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Q16512 (PKN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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):
Protease-activated kinase 1
Short name=PAK-1
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:PAK1, PKN, PRK1, PRKCL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. Ref.7 Ref.8 Ref.10 Ref.14 Ref.15 Ref.18 Ref.21 Ref.26 Ref.30 Ref.37

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.21

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-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation. Ref.9 Ref.12

Subunit structure

Interacts with ZFAND6 By similarity. 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. In case of infection, interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region). Interacts (via C-terminus) with PDPK1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.26 Ref.27

Subcellular location

Cytoplasm. Nucleus. Endosome. Cell membrane; Peripheral membrane protein. Cleavage furrow. Midbody. Note: Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-374 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis. Ref.11 Ref.15 Ref.18

Tissue specificity

Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells. Ref.30

Domain

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

Post-translational modification

Autophosphorylated; preferably on serine. Phosphorylated during mitosis. Ref.13 Ref.18

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.

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.

Biophysicochemical properties

Kinetic parameters:

KM=20.6 µM for HDAC5 Ref.26

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Endosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Traceable author statement PubMed 8805275. Source: ProtInc

epithelial cell migration

Inferred from mutant phenotype Ref.30. Source: UniProtKB

histone H3-T11 phosphorylation

Inferred from direct assay Ref.21. Source: UniProtKB

hyperosmotic response

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of cell motility

Inferred from mutant phenotype Ref.30. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.15. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcleavage furrow

Inferred from direct assay Ref.18. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.15Ref.18. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from direct assay Ref.11. Source: UniProtKB

midbody

Inferred from direct assay Ref.18. Source: UniProtKB

nucleus

Inferred from direct assay Ref.15. 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 direct assay Ref.33Ref.11. Source: UniProtKB

Rac GTPase binding

Inferred from direct assay Ref.36. Source: UniProtKB

androgen receptor binding

Inferred from direct assay Ref.15Ref.21. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.21. Source: UniProtKB

histone binding

Inferred from direct assay Ref.21. Source: UniProtKB

histone deacetylase binding

Inferred from direct assay Ref.26. Source: UniProtKB

histone kinase activity (H3-T11 specific)

Inferred from direct assay Ref.21. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay Ref.15. Source: UniProtKB

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase C binding

Inferred from physical interaction Ref.27. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.13Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.26. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16512-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16512-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MASDAVQ → MAEANNPSEQELE
Note: No experimental confirmation available.
Isoform 3 (identifier: Q16512-3)

The sequence of this isoform differs from the canonical sequence as follows:
     603-603: S → R
     604-942: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.23
Chain2 – 942941Serine/threonine-protein kinase N1
PRO_0000055719

Regions

Repeat34 – 11077REM 1
Repeat123 – 20987REM 2
Repeat210 – 29182REM 3
Domain325 – 461137C2
Domain615 – 874260Protein kinase
Domain875 – 94268AGC-kinase C-terminal
Nucleotide binding621 – 6299ATP By similarity
Region181 – 1855Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination

Sites

Active site7401Proton acceptor By similarity
Binding site6441ATP By similarity
Site108 – 1092Cleavage; by caspase-3
Site454 – 4552Cleavage; by caspase-3
Site558 – 5592Cleavage; by caspase-3

Amino acid modifications

Modified residue21N-acetylalanine Ref.23 Ref.32
Modified residue2051Phosphoserine Ref.20 Ref.24
Modified residue3741Phosphoserine By similarity
Modified residue4481N6-acetyllysine Ref.25
Modified residue5331Phosphoserine Ref.17 Ref.22 Ref.24 Ref.28
Modified residue5371Phosphoserine Ref.20 Ref.22 Ref.24 Ref.28
Modified residue7741Phosphothreonine; by PDPK1 Ref.13
Modified residue7781Phosphothreonine Ref.19
Modified residue9141Phosphothreonine Ref.24
Modified residue9161Phosphoserine Ref.22 Ref.24

