Q8BWW9 (PKN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase N2
EC=2.7.11.13

Alternative name(s):
PKN gamma
Protein kinase C-like 2
Protein-kinase C-related kinase 2

Gene names

Name:	Pkn2
Synonyms:	Prk2, Prkcl2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	983 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PKC-related serine/threonine-protein kinase and Rho/Rac effector 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). Ref.3 Ref.7 Ref.10
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Kinase activity is activated upon binding to GTP-bound Rho1/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-815 (activation loop of the kinase domain) and Thr-957 (turn motif), need to be phosphorylated for its full activation By similarity. Ref.7
Subunit structure	Interacts with RHOA (GTP-bound form preferentially) and RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation. Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity. Interacts (via C-terminus domain) with AKT1; the interaction occurs with the C-terminus cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with NCK1, NCK2 and RHOC By similarity. Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially). Interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially). Interacts with NCK1 (via SH3 domains). Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity. Interacts with CD44. Ref.3 Ref.5 Ref.7 Ref.10
Subcellular location	Cytoplasm. Nucleus By similarity. Membrane. Cell projection › lamellipodium By similarity. Cytoplasm › cytoskeleton By similarity. Cleavage furrow By similarity. Midbody By similarity. Cell junction By similarity. Note: Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells By similarity. Ref.4
Tissue specificity	Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous. Ref.3 Ref.4 Ref.6 Ref.7
Domain	The N-terminus region interferes with the interaction between AKT1 and the C-terminus region of PKN2 By similarity. The C1 domain does not bind the diacylglycerol (DAG). The apoptotic C-terminus cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations By similarity.
Post-translational modification	Phosphorylated during mitosis By similarity. Autophosphorylated. Phosphorylated. Activated by limited proteolysis with trypsin By similarity. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 1 protein kinase domain. Contains 3 REM (Hr1) repeats.

Ontologies

Keywords
Biological process	Apoptosis Cell adhesion Cell cycle Cell division Transcription Transcription regulation
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apical junction assembly Inferred from direct assay Ref.10. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell motility Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Inferred from electronic annotation. Source: InterPro transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	apical junction complex Inferred from direct assay Ref.10. Source: UniProtKB cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 12783890. Source: MGI cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay PubMed 12783890. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone deacetylase binding Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C activity Inferred from electronic annotation. Source: UniProtKB-EC protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BWW9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8BWW9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     35-45: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8BWW9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     781-787: DLKLDNL → NTIFSSI
     788-983: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 983	983	Serine/threonine-protein kinase N2		PRO_0000055723
Regions
	Repeat	44 – 119	76	REM 1
	Repeat	133 – 213	81	REM 2
	Repeat	214 – 295	82	REM 3
	Domain	329 – 462	134	C2
	Domain	656 – 915	260	Protein kinase
	Domain	916 – 983	68	AGC-kinase C-terminal
	Nucleotide binding	662 – 670	9	ATP By similarity
	Region	381 – 462	82	Necessary to rescue apical junction formation
	Region	916 – 976	61	Necessary for the catalytic activity By similarity
	Region	977 – 983	7	Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA By similarity
Sites
	Active site	781	1	Proton acceptor By similarity
	Binding site	685	1	ATP By similarity
	Site	117 – 118	2	Cleavage; by caspase-3 By similarity
	Site	699 – 700	2	Cleavage; by caspase-3 By similarity
Amino acid modifications
	Modified residue	110	1	Phosphoserine By similarity
	Modified residue	121	1	Phosphothreonine By similarity
	Modified residue	124	1	Phosphothreonine By similarity
	Modified residue	301	1	Phosphoserine By similarity
	Modified residue	305	1	Phosphoserine By similarity
	Modified residue	359	1	Phosphoserine By similarity
	Modified residue	361	1	Phosphoserine By similarity
	Modified residue	534	1	Phosphoserine By similarity
	Modified residue	582	1	Phosphoserine By similarity
	Modified residue	630	1	Phosphoserine By similarity
	Modified residue	815	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	957	1	Phosphothreonine Probable
Natural variations
	Alternative sequence	35 – 45	11	Missing in isoform 2.		VSP_012042
	Alternative sequence	781 – 787	7	DLKLDNL → NTIFSSI in isoform 3.		VSP_042185
	Alternative sequence	788 – 983	196	Missing in isoform 3.		VSP_042186
Experimental info
	Mutagenesis	66	1	A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155. Ref.10
	Mutagenesis	155	1	A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60. Ref.10
	Mutagenesis	685	1	K → M: Prevents apical junction formation. Ref.10
	Mutagenesis	781	1	D → A: Prevents apical junction formation. Ref.10
	Sequence conflict	32	1	Q → H in BAC32655. Ref.1
	Sequence conflict	84	1	N → H in BAC33888. Ref.1
	Sequence conflict	395	1	V → D in BAC38910. Ref.1
	Sequence conflict	569	1	L → F in BAC32655. Ref.1
	Sequence conflict	704	1	E → K in BAC33888. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 3961FD79D2718609	FASTA	983	111,607
	10 20 30 40 50 60 MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 70 80 90 100 110 120 KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDSTDCPR 130 140 150 160 170 180 TPDTPNSDSR SSTSNNRLMA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 190 200 210 220 230 240 QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM 250 260 270 280 290 300 KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA 310 320 330 340 350 360 SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA TSVALPGWSP 370 380 390 400 410 420 SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN TVVGQTSWKP ISNQSWDQKF 430 440 450 460 470 480 TLELDRSREL EISVYWRDWR SLCAVKFLRL EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP 490 500 510 520 530 540 VIERRPKLQR QKKIFSKQQG KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP 550 560 570 580 590 600 ATVPVVDARI PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ 610 620 630 640 650 660 GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ FSLQDFRCCA 670 680 690 700 710 720 VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS LMCEKRIFET VNSVRHPFLV 730 740 750 760 770 780 NLFACFQTKE HVCFVMEYAA GGDLMMHIHT DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR 790 800 810 820 830 840 DLKLDNLLLD TEGFVKIADF GLCKEGMGYG DRTSTFCGTP EFLAPEVLTE TSYTRAVDWW 850 860 870 880 890 900 GLGVLIYEML VGESPFPGDD EEEVFDSIVN DEVRYPRFLS TEAISIMRRL LRRNPERRLG 910 920 930 940 950 960 AGEKDAEDVK KHPFFRLTDW SALMDKKVKP PFVPTIRGRE DVSNFDDEFT SEAPILTPPR 970 980 EPRILLEEEQ EMFHDFDYVA DWC
	Isoform 2 [UniParc]. Checksum: D2806BCD710C1B29	FASTA	972	110,313
