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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. 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.10 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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei108 – 1092Cleavage; by caspase-3
    Sitei454 – 4552Cleavage; by caspase-3
    Sitei558 – 5592Cleavage; by caspase-3
    Binding sitei644 – 6441ATPPROSITE-ProRule annotation
    Active sitei740 – 7401Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi621 – 6299ATPPROSITE-ProRule annotation

    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
    • 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
    • small GTPase mediated signal transduction Source: Reactome
    • 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

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
    REACT_355542. RHO GTPases activate PKNs.
    SignaLinkiQ16512.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase N1 (EC:2.7.11.13)
    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
    ProteomesiUP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9405. PKN1.

    Subcellular locationi

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi108 – 1081D → A: Abolishes cleavage by caspase-3 and formation of AF1 fragment. 1 Publication
    Mutagenesisi181 – 1811R → A: Abolishes interaction with bacterial SspH1. 1 Publication
    Mutagenesisi181 – 1811R → K: Decreases interaction with bacterial SspH1. 1 Publication
    Mutagenesisi185 – 1851R → A: Abolishes interaction with bacterial SspH1. 1 Publication
    Mutagenesisi451 – 4511D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication
    Mutagenesisi454 – 4541D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication
    Mutagenesisi558 – 5581D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication
    Mutagenesisi560 – 5601D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication
    Mutagenesisi644 – 6441K → E: Abolishes Serine/threonine-protein kinase activity. 2 Publications
    Mutagenesisi644 – 6441K → R: Substantial reduction of autophosphorylation. 2 Publications

    Organism-specific databases

    PharmGKBiPA33769.

    Polymorphism and mutation databases

    BioMutaiPKN1.
    DMDMi259016304.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 942941Serine/threonine-protein kinase N1PRO_0000055719Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei205 – 2051Phosphoserine2 Publications
    Modified residuei374 – 3741PhosphoserineBy similarity
    Modified residuei448 – 4481N6-acetyllysine1 Publication
    Modified residuei533 – 5331Phosphoserine4 Publications
    Modified residuei537 – 5371Phosphoserine4 Publications
    Modified residuei559 – 5591Phosphoserine2 Publications
    Modified residuei562 – 5621Phosphoserine5 Publications
    Modified residuei774 – 7741Phosphothreonine; by PDPK11 Publication
    Modified residuei778 – 7781Phosphothreonine1 Publication
    Modified residuei914 – 9141Phosphothreonine1 Publication
    Modified residuei916 – 9161Phosphoserine3 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16512.
    PaxDbiQ16512.
    PRIDEiQ16512.

    PTM databases

    PhosphoSiteiQ16512.

    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

    BgeeiQ16512.
    CleanExiHS_PKN1.
    ExpressionAtlasiQ16512. baseline and differential.
    GenevisibleiQ16512. HS.

    Organism-specific databases

    HPAiCAB010278.
    HPA003982.

    Interactioni

    Subunit structurei

    Interacts with ZFAND6 (By similarity). Interacts with ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with RAC1. Interacts (via REM 1 repeat) with RHOA. Interacts with RHOB. In case of infection, interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region). Interacts (via C-terminus) with PDPK1.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC85BQ158342EBI-602382,EBI-739674
    CDR2Q018503EBI-602382,EBI-1181367
    CEP57L1Q8IYX8-23EBI-602382,EBI-10181988
    GOLGA2Q083793EBI-602382,EBI-618309
    HOMER3B2RA103EBI-602382,EBI-10175777
    KRT15P190123EBI-602382,EBI-739566
    KRT31Q153233EBI-602382,EBI-948001
    MAPK12P537782EBI-602382,EBI-602406
    MID1O153443EBI-602382,EBI-2340316
    SSX2IPQ9Y2D83EBI-602382,EBI-2212028
    VIMP086703EBI-602382,EBI-353844
    ZAKQ9NYL2-12EBI-602382,EBI-687346

    Protein-protein interaction databases

    BioGridi111571. 56 interactions.
    DIPiDIP-34240N.
    IntActiQ16512. 23 interactions.
    MINTiMINT-118694.
    STRINGi9606.ENSP00000343325.

