCT GAACGGCGCC TTGGGGCTAG CGAGAAAGAT 1740

GCAGAGGATG TAAAAAAGCA CCCATTTTTC CGGCTAATTG ATTGGAGCGC TCTGATGGAC 1800

AAAAAAGTAA AGCCACCATT TATACCTACC ATAAGAGGAC GAGAAGATGT TAGTAATTTT 1860

GATGATGAAT TTACCTCAGA AGCACCTATT CTGACTCCAC CTCGAGAACC AAGGATACTT 1920

TCGGAAGAGG AGCAGGAAAT GTTCAGAGAT TTTGACTACA TTGCTGATTG GTGTTAA 1977

Domain Profile

S: 1     frllavlgrghfgkvllseykstgelyaikalkkgdilardevesllcekrileavssvr  60

         fr++avlgrghfgkvll+eyk+t+e++aikalkkgdi+ardev+sl+cekri+e+v+svr

Q: 331   FRCCAVLGRGHFGKVLLAEYKNTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVR  390

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

S: 61    hpflvnllacfqtkehvcfvmeyaaggdlmlhihedvfsepravfyaacvvlglqflhek  120

         hpflvnl+acfqtkehvcfvmeyaaggdlm+hih+dvfsepravfyaacvvlglq+lhe+

Q: 391   HPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEH  450

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

S: 121   kivyrdlkldnllldtegyvkiadfglckeglgygdrtstfcgtpeflapevltetsytr  180

         kivyrdlkldnllldteg+vkiadfglckeg+gygdrtstfcgtpeflapevltetsytr

Q: 451   KIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTR  510

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

S: 181   avdwwglgvllyemlvgespfpgddeeevfdsivndevryprflsveaieilrrllrknp  240

         avdwwglgvl+yemlvgespfpgddeeevfdsivndevryprfls+eai+i+rrllr+np

Q: 511   AVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNP  570

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

S: 241   ekrlgaserdaedvkkqpff  260

         e+rlgase+daedvkk+pff

Q: 571   ERRLGASEKDAEDVKKHPFF  590

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

Domain Sequence
(FASTA)

FRCCAVLGRG HFGKVLLAEY KNTNEMFAIK ALKKGDIVAR DEVDSLMCEK RIFETVNSVR 60

HPFLVNLFAC FQTKEHVCFV MEYAAGGDLM MHIHTDVFSE PRAVFYAACV VLGLQYLHEH 120

KIVYRDLKLD NLLLDTEGFV KIADFGLCKE GMGYGDRTST FCGTPEFLAP EVLTETSYTR 180

AVDWWGLGVL IYEMLVGESP FPGDDEEEVF DSIVNDEVRY PRFLSTEAIS IMRRLLRRNP 240

ERRLGASEKD AEDVKKHPFF 260

Keyword

Acetylation; Alternative splicing; Apoptosis; ATP-binding; Cell adhesion; Cell cycle; Cell division; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; 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"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gorilla gorilla"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Tarsius syrichta"; ?>Vicugna pacos"; ?>Xenopus tropicalis"; ?>

Gene Ontology

GO:0043296	; C:apical junction complex
GO:0032154	; C:cleavage furrow
GO:0005737	; C:cytoplasm
GO:0005856	; C:cytoskeleton
GO:0030027	; C:lamellipodium
GO:0016020	; C:membrane
GO:0030496	; C:midbody
GO:0005634	; C:nucleus
GO:0005524	; F:ATP binding
GO:0042826	; F:histone deacetylase binding
GO:0004697	; F:protein kinase C activity
GO:0004674	; F:protein serine/threonine kinase activity
GO:0043297	; P:apical junction assembly
GO:0006915	; P:apoptotic process
GO:0007155	; P:cell adhesion
GO:0007049	; P:cell cycle
GO:0051301	; P:cell division
GO:0010631	; P:epithelial cell migration
GO:0071777	; P:positive regulation of cell cycle cytokinesis
GO:0045931	; P:positive regulation of mitotic cell cycle
GO:2000145	; P:regulation of cell motility
GO:0006355	; P:regulation of transcription, DNA-dependent
GO:0007165	; P:signal transduction
GO:0006351	; P:transcription, DNA-dependent

KEGG

hsa:5586

;

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