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Reviewed, UniProtKB/Swiss-Prot Q6P5Z2 (PKN3_HUMAN)

Last modified September 23, 2008. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase N3
    EC=2.7.11.13
Alternative name(s):
    Protein kinase PKN-beta
    Protein-kinase C-related kinase 3
Gene names
Name: PKN3
Synonyms: PKNBETA
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length889 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Contributes to invasiveness in malignant prostate cancer.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Two specific sites, Thr-718 (activation loop of the kinase domain) and Thr-860 (turn motif), need to be phosphorylated for its full activation By similarity.

Subcellular location

Nucleus. Cytoplasm › perinuclear region. Note= Nuclear and perinuclear Golgi region.

Tissue specificity

Expressed in prostate tumors and various cancer cell lines. Not expressed in adult tissues.

Domain

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

Post-translational modification

Autophosphorylated.

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 protein kinase domain.

Contains 3 REM (Hr1) repeats.

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Ontologies

Keywords

   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processprotein amino acid phosphorylation Ref.1

Traceable author statement. Source: ProtInc

signal transduction Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentGolgi apparatus Ref.1

Traceable author statement. Source: ProtInc

nucleus Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

protein kinase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGAP26Q9UNA12EBI-1384335,EBI-1390913

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 889889Serine/threonine-protein kinase N3

Regions

Repeat18 – 9073REM 1
Repeat105 – 18177REM 2
Repeat182 – 25574REM 3
Domain559 – 818260Protein kinase
Domain819 – 88971AGC-kinase C-terminal
Nucleotide binding565 – 5739ATP By similarity
Compositional bias463 – 55492Pro-rich

Sites

Active site6841Proton acceptor By similarity
Binding site5881ATP By similarity

Amino acid modifications

Modified residue5441Phosphoserine
Modified residue5501Phosphothreonine
Modified residue7181Phosphothreonine
Modified residue8601Phosphothreonine Probable

Natural variations

Natural variant1801A → E

Experimental info

Mutagenesis5881K → E: Abolishes autophosphorylation and catalytic activity
Mutagenesis5881K → R: Abolishes catalytic activity
Mutagenesis7181T → A: Abolishes phosphorylation
Sequence conflict4441A → R in BAA85625. Ref.1
Sequence conflict6271A → V in BAA85625. Ref.1
Sequence conflict6361C → R in BAA85625. Ref.1
Sequence conflict7381R → Q in BAA85625. Ref.1
Sequence conflict7441G → A in BAA85625. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q6P5Z2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F3891DA1420DF54E

FASTA88999,421
        10         20         30         40         50         60 
MEEGAPRQPG PSQWPPEDEK EVIRRAIQKE LKIKEGVENL RRVATDRRHL GHVQQLLRSS 

        70         80         90        100        110        120 
NRRLEQLHGE LRELHARILL PGPGPGPAEP VASGPRPWAE QLRARHLEAL RRQLHVELKV 

       130        140        150        160        170        180 
KQGAENMTHT CASGTPKERK LLAAAQQMLR DSQLKVALLR MKISSLEASG SPEPGPELLA 

       190        200        210        220        230        240 
EELQHRLHVE AAVAEGAKNV VKLLSSRRTQ DRKALAEAQA QLQESSQKLD LLRLALEQLL 

       250        260        270        280        290        300 
EQLPPAHPLR SRVTRELRAA VPGYPQPSGT PVKPTALTGT LQVRLLGCEQ LLTAVPGRSP 

       310        320        330        340        350        360 
AAALASSPSE GWLRTKAKHQ RGRGELASEV LAVLKVDNRV VGQTGWGQVA EQSWDQTFVI 

       370        380        390        400        410        420 
PLERARELEI GVHWRDWRQL CGVAFLRLED FLDNACHQLS LSLVPQGLLF AQVTFCDPVI 

