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A1A4I4 (PKN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PKN1
Synonyms:PKN, PRK1, PRKCL1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length944 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

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.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Endosome By similarity. Cell membrane; 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.

Domain

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

Post-translational modification

Autophosphorylated; preferably on serine. Phosphorylated during mitosis 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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 1 protein kinase domain.

Contains 3 REM (Hr1) repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Endosome
Membrane
Nucleus
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processepithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-T11 phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

hyperosmotic response

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell motility

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcleavage furrow

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP-Rho binding

Inferred from sequence or structural similarity. Source: UniProtKB

Rac GTPase binding

Inferred from sequence or structural similarity. Source: UniProtKB

androgen receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone kinase activity (H3-T11 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 944943Serine/threonine-protein kinase N1
PRO_0000394261

Regions

Repeat34 – 11178REM 1
Repeat124 – 21087REM 2
Repeat211 – 29282REM 3
Domain326 – 462137C2
Domain617 – 876260Protein kinase
Domain877 – 94468AGC-kinase C-terminal
Nucleotide binding623 – 6319ATP By similarity
Region182 – 1865Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination By similarity

Sites

Active site7421Proton acceptor By similarity
Binding site6461ATP By similarity
Site109 – 1102Cleavage; by caspase-3 By similarity
Site455 – 4562Cleavage; by caspase-3 By similarity
Site559 – 5602Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2061Phosphoserine By similarity
Modified residue3751Phosphoserine By similarity
Modified residue4491N6-acetyllysine By similarity
Modified residue5341Phosphoserine By similarity
Modified residue5381Phosphoserine By similarity
Modified residue7761Phosphothreonine; by PDPK1 By similarity
Modified residue7801Phosphothreonine By similarity
Modified residue9161Phosphothreonine By similarity
Modified residue9181Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A4I4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 11B6833ED4F8D57E

FASTA944104,133
        10         20         30         40         50         60 
MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR 

        70         80         90        100        110        120 
RATTDLGRNL GPVELVLRGS SRRLALLHQQ LQELHAHVVL PDPAVGVHDA PQSPGTGDSA 

       130        140        150        160        170        180 
CSATNLSRVA GLEKQLAIEL KVKQGAENMI QTYSNGSTKD RKLLLTAQQM LQDSKTKIDI 

       190        200        210        220        230        240 
IRMQLHRALQ ACQLESQAAP DEAQGSPDLG AVELRIEELR HHFRVEHAVA EGAKNVLRLL 

       250        260        270        280        290        300 
SAAKAPDRKA VSEAQEKLTE SNQKLGLLRE ALERRLGELP ADHPKGRLLR EELAAASSAA 

       310        320        330        340        350        360 
FSARLAGPFP ATHYSTLSKP APLTGTLEVR VVGCRDLPET IPWNPSPSVG GPGTPDSRTP 

       370        380        390        400        410        420 
FLSRPARGLY SRTGSLSGRS SLKAEAENTN EVSTVLKLDN TVVGQTSWKP CGPNAWDQSF 

       430        440        450        460        470        480 
TLELERAREL ELAVFWRDQR GLCALKFLKL EDFLDNERHE VQLDMEPQGC LVAEVTFRNP 

       490        500        510        520        530        540 
VIERIPRLRR QKKIFSKQQG KAFQRARQMN IDVATWVRLL RRLIPNATAT GTFSPGASPG 

       550        560        570        580        590        600 
PEARSTGDIS VEKLNLGTET DSSPQKSPLG PPSSPSSLSS PIQATTTTPE LPSETQETPG 

       610        620        630        640        650        660 
PTLCSPLRKS PLTLEDFKFL AVLGRGHFGK VLLSEFRPSG ELFAIKALKK GDIVARDEVE 

       670        680        690        700        710        720 
SLMCEKRILA AVTNAGHPFL VNLFGCFQTP EHVCFVMEYS AGGDLMLHIH SDVFSEPRAV 

       730        740        750        760        770        780 
FYSACVVLGL QFLHEHKIVY RDLKLDNLLL DTEGYVKIAD FGLCKEGMGY GDRTSTFCGT 

       790        800        810        820        830        840 
PEFLAPEVLT DTSYTRAVDW WGLGVLLYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL 

       850        860        870        880        890        900 
SAEAIGIMRR LLRRNPERRL GSSERDAEDV KKQPFFRTLG WDALLARRLP PPFVPTLAGR 

       910        920        930        940 
TDVSNFDEEF TGEAPTLSPP RDARPLTATE QAAFRDFDFV AGSC 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC126539 mRNA. Translation: AAI26540.1.
RefSeqNP_001073715.1. NM_001080246.1.
UniGeneBt.4993.

3D structure databases

ProteinModelPortalA1A4I4.
SMRA1A4I4. Positions 13-98, 123-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000022652.

Proteomic databases

PRIDEA1A4I4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID509080.
KEGGbta:509080.

Organism-specific databases

CTD5585.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233032.
HOVERGENHBG108317.
InParanoidA1A4I4.
KOK06071.

Family and domain databases

Gene3D1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
InterProIPR000961. 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]
PfamPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

NextBio20868812.

Entry information

Entry namePKN1_BOVIN
AccessionPrimary (citable) accession number: A1A4I4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families