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Q6P5Z2

- PKN3_HUMAN

UniProt

Q6P5Z2 - PKN3_HUMAN

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Protein

Serine/threonine-protein kinase N3

Gene

PKN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Contributes to invasiveness in malignant prostate cancer.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei588 – 5881ATPPROSITE-ProRule annotation
Active sitei684 – 6841Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi565 – 5739ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: ProtInc
  3. protein kinase C activity Source: UniProtKB-EC

GO - Biological processi

  1. epithelial cell migration Source: UniProtKB
  2. protein phosphorylation Source: ProtInc
  3. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ6P5Z2.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PKN3
Synonyms:PKNBETA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17999. PKN3.

Subcellular locationi

Nucleus 1 Publication. Cytoplasmperinuclear region 1 Publication
Note: Nuclear and perinuclear Golgi region.

GO - Cellular componenti

  1. Golgi apparatus Source: ProtInc
  2. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi588 – 5881K → E: Abolishes autophosphorylation and catalytic activity. 2 Publications
Mutagenesisi588 – 5881K → R: Abolishes catalytic activity. 2 Publications
Mutagenesisi718 – 7181T → A: Abolishes phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA134919098.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 889889Serine/threonine-protein kinase N3PRO_0000055725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei544 – 5441Phosphoserine3 Publications
Modified residuei548 – 5481Phosphoserine1 Publication
Modified residuei718 – 7181Phosphothreonine1 Publication
Modified residuei722 – 7221Phosphothreonine1 Publication
Modified residuei860 – 8601Phosphothreonine2 Publications

Post-translational modificationi

Autophosphorylated.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6P5Z2.
PaxDbiQ6P5Z2.
PRIDEiQ6P5Z2.

PTM databases

PhosphoSiteiQ6P5Z2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ6P5Z2.
CleanExiHS_PKN3.
ExpressionAtlasiQ6P5Z2. baseline and differential.
GenevestigatoriQ6P5Z2.

Organism-specific databases

HPAiHPA045390.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGAP10A1A4S64EBI-1384335,EBI-1390944
ARHGAP26Q9UNA14EBI-1384335,EBI-1390913

Protein-protein interaction databases

BioGridi118978. 11 interactions.
IntActiQ6P5Z2. 3 interactions.
MINTiMINT-192027.
STRINGi9606.ENSP00000291906.

Structurei

3D structure databases

ProteinModelPortaliQ6P5Z2.
SMRiQ6P5Z2. Positions 27-78, 109-163, 183-241, 525-884.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 9073REM 1Add
BLAST
Repeati105 – 18177REM 2Add
BLAST
Repeati182 – 25574REM 3Add
BLAST
Domaini559 – 818260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini819 – 88971AGC-kinase C-terminalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi463 – 55492Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 3 REM (Hr1) repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118891.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ6P5Z2.
KOiK06071.
OMAiQPFFRTT.
OrthoDBiEOG7X9G6Q.
PhylomeDBiQ6P5Z2.
TreeFamiTF102005.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 1 hit.
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.

Q6P5Z2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEGAPRQPG PSQWPPEDEK EVIRRAIQKE LKIKEGVENL RRVATDRRHL
60 70 80 90 100
GHVQQLLRSS NRRLEQLHGE LRELHARILL PGPGPGPAEP VASGPRPWAE
110 120 130 140 150
QLRARHLEAL RRQLHVELKV KQGAENMTHT CASGTPKERK LLAAAQQMLR
160 170 180 190 200
DSQLKVALLR MKISSLEASG SPEPGPELLA EELQHRLHVE AAVAEGAKNV
210 220 230 240 250
VKLLSSRRTQ DRKALAEAQA QLQESSQKLD LLRLALEQLL EQLPPAHPLR
260 270 280 290 300
SRVTRELRAA VPGYPQPSGT PVKPTALTGT LQVRLLGCEQ LLTAVPGRSP
310 320 330 340 350
AAALASSPSE GWLRTKAKHQ RGRGELASEV LAVLKVDNRV VGQTGWGQVA
360 370 380 390 400
EQSWDQTFVI PLERARELEI GVHWRDWRQL CGVAFLRLED FLDNACHQLS
410 420 430 440 450
LSLVPQGLLF AQVTFCDPVI ERRPRLQRQE RIFSKRRGQD FLRASQMNLG
460 470 480 490 500
MAAWGRLVMN LLPPCSSPST ISPPKGCPRT PTTLREASDP ATPSNFLPKK
510 520 530 540 550
TPLGEEMTPP PKPPRLYLPQ EPTSEETPRT KRPHMEPRTR RGPSPPASPT
560 570 580 590 600
RKPPRLQDFR CLAVLGRGHF GKVLLVQFKG TGKYYAIKAL KKQEVLSRDE
610 620 630 640 650
IESLYCEKRI LEAVGCTGHP FLLSLLACFQ TSSHACFVTE FVPGGDLMMQ
660 670 680 690 700
IHEDVFPEPQ ARFYVACVVL GLQFLHEKKI IYRDLKLDNL LLDAQGFLKI
710 720 730 740 750
ADFGLCKEGI GFGDRTSTFC GTPEFLAPEV LTQEAYTRAV DWWGLGVLLY
760 770 780 790 800
EMLVGECPFP GDTEEEVFDC IVNMDAPYPG FLSVQGLEFI QKLLQKCPEK
810 820 830 840 850
RLGAGEQDAE EIKVQPFFRT TNWQALLART IQPPFVPTLC GPADLRYFEG
860 870 880
EFTGLPPALT PPAPHSLLTA RQQAAFRDFD FVSERFLEP
Length:889
Mass (Da):99,421
Last modified:July 5, 2004 - v1
Checksum:iF3891DA1420DF54E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti444 – 4441A → R in BAA85625. (PubMed:10441506)Curated
Sequence conflicti627 – 6271A → V in BAA85625. (PubMed:10441506)Curated
Sequence conflicti636 – 6361C → R in BAA85625. (PubMed:10441506)Curated
Sequence conflicti738 – 7381R → Q in BAA85625. (PubMed:10441506)Curated
Sequence conflicti744 – 7441G → A in BAA85625. (PubMed:10441506)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti180 – 1801A → E.1 Publication
Corresponds to variant rs56251280 [ dbSNP | Ensembl ].
VAR_042346
Natural varianti404 – 4041V → L.
Corresponds to variant rs12932 [ dbSNP | Ensembl ].
VAR_050565

