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Protein

Serine/threonine-protein kinase N2

Gene

PKN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.3 Publications

Kineticsi

  1. KM=15.83 µM for HDAC51 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei686ATPPROSITE-ProRule annotation1
    Active sitei782Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi663 – 671ATPPROSITE-ProRule annotation9

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
    • histone deacetylase binding Source: UniProtKB
    • kinase activity Source: AgBase
    • poly(A) RNA binding Source: UniProtKB
    • protein kinase activity Source: ProtInc
    • protein kinase C activity Source: UniProtKB-EC
    • protein serine/threonine kinase activity Source: UniProtKB
    • RNA polymerase binding Source: AgBase

    GO - Biological processi

    • apical junction assembly Source: UniProtKB
    • apoptotic process Source: UniProtKB-KW
    • cell cycle Source: UniProtKB-KW
    • cell division Source: UniProtKB-KW
    • epithelial cell migration Source: UniProtKB
    • intracellular signal transduction Source: GO_Central
    • peptidyl-serine phosphorylation Source: GO_Central
    • positive regulation of cytokinesis Source: UniProtKB
    • positive regulation of mitotic cell cycle Source: UniProtKB
    • positive regulation of viral genome replication Source: AgBase
    • protein phosphorylation Source: UniProtKB
    • regulation of cell motility Source: UniProtKB
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • signal transduction Source: ProtInc
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell adhesion, Cell cycle, Cell division, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciZFISH:HS00834-MONOMER.
    BRENDAi2.7.11.13. 2681.
    ReactomeiR-HSA-5625740. RHO GTPases activate PKNs.
    SignaLinkiQ16513.
    SIGNORiQ16513.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:PKN2
    Synonyms:PRK2, PRKCL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9406. PKN2.

    Subcellular locationi

    • Cytoplasm 2 Publications
    • Nucleus 1 Publication
    • Membrane By similarity
    • Cell projectionlamellipodium 1 Publication
    • Cytoplasmcytoskeleton 1 Publication
    • Cleavage furrow 1 Publication
    • Midbody 1 Publication
    • Cell junction 1 Publication

    • 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.2 Publications

    GO - Cellular componenti

    • apical junction complex Source: UniProtKB
    • cell-cell adherens junction Source: BHF-UCL
    • cell junction Source: HPA
    • centrosome Source: HPA
    • cleavage furrow Source: UniProtKB
    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • intermediate filament cytoskeleton Source: HPA
    • lamellipodium Source: UniProtKB
    • midbody Source: UniProtKB
    • nucleoplasm Source: HPA
    • nucleus Source: UniProtKB
    • perinuclear region of cytoplasm Source: AgBase
    • plasma membrane Source: HPA
    • protein complex Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi117D → A: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700. 2 Publications1
    Mutagenesisi686K → R: Does not inhibit interaction with PTPN13. 1 Publication1
    Mutagenesisi700D → E: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117. 2 Publications1
    Mutagenesisi816T → A: Reduces catalytic activity. 1 Publication1
    Mutagenesisi958T → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi974F → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 1 Publication1
    Mutagenesisi977F → A or L: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%. 2 Publications1
    Mutagenesisi977F → W or Y: Reduces catalytic activity by 50%. 2 Publications1
    Mutagenesisi978D → A or S: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications1
    Mutagenesisi978D → A: Does not inhibit catalytic activity. 2 Publications1
    Mutagenesisi979Y → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications1
    Mutagenesisi979Y → A: Reduces catalytic activity by 50%. 2 Publications1
    Mutagenesisi979Y → F, L or W: Reduces catalytic activity by 25%. 2 Publications1
    Mutagenesisi984C → S: Inhibits interaction with PTPN13. 1 Publication1

    Organism-specific databases

    DisGeNETi5586.
    OpenTargetsiENSG00000065243.
    PharmGKBiPA33770.

    Chemistry databases

    ChEMBLiCHEMBL3032.
    GuidetoPHARMACOLOGYi1521.

