A1A4I4 (PKN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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-like PKN
Protein kinase PKN-alpha
Protein-kinase C-related kinase 1
Serine-threonine protein kinase N

Gene names

Name:	PKN1
Synonyms:	PKN, PRK1, PRKCL1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	944 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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', and GFAP. Able to phosphorylate RPS6 in vitro By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
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-776 (activation loop of the kinase domain) and Ser-918 (turn motif), need to be phosphorylated for its full activation By similarity.
Subunit structure	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. Interacts with ZA20D3 By similarity. Interacts (via C-terminus) with PDPK1.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Endosome By similarity. Cell membrane; Peripheral membrane protein By similarity. Cleavage furrow By similarity. Midbody By similarity. Note: Associates with chromatin in a ligand-dependent manner By similarity. Localization to endosomes is mediated via its interaction with RHOB By similarity. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis By similarity.
Domain	The C1 domain does not bind the diacylglycerol (DAG) By similarity.
Post-translational modification	Autophosphorylated; preferably on serine. Phosphorylated during mitosis By similarity. 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
Biological process	Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Endosome Membrane Nucleus
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB hyperosmotic response Inferred from electronic annotation. Source: Compara regulation of cell motility Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: Compara endosome Inferred from sequence or structural similarity. Source: UniProtKB midbody Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP-Rho binding Inferred from sequence or structural similarity. Source: UniProtKB Rac GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB androgen receptor binding Inferred from sequence or structural similarity. Source: UniProtKB chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB histone binding Inferred from sequence or structural similarity. Source: UniProtKB histone deacetylase binding Inferred from sequence or structural similarity. Source: UniProtKB histone kinase activity (H3-T11 specific) Inferred from sequence or structural similarity. Source: UniProtKB ligand-dependent nuclear receptor transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 944	944	Serine/threonine-protein kinase N1		PRO_0000394261
Regions
	Repeat	34 – 111	78	REM 1
	Repeat	124 – 210	87	REM 2
	Repeat	211 – 292	82	REM 3
	Domain	326 – 462	137	C2
	Domain	617 – 876	260	Protein kinase
	Domain	877 – 944	68	AGC-kinase C-terminal
	Nucleotide binding	623 – 631	9	ATP By similarity
Sites
	Active site	742	1	Proton acceptor By similarity
	Binding site	646	1	ATP By similarity
	Site	109 – 110	2	Cleavage; by caspase-3 By similarity
	Site	455 – 456	2	Cleavage; by caspase-3 By similarity
	Site	559 – 560	2	Cleavage; by caspase-3 By similarity
Amino acid modifications
	Modified residue	206	1	Phosphoserine By similarity
	Modified residue	375	1	Phosphoserine By similarity
	Modified residue	449	1	N6-acetyllysine By similarity
	Modified residue	534	1	Phosphoserine By similarity
	Modified residue	538	1	Phosphoserine By similarity
	Modified residue	563	1	Phosphoserine By similarity
	Modified residue	776	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	780	1	Phosphothreonine By similarity
	Modified residue	916	1	Phosphothreonine By similarity
	Modified residue	918	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1A4I4 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 11B6833ED4F8D57E	FASTA	944	104,133
	10 20 30 40 50 60 MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR 70 80 90 100 110 120 RATTDLGRNL GPVELVLRGS SRRLALLHQQ LQELHAHVVL PDPAVGVHDA PQSPGTGDSA 130 140 150 160 170 180 CSATNLSRVA GLEKQLAIEL KVKQGAENMI QTYSNGSTKD RKLLLTAQQM LQDSKTKIDI 190 200 210 220 230 240 IRMQLHRALQ ACQLESQAAP DEAQGSPDLG AVELRIEELR HHFRVEHAVA EGAKNVLRLL 250 260 270 280 290 300 SAAKAPDRKA VSEAQEKLTE SNQKLGLLRE ALERRLGELP ADHPKGRLLR EELAAASSAA 310 320 330 340 350 360 FSARLAGPFP ATHYSTLSKP APLTGTLEVR VVGCRDLPET IPWNPSPSVG GPGTPDSRTP 370 380 390 400 410 420 FLSRPARGLY SRTGSLSGRS SLKAEAENTN EVSTVLKLDN TVVGQTSWKP CGPNAWDQSF 430 440 450 460 470 480 TLELERAREL ELAVFWRDQR GLCALKFLKL EDFLDNERHE VQLDMEPQGC LVAEVTFRNP 490 500 510 520 530 540 VIERIPRLRR QKKIFSKQQG KAFQRARQMN IDVATWVRLL RRLIPNATAT GTFSPGASPG 550 560 570 580 590 600 PEARSTGDIS VEKLNLGTET DSSPQKSPLG PPSSPSSLSS PIQATTTTPE LPSETQETPG 610 620 630 640 650 660 PTLCSPLRKS PLTLEDFKFL AVLGRGHFGK VLLSEFRPSG ELFAIKALKK GDIVARDEVE 670 680 690 700 710 720 SLMCEKRILA AVTNAGHPFL VNLFGCFQTP EHVCFVMEYS AGGDLMLHIH SDVFSEPRAV 730 740 750 760 770 780 FYSACVVLGL QFLHEHKIVY RDLKLDNLLL DTEGYVKIAD FGLCKEGMGY GDRTSTFCGT 790 800 810 820 830 840 PEFLAPEVLT DTSYTRAVDW WGLGVLLYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL 850 860 870 880 890 900 SAEAIGIMRR LLRRNPERRL GSSERDAEDV KKQPFFRTLG WDALLARRLP PPFVPTLAGR 910 920 930 940 TDVSNFDEEF TGEAPTLSPP RDARPLTATE QAAFRDFDFV AGSC

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC126539 mRNA. Translation: AAI26540.1.
IPI	IPI00696739.
RefSeq	NP_001073715.1. NM_001080246.1.
UniGene	Bt.4993.
3D structure databases
ProteinModelPortal	A1A4I4.
SMR	A1A4I4. Positions 13-98, 123-200.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000022652.
Proteomic databases
PRIDE	A1A4I4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	509080.
KEGG	bta:509080.
Organism-specific databases
CTD	5585.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233032.
HOVERGEN	HBG108317.
InParanoid	A1A4I4.
KO	K06071.
OrthoDB	EOG4VDPXV.
Gene expression databases
ArrayExpress	A1A4I4.
Family and domain databases
Gene3D	1.10.287.160. 3 hits.
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR011072. HR1_rho-bd. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
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]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF56112. Kinase_like. 1 hit. SSF46585. PKN_effector. 3 hits.
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	Search...
Other
NextBio	20868812.

Entry information

Entry name

PKN1_BOVIN

Accession

Primary (citable) accession number: A1A4I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program