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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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei117 – 1182Cleavage; by caspase-3
    Binding sitei686 – 6861ATPPROSITE-ProRule annotation
    Sitei700 – 7012Cleavage; by caspase-3
    Active sitei782 – 7821Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi663 – 6719ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • 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 adhesion Source: UniProtKB-KW
    • cell cycle Source: UniProtKB-KW
    • cell division Source: UniProtKB-KW
    • epithelial cell migration Source: UniProtKB
    • 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
    • small GTPase mediated signal transduction Source: Reactome
    • 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

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_355542. RHO GTPases activate PKNs.
    SignaLinkiQ16513.

    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
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9406. PKN2.

    Subcellular locationi

    GO - Cellular componenti

    • apical junction complex Source: UniProtKB
    • 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi117 – 1171D → A: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700. 2 Publications
    Mutagenesisi686 – 6861K → R: Does not inhibit interaction with PTPN13. 1 Publication
    Mutagenesisi700 – 7001D → E: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117. 2 Publications
    Mutagenesisi816 – 8161T → A: Reduces catalytic activity. 1 Publication
    Mutagenesisi958 – 9581T → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi974 – 9741F → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 1 Publication
    Mutagenesisi977 – 9771F → A or L: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%. 2 Publications
    Mutagenesisi977 – 9771F → W or Y: Reduces catalytic activity by 50%. 2 Publications
    Mutagenesisi978 – 9781D → A or S: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications
    Mutagenesisi978 – 9781D → A: Does not inhibit catalytic activity. 2 Publications
    Mutagenesisi979 – 9791Y → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications
    Mutagenesisi979 – 9791Y → A: Reduces catalytic activity by 50%. 2 Publications
    Mutagenesisi979 – 9791Y → F, L or W: Reduces catalytic activity by 25%. 2 Publications
    Mutagenesisi984 – 9841C → S: Inhibits interaction with PTPN13. 1 Publication

    Organism-specific databases

    PharmGKBiPA33770.

    Polymorphism and mutation databases

    BioMutaiPKN2.
    DMDMi6225859.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 984984Serine/threonine-protein kinase N2PRO_0000055722Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771N6-acetyllysineBy similarity
    Modified residuei110 – 1101Phosphoserine1 Publication
    Modified residuei121 – 1211Phosphothreonine1 Publication
    Modified residuei124 – 1241Phosphothreonine1 Publication
    Modified residuei302 – 3021Phosphoserine3 Publications
    Modified residuei306 – 3061Phosphoserine3 Publications
    Modified residuei360 – 3601Phosphoserine3 Publications
    Modified residuei362 – 3621Phosphoserine1 Publication
    Modified residuei535 – 5351Phosphoserine1 Publication
    Modified residuei583 – 5831Phosphoserine1 Publication
    Modified residuei628 – 6281Phosphothreonine1 Publication
    Modified residuei631 – 6311Phosphoserine1 Publication
    Modified residuei816 – 8161Phosphothreonine; by PDPK11 Publication
    Modified residuei952 – 9521Phosphoserine1 Publication
    Modified residuei958 – 9581Phosphothreonine5 Publications

    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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ16513.
    PaxDbiQ16513.
    PRIDEiQ16513.

    PTM databases

    PhosphoSiteiQ16513.

    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

    BgeeiQ16513.
    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

    Protein-protein interaction databases

    BioGridi111572. 36 interactions.
    IntActiQ16513. 17 interactions.
    MINTiMINT-198348.
    STRINGi9606.ENSP00000359552.

    Structurei

    Secondary structure

    1
    984
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi647 – 6493Combined sources
    Beta strandi652 – 6543Combined sources
    Beta strandi657 – 6659Combined sources
    Beta strandi670 – 6767Combined sources
    Beta strandi682 – 6898Combined sources
    Helixi690 – 6956Combined sources
    Helixi699 – 71416Combined sources
    Beta strandi723 – 7297Combined sources
    Beta strandi732 – 7387Combined sources
    Helixi745 – 7495Combined sources
    Helixi756 – 77419Combined sources
    Turni775 – 7773Combined sources
    Helixi785 – 7873Combined sources
    Beta strandi788 – 7903Combined sources
    Beta strandi796 – 7983Combined sources
    Beta strandi805 – 8073Combined sources
    Helixi821 – 8233Combined sources
    Helixi826 – 8305Combined sources
    Helixi838 – 85215Combined sources
    Helixi862 – 87110Combined sources
    Helixi882 – 89110Combined sources
    Helixi896 – 8983Combined sources
    Beta strandi903 – 9053Combined sources
    Helixi907 – 9115Combined sources
    Helixi914 – 9163Combined sources
    Helixi921 – 9255Combined sources
    Beta strandi944 – 9463Combined sources
    Helixi948 – 9514Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CRSX-ray2.75A646-984[»]
    4RRVX-ray1.41B969-983[»]
    ProteinModelPortaliQ16513.
    SMRiQ16513. Positions 56-107, 136-199, 618-984.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati44 – 11976REM 1Add
    BLAST
    Repeati133 – 21381REM 2Add
    BLAST
    Repeati214 – 29582REM 3Add
    BLAST
    Domaini330 – 463134C2Add
    BLAST
    Domaini657 – 916260Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini917 – 98468AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni382 – 46382Necessary to rescue apical junction formationBy similarityAdd
    BLAST
    Regioni917 – 97761Necessary for the catalytic activityAdd
    BLAST
    Regioni978 – 9847Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA

    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

    eggNOGiCOG0515.
    GeneTreeiENSGT00770000120523.
    HOGENOMiHOG000233032.
    HOVERGENiHBG108317.
    InParanoidiQ16513.
    KOiK06071.
    OMAiEYSGIQE.
    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.
    IPR002290. Ser/Thr_dual-sp_kinase.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti483 – 4831I → V in BAG62673 (PubMed:14702039).Curated
    Sequence conflicti565 – 5651K → R in BAG60783 (PubMed:14702039).Curated
    Sequence conflicti625 – 6251K → R in BAG62673 (PubMed:14702039).Curated
    Sequence conflicti795 – 7951F → L in AAI25200 (PubMed:15489334).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941E → D.
    Corresponds to variant rs12039846 [ dbSNP | Ensembl ].
    VAR_050562
    Natural varianti197 – 1971A → E.
    Corresponds to variant rs35207128 [ dbSNP | Ensembl ].
    VAR_050563
    Natural varianti655 – 6551Q → R.
    Corresponds to variant rs12085658 [ dbSNP | Ensembl ].
    VAR_050564

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 326326Missing in isoform 5. 1 PublicationVSP_042180Add
    BLAST
    Alternative sequencei1 – 157157Missing in isoform 4. 1 PublicationVSP_042181Add
    BLAST
    Alternative sequencei327 – 3293LTG → MNS in isoform 5. 1 PublicationVSP_042182
    Alternative sequencei375 – 39016Missing in isoform 2. 1 PublicationVSP_042183Add
    BLAST
    Alternative sequencei428 – 47548Missing in isoform 3. 1 PublicationVSP_042184Add
    BLAST

    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]
    PIRiS67527.
    RefSeqiNP_006247.1. NM_006256.2. [Q16513-1]
    XP_005271088.1. XM_005271031.1. [Q16513-2]
    XP_011540074.1. XM_011541772.1. [Q16513-5]
    UniGeneiHs.440833.

    Genome annotation databases

    EnsembliENST00000370513; ENSP00000359544; ENSG00000065243. [Q16513-3]
    ENST00000370521; ENSP00000359552; ENSG00000065243.
    GeneIDi5586.
    KEGGihsa:5586.
    UCSCiuc001dmn.3. human. [Q16513-1]
    uc009wcv.3. human. [Q16513-3]
    uc010osp.2. human. [Q16513-2]

    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]
    PIRiS67527.
    RefSeqiNP_006247.1. NM_006256.2. [Q16513-1]
    XP_005271088.1. XM_005271031.1. [Q16513-2]
    XP_011540074.1. XM_011541772.1. [Q16513-5]
    UniGeneiHs.440833.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CRSX-ray2.75A646-984[»]
    4RRVX-ray1.41B969-983[»]
    ProteinModelPortaliQ16513.
    SMRiQ16513. Positions 56-107, 136-199, 618-984.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111572. 36 interactions.
    IntActiQ16513. 17 interactions.
    MINTiMINT-198348.
    STRINGi9606.ENSP00000359552.

    Chemistry

    BindingDBiQ16513.
    ChEMBLiCHEMBL3032.
    GuidetoPHARMACOLOGYi1521.

    PTM databases

    PhosphoSiteiQ16513.

    Polymorphism and mutation databases

    BioMutaiPKN2.
    DMDMi6225859.

    Proteomic databases

    MaxQBiQ16513.
    PaxDbiQ16513.
    PRIDEiQ16513.

    Protocols and materials databases

    DNASUi5586.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000370513; ENSP00000359544; ENSG00000065243. [Q16513-3]
    ENST00000370521; ENSP00000359552; ENSG00000065243.
    GeneIDi5586.
    KEGGihsa:5586.
    UCSCiuc001dmn.3. human. [Q16513-1]
    uc009wcv.3. human. [Q16513-3]
    uc010osp.2. human. [Q16513-2]

    Organism-specific databases

    CTDi5586.
    GeneCardsiGC01P089149.
    HGNCiHGNC:9406. PKN2.
    HPAiHPA034861.
    HPA057913.
    MIMi602549. gene.
    neXtProtiNX_Q16513.
    PharmGKBiPA33770.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00770000120523.
    HOGENOMiHOG000233032.
    HOVERGENiHBG108317.
    InParanoidiQ16513.
    KOiK06071.
    OMAiEYSGIQE.
    PhylomeDBiQ16513.
    TreeFamiTF102005.

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_355542. RHO GTPases activate PKNs.
    SignaLinkiQ16513.

    Miscellaneous databases

    ChiTaRSiPKN2. human.
    GeneWikiiPKN2.
    GenomeRNAii5586.
    NextBioi21666.
    PMAP-CutDBQ16513.
    PROiQ16513.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ16513.
    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.
    IPR002290. Ser/Thr_dual-sp_kinase.
    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...

    Publicationsi

    « Hide 'large scale' publications
    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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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.
    29. "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.
    30. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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.
    33. "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.
    34. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952 AND THR-958, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    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: July 22, 2015
    This is version 157 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

    External Data

    Dasty 3

    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 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.