Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q63433 (PKN1_RAT)

Entry version 177 (02 Dec 2020)
Sequence version 2 (18 May 2010)
Previous versions | rss
Add a publicationFeedback
Protein

Serine/threonine-protein kinase N1

Gene

Pkn1

Organism
Rattus norvegicus (Rat)
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 involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation (PubMed:8051089, PubMed:15375078). Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14 (By similarity). 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 (By similarity).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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 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-778 (activation loop of the kinase domain) and Ser-920 (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%5Fsection">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 sitei648ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei744Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi625 – 633ATPPROSITE-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionChromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.13, 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-5625740, RHO GTPases activate PKNs
R-RNO-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3

<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%5Fand%5Ftaxonomy%5Fsection">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 N1 (EC:2.7.11.131 Publication)
Alternative name(s):
Protease-activated kinase 1
Short name:
PAK-1
Protein kinase C-like 1
Protein kinase C-like PKN
Protein-kinase C-related kinase 1
Serine-threonine protein kinase N
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Pkn1
Synonyms:Pkn, Prk1, Prkcl1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 19

Organism-specific databases

Rat genome database

More...RGDi		69308, Pkn1

<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 membrane, Cytoplasm, Endosome, Membrane, Nucleus

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000557212 – 946Serine/threonine-protein kinase N1Add BLAST945

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 residuei2N-acetylalanineBy similarity1
Modified residuei69PhosphoserineBy similarity1
Modified residuei377Phosphoserine1 Publication1
Modified residuei451N6-acetyllysineBy similarity1
Modified residuei536PhosphoserineBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei543PhosphoserineBy similarity1
Modified residuei562PhosphoserineBy similarity1
Modified residuei565PhosphoserineBy similarity1
Modified residuei612PhosphoserineBy similarity1
Modified residuei778Phosphothreonine; by PDPK1By similarity1
Modified residuei782PhosphothreonineBy similarity1
Modified residuei918PhosphothreonineBy similarity1
Modified residuei920PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Autophosphorylated; preferably on serine. Phosphorylated during mitosis.By similarity
Activated by limited proteolysis with trypsin.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>Sitei108 – 109Cleavage; by caspase-3By similarity2
Sitei457 – 458Cleavage; by caspase-3By similarity2
Sitei561 – 562Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q63433

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

More...PaxDbi		Q63433

PRoteomics IDEntifications database

More...PRIDEi		Q63433

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q63433

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

More...PhosphoSitePlusi		Q63433

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000004131, Expressed in thymus and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q63433, RN

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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.

Interacts (via C-terminus) with PDPK1.

Interacts with CCNT2; enhances MYOD1-dependent transcription.

Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		248010, 1 interactor

Database of interacting proteins

More...DIPi		DIP-60097N

Protein interaction database and analysis system

More...IntActi		Q63433, 9 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000005770

<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		Q63433

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%5Fand%5Fdomains%5Fsection">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>Domaini25 – 100REM-1 1PROSITE-ProRule annotationAdd BLAST76
Domaini114 – 193REM-1 2PROSITE-ProRule annotationAdd BLAST80
Domaini202 – 283REM-1 3PROSITE-ProRule annotationAdd BLAST82
Domaini310 – 473C2PROSITE-ProRule annotationAdd BLAST164
Domaini619 – 878Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini879 – 946AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST68

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

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0694, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154990

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_132_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q63433

Identification of Orthologs from Complete Genome Data

More...OMAi		WNPSPSG

Database of Orthologous Groups

More...OrthoDBi		520651at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd08687, C2_PKN-like, 1 hit
cd11630, HR1_PKN1_2, 1 hit
cd11622, HR1_PKN_1, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000961, AGC-kinase_C
IPR037784, C2_PKN
IPR011072, HR1_rho-bd
IPR036274, HR1_rpt_sf
IPR011009, Kinase-like_dom_sf
IPR017892, Pkinase_C
IPR037317, PKN1_HR1_2
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

