Reviewed, UniProtKB/Swiss-Prot Q16512 (PKN1_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase N1
    EC=2.7.11.13
Alternative name(s):
    Protein kinase C-like 1
    Protein-kinase C-related kinase 1
    Protein kinase C-like PKN
    Serine-threonine protein kinase N
    Protein kinase PKN-alpha

Gene names

Name:	PKN1
Synonyms:	PKN, PRK1, PRKCL1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can phosphorylate ribosomal protein S6. Mediates GTPase Rho dependent intracellular signaling 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. Two specific sites, Thr-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation By similarity.
Subunit structure	Interacts with ZA20D3 By similarity. Interacts with RhoA and Rac1.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.
Domain	The C1 domain does not bind the diacylglycerol (DAG).
Post-translational modification	Autophosphorylated; preferably on serine. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of JUN kinase activity Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein kinase C activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAP2K3	P46734	1	EBI-602382,EBI-602462
MAP2K6	P52564	1	EBI-602382,EBI-448135
MAPK12	P53778	1	EBI-602382,EBI-602406
MAPK14	Q16539	1	EBI-602382,EBI-73946
MLTK	Q9NYL2-1	1	EBI-602382,EBI-687346
RHOA	P61586	1	EBI-602382,EBI-446668

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 942

941

Serine/threonine-protein kinase N1

PRO_0000055719

Regions

Repeat

34 – 110

77

REM 1

Repeat

123 – 209

87

REM 2

Repeat

210 – 291

82

REM 3

Domain

325 – 461

137

C2

Domain

615 – 874

260

Protein kinase

Domain

875 – 942

68

AGC-kinase C-terminal

Nucleotide binding

621 – 629

9

ATP By similarity

Sites

Active site

740

1

Proton acceptor By similarity

Binding site

644

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.14

Modified residue

205

1

Phosphoserine Ref.11 Ref.15

Modified residue

353

1

Phosphothreonine Ref.11

Modified residue

376

1

Phosphoserine Ref.7

Modified residue

448

1

N6-acetyllysine Ref.16

Modified residue

533

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15

Modified residue

537

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15

Modified residue

559

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15

Modified residue

561

1

Phosphoserine Ref.14

Modified residue

562

1

Phosphoserine Ref.8 Ref.9 Ref.12 Ref.14 Ref.15

Modified residue

774

1

Phosphothreonine Probable

Modified residue

778

1

Phosphothreonine Ref.10

Modified residue

914

1

Phosphothreonine Ref.15

Modified residue

916

1

Phosphoserine Ref.6 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence

1 – 7

7

MASDAVQ → MAEANNPSEQELE in isoform 2.

VSP_038143

Natural variant

185

1

R → C in a metastatic melanoma sample; somatic mutation. Ref.19

VAR_042337

Natural variant

197

1

A → E

VAR_042338

Natural variant

436

1

R → W: dbSNP rs35132656. Ref.19

VAR_042339

Natural variant

520

1

R → Q: dbSNP rs56273055. Ref.19

VAR_042340

Natural variant

555

1

L → I: dbSNP rs34309238. Ref.19 Ref.3

VAR_042341

Natural variant

635

1

R → Q: dbSNP rs35416389. Ref.19

VAR_042342

Natural variant

718

1

I → V: dbSNP rs2230539. Ref.19 Ref.5

VAR_042343

Natural variant

873

1

F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.19

VAR_042344

Natural variant

901

1

V → I: dbSNP rs10846. Ref.19 Ref.3 Ref.4

VAR_014937

Natural variant

921

1

A → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.19

VAR_042345

Experimental info

Mutagenesis

644

1

K → R: Substantial reduction of autophosphorylation. Ref.1

Sequence conflict

191

1

G → D in AAB33345. Ref.2

Sequence conflict

191

1

G → D in AAC50209. Ref.2

Sequence conflict

562

1

S → P in BAG36611. Ref.3

Sequence conflict

736

1

I → T Ref.5

Sequence conflict

750

1

T → A Ref.5

Sequence conflict

800

1

G → A Ref.5

Sequence conflict

812

1

E → G in BAG36611. Ref.3

Sequence conflict

887

1

L → P in BAG53845. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

942

Helix Strand Turn

Details...