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019692 mRNA. Translation: BAA85625.1.
AL441992 Genomic DNA. Translation: CAI15401.1.
BC062558 mRNA. Translation: AAH62558.1.
CCDSiCCDS6908.1.
PIRiJC7083.
RefSeqiNP_037487.2. NM_013355.3.
UniGeneiHs.300485.

Genome annotation databases

EnsembliENST00000291906; ENSP00000291906; ENSG00000160447.
GeneIDi29941.
KEGGihsa:29941.
UCSCiuc004bvw.3. human.

Polymorphism databases

DMDMi74749130.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019692 mRNA. Translation: BAA85625.1 .
AL441992 Genomic DNA. Translation: CAI15401.1 .
BC062558 mRNA. Translation: AAH62558.1 .
CCDSi CCDS6908.1.
PIRi JC7083.
RefSeqi NP_037487.2. NM_013355.3.
UniGenei Hs.300485.

3D structure databases

ProteinModelPortali Q6P5Z2.
SMRi Q6P5Z2. Positions 27-78, 109-163, 183-241, 525-884.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118978. 11 interactions.
IntActi Q6P5Z2. 3 interactions.
MINTi MINT-192027.
STRINGi 9606.ENSP00000291906.

PTM databases

PhosphoSitei Q6P5Z2.

Polymorphism databases

DMDMi 74749130.

Proteomic databases

MaxQBi Q6P5Z2.
PaxDbi Q6P5Z2.
PRIDEi Q6P5Z2.

Protocols and materials databases

DNASUi 29941.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000291906 ; ENSP00000291906 ; ENSG00000160447 .
GeneIDi 29941.
KEGGi hsa:29941.
UCSCi uc004bvw.3. human.

Organism-specific databases

CTDi 29941.
GeneCardsi GC09P131464.
HGNCi HGNC:17999. PKN3.
HPAi HPA045390.
MIMi 610714. gene.
neXtProti NX_Q6P5Z2.
PharmGKBi PA134919098.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118891.
HOGENOMi HOG000233032.
HOVERGENi HBG108317.
InParanoidi Q6P5Z2.
KOi K06071.
OMAi QPFFRTT.
OrthoDBi EOG7X9G6Q.
PhylomeDBi Q6P5Z2.
TreeFami TF102005.

Enzyme and pathway databases

SignaLinki Q6P5Z2.

Miscellaneous databases

GeneWikii PKN3_(gene).
GenomeRNAii 29941.
NextBioi 52593.
PROi Q6P5Z2.
SOURCEi Search...

Gene expression databases

Bgeei Q6P5Z2.
CleanExi HS_PKN3.
ExpressionAtlasi Q6P5Z2. baseline and differential.
Genevestigatori Q6P5Z2.

Family and domain databases

Gene3Di 1.10.287.160. 3 hits.
2.60.40.150. 1 hit.
InterProi IPR000961. 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 ]
Pfami PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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.
    , 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.

Entry informationi

Entry nameiPKN3_HUMAN
AccessioniPrimary (citable) accession number: Q6P5Z2
Secondary accession number(s): Q9UM03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3