PKN2_MOUSE
ID PKN2_MOUSE Reviewed; 983 AA.
AC Q8BWW9; Q3TBR3; Q80WS2; Q8BJL7; Q8BL62;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase N2;
DE EC=2.7.11.13;
DE AltName: Full=PKN gamma;
DE AltName: Full=Protein kinase C-like 2;
DE AltName: Full=Protein-kinase C-related kinase 2;
GN Name=Pkn2; Synonyms=Prk2, Prkcl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Spinal cord, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH NCK1, AND TISSUE SPECIFICITY.
RX PubMed=8910519; DOI=10.1074/jbc.271.46.28772;
RA Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K.,
RA Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.;
RT "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and
RT potential effector of Rho protein signaling.";
RL J. Biol. Chem. 271:28772-28776(1996).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9121475; DOI=10.1128/mcb.17.4.2247;
RA Vincent S., Settleman J.;
RT "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases
RT and regulates actin cytoskeletal organization.";
RL Mol. Cell. Biol. 17:2247-2256(1997).
RN [5]
RP INTERACTION WITH MAP3K2.
RX PubMed=10818102; DOI=10.1074/jbc.m003148200;
RA Sun W., Vincent S., Settleman J., Johnson G.L.;
RT "MEK kinase 2 binds and activates protein kinase C-related kinase 2.
RT Bifurcation of kinase regulatory pathways at the level of an MAPK kinase
RT kinase.";
RL J. Biol. Chem. 275:24421-24428(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11777936; DOI=10.1083/jcb.200105140;
RA Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J.,
RA Dotto G.P.;
RT "Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in
RT keratinocyte cell-cell adhesion.";
RL J. Cell Biol. 156:137-148(2002).
RN [7]
RP FUNCTION IN CELL MIGRATION, FUNCTION IN PHOSPHORYLATION OF CTTN, ACTIVITY
RP REGULATION, INTERACTION WITH CD44 AND RAC1, AND TISSUE SPECIFICITY.
RX PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x;
RA Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.;
RT "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase
RT activation leading to cytoskeleton function and cell migration in
RT astrocytes.";
RL J. Neurochem. 101:1002-1017(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619 AND THR-957, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, INTERACTION WITH RAC1 AND RHOA, AND MUTAGENESIS OF ALA-66;
RP ALA-155; LYS-685 AND ASP-781.
RX PubMed=20974804; DOI=10.1128/mcb.01001-10;
RA Wallace S.W., Magalhaes A., Hall A.;
RT "The Rho target PRK2 regulates apical junction formation in human bronchial
RT epithelial cells.";
RL Mol. Cell. Biol. 31:81-91(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac
CC effector protein that participates in specific signal transduction
CC responses in the cell. Plays a role in the regulation of cell cycle
CC progression, actin cytoskeleton assembly, cell migration, cell
CC adhesion, tumor cell invasion and transcription activation signaling
CC processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and
CC hence decreases CTTN ability to associate with filamentous actin.
CC Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct
CC RhoA target required for the regulation of the maturation of primordial
CC junctions into apical junction formation in bronchial epithelial cells.
CC Required for G2/M phases of the cell cycle progression and abscission
CC during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase
CC activity that is required for establishment of skin cell-cell adhesion
CC during keratinocytes differentiation. Regulates epithelial bladder
CC cells speed and direction of movement during cell migration and tumor
CC cell invasion. Inhibits Akt pro-survival-induced kinase activity.
CC Mediates Rho protein-induced transcriptional activation via the c-fos
CC serum response factor (SRF). Involved in the negative regulation of
CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q16513,
CC ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:20974804,
CC ECO:0000269|PubMed:8910519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- ACTIVITY REGULATION: Kinase activity is activated upon binding to GTP-
CC bound Rho1/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during
CC apoptosis. Activated by lipids, particularly cardiolipin and to a
CC lesser extent by other acidic phospholipids and unsaturated fatty
CC acids. Two specific sites, Thr-815 (activation loop of the kinase
CC domain) and Thr-957 (turn motif), need to be phosphorylated for its
CC full activation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the REM repeats) with RHOA (GTP-bound form
CC preferentially) and interacts (via the REM repeats) with RAC1 (GTP-
CC bound form preferentially); the interactions induce its
CC autophosphorylation (PubMed:17403031, PubMed:20974804). Interacts with
CC NCK1 (via SH3 domains) (PubMed:8910519). Interacts with RHOC. Interacts
CC with NCK1 and NCK2 (By similarity). Interacts with CD44
CC (PubMed:17403031). Interacts (via C-terminal kinase domain) with PDPK1;
CC the interaction stimulates PDPK1 kinase activity (By similarity).