       430        440        450        460        470        480 
ERRPRLQRQE RIFSKRRGQD FLRASQMNLG MAAWGRLVMN LLPPCSSPST ISPPKGCPRT 

       490        500        510        520        530        540 
PTTLREASDP ATPSNFLPKK TPLGEEMTPP PKPPRLYLPQ EPTSEETPRT KRPHMEPRTR 

       550        560        570        580        590        600 
RGPSPPASPT RKPPRLQDFR CLAVLGRGHF GKVLLVQFKG TGKYYAIKAL KKQEVLSRDE 

       610        620        630        640        650        660 
IESLYCEKRI LEAVGCTGHP FLLSLLACFQ TSSHACFVTE FVPGGDLMMQ IHEDVFPEPQ 

       670        680        690        700        710        720 
ARFYVACVVL GLQFLHEKKI IYRDLKLDNL LLDAQGFLKI ADFGLCKEGI GFGDRTSTFC 

       730        740        750        760        770        780 
GTPEFLAPEV LTQEAYTRAV DWWGLGVLLY EMLVGECPFP GDTEEEVFDC IVNMDAPYPG 

       790        800        810        820        830        840 
FLSVQGLEFI QKLLQKCPEK RLGAGEQDAE EIKVQPFFRT TNWQALLART IQPPFVPTLC 

       850        860        870        880 
GPADLRYFEG EFTGLPPALT PPAPHSLLTA RQQAAFRDFD FVSERFLEP

« Hide

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References

« Hide 'large scale' references
[1]"Identification and characterization of PKNbeta, a novel isoform of protein kinase PKN: expression and arachidonic acid dependency are different from those of PKNalpha."
Oishi K., Mukai H., Shibata H., Takahashi M., Ono Y.
Biochem. Biophys. Res. Commun. 261:808-814(1999) [PubMed: 10441506] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-588, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[4]"PKN3 is required for malignant prostate cell growth downstream of activated PI 3-kinase."
Leenders F., Moepert K., Schmiedeknecht A., Santel A., Czauderna F., Aleku M., Penschuck S., Dames S., Sternberger M., Roehl T., Wellmann A., Arnold W., Giese K., Kaufmann J., Klippel A.
EMBO J. 23:3303-3313(2004) [PubMed: 15282551] [Abstract]
Cited for: FUNCTION IN MALIGNANT CELL GROWTH, PHOSPHORYLATION AT THR-718, MUTAGENESIS OF LYS-588 AND THR-718.
[5]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND THR-550, MASS SPECTROMETRY.
[6]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-180.

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Cross-references

Sequence databases

AB019692 mRNA. Translation: BAA85625.1.
AL441992 Genomic DNA. Translation: CAI15401.1.
BC062558 mRNA. Translation: AAH62558.1.
PIRJC7083.
RefSeqNP_037487.2.
UniGeneHs.300485

3D structure databases

HSSPHSSP built from PDB template 1GZK based on UniProtKB P31751.
ModBaseSearch...

Protein-protein interaction databases

IntActQ6P5Z2.

Genome annotation databases

EnsemblENSG00000160447. Homo sapiens. [Contig view]
GeneID29941.
KEGGhsa:29941.

Organism-specific databases

H-InvDBHIX0034740.
HGNCHGNC:17999. PKN3.
MIM610714. gene.
PharmGKBPA134919098.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ6P5Z2.
HOVERGENQ6P5Z2.

Gene expression databases

ArrayExpressQ6P5Z2.
CleanExHS_PKN3.
GermOnlineENSG00000160447. Homo sapiens.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR000861. HR1-like_rho-bd.
IPR011072. HR1_rho-bd.
IPR000961. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
Gene3DG3DSA:1.10.287.160. HR1_rho-bd. 3 hits.
PfamPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
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]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

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Entry information

Entry namePKN3_HUMAN
AccessionPrimary (citable) accession number: Q6P5Z2
Secondary accession number(s): Q9UM03
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 5, 2004
Last modified: September 23, 2008
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents