Q16513 (PKN2_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	984 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). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. Ref.8 Ref.9 Ref.12 Ref.15 Ref.16 Ref.17 Ref.20 Ref.28 Ref.31 Ref.32
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Kinase activity is activated upon binding to GTP-bound Rhoa/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-816 (activation loop of the kinase domain) and Thr-958 (turn motif), need to be phosphorylated for its full activation. Ref.7 Ref.12 Ref.22
Subunit structure	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 CD44 By similarity. 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 with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent 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 HCV NS5B (via N-terminus finger domain). Interacts with NCK1, NCK2 and RHOC. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.22 Ref.31
Subcellular location	Cytoplasm. Nucleus. Membrane By similarity. Cell projection › lamellipodium. Cytoplasm › cytoskeleton. Cleavage furrow. Midbody. Cell junction. 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. In the course of viral infection, colocalizes with HCV NS5B at perinuclear region in the cytoplasm. Ref.14 Ref.20
Tissue specificity	Ubiquitous. Expressed in numerous tumor cell lines, especially in bladder tumor cells. Ref.10 Ref.32
Induction	Up-regulated during keratinocyte differentiation. Ref.7 Ref.12 Ref.16 Ref.22
Domain	The N-terminus region interferes with the interaction between AKT1 and the C-terminus region of PKN2. 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.
Post-translational modification	Autophosphorylated. Phosphorylated during mitosis. Ref.8 Ref.13 Ref.20 Activated by limited proteolysis with trypsin By similarity. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death. Ref.7
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.
Biophysicochemical properties	Kinetic parameters: KM=15.83 µM for HDAC5 Ref.28

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 Polymorphism
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 mutant phenotype Ref.31. 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 direct assay Ref.32. Source: UniProtKB positive regulation of cell cycle cytokinesis Inferred from mutant phenotype Ref.20. Source: UniProtKB positive regulation of mitotic cell cycle Inferred from mutant phenotype Ref.20. Source: UniProtKB regulation of cell motility Inferred from mutant phenotype Ref.32. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement Ref.2. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	apical junction complex Inferred from direct assay Ref.31. Source: UniProtKB cleavage furrow Inferred from direct assay Ref.20. Source: UniProtKB cytoplasm Inferred from direct assay Ref.20. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from direct assay Ref.14. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay Ref.20. Source: UniProtKB nucleus Inferred from direct assay Ref.14. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone deacetylase binding Inferred from direct assay Ref.28. Source: UniProtKB protein kinase C activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from direct assay Ref.28. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16513-1)

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: Q16513-2)

The sequence of this isoform differs from the canonical sequence as follows:
     375-390: Missing.

Isoform 3 (identifier: Q16513-3)

The sequence of this isoform differs from the canonical sequence as follows:
     428-475: Missing.

Isoform 4 (identifier: Q16513-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.