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

Superfamily database of structural and functional annotation

More...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
PS50004, C2, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q63433-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL 
        60         70         80         90        100
KLKEGAENLR RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL 
       110        120        130        140        150
PDPTAGSDAP QSLAEGSPVC SSTNLSRVAG LEKQLAIELK VKQGAENMIQ 
       160        170        180        190        200
TYSNGSTKDR KLLLTAQQML QDSKTKIDII RMQLRRALQA LQAGQLESQA 
       210        220        230        240        250
APDEAHGDPD LGAVELRIEE LRHHFRVEHA VAEGAKNVLR LLSAAKAPDR 
       260        270        280        290        300
KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS 
       310        320        330        340        350
AAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS 
       360        370        380        390        400
VGASGTPDSR TPFLSRPARG LYNRSGSLSG RSSLKGEAEN STEVSTVLKL 
       410        420        430        440        450
DNTVVGQTAW KPCGPNAWDQ SFTLELERAR ELELAVFWRD QRGLCALKFL 
       460        470        480        490        500
KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR NPIIERIPRL QRQKKIFSKQ 
       510        520        530        540        550
QGQTFQRARQ MNIDVATWVR LLRRLIPNAV ATGSFSPNAS PGSEIRSTGD 
       560        570        580        590        600
ISMEKLNLGA DSDSSSQKSP AGLPSTSCSL SSPTHESTTS PELPSETQET 
       610        620        630        640        650
PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFHS SGELFAIKAL 
       660        670        680        690        700
KKGDIVARDE VESLMCEKRI LATVTRAGHP FLVNLFGCFQ TPEHVCFVME 
       710        720        730        740        750
YSAGGDLMLH IHSDVFSEPR AVFYSACVVL GLQFLHEHKI VYRDLKLDNL 
       760        770        780        790        800
LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC GTPEFLAPEV LTDTSYTRAV 
       810        820        830        840        850
DWWGLGVLLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR FLSAEAIGIM 
       860        870        880        890        900
RRLLRRNPER RLGSTERDAE DVKKQPFFRT LDWDALLARR LPPPFVPTLS 
       910        920        930        940 
GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY
Length:946
Mass (Da):104,468
Last modified:May 18, 2010 - v2
<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:i63DF250C8D2DA444
GO

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 conflicti298A → R in AAL31374 (PubMed:8943281).Curated1
Sequence conflicti510Q → H in BAA05168 (PubMed:8135837).Curated1
Sequence conflicti650L → V in AAL31374 (PubMed:8943281).Curated1
Sequence conflicti722V → G in BAA05168 (PubMed:8135837).Curated1
Sequence conflicti808L → F in BAA05168 (PubMed:8135837).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D26180 mRNA Translation: BAA05168.1
L35634 mRNA Translation: AAL31374.1
BC061836 mRNA Translation: AAH61836.1

Protein sequence database of the Protein Information Resource

More...PIRi		JC2130

NCBI Reference Sequences

More...RefSeqi		NP_058871.2, NM_017175.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131

Database of genes from NCBI RefSeq genomes

More...GeneIDi		29355

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:29355

<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
D26180 mRNA Translation: BAA05168.1
L35634 mRNA Translation: AAL31374.1
BC061836 mRNA Translation: AAH61836.1
PIRiJC2130
RefSeqiNP_058871.2, NM_017175.2

3D structure databases

SMRiQ63433
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi248010, 1 interactor
DIPiDIP-60097N
IntActiQ63433, 9 interactors
STRINGi10116.ENSRNOP00000005770

PTM databases

iPTMnetiQ63433
PhosphoSitePlusiQ63433

Proteomic databases

jPOSTiQ63433
PaxDbiQ63433
PRIDEiQ63433

Genome annotation databases

EnsembliENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131
GeneIDi29355
KEGGirno:29355

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5585
RGDi69308, Pkn1

Phylogenomic databases

eggNOGiKOG0694, Eukaryota
GeneTreeiENSGT00940000154990
HOGENOMiCLU_000288_132_1_1
InParanoidiQ63433
OMAiWNPSPSG
OrthoDBi520651at2759

Enzyme and pathway databases

BRENDAi2.7.11.13, 5301
ReactomeiR-RNO-5625740, RHO GTPases activate PKNs
R-RNO-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q63433

Gene expression databases

BgeeiENSRNOG00000004131, Expressed in thymus and 20 other tissues
GenevisibleiQ63433, RN

Family and domain databases

CDDicd08687, C2_PKN-like, 1 hit
cd11630, HR1_PKN1_2, 1 hit
cd11622, HR1_PKN_1, 1 hit
InterProiView protein in InterPro
IPR000961, AGC-kinase_C
IPR037784, C2_PKN
IPR011072, HR1_rho-bd
IPR036274, HR1_rpt_sf
IPR011009, Kinase-like_dom_sf
IPR017892, Pkinase_C
IPR037317, PKN1_HR1_2
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
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
PS50004, C2, 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 nameiPKN1_RAT
<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: Q63433
Secondary accession number(s): Q6P748, Q8VIJ2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: December 2, 2020
This is version 177 of the entry and version 2 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again