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Protein

Serine/threonine-protein kinase N1

Gene

PKN1

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 involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Kinase activity is activated upon binding to Rho proteins (RHOA, RHOB and RAC1). Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids. Activated by caspase-3 (CASP3) cleavage during apoptosis. Two specific sites, Thr-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation.2 Publications

Kineticsi

  1. KM=20.6 µM for HDAC51 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei644ATPPROSITE-ProRule annotation1
    Active sitei740Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi621 – 629ATPPROSITE-ProRule annotation9

    GO - Molecular functioni

    • androgen receptor binding Source: UniProtKB
    • ATP binding Source: UniProtKB-KW
    • chromatin binding Source: UniProtKB
    • GTP-Rho binding Source: UniProtKB
    • histone binding Source: UniProtKB
    • histone deacetylase binding Source: UniProtKB
    • histone kinase activity (H3-T11 specific) Source: UniProtKB
    • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    • protein kinase activity Source: ProtInc
    • protein kinase C activity Source: UniProtKB-EC
    • protein kinase C binding Source: UniProtKB
    • protein serine/threonine kinase activity Source: UniProtKB
    • Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    • activation of JUN kinase activity Source: ProtInc
    • B cell apoptotic process Source: Ensembl
    • B cell homeostasis Source: Ensembl
    • epithelial cell migration Source: UniProtKB
    • histone H3-T11 phosphorylation Source: UniProtKB
    • hyperosmotic response Source: Ensembl
    • negative regulation of B cell proliferation Source: Ensembl
    • negative regulation of protein kinase activity Source: Ensembl
    • peptidyl-serine phosphorylation Source: GO_Central
    • protein phosphorylation Source: UniProtKB
    • regulation of cell motility Source: UniProtKB
    • regulation of germinal center formation Source: Ensembl
    • regulation of immunoglobulin production Source: Ensembl
    • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    • renal system process Source: Ensembl
    • signal transduction Source: ProtInc
    • spleen development Source: Ensembl
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciZFISH:HS04634-MONOMER.
    BRENDAi2.7.11.13. 2681.
    ReactomeiR-HSA-5625740. RHO GTPases activate PKNs.
    R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
    SignaLinkiQ16512.
    SIGNORiQ16512.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase N1 (EC:2.7.11.131 Publication)
    Alternative name(s):
    Protease-activated kinase 1
    Short name:
    PAK-1
    Protein kinase C-like 1
    Protein kinase C-like PKN
    Protein kinase PKN-alpha
    Protein-kinase C-related kinase 1
    Serine-threonine protein kinase N
    Gene namesi
    Name:PKN1
    Synonyms:PAK1, PKN, PRK1, PRKCL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9405. PKN1.

    Subcellular locationi

    • Cytoplasm 2 Publications
    • Nucleus 1 Publication
    • Endosome 1 Publication
    • Cell membrane By similarity; Peripheral membrane protein By similarity
    • Cleavage furrow 1 Publication
    • Midbody 1 Publication

    • Note: Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis.By similarity1 Publication

    GO - Cellular componenti

    • cleavage furrow Source: UniProtKB
    • cytoplasm Source: UniProtKB
    • cytoplasmic, membrane-bounded vesicle Source: Ensembl
    • cytosol Source: Reactome
    • endosome Source: UniProtKB
    • midbody Source: UniProtKB
    • nucleoplasm Source: Reactome
    • nucleus Source: UniProtKB
    • plasma membrane Source: UniProtKB-SubCell
    • protein complex Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi108D → A: Abolishes cleavage by caspase-3 and formation of AF1 fragment. 1 Publication1
    Mutagenesisi181R → A: Abolishes interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi181R → K: Decreases interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi185R → A: Abolishes interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi451D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication1
    Mutagenesisi454D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication1
    Mutagenesisi558D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication1
    Mutagenesisi560D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication1
    Mutagenesisi644K → E: Abolishes Serine/threonine-protein kinase activity. 2 Publications1
    Mutagenesisi644K → R: Substantial reduction of autophosphorylation. 2 Publications1

    Organism-specific databases

    DisGeNETi5585.
    OpenTargetsiENSG00000123143.
    PharmGKBiPA33769.

