Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1A4I4

- PKN1_BOVIN

UniProt

A1A4I4 - PKN1_BOVIN

Protein

Serine/threonine-protein kinase N1

Gene

PKN1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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', and GFAP. Able to phosphorylate RPS6 in vitro By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    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-776 (activation loop of the kinase domain) and Ser-918 (turn motif), need to be phosphorylated for its full activation By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei109 – 1102Cleavage; by caspase-3By similarity
    Sitei455 – 4562Cleavage; by caspase-3By similarity
    Sitei559 – 5602Cleavage; by caspase-3By similarity
    Binding sitei646 – 6461ATPPROSITE-ProRule annotation
    Active sitei742 – 7421Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi623 – 6319ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. chromatin binding Source: UniProtKB
    4. GTP-Rho binding Source: UniProtKB
    5. histone binding Source: UniProtKB
    6. histone deacetylase binding Source: UniProtKB
    7. histone kinase activity (H3-T11 specific) Source: UniProtKB
    8. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    9. protein kinase C activity Source: UniProtKB-EC
    10. protein serine/threonine kinase activity Source: UniProtKB
    11. Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    1. epithelial cell migration Source: UniProtKB
    2. histone H3-T11 phosphorylation Source: UniProtKB
    3. hyperosmotic response Source: Ensembl
    4. protein phosphorylation Source: UniProtKB
    5. regulation of cell motility Source: UniProtKB
    6. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. signal transduction Source: InterPro
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase N1 (EC:2.7.11.13)
    Alternative name(s):
    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:PKN, PRK1, PRKCL1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Endosome By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Cleavage furrow By similarity. Midbody By similarity
    Note: Associates with chromatin in a ligand-dependent manner By similarity. Localization to endosomes is mediated via its interaction with RHOB By similarity. 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 similarity.By similarity

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic membrane-bounded vesicle Source: Ensembl
    4. endosome Source: UniProtKB
    5. midbody Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 944943Serine/threonine-protein kinase N1PRO_0000394261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei206 – 2061PhosphoserineBy similarity
    Modified residuei375 – 3751PhosphoserineBy similarity
    Modified residuei449 – 4491N6-acetyllysineBy similarity
    Modified residuei534 – 5341PhosphoserineBy similarity
    Modified residuei538 – 5381PhosphoserineBy similarity
    Modified residuei776 – 7761Phosphothreonine; by PDPK1By similarity
    Modified residuei780 – 7801PhosphothreonineBy similarity
    Modified residuei916 – 9161PhosphothreonineBy similarity
    Modified residuei918 – 9181PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylated; preferably on serine. Phosphorylated during mitosis By similarity.By similarity
    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.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiA1A4I4.

    Interactioni

    Subunit structurei

    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. Interacts with ZFAND6. Interacts (via C-terminus) with PDPK1. In case of infection, interacts with S.typhimurium protein SspH1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000022652.

    Structurei

    3D structure databases

    ProteinModelPortaliA1A4I4.
    SMRiA1A4I4. Positions 13-98, 123-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati34 – 11178REM 1Add
    BLAST
    Repeati124 – 21087REM 2Add
    BLAST
    Repeati211 – 29282REM 3Add
    BLAST
    Domaini326 – 462137C2Add
    BLAST
    Domaini617 – 876260Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini877 – 94468AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni182 – 1865Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitinationBy similarity

    Domaini

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

    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.
    HOGENOMiHOG000233032.
    HOVERGENiHBG108317.
    InParanoidiA1A4I4.
    KOiK06071.

    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_dom.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    A1A4I4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL    50
    KLKEGAENLR RATTDLGRNL GPVELVLRGS SRRLALLHQQ LQELHAHVVL 100
    PDPAVGVHDA PQSPGTGDSA CSATNLSRVA GLEKQLAIEL KVKQGAENMI 150
    QTYSNGSTKD RKLLLTAQQM LQDSKTKIDI IRMQLHRALQ ACQLESQAAP 200
    DEAQGSPDLG AVELRIEELR HHFRVEHAVA EGAKNVLRLL SAAKAPDRKA 250
    VSEAQEKLTE SNQKLGLLRE ALERRLGELP ADHPKGRLLR EELAAASSAA 300
    FSARLAGPFP ATHYSTLSKP APLTGTLEVR VVGCRDLPET IPWNPSPSVG 350
    GPGTPDSRTP FLSRPARGLY SRTGSLSGRS SLKAEAENTN EVSTVLKLDN 400
    TVVGQTSWKP CGPNAWDQSF TLELERAREL ELAVFWRDQR GLCALKFLKL 450
    EDFLDNERHE VQLDMEPQGC LVAEVTFRNP VIERIPRLRR QKKIFSKQQG 500
    KAFQRARQMN IDVATWVRLL RRLIPNATAT GTFSPGASPG PEARSTGDIS 550
    VEKLNLGTET DSSPQKSPLG PPSSPSSLSS PIQATTTTPE LPSETQETPG 600
    PTLCSPLRKS PLTLEDFKFL AVLGRGHFGK VLLSEFRPSG ELFAIKALKK 650
    GDIVARDEVE SLMCEKRILA AVTNAGHPFL VNLFGCFQTP EHVCFVMEYS 700
    AGGDLMLHIH SDVFSEPRAV FYSACVVLGL QFLHEHKIVY RDLKLDNLLL 750
    DTEGYVKIAD FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT DTSYTRAVDW 800
    WGLGVLLYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL SAEAIGIMRR 850
    LLRRNPERRL GSSERDAEDV KKQPFFRTLG WDALLARRLP PPFVPTLAGR 900
    TDVSNFDEEF TGEAPTLSPP RDARPLTATE QAAFRDFDFV AGSC 944
    Length:944
    Mass (Da):104,133
    Last modified:January 23, 2007 - v1
    Checksum:i11B6833ED4F8D57E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC126539 mRNA. Translation: AAI26540.1.
    RefSeqiNP_001073715.1. NM_001080246.1.
    UniGeneiBt.4993.

    Genome annotation databases

    GeneIDi509080.
    KEGGibta:509080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC126539 mRNA. Translation: AAI26540.1 .
    RefSeqi NP_001073715.1. NM_001080246.1.
    UniGenei Bt.4993.

    3D structure databases

    ProteinModelPortali A1A4I4.
    SMRi A1A4I4. Positions 13-98, 123-200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000022652.

    Proteomic databases

    PRIDEi A1A4I4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 509080.
    KEGGi bta:509080.

    Organism-specific databases

    CTDi 5585.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233032.
    HOVERGENi HBG108317.
    InParanoidi A1A4I4.
    KOi K06071.

    Miscellaneous databases

    NextBioi 20868812.

    Family and domain databases

    Gene3Di 1.10.287.160. 3 hits.
    2.60.40.150. 2 hits.
    InterProi IPR000961. 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_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF02185. HR1. 3 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00742. Hr1. 3 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46585. SSF46585. 3 hits.
    SSF49562. SSF49562. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Fetal brain.

    Entry informationi

    Entry nameiPKN1_BOVIN
    AccessioniPrimary (citable) accession number: A1A4I4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3