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Protein

Serine/threonine-protein kinase N1

Gene

PKN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

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)DescriptionActionsGraphical viewLength
Binding sitei646ATPPROSITE-ProRule annotation1
Active sitei742Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi623 – 631ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase N1 (EC:2.7.11.13By similarity)
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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003942612 – 944Serine/threonine-protein kinase N1Add BLAST943

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei206PhosphoserineBy similarity1
Modified residuei375PhosphoserineBy similarity1
Modified residuei449N6-acetyllysineBy similarity1
Modified residuei534PhosphoserineBy similarity1
Modified residuei538PhosphoserineBy similarity1
Modified residuei563PhosphoserineBy similarity1
Modified residuei610PhosphoserineBy similarity1
Modified residuei776Phosphothreonine; by PDPK1By similarity1
Modified residuei780PhosphothreonineBy similarity1
Modified residuei916PhosphothreonineBy similarity1
Modified residuei918PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylated; preferably on serine. Phosphorylated during mitosis.By similarity
Activated by limited proteolysis with trypsin.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei109 – 110Cleavage; by caspase-3By similarity2
Sitei455 – 456Cleavage; by caspase-3By similarity2
Sitei559 – 560Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiA1A4I4.
PRIDEiA1A4I4.

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. Interacts (via C-terminus) with PDPK1. Interacts with CCNT2; enhances MYOD1-dependent transcription. 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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022652.

Structurei

3D structure databases

ProteinModelPortaliA1A4I4.
SMRiA1A4I4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati34 – 111REM 1Add BLAST78
Repeati124 – 210REM 2Add BLAST87
Repeati211 – 292REM 3Add BLAST82
Domaini326 – 462C2Add BLAST137
Domaini617 – 876Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini877 – 944AGC-kinase C-terminalAdd BLAST68

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiA1A4I4.
KOiK06071.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiView protein in InterPro
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.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
SMARTiView protein in SMART
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A1A4I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL
60 70 80 90 100
KLKEGAENLR RATTDLGRNL GPVELVLRGS SRRLALLHQQ LQELHAHVVL
110 120 130 140 150
PDPAVGVHDA PQSPGTGDSA CSATNLSRVA GLEKQLAIEL KVKQGAENMI
160 170 180 190 200
QTYSNGSTKD RKLLLTAQQM LQDSKTKIDI IRMQLHRALQ ACQLESQAAP
210 220 230 240 250
DEAQGSPDLG AVELRIEELR HHFRVEHAVA EGAKNVLRLL SAAKAPDRKA
260 270 280 290 300
VSEAQEKLTE SNQKLGLLRE ALERRLGELP ADHPKGRLLR EELAAASSAA
310 320 330 340 350
FSARLAGPFP ATHYSTLSKP APLTGTLEVR VVGCRDLPET IPWNPSPSVG
360 370 380 390 400
GPGTPDSRTP FLSRPARGLY SRTGSLSGRS SLKAEAENTN EVSTVLKLDN
410 420 430 440 450
TVVGQTSWKP CGPNAWDQSF TLELERAREL ELAVFWRDQR GLCALKFLKL
460 470 480 490 500
EDFLDNERHE VQLDMEPQGC LVAEVTFRNP VIERIPRLRR QKKIFSKQQG
510 520 530 540 550
KAFQRARQMN IDVATWVRLL RRLIPNATAT GTFSPGASPG PEARSTGDIS
560 570 580 590 600
VEKLNLGTET DSSPQKSPLG PPSSPSSLSS PIQATTTTPE LPSETQETPG
610 620 630 640 650
PTLCSPLRKS PLTLEDFKFL AVLGRGHFGK VLLSEFRPSG ELFAIKALKK
660 670 680 690 700
GDIVARDEVE SLMCEKRILA AVTNAGHPFL VNLFGCFQTP EHVCFVMEYS
710 720 730 740 750
AGGDLMLHIH SDVFSEPRAV FYSACVVLGL QFLHEHKIVY RDLKLDNLLL
760 770 780 790 800
DTEGYVKIAD FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT DTSYTRAVDW
810 820 830 840 850
WGLGVLLYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL SAEAIGIMRR
860 870 880 890 900
LLRRNPERRL GSSERDAEDV KKQPFFRTLG WDALLARRLP PPFVPTLAGR
910 920 930 940
TDVSNFDEEF TGEAPTLSPP RDARPLTATE QAAFRDFDFV AGSC
Length:944
Mass (Da):104,133
Last modified:January 23, 2007 - v1
Checksum:i11B6833ED4F8D57E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC126539 mRNA. Translation: AAI26540.1.
RefSeqiNP_001073715.1. NM_001080246.1.
UniGeneiBt.4993.

Genome annotation databases

GeneIDi509080.
KEGGibta:509080.

Similar proteinsi

Entry informationi

Entry nameiPKN1_BOVIN
AccessioniPrimary (citable) accession number: A1A4I4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 83 of the entry and version 1 of the sequence. See 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