    Chemistry databases

    ChEMBLiCHEMBL3384.
    GuidetoPHARMACOLOGYi1520.

    Polymorphism and mutation databases

    BioMutaiPKN1.
    DMDMi259016304.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000557192 – 942Serine/threonine-protein kinase N1Add BLAST941

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei69PhosphoserineCombined sources1
    Modified residuei205PhosphoserineCombined sources1
    Modified residuei374PhosphoserineBy similarity1
    Modified residuei448N6-acetyllysineCombined sources1
    Modified residuei533PhosphoserineCombined sources1
    Modified residuei537PhosphoserineCombined sources1
    Modified residuei540PhosphoserineCombined sources1
    Modified residuei559PhosphoserineCombined sources1
    Modified residuei562PhosphoserineCombined sources1
    Modified residuei608PhosphoserineCombined sources1
    Modified residuei774Phosphothreonine; by PDPK11 Publication1
    Modified residuei778PhosphothreonineCombined sources1
    Modified residuei914PhosphothreonineCombined sources1
    Modified residuei916PhosphoserineCombined sources1

    Post-translational modificationi

    Autophosphorylated; preferably on serine. Phosphorylated during mitosis.2 Publications
    Activated by limited proteolysis with trypsin.By similarity
    (Microbial infection) In case of infection, polyubiquitinated by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its proteasomal degradation.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei108 – 109Cleavage; by caspase-32
    Sitei454 – 455Cleavage; by caspase-32
    Sitei558 – 559Cleavage; by caspase-32

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiQ16512.
    MaxQBiQ16512.
    PaxDbiQ16512.
    PeptideAtlasiQ16512.
    PRIDEiQ16512.

    PTM databases

    iPTMnetiQ16512.
    PhosphoSitePlusiQ16512.

    Miscellaneous databases

    PMAP-CutDBQ16512.

    Expressioni

    Tissue specificityi

    Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells.1 Publication

    Gene expression databases

    BgeeiENSG00000123143.
    CleanExiHS_PKN1.
    ExpressionAtlasiQ16512. baseline and differential.
    GenevisibleiQ16512. HS.

    Organism-specific databases

    HPAiCAB010278.
    HPA003982.

    Interactioni

    Subunit structurei

    Interacts with ZFAND6 (By similarity). Interacts with ANDR (PubMed:12514133). Interacts with PRKCB (PubMed:20228790). Interacts (via REM 1 and REM 2 repeats) with RAC1 (PubMed:14514689, PubMed:18006505). Interacts (via REM 1 repeat) with RHOA (PubMed:10619026, PubMed:8571126). Interacts with RHOB (PubMed:9478917). Interacts (via C-terminus) with PDPK1 (PubMed:10792047). Interacts with CCNT2; enhances MYOD1-dependent transcription (PubMed:16331689). Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (PubMed:21224381).By similarity10 Publications
    (Microbial infection) Interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region) (PubMed:16611232, PubMed:24248594).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC85BQ158342EBI-602382,EBI-739674
    CDR2Q018505EBI-602382,EBI-1181367
    CEP57L1Q8IYX8-23EBI-602382,EBI-10181988
    GOLGA2Q083793EBI-602382,EBI-618309
    HOMER3B2RA103EBI-602382,EBI-10175777
    HOMER3Q9NSC53EBI-602382,EBI-748420
    KRT15P190123EBI-602382,EBI-739566
    KRT31Q153235EBI-602382,EBI-948001
    MAPK12P537782EBI-602382,EBI-602406
    MID1O153443EBI-602382,EBI-2340316
    SSX2IPQ9Y2D83EBI-602382,EBI-2212028
    VIMP086703EBI-602382,EBI-353844
    ZAKQ9NYL2-12EBI-602382,EBI-687346

    GO - Molecular functioni

    • androgen receptor binding Source: UniProtKB
    • GTP-Rho binding Source: UniProtKB
    • histone binding Source: UniProtKB
    • histone deacetylase binding Source: UniProtKB
    • protein kinase C binding Source: UniProtKB
    • Rac GTPase binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi111571. 62 interactors.
    DIPiDIP-34240N.
    IntActiQ16512. 56 interactors.
    MINTiMINT-118694.
    STRINGi9606.ENSP00000343325.

