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UniProtKB - Q16512 (PKN1_HUMAN)

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Protein

Serine/threonine-protein kinase N1

Gene

PKN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. 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.11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme 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-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation.2 Publications

Kineticsi

  1. KM=20.6 µM for HDAC51 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei644ATPPROSITE-ProRule annotation1
    Active sitei740Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi621 – 629ATPPROSITE-ProRule annotation9

    GO - Molecular functioni

    • androgen receptor binding Source: UniProtKB
    • ATP binding Source: UniProtKB-KW
    • chromatin binding Source: UniProtKB
    • GTP-Rho binding Source: UniProtKB
    • histone binding Source: UniProtKB
    • histone deacetylase binding Source: UniProtKB
    • histone kinase activity (H3-T11 specific) Source: UniProtKB
    • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    • protein kinase activity Source: ProtInc
    • protein kinase C activity Source: UniProtKB-EC
    • protein kinase C binding Source: UniProtKB
    • protein serine/threonine kinase activity Source: UniProtKB
    • Rac GTPase binding Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    • activation of JUN kinase activity Source: ProtInc
    • B cell apoptotic process Source: Ensembl
    • B cell homeostasis Source: Ensembl
    • epithelial cell migration Source: UniProtKB
    • histone H3-T11 phosphorylation Source: UniProtKB
    • hyperosmotic response Source: Ensembl
    • negative regulation of B cell proliferation Source: Ensembl
    • negative regulation of protein kinase activity Source: Ensembl
    • peptidyl-serine phosphorylation Source: GO_Central
    • protein phosphorylation Source: UniProtKB
    • regulation of cell motility Source: UniProtKB
    • regulation of germinal center formation Source: Ensembl
    • regulation of immunoglobulin production Source: Ensembl
    • regulation of transcription by RNA polymerase II Source: UniProtKB
    • renal system process Source: Ensembl
    • signal transduction Source: ProtInc
    • spleen development Source: Ensembl
    • transcription, DNA-templated Source: UniProtKB-KW
    View the complete GO annotation on QuickGO ...

    Keywordsi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.13 2681
    ReactomeiR-HSA-5625740 RHO GTPases activate PKNs
    R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
    SABIO-RKiQ16512
    SignaLinkiQ16512
    SIGNORiQ16512

    Names & Taxonomyi

    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 PKN-alpha
    Protein-kinase C-related kinase 1
    Serine-threonine protein kinase N
    Gene namesi
    Name:PKN1
    Synonyms:PAK1, PKN, PRK1, PRKCL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    Proteomesi
    • UP000005640 Componenti: Chromosome 19

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000123143.12
    HGNCiHGNC:9405 PKN1
    MIMi601032 gene
    neXtProtiNX_Q16512

    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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi108D → A: Abolishes cleavage by caspase-3 and formation of AF1 fragment. 1 Publication1
    Mutagenesisi181R → A: Abolishes interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi181R → K: Decreases interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi185R → A: Abolishes interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi451D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication1
    Mutagenesisi454D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication1
    Mutagenesisi558D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication1
    Mutagenesisi560D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication1
    Mutagenesisi644K → E: Abolishes Serine/threonine-protein kinase activity. 2 Publications1
    Mutagenesisi644K → R: Substantial reduction of autophosphorylation. 2 Publications1

    Organism-specific databases

    DisGeNETi5585
    OpenTargetsiENSG00000123143
    PharmGKBiPA33769

    Chemistry databases

    ChEMBLiCHEMBL3384
    GuidetoPHARMACOLOGYi1520

    Polymorphism and mutation databases

    BioMutaiPKN1
    DMDMi259016304

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000557192 – 942Serine/threonine-protein kinase N1Add BLAST941

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei69PhosphoserineCombined sources1
    Modified residuei205PhosphoserineCombined sources1
    Modified residuei374PhosphoserineBy similarity1
    Modified residuei448N6-acetyllysineCombined sources1
    Modified residuei533PhosphoserineCombined sources1
    Modified residuei537PhosphoserineCombined sources1
    Modified residuei540PhosphoserineCombined sources1
    Modified residuei559PhosphoserineCombined sources1
    Modified residuei562PhosphoserineCombined sources1
    Modified residuei608PhosphoserineCombined sources1
    Modified residuei774Phosphothreonine; by PDPK11 Publication1
    Modified residuei778PhosphothreonineCombined sources1
    Modified residuei914PhosphothreonineCombined sources1
    Modified residuei916PhosphoserineCombined sources1

    Post-translational modificationi

    Autophosphorylated; preferably on serine. Phosphorylated during mitosis.2 Publications
    Activated by limited proteolysis with trypsin.By similarity
    (Microbial infection) In case of infection, polyubiquitinated by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its proteasomal degradation.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei108 – 109Cleavage; by caspase-32
    Sitei454 – 455Cleavage; by caspase-32
    Sitei558 – 559Cleavage; by caspase-32