Natural variations

Alternative sequence1 – 77MASDAVQ → MAEANNPSEQELE in isoform 2.
VSP_038143
Alternative sequence6031S → R in isoform 3.
VSP_039213
Alternative sequence604 – 942339Missing in isoform 3.
VSP_039214
Natural variant1851R → C in a metastatic melanoma sample; somatic mutation. Ref.38
VAR_042337
Natural variant1971A → E. Ref.38
VAR_042338
Natural variant4361R → W. Ref.38
Corresponds to variant rs35132656 [ dbSNP | Ensembl ].
VAR_042339
Natural variant5201R → Q. Ref.38
Corresponds to variant rs56273055 [ dbSNP | Ensembl ].
VAR_042340
Natural variant5551L → I. Ref.3 Ref.38
Corresponds to variant rs34309238 [ dbSNP | Ensembl ].
VAR_042341
Natural variant6351R → Q. Ref.38
Corresponds to variant rs35416389 [ dbSNP | Ensembl ].
VAR_042342
Natural variant7181I → V. Ref.6 Ref.38
Corresponds to variant rs2230539 [ dbSNP | Ensembl ].
VAR_042343
Natural variant8731F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.38
VAR_042344
Natural variant9011V → I. Ref.3 Ref.5 Ref.38
Corresponds to variant rs10846 [ dbSNP | Ensembl ].
VAR_014937
Natural variant9211A → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.38
VAR_042345

Experimental info

Mutagenesis1081D → A: Abolishes cleavage by caspase-3 and formation of AF1 fragment. Ref.12
Mutagenesis1811R → A: Abolishes interaction with bacterial SspH1. Ref.37
Mutagenesis1811R → K: Decreases interaction with bacterial SspH1. Ref.37
Mutagenesis1851R → A: Abolishes interaction with bacterial SspH1. Ref.37
Mutagenesis4511D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. Ref.12
Mutagenesis4541D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. Ref.12
Mutagenesis5581D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. Ref.12
Mutagenesis5601D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. Ref.12
Mutagenesis6441K → E: Abolishes Serine/threonine-protein kinase activity. Ref.1 Ref.21
Mutagenesis6441K → R: Substantial reduction of autophosphorylation. Ref.1 Ref.21
Sequence conflict1911G → D in AAB33345. Ref.2
Sequence conflict1911G → D in AAC50209. Ref.2
Sequence conflict5621S → P in BAG36611. Ref.3
Sequence conflict7361I → T no nucleotide entry Ref.6
Sequence conflict7501T → A no nucleotide entry Ref.6
Sequence conflict8001G → A no nucleotide entry Ref.6
Sequence conflict8121E → G in BAG36611. Ref.3
Sequence conflict8871L → P in BAG53845. Ref.3

Secondary structure

................ 942
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 61360295EC70BB8E

FASTA942103,932
        10         20         30         40         50         60 
MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR 

        70         80         90        100        110        120 
RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL PDPAATHDGP QSPGAGGPTC 

       130        140        150        160        170        180 
SATNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSTKDR KLLLTAQQML QDSKTKIDII 

       190        200        210        220        230        240 
RMQLRRALQA GQLENQAAPD DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS 

       250        260        270        280        290        300 
AAKAPDRKAV SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF 

       310        320        330        340        350        360 
STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG PGTPDSRPPF 

       370        380        390        400        410        420 
LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT VVGQTSWKPC GPNAWDQSFT 

       430        440        450        460        470        480 
LELERARELE LAVFWRDQRG LCALKFLKLE DFLDNERHEV QLDMEPQGCL VAEVTFRNPV 

       490        500        510        520        530        540 
IERIPRLRRQ KKIFSKQQGK AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS 

       550        560        570        580        590        600 
EARTTGDISV EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA 

       610        620        630        640        650        660 
LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD IVARDEVESL 

       670        680        690        700        710        720 
MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG GDLMLHIHSD VFSEPRAIFY 

       730        740        750        760        770        780 
SACVVLGLQF LHEHKIVYRD LKLDNLLLDT EGYVKIADFG LCKEGMGYGD RTSTFCGTPE 

       790        800        810        820        830        840 
FLAPEVLTDT SYTRAVDWWG LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA 

       850        860        870        880        890        900 
EAIGIMRRLL RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD 

       910        920        930        940 
VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC 

« Hide

Isoform 2 [UniParc].