    Chemistry databases

    BindingDBiQ16512.

    Structurei

    Secondary structure

    1942
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi15 – 18Combined sources4
    Helixi29 – 66Combined sources38
    Helixi71 – 95Combined sources25
    Turni122 – 124Combined sources3
    Helixi126 – 151Combined sources26
    Turni157 – 159Combined sources3
    Helixi160 – 187Combined sources28
    Beta strandi194 – 196Combined sources3
    Helixi612 – 614Combined sources3
    Beta strandi615 – 624Combined sources10
    Beta strandi627 – 634Combined sources8
    Turni635 – 637Combined sources3
    Beta strandi640 – 647Combined sources8
    Helixi648 – 653Combined sources6
    Helixi657 – 671Combined sources15
    Turni672 – 674Combined sources3
    Beta strandi681 – 686Combined sources6
    Beta strandi688 – 696Combined sources9
    Beta strandi700 – 702Combined sources3
    Helixi703 – 706Combined sources4
    Turni707 – 709Combined sources3
    Helixi714 – 733Combined sources20
    Helixi743 – 745Combined sources3
    Beta strandi746 – 748Combined sources3
    Beta strandi750 – 752Combined sources3
    Beta strandi754 – 756Combined sources3
    Beta strandi763 – 765Combined sources3
    Helixi779 – 781Combined sources3
    Helixi784 – 788Combined sources5
    Helixi794 – 810Combined sources17
    Helixi820 – 829Combined sources10
    Helixi840 – 849Combined sources10
    Turni854 – 856Combined sources3
    Turni862 – 864Combined sources3
    Helixi865 – 869Combined sources5
    Helixi872 – 874Combined sources3
    Helixi879 – 883Combined sources5
    Helixi906 – 909Combined sources4
    Helixi926 – 930Combined sources5
    Turni931 – 934Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CXZX-ray2.20B13-98[»]
    1URFNMR-A122-199[»]
    2RMKNMR-B122-199[»]
    4NKGX-ray2.90B/D122-199[»]
    4OTDX-ray2.00A605-942[»]
    4OTGX-ray2.60A605-942[»]
    4OTHX-ray1.80A605-942[»]
    4OTIX-ray1.93A605-942[»]
    ProteinModelPortaliQ16512.
    SMRiQ16512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16512.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Repeati34 – 110REM 1Add BLAST77
    Repeati123 – 209REM 2Add BLAST87
    Repeati210 – 291REM 3Add BLAST82
    Domaini325 – 461C2Add BLAST137
    Domaini615 – 874Protein kinasePROSITE-ProRule annotationAdd BLAST260
    Domaini875 – 942AGC-kinase C-terminalAdd BLAST68

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni181 – 185Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination1 Publication5

    Domaini

    The C1 domain does not bind the diacylglycerol (DAG).

    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.
    HOVERGENiHBG108317.
    InParanoidiQ16512.
    KOiK06071.
    OMAiEFRSSGE.
    OrthoDBiEOG091G00YT.
    PhylomeDBiQ16512.
    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]
    SMARTiSM00742. Hr1. 3 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF46585. SSF46585. 3 hits.
    SSF49562. SSF49562. 2 hits.
    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 (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q16512-1) [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
    MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL
    60 70 80 90 100
    KLKEGAENLR RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL
    110 120 130 140 150
    PDPAATHDGP QSPGAGGPTC SATNLSRVAG LEKQLAIELK VKQGAENMIQ
    160 170 180 190 200
    TYSNGSTKDR KLLLTAQQML QDSKTKIDII RMQLRRALQA GQLENQAAPD
    210 220 230 240 250
    DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS AAKAPDRKAV
    260 270 280 290 300
    SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF
    310 320 330 340 350
    STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG
    360 370 380 390 400
    PGTPDSRPPF LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT
    410 420 430 440 450
    VVGQTSWKPC GPNAWDQSFT LELERARELE LAVFWRDQRG LCALKFLKLE
    460 470 480 490 500
    DFLDNERHEV QLDMEPQGCL VAEVTFRNPV IERIPRLRRQ KKIFSKQQGK
    510 520 530 540 550
    AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS EARTTGDISV
    560 570 580 590 600
    EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA
    610 620 630 640 650
    LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD
    660 670 680 690 700
    IVARDEVESL MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG
    710 720 730 740 750
    GDLMLHIHSD VFSEPRAIFY SACVVLGLQF LHEHKIVYRD LKLDNLLLDT
    760 770 780 790 800
    EGYVKIADFG LCKEGMGYGD RTSTFCGTPE FLAPEVLTDT SYTRAVDWWG
    810 820 830 840 850
    LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA EAIGIMRRLL
    860 870 880 890 900
    RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD
    910 920 930 940
    VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC
    Length:942
    Mass (Da):103,932
    Last modified:September 22, 2009 - v2
    Checksum:i61360295EC70BB8E
    GO
    Isoform 2 (identifier: Q16512-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: MASDAVQ → MAEANNPSEQELE

