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Reviewed, UniProtKB/Swiss-Prot Q16513 (PKN2_HUMAN)

Last modified February 9, 2010. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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 N2
    EC=2.7.11.13
Alternative name(s):
    Protein kinase C-like 2
    Protein-kinase C-related kinase 2
Gene names
Name: PKN2
Synonyms: PRK2, PRKCL2
OrganismHomo sapiens (Human) [Complete proteome]
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 length984 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Exhibits a preference for highly basic protein substrates By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-816 (activation loop of the kinase domain) and Thr-958 (turn motif), need to be phosphorylated for its full activation By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

Post-translational modification

Autophosphorylated. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Activated by limited proteolysis with trypsin 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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid phosphorylation

Traceable author statement. Source: ProtInc

signal transduction Ref.2

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 984983Serine/threonine-protein kinase N2
PRO_0000055722

Regions

Repeat44 – 11976REM 1
Repeat133 – 21381REM 2
Repeat214 – 29582REM 3
Domain330 – 463134C2
Domain657 – 916260Protein kinase
Domain917 – 98468AGC-kinase C-terminal
Nucleotide binding663 – 6719ATP By similarity

Sites

Active site7821Proton acceptor By similarity
Binding site6861ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue1101Phosphoserine Ref.11
Modified residue1211Phosphothreonine Ref.11
Modified residue1241Phosphothreonine Ref.11
Modified residue2891Phosphoserine Ref.6
Modified residue3021Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue3061Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue3601Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.13
Modified residue3621Phosphoserine Ref.11
Modified residue3671Phosphoserine By similarity
Modified residue5311Phosphoserine Ref.8 Ref.9
Modified residue5351Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11
Modified residue5591Phosphoserine Ref.5
Modified residue5611Phosphoserine Ref.5
Modified residue5821Phosphoserine Ref.4
Modified residue5831Phosphoserine Ref.6 Ref.10 Ref.13
Modified residue6281Phosphothreonine Ref.11
Modified residue6311Phosphoserine Ref.11
Modified residue8141Phosphothreonine
Modified residue8161Phosphothreonine Ref.4
Modified residue9581Phosphothreonine Ref.6 Ref.10 Ref.11

Natural variations

Natural variant941E → D: dbSNP rs12039846.
VAR_050562
Natural variant1971A → E: dbSNP rs35207128.
VAR_050563
Natural variant6551Q → R: dbSNP rs12085658.
VAR_050564

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Sequences

Sequence LengthMass (Da)Tools
Q16513-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 687EC417A0F51C1D

FASTA984112,035
        10         20         30         40         50         60 
MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 

        70         80         90        100        110        120 
KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDITDCPR 

       130        140        150        160        170        180 
TPDTPNNDPR CSTSNNRLKA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 

       190        200        210        220        230        240 
QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM 

       250        260        270        280        290        300 
KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA 

       310        320        330        340        350        360 
ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK ATSVALPGWS 

       370        380        390        400        410        420 
PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD NTVVGQTSWK PISNQSWDQK 

       430        440        450        460        470        480 
FTLELDRSRE LEISVYWRDW RSLCAVKFLR LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN 

       490        500        510        520        530        540 
PVIERRPKLQ RQKKIFSKQQ GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV 

       550        560        570        580        590        600 
PTTVPVVDVR IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG 

       610        620        630        640        650        660 
QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF QFNLQDFRCC 

       670        680        690        700        710        720 
AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD SLMCEKRIFE TVNSVRHPFL 

       730        740        750        760        770        780 
VNLFACFQTK EHVCFVMEYA AGGDLMMHIH TDVFSEPRAV FYAACVVLGL QYLHEHKIVY 

       790        800        810        820        830        840 
RDLKLDNLLL DTEGFVKIAD FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW 

       850        860        870        880        890        900 
WGLGVLIYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL 

       910        920        930        940        950        960 
GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF TSEAPILTPP 

       970        980 
REPRILSEEE QEMFRDFDYI ADWC

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References

« Hide 'large scale' references
[1]"Identification of multiple, novel, protein kinase C-related gene products."
Palmer R.H., Ridden J., Parker P.J.
FEBS Lett. 356:5-8(1994) [PubMed: 7988719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family."
Palmer R.H., Ridden J., Parker P.J.
Eur. J. Biochem. 227:344-351(1995) [PubMed: 7851406] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: B-cell.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND THR-816, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Phosphoproteomic analysis of synaptosomes from human cerebral cortex."
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A.
J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, MASS SPECTROMETRY.
Tissue: Brain cortex.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-583 AND THR-958, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306 AND SER-360, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531 AND SER-535, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-531 AND SER-535, MASS SPECTROMETRY.
[10]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306; SER-360; SER-535; SER-583 AND THR-958, MASS SPECTROMETRY.
[11]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-121; THR-124; SER-302; SER-306; SER-360; SER-362; SER-535; THR-628; SER-631 AND THR-958, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-583, MASS SPECTROMETRY.
[14]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-583 AND THR-814, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U33052 mRNA. Translation: AAC50208.1.
S75548 mRNA. Translation: AAB33346.1.
AL136381, AC119426 Genomic DNA. Translation: CAI23271.1.
IPIIPI00002804.
PIRS67527.
RefSeqNP_006247.1.
UniGeneHs.440833

3D structure databases

SMRQ16513. Positions 29-107, 132-203, 215-278, 326-479, 654-982.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ16513.

PTM databases

PhosphoSiteQ16513.

Proteomic databases

PRIDEQ16513.

Genome annotation databases

EnsemblENST00000370521; ENSP00000359552; ENSG00000065243; Homo sapiens. [Genome view]
GeneID5586.
KEGGhsa:5586.
UCSCuc001dmn.1. human.

Organism-specific databases

CTD5586.
GeneCardsGC01P088862.
H-InvDBHIX0000758.
HGNCHGNC:9406. PKN2.
MIM602549. gene.
PharmGKBPA33770.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG387623.
HOVERGENQ16513.
InParanoidQ16513.
OMACPRTPDT.
OrthoDBEOG9K9DXJ.
PhylomeDBQ16513.

Enzyme and pathway databases

BRENDA2.7.11.13. 247.

Gene expression databases

ArrayExpressQ16513.
BgeeQ16513.
CleanExHS_PKN2.
GenevestigatorQ16513.
GermOnlineENSG00000065243. Homo sapiens.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR000861. HR1-like_rho-bd.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[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]
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.
PS50004. C2. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21666.
PMAP-CutDBQ16513.
SOURCESearch...

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Entry information

Entry namePKN2_HUMAN
AccessionPrimary (citable) accession number: Q16513
Secondary accession number(s): Q9H1W4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

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