Checksum: 882D58AABCFDCEE1
Show »

FASTA948104,673
Isoform 3 [UniParc].

Checksum: 9CC7C140CE6C5547
Show »

FASTA60366,060

References

« Hide 'large scale' references
[1]"A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C."
Mukai H., Ono Y.
Biochem. Biophys. Res. Commun. 199:897-904(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-644.
Tissue: Hippocampus.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ILE-555 AND ILE-901.
Tissue: Kidney, Synovium and Thymus.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 3), VARIANT ILE-901.
Tissue: Brain and Placenta.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 700-800 (ISOFORMS 1/2), VARIANT VAL-718.
[7]"PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163."
Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T., Parker P.J.
FEBS Lett. 378:281-285(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MARCKS.
[8]"PKN associates and phosphorylates the head-rod domain of neurofilament protein."
Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M., Miyahara M., Sunakawa H., Ono Y.
J. Biol. Chem. 271:9816-9822(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NEFH; NEFL AND NEFM.
[9]"Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho."
Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N., Mukai H., Ono Y., Kakizuka A., Narumiya S.
Science 271:645-648(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH RHOA.
[10]"Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN."
Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.
Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GFAP AND VIM.
[11]"PRK1 is targeted to endosomes by the small GTPase, RhoB."
Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.
J. Biol. Chem. 273:4811-4814(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHOB.
[12]"Proteolytic activation of PKN by caspase-3 or related protease during apoptosis."
Takahashi M., Mukai H., Toshimori M., Miyamoto M., Ono Y.
Proc. Natl. Acad. Sci. U.S.A. 95:11566-11571(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-108; ASP-451; ASP-454; ASP-558 AND ASP-560.
[13]"Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton."
Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.
Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-774 BY PDPK1, INTERACTION WITH PDPK1.
[14]"Phosphorylation of tau is regulated by PKN."
Taniguchi T., Kawamata T., Mukai H., Hasegawa H., Isagawa T., Yasuda M., Hashimoto T., Terashima A., Nakai M., Mori H., Ono Y., Tanaka C.
J. Biol. Chem. 276:10025-10031(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPT.
[15]"A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer."
Metzger E., Muller J.M., Ferrari S., Buettner R., Schule R.
EMBO J. 22:270-280(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ANDR.
[16]"A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1."
Haraga A., Miller S.I.
Cell. Microbiol. 8:837-846(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S.TYPHIMURIUM SSPH1.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis."
Schmidt A., Durgan J., Magalhaes A., Hall A.
EMBO J. 26:1624-1636(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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-205 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation."
Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R.
Nat. Cell Biol. 10:53-60(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-644.
[22]"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-533; SER-537 AND SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537; THR-914 AND SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases."
Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A.
FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH HDAC5; HDAC7 AND HDAC9.
[27]"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4."
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Gunther T., Buettner R., Schule R.
Nature 464:792-796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCB.
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration."
Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S., Collazos A., Parker P.J.
PLoS ONE 6:E21732-E21732(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION, TISSUE SPECIFICITY.
[31]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1."
Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K., Hakoshima T.
Mol. Cell 4:793-803(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98 IN COMPLEX WITH RHOA.
[34]"Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
J. Struct. Biol. 126:166-170(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
[35]"Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)."
Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y., Parker P.J., Blundell T.L., Mott H.R.
J. Biol. Chem. 278:50578-50587(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 116-199 IN COMPLEX WITH RAC1.
[36]"The Rac1 polybasic region is required for interaction with its effector PRK1."
Modha R., Campbell L.J., Nietlispach D., Buhecha H.R., Owen D., Mott H.R.
J. Biol. Chem. 283:1492-1500(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 122-199 IN COMPLEX WITH RAC1.
[37]"Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase."
Keszei A.F., Tang X., McCormick C., Zeqiraj E., Rohde J.R., Tyers M., Sicheri F.
Mol. Cell. Biol. 34:362-373(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 122-199 IN COMPLEX WITH SALMONELLA SSPH1, UBIQUITINATION, MUTAGENESIS OF ARG-181 AND ARG-185, FUNCTION AS ANDROGEN RECEPTOR COACTIVATOR.
[38]"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: VARIANTS [LARGE SCALE ANALYSIS] CYS-185; GLU-197; TRP-436; GLN-520; ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26181 mRNA. Translation: BAA05169.1.
S75546 mRNA. Translation: AAB33345.1.
U33053 mRNA. Translation: AAC50209.1.
AK123007 mRNA. Translation: BAG53845.1.
AK292130 mRNA. Translation: BAF84819.1.
AK313886 mRNA. Translation: BAG36611.1.
AC008569 Genomic DNA. No translation available.
BC040061 mRNA. Translation: AAH40061.1.
BC094766 mRNA. Translation: AAH94766.1.
PIRJC2129.
S51162.
RefSeqNP_002732.3. NM_002741.3.
NP_998725.1. NM_213560.1.
UniGeneHs.466044.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXZX-ray2.20B13-98[»]
1URFNMR-A122-199[»]
2RMKNMR-B122-199[»]
4NKGX-ray2.90B/D122-199[»]
ProteinModelPortalQ16512.
SMRQ16512. Positions 13-98, 122-199, 577-941.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111571. 42 interactions.
DIPDIP-34240N.
IntActQ16512. 14 interactions.
MINTMINT-118694.
STRING9606.ENSP00000343325.