    Note: No experimental confirmation available.
    Show »
    Length:948
    Mass (Da):104,673
    Checksum:i882D58AABCFDCEE1
    GO
    Isoform 3 (identifier: Q16512-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         603-603: S → R
         604-942: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:603
    Mass (Da):66,060
    Checksum:i9CC7C140CE6C5547
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti191G → D in AAB33345 (PubMed:7851406).Curated1
    Sequence conflicti191G → D in AAC50209 (PubMed:7851406).Curated1
    Sequence conflicti562S → P in BAG36611 (PubMed:14702039).Curated1
    Sequence conflicti736I → T no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti750T → A no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti800G → A no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti812E → G in BAG36611 (PubMed:14702039).Curated1
    Sequence conflicti887L → P in BAG53845 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_042337185R → C in a metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant rs267605306dbSNPEnsembl.1
    Natural variantiVAR_042338197A → E.1 Publication1
    Natural variantiVAR_042339436R → W.1 PublicationCorresponds to variant rs35132656dbSNPEnsembl.1
    Natural variantiVAR_042340520R → Q.1 PublicationCorresponds to variant rs56273055dbSNPEnsembl.1
    Natural variantiVAR_042341555L → I.2 PublicationsCorresponds to variant rs34309238dbSNPEnsembl.1
    Natural variantiVAR_042342635R → Q.1 PublicationCorresponds to variant rs35416389dbSNPEnsembl.1
    Natural variantiVAR_042343718I → V.2 PublicationsCorresponds to variant rs2230539dbSNPEnsembl.1
    Natural variantiVAR_042344873F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1
    Natural variantiVAR_014937901V → I.3 PublicationsCorresponds to variant rs10846dbSNPEnsembl.1
    Natural variantiVAR_042345921A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0381431 – 7MASDAVQ → MAEANNPSEQELE in isoform 2. 1 Publication7
    Alternative sequenceiVSP_039213603S → R in isoform 3. 1 Publication1
    Alternative sequenceiVSP_039214604 – 942Missing in isoform 3. 1 PublicationAdd BLAST339

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D26181 mRNA. Translation: BAA05169.1.
    S75546 mRNA. Translation: AAB33345.1.
    U33053 mRNA. Translation: AAC50209.1.
    AK123007 mRNA. Translation: BAG53845.1.
    AK292130 mRNA. Translation: BAF84819.1.
    AK313886 mRNA. Translation: BAG36611.1.
    AC008569 Genomic DNA. No translation available.
    BC040061 mRNA. Translation: AAH40061.1.
    BC094766 mRNA. Translation: AAH94766.1.
    CCDSiCCDS42513.1. [Q16512-1]
    CCDS42514.1. [Q16512-2]
    PIRiJC2129.
    S51162.
    RefSeqiNP_002732.3. NM_002741.3. [Q16512-1]
    NP_998725.1. NM_213560.1. [Q16512-2]
    UniGeneiHs.466044.

