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Protein

Serine/threonine-protein kinase N1

Gene

Pkn1

Organism
Rattus norvegicus (Rat)
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 (PubMed:8051089, PubMed:15375078). Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14 (By similarity). 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).By similarity2 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-778 (activation loop of the kinase domain) and Ser-920 (turn motif), need to be phosphorylated for its full activation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei648 – 6481ATPPROSITE-ProRule annotation
Active sitei744 – 7441Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi625 – 6339ATPPROSITE-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

BRENDAi2.7.11.13. 5301.
ReactomeiR-RNO-5625740. RHO GTPases activate PKNs.
R-RNO-5625886. 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:2.7.11.131 Publication)
Alternative name(s):
Protease-activated kinase 1
Short name:
PAK-1
Protein kinase C-like 1
Protein kinase C-like PKN
Protein-kinase C-related kinase 1
Serine-threonine protein kinase N
Gene namesi
Name:Pkn1
Synonyms:Pkn, Prk1, Prkcl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi69308. Pkn1.

Subcellular locationi

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 methionineiRemovedBy similarity
Chaini2 – 946945Serine/threonine-protein kinase N1PRO_0000055721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei69 – 691PhosphoserineBy similarity
Modified residuei377 – 3771Phosphoserine1 Publication
Modified residuei451 – 4511N6-acetyllysineBy similarity
Modified residuei536 – 5361PhosphoserineBy similarity
Modified residuei540 – 5401PhosphoserineBy similarity
Modified residuei543 – 5431PhosphoserineBy similarity
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei612 – 6121PhosphoserineBy similarity
Modified residuei778 – 7781Phosphothreonine; by PDPK1By similarity
Modified residuei782 – 7821PhosphothreonineBy similarity
Modified residuei918 – 9181PhosphothreonineBy similarity
Modified residuei920 – 9201PhosphoserineCombined sources

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei108 – 1092Cleavage; by caspase-3By similarity
Sitei457 – 4582Cleavage; by caspase-3By similarity
Sitei561 – 5622Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63433.
PRIDEiQ63433.

PTM databases

iPTMnetiQ63433.
PhosphoSiteiQ63433.

Expressioni

Gene expression databases

GenevisibleiQ63433. RN.

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

BioGridi248010. 1 interaction.
DIPiDIP-60097N.
STRINGi10116.ENSRNOP00000005770.

Structurei

3D structure databases

ProteinModelPortaliQ63433.
SMRiQ63433. Positions 13-98, 122-202, 616-894.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 11077REM 1Add
BLAST
Repeati123 – 21290REM 2Add
BLAST
Repeati213 – 29482REM 3Add
BLAST
Domaini328 – 464137C2Add
BLAST
Domaini619 – 878260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini879 – 94668AGC-kinase C-terminalAdd
BLAST

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

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ63433.
KOiK06071.
OMAiEFRSSGE.
OrthoDBiEOG7X9G6Q.

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]

Sequencei

Sequence statusi: Complete.