CC Interacts with MAP3K2; the interaction activates PRK2 kinase activity
CC in a MAP3K2-independent kinase activity (PubMed:10818102). Interacts
CC (via C-terminal domain) with AKT1; the interaction occurs with the C-
CC terminal cleavage product of PRK2 in apoptotic cells. Interacts (via C-
CC terminus) with PTPN13 (via PDZ 3 domain). Interacts with CDK10 (By
CC similarity). {ECO:0000250|UniProtKB:Q16513,
CC ECO:0000269|PubMed:10818102, ECO:0000269|PubMed:17403031,
CC ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9121475}. Nucleus
CC {ECO:0000250|UniProtKB:Q16513}. Membrane {ECO:0000269|PubMed:9121475}.
CC Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q16513}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16513}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q16513}. Midbody {ECO:0000250|UniProtKB:Q16513}.
CC Cell junction {ECO:0000250|UniProtKB:Q16513}. Note=Colocalizes with
CC PTPN13 in lamellipodia-like structures, regions of large actin
CC turnover. Accumulates during telophase at the cleavage furrow and
CC concentrates finally around the midbody in cytokinesis. Recruited to
CC nascent cell-cell contacts at the apical surface of cells.
CC {ECO:0000250|UniProtKB:Q16513}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BWW9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BWW9-2; Sequence=VSP_012042;
CC Name=3;
CC IsoId=Q8BWW9-3; Sequence=VSP_042185, VSP_042186;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in liver and lung
CC Expressed in astrocytes (at protein level). Ubiquitous.
CC {ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:17403031,
CC ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475}.
CC -!- DOMAIN: The N-terminal regioninterferes with the interaction between
CC AKT1 and the C-terminal regionof PKN2. {ECO:0000250}.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC -!- DOMAIN: The apoptotic C-terminal cleavage product inhibits EGF-induced
CC kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473'
CC sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ
CC phosphorylations. {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated.
CC Phosphorylated. Phosphorylated by CDK10 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q16513}.
CC -!- PTM: Activated by limited proteolysis with trypsin. Proteolytically
CC cleaved by caspase-3 during the induction of apoptotic cell death.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; AK046248; BAC32655.1; -; mRNA.
DR EMBL; AK133298; BAE21599.1; -; mRNA.
DR EMBL; AK171092; BAE42244.1; -; mRNA.
DR EMBL; AK049713; BAC33888.1; -; mRNA.
DR EMBL; AK083425; BAC38910.1; -; mRNA.
DR EMBL; BC052073; AAH52073.1; -; mRNA.
DR CCDS; CCDS51084.1; -. [Q8BWW9-1]
DR RefSeq; NP_848769.2; NM_178654.4. [Q8BWW9-1]
DR AlphaFoldDB; Q8BWW9; -.
DR SMR; Q8BWW9; -.
DR BioGRID; 224651; 4.
DR IntAct; Q8BWW9; 1.
DR STRING; 10090.ENSMUSP00000039566; -.
DR iPTMnet; Q8BWW9; -.
DR PhosphoSitePlus; Q8BWW9; -.
DR EPD; Q8BWW9; -.
DR jPOST; Q8BWW9; -.
DR MaxQB; Q8BWW9; -.
DR PaxDb; Q8BWW9; -.
DR PeptideAtlas; Q8BWW9; -.
DR PRIDE; Q8BWW9; -.
DR ProteomicsDB; 289664; -. [Q8BWW9-1]
DR ProteomicsDB; 289665; -. [Q8BWW9-2]
DR ProteomicsDB; 289666; -. [Q8BWW9-3]
DR Antibodypedia; 33594; 256 antibodies from 34 providers.
DR DNASU; 109333; -.
DR Ensembl; ENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591. [Q8BWW9-1]
DR GeneID; 109333; -.
DR KEGG; mmu:109333; -.
DR UCSC; uc008rpe.2; mouse. [Q8BWW9-1]
DR CTD; 5586; -.
DR MGI; MGI:109211; Pkn2.
DR VEuPathDB; HostDB:ENSMUSG00000004591; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000154339; -.
DR InParanoid; Q8BWW9; -.
DR OMA; EVTINGC; -.
DR OrthoDB; 520651at2759; -.
DR PhylomeDB; Q8BWW9; -.
DR TreeFam; TF102005; -.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 109333; 14 hits in 75 CRISPR screens.
DR ChiTaRS; Pkn2; mouse.
DR PRO; PR:Q8BWW9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BWW9; protein.
DR Bgee; ENSMUSG00000004591; Expressed in superior cervical ganglion and 237 other tissues.
DR ExpressionAtlas; Q8BWW9; baseline and differential.
DR Genevisible; Q8BWW9; MM.
DR GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0043297; P:apical junction assembly; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Cell adhesion;
KW Cell cycle; Cell division; Cell junction; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..983
FT /note="Serine/threonine-protein kinase N2"
FT /id="PRO_0000055723"
FT DOMAIN 33..109
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 121..203
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 204..284
FT /note="REM-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 352..472
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 656..915
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 916..983
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 107..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..462
FT /note="Necessary to rescue apical junction formation"
FT REGION 553..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..976
FT /note="Necessary for the catalytic activity"
FT /evidence="ECO:0000250"
FT REGION 977..983
FT /note="Negatively regulates the responsiveness of the
FT catalytic activity by cardiolipin and is required for
FT optimal activation by the GTP-bound RhoA"
FT /evidence="ECO:0000250"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 781
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 662..670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 117..118
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 699..700
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 815
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 957
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 35..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012042"
FT VAR_SEQ 781..787
FT /note="DLKLDNL -> NTIFSSI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042185"
FT VAR_SEQ 788..983
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042186"
FT MUTAGEN 66
FT /note="A->K: Inhibits interaction with RHOA, reduces
FT localization at junctions and prevents apical junction
FT formation; when associated with K-155."
FT /evidence="ECO:0000269|PubMed:20974804"
FT MUTAGEN 155
FT /note="A->K: Inhibits interaction with RHOA, reduces
FT localization at junctions and prevents apical junction
FT formation; when associated with K-60."
FT /evidence="ECO:0000269|PubMed:20974804"
FT MUTAGEN 685
FT /note="K->M: Prevents apical junction formation."
FT /evidence="ECO:0000269|PubMed:20974804"
FT MUTAGEN 781
FT /note="D->A: Prevents apical junction formation."
FT /evidence="ECO:0000269|PubMed:20974804"
FT CONFLICT 32
FT /note="Q -> H (in Ref. 1; BAC32655)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="N -> H (in Ref. 1; BAC33888)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="V -> D (in Ref. 1; BAC38910)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="L -> F (in Ref. 1; BAC32655)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="E -> K (in Ref. 1; BAC33888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 111607 MW; 3961FD79D2718609 CRC64;
MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL
KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDSTDCPR
TPDTPNSDSR SSTSNNRLMA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL
QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM
KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA
SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA TSVALPGWSP
SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN TVVGQTSWKP ISNQSWDQKF
TLELDRSREL EISVYWRDWR SLCAVKFLRL EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP
VIERRPKLQR QKKIFSKQQG KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP
ATVPVVDARI PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ
GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ FSLQDFRCCA
VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS LMCEKRIFET VNSVRHPFLV
NLFACFQTKE HVCFVMEYAA GGDLMMHIHT DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR
DLKLDNLLLD TEGFVKIADF GLCKEGMGYG DRTSTFCGTP EFLAPEVLTE TSYTRAVDWW
GLGVLIYEML VGESPFPGDD EEEVFDSIVN DEVRYPRFLS TEAISIMRRL LRRNPERRLG
AGEKDAEDVK KHPFFRLTDW SALMDKKVKP PFVPTIRGRE DVSNFDDEFT SEAPILTPPR
EPRILLEEEQ EMFHDFDYVA DWC
