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Entry version 159 (13 Nov 2019)
Sequence version 3 (27 Jul 2011)
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Protein

Serine/threonine-protein kinase N2

Gene

Pkn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (By similarity).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Kinase activity is activated upon binding to GTP-bound Rho1/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-815 (activation loop of the kinase domain) and Thr-957 (turn motif), need to be phosphorylated for its full activation (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei685ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei781Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi662 – 670ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell adhesion, Cell cycle, Cell division, Cilium biogenesis/degradation, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-5625740 RHO GTPases activate PKNs

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein kinase N2 (EC:2.7.11.13)
Alternative name(s):
PKN gamma
Protein kinase C-like 2
Protein-kinase C-related kinase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Pkn2
Synonyms:Prk2, Prkcl2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:109211 Pkn2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi66A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155. 1 Publication1
Mutagenesisi155A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60. 1 Publication1
Mutagenesisi685K → M: Prevents apical junction formation. 1 Publication1
Mutagenesisi781D → A: Prevents apical junction formation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000557231 – 983Serine/threonine-protein kinase N2Add BLAST983

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei77N6-acetyllysineCombined sources1
Modified residuei110PhosphoserineBy similarity1
Modified residuei121PhosphothreonineBy similarity1
Modified residuei124PhosphothreonineBy similarity1
Modified residuei301PhosphoserineBy similarity1
Modified residuei305PhosphoserineBy similarity1
Modified residuei359PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei534PhosphoserineBy similarity1
Modified residuei582PhosphoserineBy similarity1
Modified residuei619PhosphoserineCombined sources1
Modified residuei630PhosphoserineBy similarity1
Modified residuei815Phosphothreonine; by PDPK1By similarity1
Modified residuei951PhosphoserineBy similarity1
Modified residuei957PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Phosphorylated by CDK10 (By similarity).By similarity
Activated by limited proteolysis with trypsin. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei117 – 118Cleavage; by caspase-3By similarity2
Sitei699 – 700Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8BWW9

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q8BWW9

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8BWW9

PeptideAtlas

More...
PeptideAtlasi
Q8BWW9

PRoteomics IDEntifications database

More...
PRIDEi
Q8BWW9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8BWW9

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8BWW9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000004591 Expressed in 258 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8BWW9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8BWW9 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially) and interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation (PubMed:17403031, PubMed:20974804).

Interacts with NCK1 (via SH3 domains) (PubMed:8910519).

Interacts with RHOC.

Interacts with NCK1 and NCK2 (By similarity).

Interacts with CD44 (PubMed:17403031).

Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity (By similarity).

Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity (PubMed:10818102).

Interacts (via C-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells.

Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain).

Interacts with CDK10 (By similarity).

By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
224651, 2 interactors

Protein interaction database and analysis system

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IntActi
Q8BWW9, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000039566

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8BWW9

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini33 – 109REM-1 1PROSITE-ProRule annotationAdd BLAST77
Domaini121 – 203REM-1 2PROSITE-ProRule annotationAdd BLAST83
Domaini204 – 284REM-1 3PROSITE-ProRule annotationAdd BLAST81
Domaini329 – 462C2Add BLAST134
Domaini656 – 915Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini916 – 983AGC-kinase C-terminalAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni381 – 462Necessary to rescue apical junction formationAdd BLAST82
Regioni916 – 976Necessary for the catalytic activityBy similarityAdd BLAST61
Regioni977 – 983Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoABy similarity7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2.By similarity
The C1 domain does not bind the diacylglycerol (DAG).
The apoptotic C-terminal cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0694 Eukaryota
ENOG410XNPH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154339

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233032

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8BWW9

KEGG Orthology (KO)

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KOi
K23691

Identification of Orthologs from Complete Genome Data

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OMAi
RHISWEW

Database of Orthologous Groups

More...
OrthoDBi
520651at2759

TreeFam database of animal gene trees

More...
TreeFami
TF102005

Family and domain databases

Conserved Domains Database

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CDDi
cd08687 C2_PKN-like, 1 hit
cd11622 HR1_PKN_1, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000961 AGC-kinase_C
IPR000008 C2_dom
IPR037784 C2_PKN
IPR011072 HR1_rho-bd
IPR036274 HR1_rpt_sf
IPR011009 Kinase-like_dom_sf
IPR017892 Pkinase_C
IPR037313 PKN_HR1_1
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02185 HR1, 3 hits
PF00069 Pkinase, 1 hit
PF00433 Pkinase_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00239 C2, 1 hit
SM00742 Hr1, 3 hits
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46585 SSF46585, 3 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS51860 REM_1, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8BWW9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD
60 70 80 90 100
RIKREIRKEL KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL
110 120 130 140 150
QELNAHIVVS DPEDSTDCPR TPDTPNSDSR SSTSNNRLMA LQKQLDIELK
160 170 180 190 200
VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL QDSKTKIEVI RMQILQAVQT
210 220 230 240 250
NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM KLLGSGKVTD
260 270 280 290 300
RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA
310 320 330 340 350
SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA
360 370 380 390 400
TSVALPGWSP SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN
410 420 430 440 450
TVVGQTSWKP ISNQSWDQKF TLELDRSREL EISVYWRDWR SLCAVKFLRL
460 470 480 490 500
EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP VIERRPKLQR QKKIFSKQQG
510 520 530 540 550
KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP ATVPVVDARI
560 570 580 590 600
PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ
610 620 630 640 650
GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ
660 670 680 690 700
FSLQDFRCCA VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS
710 720 730 740 750
LMCEKRIFET VNSVRHPFLV NLFACFQTKE HVCFVMEYAA GGDLMMHIHT
760 770 780 790 800
DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR DLKLDNLLLD TEGFVKIADF
810 820 830 840 850
GLCKEGMGYG DRTSTFCGTP EFLAPEVLTE TSYTRAVDWW GLGVLIYEML
860 870 880 890 900
VGESPFPGDD EEEVFDSIVN DEVRYPRFLS TEAISIMRRL LRRNPERRLG
910 920 930 940 950
AGEKDAEDVK KHPFFRLTDW SALMDKKVKP PFVPTIRGRE DVSNFDDEFT
960 970 980
SEAPILTPPR EPRILLEEEQ EMFHDFDYVA DWC
Length:983
Mass (Da):111,607
Last modified:July 27, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3961FD79D2718609
GO
Isoform 2 (identifier: Q8BWW9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-45: Missing.