Isoform 5 (identifier: Q16513-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-329: LTG → MNS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 984	984	Serine/threonine-protein kinase N2		PRO_0000055722
Regions
	Repeat	44 – 119	76	REM 1
	Repeat	133 – 213	81	REM 2
	Repeat	214 – 295	82	REM 3
	Domain	330 – 463	134	C2
	Domain	657 – 916	260	Protein kinase
	Domain	917 – 984	68	AGC-kinase C-terminal
	Nucleotide binding	663 – 671	9	ATP By similarity
	Region	382 – 463	82	Necessary to rescue apical junction formation By similarity
	Region	917 – 977	61	Necessary for the catalytic activity
	Region	978 – 984	7	Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA
Sites
	Active site	782	1	Proton acceptor By similarity
	Binding site	686	1	ATP By similarity
	Site	117 – 118	2	Cleavage; by caspase-3
	Site	700 – 701	2	Cleavage; by caspase-3
Amino acid modifications
	Modified residue	110	1	Phosphoserine Ref.25
	Modified residue	121	1	Phosphothreonine Ref.25
	Modified residue	124	1	Phosphothreonine Ref.25
	Modified residue	302	1	Phosphoserine Ref.19 Ref.25 Ref.29
	Modified residue	306	1	Phosphoserine Ref.19 Ref.25 Ref.29
	Modified residue	360	1	Phosphoserine Ref.19 Ref.25 Ref.29
	Modified residue	362	1	Phosphoserine Ref.25
	Modified residue	367	1	Phosphoserine By similarity
	Modified residue	535	1	Phosphoserine Ref.25
	Modified residue	583	1	Phosphoserine Ref.29
	Modified residue	628	1	Phosphothreonine Ref.25
	Modified residue	631	1	Phosphoserine Ref.25
	Modified residue	816	1	Phosphothreonine; by PDPK1 Ref.13
	Modified residue	958	1	Phosphothreonine Ref.18 Ref.24 Ref.25 Ref.29
Natural variations
	Alternative sequence	1 – 326	326	Missing in isoform 5.		VSP_042180
	Alternative sequence	1 – 157	157	Missing in isoform 4.		VSP_042181
	Alternative sequence	327 – 329	3	LTG → MNS in isoform 5.		VSP_042182
	Alternative sequence	375 – 390	16	Missing in isoform 2.		VSP_042183
	Alternative sequence	428 – 475	48	Missing in isoform 3.		VSP_042184
	Natural variant	94	1	E → D. Corresponds to variant rs12039846 [ dbSNP | Ensembl ].		VAR_050562
	Natural variant	197	1	A → E. Corresponds to variant rs35207128 [ dbSNP | Ensembl ].		VAR_050563
	Natural variant	655	1	Q → R. Corresponds to variant rs12085658 [ dbSNP | Ensembl ].		VAR_050564
Experimental info
	Mutagenesis	117	1	D → A: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700. Ref.7 Ref.12
	Mutagenesis	686	1	K → R: Does not inhibit interaction with PTPN13. Ref.14
	Mutagenesis	700	1	D → E: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117. Ref.7 Ref.12
	Mutagenesis	816	1	T → A: Reduces catalytic activity. Ref.22