    Polymorphism and mutation databases

    BioMutaiPKN2.
    DMDMi6225859.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000557221 – 984Serine/threonine-protein kinase N2Add BLAST984

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei21PhosphoserineCombined sources1
    Modified residuei77N6-acetyllysineBy similarity1
    Modified residuei110PhosphoserineCombined sources1
    Modified residuei121PhosphothreonineCombined sources1
    Modified residuei124PhosphothreonineCombined sources1
    Modified residuei302PhosphoserineCombined sources1
    Modified residuei306PhosphoserineCombined sources1
    Modified residuei360PhosphoserineCombined sources1
    Modified residuei362PhosphoserineCombined sources1
    Modified residuei535PhosphoserineCombined sources1
    Modified residuei583PhosphoserineCombined sources1
    Modified residuei620PhosphoserineBy similarity1
    Modified residuei628PhosphothreonineCombined sources1
    Modified residuei631PhosphoserineCombined sources1
    Modified residuei816Phosphothreonine; by PDPK11 Publication1
    Modified residuei952PhosphoserineCombined sources1
    Modified residuei958PhosphothreonineCombined sources1

    Post-translational modificationi

    Autophosphorylated. Phosphorylated during mitosis.2 Publications
    Activated by limited proteolysis with trypsin (By similarity). Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death.By similarity1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei117 – 118Cleavage; by caspase-32
    Sitei700 – 701Cleavage; by caspase-32

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ16513.
    MaxQBiQ16513.
    PaxDbiQ16513.
    PeptideAtlasiQ16513.
    PRIDEiQ16513.

    PTM databases

    iPTMnetiQ16513.
    PhosphoSitePlusiQ16513.

    Miscellaneous databases

    PMAP-CutDBQ16513.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed in numerous tumor cell lines, especially in bladder tumor cells.2 Publications

    Inductioni

    Up-regulated during keratinocyte differentiation.1 Publication

    Gene expression databases

    BgeeiENSG00000065243.
    CleanExiHS_PKN2.
    ExpressionAtlasiQ16513. baseline and differential.
    GenevisibleiQ16513. HS.

    Organism-specific databases

    HPAiHPA034861.
    HPA057913.

    Interactioni

    Subunit structurei

    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-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with HCV NS5B (via N-terminal finger domain). Interacts with NCK1, NCK2 and RHOC.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    O929727EBI-2511350,EBI-10006231From a different organism.
    PDK1Q151186EBI-2511350,EBI-7016221

    GO - Molecular functioni

    • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
    • histone deacetylase binding Source: UniProtKB
    • RNA polymerase binding Source: AgBase

    Protein-protein interaction databases

    BioGridi111572. 85 interactors.
    IntActiQ16513. 50 interactors.
    MINTiMINT-198348.
    STRINGi9606.ENSP00000359552.

    Chemistry databases

    BindingDBiQ16513.

    Structurei

    Secondary structure

    1984
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi647 – 649Combined sources3
    Beta strandi652 – 654Combined sources3
    Beta strandi657 – 665Combined sources9
    Beta strandi670 – 676Combined sources7
    Beta strandi682 – 689Combined sources8
    Helixi690 – 695Combined sources6
    Helixi699 – 714Combined sources16
    Beta strandi723 – 729Combined sources7
    Beta strandi732 – 738Combined sources7
    Helixi745 – 749Combined sources5
    Helixi756 – 774Combined sources19
    Turni775 – 777Combined sources3
    Helixi785 – 787Combined sources3
    Beta strandi788 – 790Combined sources3
    Beta strandi796 – 798Combined sources3
    Beta strandi805 – 807Combined sources3
    Helixi821 – 823Combined sources3
    Helixi826 – 830Combined sources5
    Helixi838 – 852Combined sources15
    Helixi862 – 871Combined sources10
    Helixi882 – 891Combined sources10
    Helixi896 – 898Combined sources3
    Beta strandi903 – 905Combined sources3
    Helixi907 – 911Combined sources5
    Helixi914 – 916Combined sources3
    Helixi921 – 925Combined sources5
    Beta strandi944 – 946Combined sources3
    Helixi948 – 951Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4CRSX-ray2.75A646-984[»]
    4RRVX-ray1.41B969-983[»]
    ProteinModelPortaliQ16513.
    SMRiQ16513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Repeati44 – 119REM 1Add BLAST76
    Repeati133 – 213REM 2Add BLAST81
    Repeati214 – 295REM 3Add BLAST82
    Domaini330 – 463C2Add BLAST134
    Domaini657 – 916Protein kinasePROSITE-ProRule annotationAdd BLAST260
    Domaini917 – 984AGC-kinase C-terminalAdd BLAST68

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni382 – 463Necessary to rescue apical junction formationBy similarityAdd BLAST82
    Regioni917 – 977Necessary for the catalytic activityAdd BLAST61
    Regioni978 – 984Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA7

    Domaini

    The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2.
    The C1 domain does not bind the diacylglycerol (DAG).
    The apoptotic C-terminal 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.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 C2 domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 3 REM (Hr1) repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiKOG0694. Eukaryota.
    ENOG410XNPH. LUCA.
    GeneTreeiENSGT00820000126964.
    HOGENOMiHOG000233032.
    HOVERGENiHBG108317.
    InParanoidiQ16513.
    KOiK06071.
    OMAiPRAPQMN.
    OrthoDBiEOG091G00YT.
    PhylomeDBiQ16513.
    TreeFamiTF102005.