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

Q63433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL
60 70 80 90 100
KLKEGAENLR RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL
110 120 130 140 150
PDPTAGSDAP QSLAEGSPVC SSTNLSRVAG LEKQLAIELK VKQGAENMIQ
160 170 180 190 200
TYSNGSTKDR KLLLTAQQML QDSKTKIDII RMQLRRALQA LQAGQLESQA
210 220 230 240 250
APDEAHGDPD LGAVELRIEE LRHHFRVEHA VAEGAKNVLR LLSAAKAPDR
260 270 280 290 300
KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS
310 320 330 340 350
AAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS
360 370 380 390 400
VGASGTPDSR TPFLSRPARG LYNRSGSLSG RSSLKGEAEN STEVSTVLKL
410 420 430 440 450
DNTVVGQTAW KPCGPNAWDQ SFTLELERAR ELELAVFWRD QRGLCALKFL
460 470 480 490 500
KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR NPIIERIPRL QRQKKIFSKQ
510 520 530 540 550
QGQTFQRARQ MNIDVATWVR LLRRLIPNAV ATGSFSPNAS PGSEIRSTGD
560 570 580 590 600
ISMEKLNLGA DSDSSSQKSP AGLPSTSCSL SSPTHESTTS PELPSETQET
610 620 630 640 650
PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFHS SGELFAIKAL
660 670 680 690 700
KKGDIVARDE VESLMCEKRI LATVTRAGHP FLVNLFGCFQ TPEHVCFVME
710 720 730 740 750
YSAGGDLMLH IHSDVFSEPR AVFYSACVVL GLQFLHEHKI VYRDLKLDNL
760 770 780 790 800
LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC GTPEFLAPEV LTDTSYTRAV
810 820 830 840 850
DWWGLGVLLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR FLSAEAIGIM
860 870 880 890 900
RRLLRRNPER RLGSTERDAE DVKKQPFFRT LDWDALLARR LPPPFVPTLS
910 920 930 940
GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY
Length:946
Mass (Da):104,468
Last modified:May 18, 2010 - v2
Checksum:i63DF250C8D2DA444
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti298 – 2981A → R in AAL31374 (PubMed:8943281).Curated
Sequence conflicti510 – 5101Q → H in BAA05168 (PubMed:8135837).Curated
Sequence conflicti650 – 6501L → V in AAL31374 (PubMed:8943281).Curated
Sequence conflicti722 – 7221V → G in BAA05168 (PubMed:8135837).Curated
Sequence conflicti808 – 8081L → F in BAA05168 (PubMed:8135837).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26180 mRNA. Translation: BAA05168.1.
L35634 mRNA. Translation: AAL31374.1.
BC061836 mRNA. Translation: AAH61836.1.
PIRiJC2130.
RefSeqiNP_058871.2. NM_017175.2.
UniGeneiRn.49880.

Genome annotation databases

EnsembliENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131.
GeneIDi29355.
KEGGirno:29355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26180 mRNA. Translation: BAA05168.1.
L35634 mRNA. Translation: AAL31374.1.
BC061836 mRNA. Translation: AAH61836.1.
PIRiJC2130.
RefSeqiNP_058871.2. NM_017175.2.
UniGeneiRn.49880.

3D structure databases

ProteinModelPortaliQ63433.
SMRiQ63433. Positions 13-98, 122-202, 616-894.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248010. 1 interaction.
DIPiDIP-60097N.
STRINGi10116.ENSRNOP00000005770.

PTM databases

iPTMnetiQ63433.
PhosphoSiteiQ63433.

Proteomic databases

PaxDbiQ63433.
PRIDEiQ63433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131.
GeneIDi29355.
KEGGirno:29355.

Organism-specific databases

CTDi5585.
RGDi69308. Pkn1.

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ63433.
KOiK06071.
OMAiEFRSSGE.
OrthoDBiEOG7X9G6Q.

Enzyme and pathway databases

BRENDAi2.7.11.13. 5301.
ReactomeiR-RNO-5625740. RHO GTPases activate PKNs.
R-RNO-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Miscellaneous databases

PROiQ63433.

Gene expression databases

GenevisibleiQ63433. RN.

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...

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].
    Tissue: Lung.
  2. "Phosphorylation events associated with different states of activation of a hepatic cardiolipin/protease-activated protein kinase. Structural identity to the protein kinase N-type protein kinases."
    Peng B., Morrice N.A., Groenen L.C., Wettenhall R.E.
    J. Biol. Chem. 271:32233-32240(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "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].
    Tissue: Prostate.
  4. "A cardiolipin-activated protein kinase from rat liver structurally distinct from the protein kinases C."
    Morrice N.A., Gabrielli B., Kemp B.E., Wettenhall R.E.
    J. Biol. Chem. 269:20040-20046(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 633-648; 747-767; 776-822; 880-889 AND 938-946, FUNCTION, CATALYTIC ACTIVITY.
    Tissue: Liver.
  5. "Signaling via a novel integral plasma membrane pool of a serine/threonine protein kinase PRK1 in mammalian cells."
    Zhu Y., Stolz D.B., Guo F., Ross M.A., Watkins S.C., Tan B.J., Qi R.Z., Manser E., Li Q.T., Bay B.H., Teo T.S., Duan W.
    FASEB J. 18:1722-1724(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-377.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPKN1_RAT
AccessioniPrimary (citable) accession number: Q63433
Secondary accession number(s): Q6P748, Q8VIJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.