Helix

15 – 18

4

Helix

29 – 66

38

Helix

71 – 95

25

Helix

124 – 153

30

Helix

160 – 192

33

Beta strand

194 – 196

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 61360295EC70BB8E	FASTA	942	103,932
	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
	Isoform 2. Checksum: 882D58AABCFDCEE1	FASTA	948	104,673
	10 20 30 40 50 60 MAEANNPSEQ ELESEPRSWS LLEQLGLAGA DLAAPGVQQQ LELERERLRR EIRKELKLKE 70 80 90 100 110 120 GAENLRRATT DLGRSLGPVE LLLRGSSRRL DLLHQQLQEL HAHVVLPDPA ATHDGPQSPG 130 140 150 160 170 180 AGGPTCSATN LSRVAGLEKQ LAIELKVKQG AENMIQTYSN GSTKDRKLLL TAQQMLQDSK 190 200 210 220 230 240 TKIDIIRMQL RRALQAGQLE NQAAPDDTQG SPDLGAVELR IEELRHHFRV EHAVAEGAKN 250 260 270 280 290 300 VLRLLSAAKA PDRKAVSEAQ EKLTESNQKL GLLREALERR LGELPADHPK GRLLREELAA 310 320 330 340 350 360 ASSAAFSTRL AGPFPATHYS TLCKPAPLTG TLEVRVVGCR DLPETIPWNP TPSMGGPGTP 370 380 390 400 410 420 DSRPPFLSRP ARGLYSRSGS LSGRSSLKAE AENTSEVSTV LKLDNTVVGQ TSWKPCGPNA 430 440 450 460 470 480 WDQSFTLELE RARELELAVF WRDQRGLCAL KFLKLEDFLD NERHEVQLDM EPQGCLVAEV 490 500 510 520 530 540 TFRNPVIERI PRLRRQKKIF SKQQGKAFQR ARQMNIDVAT WVRLLRRLIP NATGTGTFSP 550 560 570 580 590 600 GASPGSEART TGDISVEKLN LGTDSDSSPQ KSSRDPPSSP SSLSSPIQES TAPELPSETQ 610 620 630 640 650 660 ETPGPALCSP LRKSPLTLED FKFLAVLGRG HFGKVLLSEF RPSGELFAIK ALKKGDIVAR 670 680 690 700 710 720 DEVESLMCEK RILAAVTSAG HPFLVNLFGC FQTPEHVCFV MEYSAGGDLM LHIHSDVFSE 730 740 750 760 770 780 PRAIFYSACV VLGLQFLHEH KIVYRDLKLD NLLLDTEGYV KIADFGLCKE GMGYGDRTST 790 800 810 820 830 840 FCGTPEFLAP EVLTDTSYTR AVDWWGLGVL LYEMLVGESP FPGDDEEEVF DSIVNDEVRY 850 860 870 880 890 900 PRFLSAEAIG IMRRLLRRNP ERRLGSSERD AEDVKKQPFF RTLGWEALLA RRLPPPFVPT 910 920 930 940 LSGRTDVSNF DEEFTGEAPT LSPPRDARPL TAAEQAAFLD FDFVAGGC

References

	« Hide 'large scale' referencesShow '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: 8135837] [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: 7851406] [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. , 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: 14702039] [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 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] (ISOFORM 1), VARIANT ILE-901. Tissue: Brain.
[5]	"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] OF 700-800 (ISOFORMS 1/2), VARIANT VAL-718.
[6]	"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-916, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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-376, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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-562, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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-562 AND SER-916, MASS SPECTROMETRY.
[10]	"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 THR-778, MASS SPECTROMETRY.
[11]	"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-205; THR-353; SER-533; SER-537; SER-559 AND SER-916, MASS SPECTROMETRY.
[12]	"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-533; SER-537; SER-559; SER-562 AND SER-916, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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-533; SER-537; SER-559; SER-561; SER-562 AND SER-916, MASS SPECTROMETRY.
[15]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537; SER-559; SER-562; THR-914 AND SER-916, MASS SPECTROMETRY. Tissue: T-cell.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, MASS SPECTROMETRY.
[17]	"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: 10388627] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
[18]	"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: 14514689] [Abstract] Cited for: STRUCTURE BY NMR OF 116-199.
[19]	"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: 17344846] [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.
BC040061 mRNA. Translation: AAH40061.1.

IPI

IPI00002803.
IPI00412672.

PIR

JC2129.
S51162.

RefSeq

NP_002732.3.
NP_998725.1.

UniGene

Hs.466044

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CXZ	X-ray	2.20	B	13-98	[»]
1URF	NMR	-	A	122-199	[»]
2RMK	NMR	-	B	122-199	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16512. 9 interactions.

STRING

Q16512.

PTM databases

PhosphoSite

Q16512.

Proteomic databases

PRIDE

Q16512.

Genome annotation databases

Ensembl

ENST00000242783; ENSP00000242783; ENSG00000123143; Homo sapiens. [Genome view]
ENST00000342216; ENSP00000343325; ENSG00000123143; Homo sapiens. [Genome view]

GeneID

5585.

KEGG

hsa:5585.

Organism-specific databases

CTD

5585.

GeneCards

GC19P014406.

H-InvDB

HIX0027472.

HGNC

HGNC:9405. PKN1.

HPA

CAB010278.
HPA003982.

MIM

601032. gene.

PharmGKB

PA33769.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11664.

HOVERGEN

Q16512.

OMA

TRAGHPF.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.
p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.

Gene expression databases

ArrayExpress

Q16512.

Bgee

Q16512.

CleanEx

HS_PKN1.

Genevestigator

Q16512.

GermOnline

ENSG00000123143. Homo sapiens.

Family and domain databases

InterPro

IPR000961. 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]

Gene3D

G3DSA:1.10.287.160. HR1_rho-bd. 3 hits.

Pfam

PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

SMART

SM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS51285. 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]

ProtoNet

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Other Resources

NextBio

21660.

PMAP-CutDB

Q16512.

SOURCE

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Entry information

Entry name

PKN1_HUMAN

Accession

Primary (citable) accession number: Q16512
Secondary accession number(s): A8K7W5 , B2R9R4, B3KVN3, Q15143, Q8IUV5, Q9UD44

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	September 22, 2009
Last modified:	January 19, 2010
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.