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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. 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

GO - Biological processi

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

ReactomeiREACT_358115. RHO GTPases activate PKNs.
REACT_362231. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

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 Componenti: 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

Complete GO annotation...

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 residuei563 – 5631PhosphoserineBy 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.

Expressioni

Gene expression databases

ExpressionAtlasiA1A4I4. baseline.

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.
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

        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.

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022652.

Proteomic databases

PRIDEiA1A4I4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi509080.
KEGGibta:509080.

Organism-specific databases

CTDi5585.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiA1A4I4.
KOiK06071.

Enzyme and pathway databases

ReactomeiREACT_358115. RHO GTPases activate PKNs.
REACT_362231. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Miscellaneous databases

NextBioi20868812.

Gene expression databases

ExpressionAtlasiA1A4I4. baseline.

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

  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: July 22, 2015
This is version 68 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

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.