Note: No experimental confirmation available.
Show »
Length:972
Mass (Da):110,313
Checksum:iD2806BCD710C1B29
GO
Isoform 3 (identifier: Q8BWW9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     781-787: DLKLDNL → NTIFSSI
     788-983: Missing.

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Length:787
Mass (Da):88,961
Checksum:i6B762C942B96D5EF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3UZM9G3UZM9_MOUSE
Serine/threonine-protein kinase N2
Pkn2
967Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3UXH4G3UXH4_MOUSE
Serine/threonine-protein kinase N2
Pkn2
935Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3UYE1G3UYE1_MOUSE
Serine/threonine-protein kinase N2
Pkn2
37Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3UYD6G3UYD6_MOUSE
Serine/threonine-protein kinase N2
Pkn2
210Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3UWT9G3UWT9_MOUSE
Serine/threonine-protein kinase N2
Pkn2
29Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti32Q → H in BAC32655 (PubMed:16141072).Curated1
Sequence conflicti84N → H in BAC33888 (PubMed:16141072).Curated1
Sequence conflicti395V → D in BAC38910 (PubMed:16141072).Curated1
Sequence conflicti569L → F in BAC32655 (PubMed:16141072).Curated1
Sequence conflicti704E → K in BAC33888 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_01204235 – 45Missing in isoform 2. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_042185781 – 787DLKLDNL → NTIFSSI in isoform 3. 1 Publication7
Alternative sequenceiVSP_042186788 – 983Missing in isoform 3. 1 PublicationAdd BLAST196

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AK046248 mRNA Translation: BAC32655.1
AK133298 mRNA Translation: BAE21599.1
AK171092 mRNA Translation: BAE42244.1
AK049713 mRNA Translation: BAC33888.1
AK083425 mRNA Translation: BAC38910.1
BC052073 mRNA Translation: AAH52073.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS51084.1 [Q8BWW9-1]

NCBI Reference Sequences

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RefSeqi
NP_848769.2, NM_178654.4 [Q8BWW9-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591 [Q8BWW9-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
109333

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:109333

UCSC genome browser

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UCSCi
uc008rpe.2 mouse [Q8BWW9-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046248 mRNA Translation: BAC32655.1
AK133298 mRNA Translation: BAE21599.1
AK171092 mRNA Translation: BAE42244.1
AK049713 mRNA Translation: BAC33888.1
AK083425 mRNA Translation: BAC38910.1
BC052073 mRNA Translation: AAH52073.1
CCDSiCCDS51084.1 [Q8BWW9-1]
RefSeqiNP_848769.2, NM_178654.4 [Q8BWW9-1]

3D structure databases

SMRiQ8BWW9
ModBaseiSearch...

Protein-protein interaction databases

BioGridi224651, 2 interactors
IntActiQ8BWW9, 1 interactor
STRINGi10090.ENSMUSP00000039566

PTM databases

iPTMnetiQ8BWW9
PhosphoSitePlusiQ8BWW9

Proteomic databases

EPDiQ8BWW9
jPOSTiQ8BWW9
PaxDbiQ8BWW9
PeptideAtlasiQ8BWW9
PRIDEiQ8BWW9

Genome annotation databases

EnsembliENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591 [Q8BWW9-1]
GeneIDi109333
KEGGimmu:109333
UCSCiuc008rpe.2 mouse [Q8BWW9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5586
MGIiMGI:109211 Pkn2

Phylogenomic databases

eggNOGiKOG0694 Eukaryota
ENOG410XNPH LUCA
GeneTreeiENSGT00940000154339
HOGENOMiHOG000233032
InParanoidiQ8BWW9
KOiK23691
OMAiRHISWEW
OrthoDBi520651at2759
TreeFamiTF102005

Enzyme and pathway databases

ReactomeiR-MMU-5625740 RHO GTPases activate PKNs

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Pkn2 mouse

Protein Ontology

More...
PROi
PR:Q8BWW9

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000004591 Expressed in 258 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ8BWW9 baseline and differential
GenevisibleiQ8BWW9 MM

Family and domain databases

CDDicd08687 C2_PKN-like, 1 hit
cd11622 HR1_PKN_1, 1 hit
InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR000008 C2_dom
IPR037784 C2_PKN
IPR011072 HR1_rho-bd
IPR036274 HR1_rpt_sf
IPR011009 Kinase-like_dom_sf
IPR017892 Pkinase_C
IPR037313 PKN_HR1_1
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF02185 HR1, 3 hits
PF00069 Pkinase, 1 hit
PF00433 Pkinase_C, 1 hit
SMARTiView protein in SMART
SM00239 C2, 1 hit
SM00742 Hr1, 3 hits
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF46585 SSF46585, 3 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS51860 REM_1, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPKN2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8BWW9
Secondary accession number(s): Q3TBR3
, Q80WS2, Q8BJL7, Q8BL62
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 27, 2011
Last modified: November 13, 2019
This is version 159 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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