	Mutagenesis	958	1	T → A: Abolishes catalytic activity. Ref.22
	Mutagenesis	974	1	F → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Ref.9
	Mutagenesis	977	1	F → A or L: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%. Ref.9 Ref.22
	Mutagenesis	977	1	F → W or Y: Reduces catalytic activity by 50%. Ref.9 Ref.22
	Mutagenesis	978	1	D → A or S: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Ref.9 Ref.22
	Mutagenesis	978	1	D → A: Does not inhibit catalytic activity. Ref.9 Ref.22
	Mutagenesis	979	1	Y → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Ref.9 Ref.22
	Mutagenesis	979	1	Y → A: Reduces catalytic activity by 50%. Ref.9 Ref.22
	Mutagenesis	979	1	Y → F, L or W: Reduces catalytic activity by 25%. Ref.9 Ref.22
	Mutagenesis	984	1	C → S: Inhibits interaction with PTPN13. Ref.14
	Sequence conflict	483	1	I → V in BAG62673. Ref.3
	Sequence conflict	565	1	K → R in BAG60783. Ref.3
	Sequence conflict	625	1	K → R in BAG62673. Ref.3
	Sequence conflict	795	1	F → L in AAI25200. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 687EC417A0F51C1D	FASTA	984	112,035
	10 20 30 40 50 60 MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 70 80 90 100 110 120 KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDITDCPR 130 140 150 160 170 180 TPDTPNNDPR CSTSNNRLKA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 190 200 210 220 230 240 QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM 250 260 270 280 290 300 KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA 310 320 330 340 350 360 ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK ATSVALPGWS 370 380 390 400 410 420 PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD NTVVGQTSWK PISNQSWDQK 430 440 450 460 470 480 FTLELDRSRE LEISVYWRDW RSLCAVKFLR LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN 490 500 510 520 530 540 PVIERRPKLQ RQKKIFSKQQ GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV 550 560 570 580 590 600 PTTVPVVDVR IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG 610 620 630 640 650 660 QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF QFNLQDFRCC 670 680 690 700 710 720 AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD SLMCEKRIFE TVNSVRHPFL 730 740 750 760 770 780 VNLFACFQTK EHVCFVMEYA AGGDLMMHIH TDVFSEPRAV FYAACVVLGL QYLHEHKIVY 790 800 810 820 830 840 RDLKLDNLLL DTEGFVKIAD FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW 850 860 870 880 890 900 WGLGVLIYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL 910 920 930 940 950 960 GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF TSEAPILTPP 970 980 REPRILSEEE QEMFRDFDYI ADWC
	Isoform 2 [UniParc]. Checksum: BE8D7EDA728D78EE	FASTA	968	110,345