    Family and domain databases

    Gene3Di1.10.287.160. 3 hits.
    2.60.40.150. 2 hits.
    InterProiIPR000961. 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.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF02185. HR1. 3 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00742. Hr1. 3 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF46585. SSF46585. 3 hits.
    SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q16513-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD
    60 70 80 90 100
    RIKREIRKEL KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL
    110 120 130 140 150
    QELNAHIVVS DPEDITDCPR TPDTPNNDPR CSTSNNRLKA LQKQLDIELK
    160 170 180 190 200
    VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL QDSKTKIEVI RMQILQAVQT
    210 220 230 240 250
    NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM KLLGSGKVTD
    260 270 280 290 300
    RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA
    310 320 330 340 350
    ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK
    360 370 380 390 400
    ATSVALPGWS PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD
    410 420 430 440 450
    NTVVGQTSWK PISNQSWDQK FTLELDRSRE LEISVYWRDW RSLCAVKFLR
    460 470 480 490 500
    LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN PVIERRPKLQ RQKKIFSKQQ
    510 520 530 540 550
    GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV PTTVPVVDVR
    560 570 580 590 600
    IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG
    610 620 630 640 650
    QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF
    660 670 680 690 700
    QFNLQDFRCC AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD
    710 720 730 740 750
    SLMCEKRIFE TVNSVRHPFL VNLFACFQTK EHVCFVMEYA AGGDLMMHIH
    760 770 780 790 800
    TDVFSEPRAV FYAACVVLGL QYLHEHKIVY RDLKLDNLLL DTEGFVKIAD
    810 820 830 840 850
    FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW WGLGVLIYEM
    860 870 880 890 900
    LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL
    910 920 930 940 950
    GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF
    960 970 980
    TSEAPILTPP REPRILSEEE QEMFRDFDYI ADWC
    Length:984
    Mass (Da):112,035
    Last modified:November 1, 1996 - v1
    Checksum:i687EC417A0F51C1D
    GO
    Isoform 2 (identifier: Q16513-2) [UniParc]FASTAAdd to basket

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

    Show »
    Length:968
    Mass (Da):110,345
    Checksum:iBE8D7EDA728D78EE
    GO
    Isoform 3 (identifier: Q16513-3) [UniParc]FASTAAdd to basket

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

    Show »
    Length:936
    Mass (Da):106,217
    Checksum:i43128E92FEDC05B4
    GO
    Isoform 4 (identifier: Q16513-4) [UniParc]FASTAAdd to basket

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

    Show »
    Length:827
    Mass (Da):94,136
    Checksum:iB08B24A67D1697CE
    GO
    Isoform 5 (identifier: Q16513-5) [UniParc]FASTAAdd to basket

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

    Show »
    Length:658
    Mass (Da):75,171
    Checksum:iD0B6E1DEA98B3C0D
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti483I → V in BAG62673 (PubMed:14702039).Curated1
    Sequence conflicti565K → R in BAG60783 (PubMed:14702039).Curated1
    Sequence conflicti625K → R in BAG62673 (PubMed:14702039).Curated1
    Sequence conflicti795F → L in AAI25200 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05056294E → D.Corresponds to variant rs12039846dbSNPEnsembl.1
    Natural variantiVAR_050563197A → E.Corresponds to variant rs35207128dbSNPEnsembl.1
    Natural variantiVAR_050564655Q → R.Corresponds to variant rs12085658dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0421801 – 326Missing in isoform 5. 1 PublicationAdd BLAST326
    Alternative sequenceiVSP_0421811 – 157Missing in isoform 4. 1 PublicationAdd BLAST157
    Alternative sequenceiVSP_042182327 – 329LTG → MNS in isoform 5. 1 Publication3
    Alternative sequenceiVSP_042183375 – 390Missing in isoform 2. 1 PublicationAdd BLAST16
    Alternative sequenceiVSP_042184428 – 475Missing in isoform 3. 1 PublicationAdd BLAST48

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS714.1. [Q16513-1]
    CCDS81350.1. [Q16513-3]
    PIRiS67527.
    RefSeqiNP_001307636.1. NM_001320707.1. [Q16513-3]
    NP_001307637.1. NM_001320708.1. [Q16513-4]
    NP_001307638.1. NM_001320709.1. [Q16513-2]
    NP_006247.1. NM_006256.3. [Q16513-1]
    XP_011540074.1. XM_011541772.2. [Q16513-5]
    UniGeneiHs.440833.