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiQ16512
    MaxQBiQ16512
    PaxDbiQ16512
    PeptideAtlasiQ16512
    PRIDEiQ16512
    ProteomicsDBi60877
    60878 [Q16512-2]
    60879 [Q16512-3]

    PTM databases

    iPTMnetiQ16512
    PhosphoSitePlusiQ16512

    Miscellaneous databases

    PMAP-CutDBiQ16512

    Expressioni

    Tissue specificityi

    Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells.1 Publication

    Gene expression databases

    BgeeiENSG00000123143
    CleanExiHS_PKN1
    ExpressionAtlasiQ16512 baseline and differential
    GenevisibleiQ16512 HS

    Organism-specific databases

    HPAiCAB010278
    HPA003982

    Interactioni

    Subunit structurei

    Interacts with ZFAND6 (By similarity). Interacts with ANDR (PubMed:12514133). Interacts with PRKCB (PubMed:20228790). Interacts (via REM 1 and REM 2 repeats) with RAC1 (PubMed:14514689, PubMed:18006505). Interacts (via REM 1 repeat) with RHOA (PubMed:10619026, PubMed:8571126). Interacts with RHOB (PubMed:9478917). Interacts (via C-terminus) with PDPK1 (PubMed:10792047). Interacts with CCNT2; enhances MYOD1-dependent transcription (PubMed:16331689). 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 (PubMed:21224381).By similarity10 Publications
    (Microbial infection) Interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region) (PubMed:16611232, PubMed:24248594).2 Publications

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • androgen receptor binding Source: UniProtKB
    • GTP-Rho binding Source: UniProtKB
    • histone binding Source: UniProtKB
    • histone deacetylase binding Source: UniProtKB
    • protein kinase C binding Source: UniProtKB
    • Rac GTPase binding Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    BioGridi111571, 65 interactors
    DIPiDIP-34240N
    ELMiQ16512
    IntActiQ16512, 72 interactors
    MINTiQ16512
    STRINGi9606.ENSP00000343325

    Chemistry databases

    BindingDBiQ16512

    Structurei

    Secondary structure

    1942
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi15 – 18Combined sources4
    Helixi29 – 66Combined sources38
    Helixi71 – 95Combined sources25
    Turni122 – 124Combined sources3
    Helixi126 – 151Combined sources26
    Turni157 – 159Combined sources3
    Helixi160 – 187Combined sources28
    Beta strandi194 – 196Combined sources3
    Helixi612 – 614Combined sources3
    Beta strandi615 – 624Combined sources10
    Beta strandi627 – 634Combined sources8
    Turni635 – 637Combined sources3
    Beta strandi640 – 647Combined sources8
    Helixi648 – 653Combined sources6
    Helixi657 – 671Combined sources15
    Turni672 – 674Combined sources3
    Beta strandi681 – 686Combined sources6
    Beta strandi688 – 696Combined sources9
    Beta strandi700 – 702Combined sources3
    Helixi703 – 706Combined sources4
    Turni707 – 709Combined sources3
    Helixi714 – 733Combined sources20
    Helixi743 – 745Combined sources3
    Beta strandi746 – 748Combined sources3
    Beta strandi750 – 752Combined sources3
    Beta strandi754 – 756Combined sources3
    Beta strandi763 – 765Combined sources3
    Helixi779 – 781Combined sources3
    Helixi784 – 788Combined sources5
    Helixi794 – 810Combined sources17
    Helixi820 – 829Combined sources10
    Helixi840 – 849Combined sources10
    Turni854 – 856Combined sources3
    Turni862 – 864Combined sources3
    Helixi865 – 869Combined sources5
    Helixi872 – 874Combined sources3
    Helixi879 – 883Combined sources5
    Helixi906 – 909Combined sources4
    Helixi926 – 930Combined sources5
    Turni931 – 934Combined sources4

    3D structure databases

    ProteinModelPortaliQ16512
    SMRiQ16512
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16512

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini25 – 100REM-1 1PROSITE-ProRule annotationAdd BLAST76
    Domaini112 – 193REM-1 2PROSITE-ProRule annotationAdd BLAST82
    Domaini201 – 280REM-1 3PROSITE-ProRule annotationAdd BLAST80
    Domaini325 – 461C2Add BLAST137
    Domaini615 – 874Protein kinasePROSITE-ProRule annotationAdd BLAST260
    Domaini875 – 942AGC-kinase C-terminalAdd BLAST68

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni181 – 185Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination1 Publication5