	10 20 30 40 50 60 MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 70 80 90 100 110 120 KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDITDCPR 130 140 150 160 170 180 TPDTPNNDPR CSTSNNRLKA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 190 200 210 220 230 240 QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM 250 260 270 280 290 300 KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA 310 320 330 340 350 360 ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK ATSVALPGWS 370 380 390 400 410 420 PSETRSSFMS RTSKNDVCAV LKLDNTVVGQ TSWKPISNQS WDQKFTLELD RSRELEISVY 430 440 450 460 470 480 WRDWRSLCAV KFLRLEDFLD NQRHGMCLYL EPQGTLFAEV TFFNPVIERR PKLQRQKKIF 490 500 510 520 530 540 SKQQGKTFLR APQMNINIAT WGRLVRRAIP TVNHSGTFSP QAPVPTTVPV VDVRIPQLAP 550 560 570 580 590 600 PASDSTVTKL DFDLEPEPPP APPRASSLGE IDESSELRVL DIPGQDSETV FDIQNDRNSI 610 620 630 640 650 660 LPKSQSEYKP DTPQSGLEYS GIQELEDRRS QQRFQFNLQD FRCCAVLGRG HFGKVLLAEY 670 680 690 700 710 720 KNTNEMFAIK ALKKGDIVAR DEVDSLMCEK RIFETVNSVR HPFLVNLFAC FQTKEHVCFV 730 740 750 760 770 780 MEYAAGGDLM MHIHTDVFSE PRAVFYAACV VLGLQYLHEH KIVYRDLKLD NLLLDTEGFV 790 800 810 820 830 840 KIADFGLCKE GMGYGDRTST FCGTPEFLAP EVLTETSYTR AVDWWGLGVL IYEMLVGESP 850 860 870 880 890 900 FPGDDEEEVF DSIVNDEVRY PRFLSTEAIS IMRRLLRRNP ERRLGASEKD AEDVKKHPFF 910 920 930 940 950 960 RLIDWSALMD KKVKPPFIPT IRGREDVSNF DDEFTSEAPI LTPPREPRIL SEEEQEMFRD FDYIADWC
	Isoform 3 [UniParc]. Checksum: 43128E92FEDC05B4	FASTA	936	106,217
	10 20 30 40 50 60 MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 70 80 90 100 110 120 KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDITDCPR 130 140 150 160 170 180 TPDTPNNDPR CSTSNNRLKA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 190 200 210 220 230 240 QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM 250 260 270 280 290 300 KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA 310 320 330 340 350 360 ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK ATSVALPGWS 370 380 390 400 410 420 PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD NTVVGQTSWK PISNQSWDQK 430 440 450 460 470 480 FTLELDRVTF FNPVIERRPK LQRQKKIFSK QQGKTFLRAP QMNINIATWG RLVRRAIPTV 490 500 510 520 530 540 NHSGTFSPQA PVPTTVPVVD VRIPQLAPPA SDSTVTKLDF DLEPEPPPAP PRASSLGEID 550 560 570 580 590 600 ESSELRVLDI PGQDSETVFD IQNDRNSILP KSQSEYKPDT PQSGLEYSGI QELEDRRSQQ 610 620 630 640 650 660 RFQFNLQDFR CCAVLGRGHF GKVLLAEYKN TNEMFAIKAL KKGDIVARDE VDSLMCEKRI 670 680 690 700 710 720 FETVNSVRHP FLVNLFACFQ TKEHVCFVME YAAGGDLMMH IHTDVFSEPR AVFYAACVVL 730 740 750 760 770 780 GLQYLHEHKI VYRDLKLDNL LLDTEGFVKI ADFGLCKEGM GYGDRTSTFC GTPEFLAPEV 790 800 810 820 830 840 LTETSYTRAV DWWGLGVLIY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR FLSTEAISIM 850 860 870 880 890 900 RRLLRRNPER RLGASEKDAE DVKKHPFFRL IDWSALMDKK VKPPFIPTIR GREDVSNFDD 910 920 930 EFTSEAPILT PPREPRILSE EEQEMFRDFD YIADWC