    Genome annotation databases

    EnsembliENST00000370513; ENSP00000359544; ENSG00000065243. [Q16513-3]
    ENST00000370521; ENSP00000359552; ENSG00000065243. [Q16513-1]
    GeneIDi5586.
    KEGGihsa:5586.
    UCSCiuc001dmn.4. human. [Q16513-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS714.1. [Q16513-1]
    CCDS81350.1. [Q16513-3]
    PIRiS67527.
    RefSeqiNP_001307636.1. NM_001320707.1. [Q16513-3]
    NP_001307637.1. NM_001320708.1. [Q16513-4]
    NP_001307638.1. NM_001320709.1. [Q16513-2]
    NP_006247.1. NM_006256.3. [Q16513-1]
    XP_011540074.1. XM_011541772.2. [Q16513-5]
    UniGeneiHs.440833.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4CRSX-ray2.75A646-984[»]
    4RRVX-ray1.41B969-983[»]
    ProteinModelPortaliQ16513.
    SMRiQ16513.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111572. 85 interactors.
    IntActiQ16513. 50 interactors.
    MINTiMINT-198348.
    STRINGi9606.ENSP00000359552.

    Chemistry databases

    BindingDBiQ16513.
    ChEMBLiCHEMBL3032.
    GuidetoPHARMACOLOGYi1521.

    PTM databases

    iPTMnetiQ16513.
    PhosphoSitePlusiQ16513.

    Polymorphism and mutation databases

    BioMutaiPKN2.
    DMDMi6225859.

    Proteomic databases

    EPDiQ16513.
    MaxQBiQ16513.
    PaxDbiQ16513.
    PeptideAtlasiQ16513.
    PRIDEiQ16513.

    Protocols and materials databases

    DNASUi5586.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000370513; ENSP00000359544; ENSG00000065243. [Q16513-3]
    ENST00000370521; ENSP00000359552; ENSG00000065243. [Q16513-1]
    GeneIDi5586.
    KEGGihsa:5586.
    UCSCiuc001dmn.4. human. [Q16513-1]

    Organism-specific databases

    CTDi5586.
    DisGeNETi5586.
    GeneCardsiPKN2.
    HGNCiHGNC:9406. PKN2.
    HPAiHPA034861.
    HPA057913.
    MIMi602549. gene.
    neXtProtiNX_Q16513.
    OpenTargetsiENSG00000065243.
    PharmGKBiPA33770.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0694. Eukaryota.
    ENOG410XNPH. LUCA.
    GeneTreeiENSGT00820000126964.
    HOGENOMiHOG000233032.
    HOVERGENiHBG108317.
    InParanoidiQ16513.
    KOiK06071.
    OMAiPRAPQMN.
    OrthoDBiEOG091G00YT.
    PhylomeDBiQ16513.
    TreeFamiTF102005.

    Enzyme and pathway databases

    BioCyciZFISH:HS00834-MONOMER.
    BRENDAi2.7.11.13. 2681.
    ReactomeiR-HSA-5625740. RHO GTPases activate PKNs.
    SignaLinkiQ16513.
    SIGNORiQ16513.

    Miscellaneous databases

    ChiTaRSiPKN2. human.
    GeneWikiiPKN2.
    GenomeRNAii5586.
    PMAP-CutDBQ16513.
    PROiQ16513.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000065243.
    CleanExiHS_PKN2.
    ExpressionAtlasiQ16513. baseline and differential.
    GenevisibleiQ16513. HS.

    Family and domain databases

    Gene3Di1.10.287.160. 3 hits.
    2.60.40.150. 2 hits.
    InterProiIPR000961. 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.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF02185. HR1. 3 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00742. Hr1. 3 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF46585. SSF46585. 3 hits.
    SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPKN2_HUMAN
    AccessioniPrimary (citable) accession number: Q16513
    Secondary accession number(s): B4DQ21
    , B4DTP5, B4DVG1, D3DT24, Q08AF4, Q9H1W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: November 2, 2016
    This is version 171 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.