    Genome annotation databases

    EnsembliENST00000242783; ENSP00000242783; ENSG00000123143. [Q16512-1]
    ENST00000342216; ENSP00000343325; ENSG00000123143. [Q16512-2]
    GeneIDi5585.
    KEGGihsa:5585.
    UCSCiuc002myp.4. human. [Q16512-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D26181 mRNA. Translation: BAA05169.1.
    S75546 mRNA. Translation: AAB33345.1.
    U33053 mRNA. Translation: AAC50209.1.
    AK123007 mRNA. Translation: BAG53845.1.
    AK292130 mRNA. Translation: BAF84819.1.
    AK313886 mRNA. Translation: BAG36611.1.
    AC008569 Genomic DNA. No translation available.
    BC040061 mRNA. Translation: AAH40061.1.
    BC094766 mRNA. Translation: AAH94766.1.
    CCDSiCCDS42513.1. [Q16512-1]
    CCDS42514.1. [Q16512-2]
    PIRiJC2129.
    S51162.
    RefSeqiNP_002732.3. NM_002741.3. [Q16512-1]
    NP_998725.1. NM_213560.1. [Q16512-2]
    UniGeneiHs.466044.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CXZX-ray2.20B13-98[»]
    1URFNMR-A122-199[»]
    2RMKNMR-B122-199[»]
    4NKGX-ray2.90B/D122-199[»]
    4OTDX-ray2.00A605-942[»]
    4OTGX-ray2.60A605-942[»]
    4OTHX-ray1.80A605-942[»]
    4OTIX-ray1.93A605-942[»]
    ProteinModelPortaliQ16512.
    SMRiQ16512.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111571. 62 interactors.
    DIPiDIP-34240N.
    IntActiQ16512. 56 interactors.
    MINTiMINT-118694.
    STRINGi9606.ENSP00000343325.

    Chemistry databases

    BindingDBiQ16512.
    ChEMBLiCHEMBL3384.
    GuidetoPHARMACOLOGYi1520.

    PTM databases

    iPTMnetiQ16512.
    PhosphoSitePlusiQ16512.

    Polymorphism and mutation databases

    BioMutaiPKN1.
    DMDMi259016304.

    Proteomic databases

    EPDiQ16512.
    MaxQBiQ16512.
    PaxDbiQ16512.
    PeptideAtlasiQ16512.
    PRIDEiQ16512.

    Protocols and materials databases

    DNASUi5585.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000242783; ENSP00000242783; ENSG00000123143. [Q16512-1]
    ENST00000342216; ENSP00000343325; ENSG00000123143. [Q16512-2]
    GeneIDi5585.
    KEGGihsa:5585.
    UCSCiuc002myp.4. human. [Q16512-1]

    Organism-specific databases

    CTDi5585.
    DisGeNETi5585.
    GeneCardsiPKN1.
    H-InvDBHIX0027472.
    HGNCiHGNC:9405. PKN1.
    HPAiCAB010278.
    HPA003982.
    MIMi601032. gene.
    neXtProtiNX_Q16512.
    OpenTargetsiENSG00000123143.
    PharmGKBiPA33769.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0694. Eukaryota.
    ENOG410XNPH. LUCA.
    GeneTreeiENSGT00820000126964.
    HOVERGENiHBG108317.
    InParanoidiQ16512.
    KOiK06071.
    OMAiEFRSSGE.
    OrthoDBiEOG091G00YT.
    PhylomeDBiQ16512.
    TreeFamiTF102005.

    Enzyme and pathway databases

    BioCyciZFISH:HS04634-MONOMER.
    BRENDAi2.7.11.13. 2681.
    ReactomeiR-HSA-5625740. RHO GTPases activate PKNs.
    R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
    SignaLinkiQ16512.
    SIGNORiQ16512.

    Miscellaneous databases

    ChiTaRSiPKN1. human.
    EvolutionaryTraceiQ16512.
    GeneWikiiProtein_kinase_N1.
    GenomeRNAii5585.
    PMAP-CutDBQ16512.
    PROiQ16512.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000123143.
    CleanExiHS_PKN1.
    ExpressionAtlasiQ16512. baseline and differential.
    GenevisibleiQ16512. 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]
    SMARTiSM00742. Hr1. 3 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF46585. SSF46585. 3 hits.
    SSF49562. SSF49562. 2 hits.
    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 nameiPKN1_HUMAN
    AccessioniPrimary (citable) accession number: Q16512
    Secondary accession number(s): A8K7W5
    , B2R9R4, B3KVN3, Q15143, Q504U4, Q8IUV5, Q9UD44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 22, 2009
    Last modified: November 30, 2016
    This is version 192 of the entry and version 2 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 19
      Human chromosome 19: 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.