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Q6P5Z2 (PKN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length889 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to invasiveness in malignant prostate cancer. Ref.4

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. Cytoplasmperinuclear region. Note: Nuclear and perinuclear Golgi region. Ref.1

Tissue specificity

Expressed in prostate tumors and various cancer cell lines. Not expressed in adult tissues. Ref.1

Domain

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

Post-translational modification

Autophosphorylated. Ref.1 Ref.4

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGAP10A1A4S64EBI-1384335,EBI-1390944
ARHGAP26Q9UNA14EBI-1384335,EBI-1390913

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 889889Serine/threonine-protein kinase N3
PRO_0000055725

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 Ref.5 Ref.6 Ref.7
Modified residue5481Phosphoserine Ref.6
Modified residue7181Phosphothreonine Ref.4
Modified residue7221Phosphothreonine Ref.5
Modified residue8601Phosphothreonine Ref.5 Ref.7

Natural variations

Natural variant1801A → E. Ref.8
Corresponds to variant rs56251280 [ dbSNP | Ensembl ].
VAR_042346
Natural variant4041V → L.
Corresponds to variant rs12932 [ dbSNP | Ensembl ].
VAR_050565

Experimental info

Mutagenesis5881K → E: Abolishes autophosphorylation and catalytic activity. Ref.1 Ref.4
Mutagenesis5881K → R: Abolishes catalytic activity. Ref.1 Ref.4
Mutagenesis7181T → A: Abolishes phosphorylation. Ref.4
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

Sequences

Sequence LengthMass (Da)Tools
Q6P5Z2 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MALIGNANT CELL GROWTH, PHOSPHORYLATION AT THR-718, MUTAGENESIS OF LYS-588 AND THR-718.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; THR-722 AND THR-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND THR-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-180.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB019692 mRNA. Translation: BAA85625.1.
AL441992 Genomic DNA. Translation: CAI15401.1.
BC062558 mRNA. Translation: AAH62558.1.
PIRJC7083.
RefSeqNP_037487.2. NM_013355.3.
UniGeneHs.300485.

3D structure databases

ProteinModelPortalQ6P5Z2.
SMRQ6P5Z2. Positions 27-78, 109-163, 183-241, 525-889.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118978. 5 interactions.
IntActQ6P5Z2. 2 interactions.
MINTMINT-192027.
STRING9606.ENSP00000291906.

PTM databases

PhosphoSiteQ6P5Z2.

Polymorphism databases

DMDM74749130.

Proteomic databases

PaxDbQ6P5Z2.
PRIDEQ6P5Z2.

Protocols and materials databases

DNASU29941.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291906; ENSP00000291906; ENSG00000160447.
GeneID29941.
KEGGhsa:29941.
UCSCuc004bvw.3. human.

Organism-specific databases

CTD29941.
GeneCardsGC09P131464.
HGNCHGNC:17999. PKN3.
HPAHPA045390.
MIM610714. gene.
neXtProtNX_Q6P5Z2.
PharmGKBPA134919098.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233032.
HOVERGENHBG108317.
InParanoidQ6P5Z2.
KOK06071.
OMAQPFFRTT.
OrthoDBEOG7X9G6Q.
PhylomeDBQ6P5Z2.
TreeFamTF102005.

Enzyme and pathway databases

SignaLinkQ6P5Z2.

Gene expression databases

ArrayExpressQ6P5Z2.
BgeeQ6P5Z2.
CleanExHS_PKN3.
GenevestigatorQ6P5Z2.

Family and domain databases

Gene3D1.10.287.160. 3 hits.
2.60.40.150. 1 hit.
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

GeneWikiPKN3_(gene).
GenomeRNAi29941.
NextBio52593.
PROQ6P5Z2.
SOURCESearch...

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: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

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