	10 20 30 40 50 60 MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDDIKDR IKREIRKELK IKEGAENLRK 70 80 90 100 110 120 VTTDKKNLAY VDNILKKSNK KLEELHHKLQ ELNAHIVVSD PEDSTDCPRT PDTPNSDSRS 130 140 150 160 170 180 STSNNRLMAL QKQLDIELKV KQGAENMIQM YSNGSSKDRK LHGTAQQLLQ DSKTKIEVIR 190 200 210 220 230 240 MQILQAVQTN ELAFDNAKPV ISPLELRMEE LRHHFKIEFA VAEGAKNVMK LLGSGKVTDR 250 260 270 280 290 300 KALSEAQARF NESSQKLDLL KYSLEQRLNE LPRNHPKSSV VIEELSLVAS PTLSPRQSML 310 320 330 340 350 360 STQNQYSTLS KPAALTGTLE VRLMGCQDIL ENVPGRSKAT SVALPGWSPS DNRSSFMSRT 370 380 390 400 410 420 SKSKSGSSRN LLKTDDLSND VCAVLKLDNT VVGQTSWKPI SNQSWDQKFT LELDRSRELE 430 440 450 460 470 480 ISVYWRDWRS LCAVKFLRLE DFLDNQRHGM CLYLEPQGTL FAEVTFFNPV IERRPKLQRQ 490 500 510 520 530 540 KKIFSKQQGK TFLRAPQMNI NIATWGRLVR RAIPTVNHSG TFSPQTPVPA TVPVVDARIP 550 560 570 580 590 600 DLAPPASDST VTKLDFDLEP EPPPAPPRAS SLGETDESSE LRVLDIPGQG SETVFNIEND 610 620 630 640 650 660 RNNLRPKSKS EYELSIPDSG RSCWGVGELD DKRAQQRFQF SLQDFRCCAV LGRGHFGKVL 670 680 690 700 710 720 LAEYKHTNEM FAIKALKKGD IVARDEVDSL MCEKRIFETV NSVRHPFLVN LFACFQTKEH 730 740 750 760 770 780 VCFVMEYAAG GDLMMHIHTD VFSEPRAVFY AACVVLGLQY LHEHKIVYRD LKLDNLLLDT 790 800 810 820 830 840 EGFVKIADFG LCKEGMGYGD RTSTFCGTPE FLAPEVLTET SYTRAVDWWG LGVLIYEMLV 850 860 870 880 890 900 GESPFPGDDE EEVFDSIVND EVRYPRFLST EAISIMRRLL RRNPERRLGA GEKDAEDVKK 910 920 930 940 950 960 HPFFRLTDWS ALMDKKVKPP FVPTIRGRED VSNFDDEFTS EAPILTPPRE PRILLEEEQE 970 MFHDFDYVAD WC
	Isoform 3 [UniParc]. Checksum: 6B762C942B96D5EF	FASTA	787	88,961
	10 20 30 40 50 60 MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 70 80 90 100 110 120 KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDSTDCPR 130 140 150 160 170 180 TPDTPNSDSR SSTSNNRLMA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 190 200 210 220 230 240 QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM 250 260 270 280 290 300 KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA 310 320 330 340 350 360 SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA TSVALPGWSP 370 380 390 400 410 420 SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN TVVGQTSWKP ISNQSWDQKF 430 440 450 460 470 480 TLELDRSREL EISVYWRDWR SLCAVKFLRL EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP 490 500 510 520 530 540 VIERRPKLQR QKKIFSKQQG KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP 550 560 570 580 590 600 ATVPVVDARI PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ 610 620 630 640 650 660 GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ FSLQDFRCCA 670 680 690 700 710 720 VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS LMCEKRIFET VNSVRHPFLV 730 740 750 760 770 780 NLFACFQTKE HVCFVMEYAA GGDLMMHIHT DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR NTIFSSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Strain: C57BL/6J and NOD. Tissue: Corpora quadrigemina, Spinal cord and Testis.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Brain.
[3]	"Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling." Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J. J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NCK1, TISSUE SPECIFICITY.
[4]	"The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization." Vincent S., Settleman J. Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase." Sun W., Vincent S., Settleman J., Johnson G.L. J. Biol. Chem. 275:24421-24428(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAP3K2.
[6]	"Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion." Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P. J. Cell Biol. 156:137-148(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes." Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A. J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN PHOSPHORYLATION OF CTTN, ENZYME REGULATION, INTERACTION WITH CD44 AND RAC1, TISSUE SPECIFICITY.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[9]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells." Wallace S.W., Magalhaes A., Hall A. Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAC1 AND RHOA, MUTAGENESIS OF ALA-66; ALA-155; LYS-685 AND ASP-781.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK046248 mRNA. Translation: BAC32655.1. AK133298 mRNA. Translation: BAE21599.1. AK171092 mRNA. Translation: BAE42244.1. AK049713 mRNA. Translation: BAC33888.1. AK083425 mRNA. Translation: BAC38910.1. BC052073 mRNA. Translation: AAH52073.1.
RefSeq	NP_848769.2. NM_178654.4.
UniGene	Mm.244236.
3D structure databases
ProteinModelPortal	Q8BWW9.
SMR	Q8BWW9. Positions 56-107, 132-203, 613-979.
ModBase	Search...
MobiDB	Search...
PTM databases
PhosphoSite	Q8BWW9.
Proteomic databases
PaxDb	Q8BWW9.
PRIDE	Q8BWW9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591.
GeneID	109333.
KEGG	mmu:109333.
UCSC	uc008rpe.2. mouse.
Organism-specific databases
CTD	5586.
MGI	MGI:109211. Pkn2.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00740000115079.
HOGENOM	HOG000233032.
HOVERGEN	HBG108317.
InParanoid	Q3TBR3.
KO	K06071.
OMA	RSQQMFQ.
OrthoDB	EOG7X9G6Q.
TreeFam	TF102005.
Gene expression databases
ArrayExpress	Q8BWW9.
Bgee	Q8BWW9.
CleanEx	MM_PKN2.
Genevestigator	Q8BWW9.
Family and domain databases
Gene3D	1.10.287.160. 3 hits.
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_dom. IPR011072. HR1_rho-bd. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF02185. HR1. 3 hits. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. SM00742. Hr1. 3 hits. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF46585. SSF46585. 3 hits. SSF49562. SSF49562. 1 hit. SSF56112. SSF56112. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PKN2. mouse.
NextBio	361929.
PRO	Q8BWW9.
SOURCE	Search...

Entry information

Entry name

PKN2_MOUSE

Accession

Primary (citable) accession number: Q8BWW9
Secondary accession number(s): Q3TBR3 , Q80WS2, Q8BJL7, Q8BL62

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	July 27, 2011
Last modified:	February 19, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program