	Isoform 4 [UniParc]. Checksum: B08B24A67D1697CE	FASTA	827	94,136
	10 20 30 40 50 60 MIQMYSNGSS KDRKLHGTAQ QLLQDSKTKI EVIRMQILQA VQTNELAFDN AKPVISPLEL 70 80 90 100 110 120 RMEELRHHFR IEFAVAEGAK NVMKLLGSGK VTDRKALSEA QARFNESSQK LDLLKYSLEQ 130 140 150 160 170 180 RLNEVPKNHP KSRIIIEELS LVAASPTLSP RQSMISTQNQ YSTLSKPAAL TGTLEVRLMG 190 200 210 220 230 240 CQDILENVPG RSKATSVALP GWSPSETRSS FMSRTSKSKS GSSRNLLKTD DLSNDVCAVL 250 260 270 280 290 300 KLDNTVVGQT SWKPISNQSW DQKFTLELDR SRELEISVYW RDWRSLCAVK FLRLEDFLDN 310 320 330 340 350 360 QRHGMCLYLE PQGTLFAEVT FFNPVIERRP KLQRQKKIFS KQQGKTFLRA PQMNINIATW 370 380 390 400 410 420 GRLVRRAIPT VNHSGTFSPQ APVPTTVPVV DVRIPQLAPP ASDSTVTKLD FDLEPEPPPA 430 440 450 460 470 480 PPRASSLGEI DESSELRVLD IPGQDSETVF DIQNDRNSIL PKSQSEYKPD TPQSGLEYSG 490 500 510 520 530 540 IQELEDRRSQ QRFQFNLQDF RCCAVLGRGH FGKVLLAEYK NTNEMFAIKA LKKGDIVARD 550 560 570 580 590 600 EVDSLMCEKR IFETVNSVRH PFLVNLFACF QTKEHVCFVM EYAAGGDLMM HIHTDVFSEP 610 620 630 640 650 660 RAVFYAACVV LGLQYLHEHK IVYRDLKLDN LLLDTEGFVK IADFGLCKEG MGYGDRTSTF 670 680 690 700 710 720 CGTPEFLAPE VLTETSYTRA VDWWGLGVLI YEMLVGESPF PGDDEEEVFD SIVNDEVRYP 730 740 750 760 770 780 RFLSTEAISI MRRLLRRNPE RRLGASEKDA EDVKKHPFFR LIDWSALMDK KVKPPFIPTI 790 800 810 820 RGREDVSNFD DEFTSEAPIL TPPREPRILS EEEQEMFRDF DYIADWC
	Isoform 5 [UniParc]. Checksum: D0B6E1DEA98B3C0D	FASTA	658	75,171
	10 20 30 40 50 60 MNSTLEVRLM GCQDILENVP GRSKATSVAL PGWSPSETRS SFMSRTSKSK SGSSRNLLKT 70 80 90 100 110 120 DDLSNDVCAV LKLDNTVVGQ TSWKPISNQS WDQKFTLELD RSRELEISVY WRDWRSLCAV 130 140 150 160 170 180 KFLRLEDFLD NQRHGMCLYL EPQGTLFAEV TFFNPVIERR PKLQRQKKIF SKQQGKTFLR 190 200 210 220 230 240 APQMNINIAT WGRLVRRAIP TVNHSGTFSP QAPVPTTVPV VDVRIPQLAP PASDSTVTKL 250 260 270 280 290 300 DFDLEPEPPP APPRASSLGE IDESSELRVL DIPGQDSETV FDIQNDRNSI LPKSQSEYKP 310 320 330 340 350 360 DTPQSGLEYS GIQELEDRRS QQRFQFNLQD FRCCAVLGRG HFGKVLLAEY KNTNEMFAIK 370 380 390 400 410 420 ALKKGDIVAR DEVDSLMCEK RIFETVNSVR HPFLVNLFAC FQTKEHVCFV MEYAAGGDLM 430 440 450 460 470 480 MHIHTDVFSE PRAVFYAACV VLGLQYLHEH KIVYRDLKLD NLLLDTEGFV KIADFGLCKE 490 500 510 520 530 540 GMGYGDRTST FCGTPEFLAP EVLTETSYTR AVDWWGLGVL IYEMLVGESP FPGDDEEEVF 550 560 570 580 590 600 DSIVNDEVRY PRFLSTEAIS IMRRLLRRNP ERRLGASEKD AEDVKKHPFF RLIDWSALMD 610 620 630 640 650 KKVKPPFIPT IRGREDVSNF DDEFTSEAPI LTPPREPRIL SEEEQEMFRD FDYIADWC