    Structurei

    Secondary structure

    1
    942
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 184Combined sources
    Helixi29 – 6638Combined sources
    Helixi71 – 9525Combined sources
    Turni122 – 1243Combined sources
    Helixi126 – 15126Combined sources
    Turni157 – 1593Combined sources
    Helixi160 – 18728Combined sources
    Beta strandi194 – 1963Combined sources
    Helixi612 – 6143Combined sources
    Beta strandi615 – 62410Combined sources
    Beta strandi627 – 6348Combined sources
    Turni635 – 6373Combined sources
    Beta strandi640 – 6478Combined sources
    Helixi648 – 6536Combined sources
    Helixi657 – 67115Combined sources
    Turni672 – 6743Combined sources
    Beta strandi681 – 6866Combined sources
    Beta strandi688 – 6969Combined sources
    Beta strandi700 – 7023Combined sources
    Helixi703 – 7064Combined sources
    Turni707 – 7093Combined sources
    Helixi714 – 73320Combined sources
    Helixi743 – 7453Combined sources
    Beta strandi746 – 7483Combined sources
    Beta strandi750 – 7523Combined sources
    Beta strandi754 – 7563Combined sources
    Beta strandi763 – 7653Combined sources
    Helixi779 – 7813Combined sources
    Helixi784 – 7885Combined sources
    Helixi794 – 81017Combined sources
    Helixi820 – 82910Combined sources
    Helixi840 – 84910Combined sources
    Turni854 – 8563Combined sources
    Turni862 – 8643Combined sources
    Helixi865 – 8695Combined sources
    Helixi872 – 8743Combined sources
    Helixi879 – 8835Combined sources
    Helixi906 – 9094Combined sources
    Helixi926 – 9305Combined sources
    Turni931 – 9344Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 13-98, 125-190, 581-940.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16512.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati34 – 11077REM 1Add
    BLAST
    Repeati123 – 20987REM 2Add
    BLAST
    Repeati210 – 29182REM 3Add
    BLAST
    Domaini325 – 461137C2Add
    BLAST
    Domaini615 – 874260Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini875 – 94268AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni181 – 1855Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination

    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

    eggNOGiCOG0515.
    GeneTreeiENSGT00770000120523.
    HOVERGENiHBG108317.
    InParanoidiQ16512.
    KOiK06071.
    OMAiPDPAATH.
    OrthoDBiEOG7X9G6Q.
    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.
    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. 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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911G → D in AAB33345 (PubMed:7851406).Curated
    Sequence conflicti191 – 1911G → D in AAC50209 (PubMed:7851406).Curated
    Sequence conflicti562 – 5621S → P in BAG36611 (PubMed:14702039).Curated
    Sequence conflicti736 – 7361I → T no nucleotide entry (PubMed:7988719).Curated
    Sequence conflicti750 – 7501T → A no nucleotide entry (PubMed:7988719).Curated
    Sequence conflicti800 – 8001G → A no nucleotide entry (PubMed:7988719).Curated
    Sequence conflicti812 – 8121E → G in BAG36611 (PubMed:14702039).Curated
    Sequence conflicti887 – 8871L → P in BAG53845 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti185 – 1851R → C in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_042337
    Natural varianti197 – 1971A → E.1 Publication
    VAR_042338
    Natural varianti436 – 4361R → W.1 Publication
    Corresponds to variant rs35132656 [ dbSNP | Ensembl ].
    VAR_042339
    Natural varianti520 – 5201R → Q.1 Publication
    Corresponds to variant rs56273055 [ dbSNP | Ensembl ].
    VAR_042340
    Natural varianti555 – 5551L → I.2 Publications
    Corresponds to variant rs34309238 [ dbSNP | Ensembl ].
    VAR_042341
    Natural varianti635 – 6351R → Q.1 Publication
    Corresponds to variant rs35416389 [ dbSNP | Ensembl ].
    VAR_042342
    Natural varianti718 – 7181I → V.2 Publications
    Corresponds to variant rs2230539 [ dbSNP | Ensembl ].
    VAR_042343
    Natural varianti873 – 8731F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_042344
    Natural varianti901 – 9011V → I.3 Publications
    Corresponds to variant rs10846 [ dbSNP | Ensembl ].
    VAR_014937
    Natural varianti921 – 9211A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042345

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 77MASDAVQ → MAEANNPSEQELE in isoform 2. 1 PublicationVSP_038143
    Alternative sequencei603 – 6031S → R in isoform 3. 1 PublicationVSP_039213
    Alternative sequencei604 – 942339Missing in isoform 3. 1 PublicationVSP_039214Add
    BLAST

    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.
    ENST00000342216; ENSP00000343325; ENSG00000123143. [Q16512-2]
    GeneIDi5585.
    KEGGihsa:5585.
    UCSCiuc002myp.3. human. [Q16512-1]
    uc002myq.3. human. [Q16512-2]

    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
    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. Positions 13-98, 125-190, 581-940.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111571. 56 interactions.
    DIPiDIP-34240N.
    IntActiQ16512. 23 interactions.
    MINTiMINT-118694.
    STRINGi9606.ENSP00000343325.

    Chemistry

    BindingDBiQ16512.
    ChEMBLiCHEMBL3384.
    GuidetoPHARMACOLOGYi1520.

    PTM databases

    PhosphoSiteiQ16512.

    Polymorphism and mutation databases

    BioMutaiPKN1.
    DMDMi259016304.

    Proteomic databases

    MaxQBiQ16512.
    PaxDbiQ16512.
    PRIDEiQ16512.

    Protocols and materials databases

    DNASUi5585.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000242783; ENSP00000242783; ENSG00000123143.
    ENST00000342216; ENSP00000343325; ENSG00000123143. [Q16512-2]
    GeneIDi5585.
    KEGGihsa:5585.
    UCSCiuc002myp.3. human. [Q16512-1]
    uc002myq.3. human. [Q16512-2]

    Organism-specific databases

    CTDi5585.
    GeneCardsiGC19P014544.
    H-InvDBHIX0027472.
    HGNCiHGNC:9405. PKN1.
    HPAiCAB010278.
    HPA003982.
    MIMi601032. gene.
    neXtProtiNX_Q16512.
    PharmGKBiPA33769.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00770000120523.
    HOVERGENiHBG108317.
    InParanoidiQ16512.
    KOiK06071.
    OMAiPDPAATH.
    OrthoDBiEOG7X9G6Q.
    PhylomeDBiQ16512.
    TreeFamiTF102005.

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
    REACT_355542. RHO GTPases activate PKNs.
    SignaLinkiQ16512.

    Miscellaneous databases

    ChiTaRSiPKN1. human.
    EvolutionaryTraceiQ16512.
    GeneWikiiProtein_kinase_N1.
    GenomeRNAii5585.
    NextBioi21660.
    PMAP-CutDBQ16512.
    PROiQ16512.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ16512.
    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.
    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. 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...

    Publicationsi

    « Hide 'large scale' publications
    1. "A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C."
      Mukai H., Ono Y.
      Biochem. Biophys. Res. Commun. 199:897-904(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-644.
      Tissue: Hippocampus.
    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: Fetal brain.
    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 1 AND 2), VARIANTS ILE-555 AND ILE-901.
      Tissue: Kidney, Synovium and Thymus.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 3), VARIANT ILE-901.
      Tissue: Brain and Placenta.
    6. "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] OF 700-800 (ISOFORMS 1/2), VARIANT VAL-718.
    7. "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163."
      Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T., Parker P.J.
      FEBS Lett. 378:281-285(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MARCKS.
    8. "PKN associates and phosphorylates the head-rod domain of neurofilament protein."
      Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M., Miyahara M., Sunakawa H., Ono Y.
      J. Biol. Chem. 271:9816-9822(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEFH; NEFL AND NEFM.
    9. "Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho."
      Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N., Mukai H., Ono Y., Kakizuka A., Narumiya S.
      Science 271:645-648(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH RHOA.
    10. "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN."
      Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.
      Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GFAP AND VIM.
    11. "PRK1 is targeted to endosomes by the small GTPase, RhoB."
      Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.
      J. Biol. Chem. 273:4811-4814(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHOB.
    12. "Proteolytic activation of PKN by caspase-3 or related protease during apoptosis."
      Takahashi M., Mukai H., Toshimori M., Miyamoto M., Ono Y.
      Proc. Natl. Acad. Sci. U.S.A. 95:11566-11571(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-108; ASP-451; ASP-454; ASP-558 AND ASP-560.
    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-774 BY PDPK1, INTERACTION WITH PDPK1.
    14. Cited for: FUNCTION, INTERACTION WITH MAPT.
    15. "A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer."
      Metzger E., Muller J.M., Ferrari S., Buettner R., Schule R.
      EMBO J. 22:270-280(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ANDR.
    16. "A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1."
      Haraga A., Miller S.I.
      Cell. Microbiol. 8:837-846(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH S.TYPHIMURIUM SSPH1.
    17. "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-533 AND SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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.
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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 SER-205 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation."
      Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R.
      Nat. Cell Biol. 10:53-60(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-644.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559; SER-562 AND SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537; SER-559; SER-562; THR-914 AND SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH HDAC5; HDAC7 AND HDAC9.
    27. Cited for: INTERACTION WITH PRKCB.
    28. "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-533; SER-537 AND SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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.
    31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    33. "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-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    34. "The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1."
      Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K., Hakoshima T.
      Mol. Cell 4:793-803(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98 IN COMPLEX WITH RHOA.
    35. "Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
      Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
      J. Struct. Biol. 126:166-170(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
    36. "Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)."
      Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y., Parker P.J., Blundell T.L., Mott H.R.
      J. Biol. Chem. 278:50578-50587(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 116-199 IN COMPLEX WITH RAC1.
    37. "The Rac1 polybasic region is required for interaction with its effector PRK1."
      Modha R., Campbell L.J., Nietlispach D., Buhecha H.R., Owen D., Mott H.R.
      J. Biol. Chem. 283:1492-1500(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 122-199 IN COMPLEX WITH RAC1.
    38. "Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase."
      Keszei A.F., Tang X., McCormick C., Zeqiraj E., Rohde J.R., Tyers M., Sicheri F.
      Mol. Cell. Biol. 34:362-373(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 122-199 IN COMPLEX WITH SALMONELLA SSPH1, UBIQUITINATION, MUTAGENESIS OF ARG-181 AND ARG-185, FUNCTION AS ANDROGEN RECEPTOR COACTIVATOR.
    39. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-185; GLU-197; TRP-436; GLN-520; ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.

    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: July 22, 2015
    This is version 177 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

    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.