Chemistry

BindingDBQ16512.
ChEMBLCHEMBL3384.
GuidetoPHARMACOLOGY1520.

PTM databases

PhosphoSiteQ16512.

Polymorphism databases

DMDM259016304.

Proteomic databases

PaxDbQ16512.
PRIDEQ16512.

Protocols and materials databases

DNASU5585.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242783; ENSP00000242783; ENSG00000123143. [Q16512-1]
ENST00000342216; ENSP00000343325; ENSG00000123143. [Q16512-2]
GeneID5585.
KEGGhsa:5585.
UCSCuc002myp.3. human. [Q16512-1]
uc002myq.3. human. [Q16512-2]

Organism-specific databases

CTD5585.
GeneCardsGC19P014544.
H-InvDBHIX0027472.
HGNCHGNC:9405. PKN1.
HPACAB010278.
HPA003982.
MIM601032. gene.
neXtProtNX_Q16512.
PharmGKBPA33769.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108317.
KOK06071.
OMAEFRSSGE.
OrthoDBEOG7X9G6Q.
PhylomeDBQ16512.
TreeFamTF102005.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
SignaLinkQ16512.

Gene expression databases

ArrayExpressQ16512.
BgeeQ16512.
CleanExHS_PKN1.
GenevestigatorQ16512.

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

ChiTaRSPKN1. human.
EvolutionaryTraceQ16512.
GeneWikiProtein_kinase_N1.
GenomeRNAi5585.
NextBio21660.
PMAP-CutDBQ16512.
PROQ16512.
SOURCESearch...

Entry information

Entry namePKN1_HUMAN
AccessionPrimary (citable) accession number: Q16512
Secondary accession number(s): A8K7W5 expand/collapse secondary AC list , B2R9R4, B3KVN3, Q15143, Q504U4, Q8IUV5, Q9UD44
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 164 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 19

Human chromosome 19: entries, gene names and cross-references to MIM