References

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[1]	"Identification of multiple, novel, protein kinase C-related gene products." Palmer R.H., Ridden J., Parker P.J. FEBS Lett. 356:5-8(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family." Palmer R.H., Ridden J., Parker P.J. Eur. J. Biochem. 227:344-351(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: B-cell and Spleen.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5). Tissue: Placenta and Spleen.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 3).
[7]	"Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy." Cryns V.L., Byun Y., Rana A., Mellor H., Lustig K.D., Ghanem L., Parker P.J., Kirschner M.W., Yuan J. J. Biol. Chem. 272:29449-29453(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-117 AND ASP-700.
[8]	"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: FUNCTION, INTERACTION WITH RAC1 AND RHOA, AUTOPHOSPHORYLATION.
[9]	"PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2." Balendran A., Casamayor A., Deak M., Paterson A., Gaffney P., Currie R., Downes C.P., Alessi D.R. Curr. Biol. 9:393-404(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PDPK1, MUTAGENESIS OF PHE-974; PHE-977; ASP-978 AND TYR-979.
[10]	"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck." Braverman L.E., Quilliam L.A. J. Biol. Chem. 274:5542-5549(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCK1 AND NCK2, TISSUE SPECIFICITY.
[11]	"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.
[12]	"Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage." Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J. J. Biol. Chem. 275:34451-34458(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS, FUNCTION IN AKT1 ACTIVITY INHIBITION, ENZYME REGULATION, INTERACTION WITH AKT1, MUTAGENESIS OF ASP-117 AND ASP-700.
[13]	"Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton." Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F. Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-816 BY PDPK1, INTERACTION WITH PDPK1.
[14]	"The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif." Gross C., Heumann R., Erdmann K.S. FEBS Lett. 496:101-104(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN13, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-686 AND CYS-984.
[15]	"Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment." Hodgkinson C.P., Sale G.J. Biochemistry 41:561-569(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN KINASE ACTIVITY INHIBITION, INTERACTION WITH PDPK1.
[16]	"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: FUNCTION IN CELL ADHESION, INDUCTION.
[17]	"Protein kinase C-related kinase 2 regulates hepatitis C virus RNA polymerase function by phosphorylation." Kim S.J., Kim J.H., Kim Y.G., Lim H.S., Oh J.W. J. Biol. Chem. 279:50031-50041(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HCV REPLICATION, FUNCTION IN PHOSPHORYLATION OF NS5B, INTERACTION WITH HCV NS5B.
[18]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-958, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306 AND SER-360, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis." Schmidt A., Durgan J., Magalhaes A., Hall A. EMBO J. 26:1624-1636(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[21]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[22]	"The C-terminus of PRK2/PKNgamma is required for optimal activation by RhoA in a GTP-dependent manner." Lim W.G., Chen X., Liu J.P., Tan B.J., Zhou S., Smith A., Lees N., Hou L., Gu F., Yu X.Y., Du Y., Smith D., Verma C., Liu K., Duan W. Arch. Biochem. Biophys. 479:170-178(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH PDPK1, MUTAGENESIS OF THR-816; THR-958; PHE-977; ASP-978 AND TYR-979.
[23]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[24]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-958, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-121; THR-124; SER-302; SER-306; SER-360; SER-362; SER-535; THR-628; SER-631 AND THR-958, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[28]	"Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases." Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A. FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5, BIOPHYSICOCHEMICAL PROPERTIES.
[29]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306; SER-360; SER-583 AND THR-958, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]	"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; RHOA AND RHOC.
[32]	"Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration." Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S., Collazos A., Parker P.J. PLoS ONE 6:E21732-E21732(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL MIGRATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33052 mRNA. Translation: AAC50208.1. S75548 mRNA. Translation: AAB33346.1. AK298595 mRNA. Translation: BAG60783.1. AK300304 mRNA. Translation: BAG62057.1. AK301066 mRNA. Translation: BAG62673.1. AL136381, AC119426 Genomic DNA. Translation: CAI23271.1. CH471097 Genomic DNA. Translation: EAW73161.1. CH471097 Genomic DNA. Translation: EAW73164.1. BC125199 mRNA. Translation: AAI25200.1.
IPI	IPI00002804. IPI00514557.
PIR	S67527.
RefSeq	NP_006247.1. NM_006256.2.
UniGene	Hs.440833.
3D structure databases
ProteinModelPortal	Q16513.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16513. 3 interactions.
MINT	MINT-198348.
STRING	9606.ENSP00000359552.
PTM databases
PhosphoSite	Q16513.
Polymorphism databases
DMDM	6225859.
Proteomic databases
PaxDb	Q16513.
PRIDE	Q16513.
Protocols and materials databases
DNASU	5586.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370505; ENSP00000359536; ENSG00000065243. ENST00000370513; ENSP00000359544; ENSG00000065243. ENST00000370521; ENSP00000359552; ENSG00000065243. ENST00000544045; ENSP00000439643; ENSG00000065243.
GeneID	5586.
KEGG	hsa:5586.
UCSC	uc001dmn.3. human.
Organism-specific databases
CTD	5586.
GeneCards	GC01P089149.
HGNC	HGNC:9406. PKN2.
HPA	HPA034861.
MIM	602549. gene.
neXtProt	NX_Q16513.
PharmGKB	PA33770.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233032.
HOVERGEN	HBG108317.
InParanoid	Q16513.
KO	K06071.
OMA	WSALMDK.
OrthoDB	EOG40ZQWW.
PhylomeDB	Q16513.
Enzyme and pathway databases
BRENDA	2.7.11.13. 2681.
Gene expression databases
ArrayExpress	Q16513.
Bgee	Q16513.
CleanEx	HS_PKN2.
Genevestigator	Q16513.
GermOnline	ENSG00000065243. Homo sapiens.
Family and domain databases
Gene3D	1.10.287.160. 3 hits.
InterPro	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. [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	SSF49562. C2_CaLB. 1 hit. SSF56112. Kinase_like. 1 hit. SSF46585. PKN_effector. 3 hits.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50004. C2. False negative. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q16513.
ChEMBL	CHEMBL3032.
ChiTaRS	PKN2. human.
GenomeRNAi	5586.
NextBio	21666.
PMAP-CutDB	Q16513.
SOURCE	Search...

Entry information

Entry name

PKN2_HUMAN

Accession

Primary (citable) accession number: Q16513
Secondary accession number(s): B4DQ21 , B4DTP5, B4DVG1, D3DT24, Q08AF4, Q9H1W4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.