    Domaini

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

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiKOG0694 Eukaryota
    ENOG410XNPH LUCA
    GeneTreeiENSGT00920000149020
    HOVERGENiHBG108317
    InParanoidiQ16512
    KOiK06071
    OMAiTMYAIKA
    OrthoDBiEOG091G00YT
    PhylomeDBiQ16512
    TreeFamiTF102005

    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
    PS00107 PROTEIN_KINASE_ATP, 1 hit
    PS50011 PROTEIN_KINASE_DOM, 1 hit
    PS00108 PROTEIN_KINASE_ST, 1 hit
    PS51860 REM_1, 3 hits

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q16512-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL 
            60         70         80         90        100
    KLKEGAENLR RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL 
           110        120        130        140        150
    PDPAATHDGP QSPGAGGPTC SATNLSRVAG LEKQLAIELK VKQGAENMIQ 
           160        170        180        190        200
    TYSNGSTKDR KLLLTAQQML QDSKTKIDII RMQLRRALQA GQLENQAAPD 
           210        220        230        240        250
    DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS AAKAPDRKAV 
           260        270        280        290        300
    SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF 
           310        320        330        340        350
    STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG 
           360        370        380        390        400
    PGTPDSRPPF LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT 
           410        420        430        440        450
    VVGQTSWKPC GPNAWDQSFT LELERARELE LAVFWRDQRG LCALKFLKLE 
           460        470        480        490        500
    DFLDNERHEV QLDMEPQGCL VAEVTFRNPV IERIPRLRRQ KKIFSKQQGK 
           510        520        530        540        550
    AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS EARTTGDISV 
           560        570        580        590        600
    EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA 
           610        620        630        640        650
    LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD 
           660        670        680        690        700
    IVARDEVESL MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG 
           710        720        730        740        750
    GDLMLHIHSD VFSEPRAIFY SACVVLGLQF LHEHKIVYRD LKLDNLLLDT 
           760        770        780        790        800
    EGYVKIADFG LCKEGMGYGD RTSTFCGTPE FLAPEVLTDT SYTRAVDWWG 
           810        820        830        840        850
    LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA EAIGIMRRLL 
           860        870        880        890        900
    RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD 
           910        920        930        940 
    VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC
    Length:942
    Mass (Da):103,932
    Last modified:September 22, 2009 - v2
    Checksum:i61360295EC70BB8E
    GO
    Isoform 2 (identifier: Q16512-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: MASDAVQ → MAEANNPSEQELE

    Note: No experimental confirmation available.
    Show »
    Length:948
    Mass (Da):104,673
    Checksum:i882D58AABCFDCEE1
    GO
    Isoform 3 (identifier: Q16512-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         603-603: S → R
         604-942: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:603
    Mass (Da):66,060
    Checksum:i9CC7C140CE6C5547
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti191G → D in AAB33345 (PubMed:7851406).Curated1
    Sequence conflicti191G → D in AAC50209 (PubMed:7851406).Curated1
    Sequence conflicti562S → P in BAG36611 (PubMed:14702039).Curated1
    Sequence conflicti736I → T no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti750T → A no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti800G → A no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti812E → G in BAG36611 (PubMed:14702039).Curated1
    Sequence conflicti887L → P in BAG53845 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_042337185R → C in a metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs267605306Ensembl.1
    Natural variantiVAR_042338197A → E1 Publication1
    Natural variantiVAR_042339436R → W1 PublicationCorresponds to variant dbSNP:rs35132656Ensembl.1
    Natural variantiVAR_042340520R → Q1 PublicationCorresponds to variant dbSNP:rs56273055Ensembl.1
    Natural variantiVAR_042341555L → I2 PublicationsCorresponds to variant dbSNP:rs34309238Ensembl.1
    Natural variantiVAR_042342635R → Q1 PublicationCorresponds to variant dbSNP:rs35416389Ensembl.1
    Natural variantiVAR_042343718I → V2 PublicationsCorresponds to variant dbSNP:rs2230539Ensembl.1
    Natural variantiVAR_042344873F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1
    Natural variantiVAR_014937901V → I3 PublicationsCorresponds to variant dbSNP:rs10846Ensembl.1
    Natural variantiVAR_042345921A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0381431 – 7MASDAVQ → MAEANNPSEQELE in isoform 2. 1 Publication7
    Alternative sequenceiVSP_039213603S → R in isoform 3. 1 Publication1
    Alternative sequenceiVSP_039214604 – 942Missing in isoform 3. 1 PublicationAdd BLAST339

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		D26181 mRNA Translation: BAA05169.1
    S75546 mRNA Translation: AAB33345.1
    U33053 mRNA Translation: AAC50209.1
    AK123007 mRNA Translation: BAG53845.1
    AK292130 mRNA Translation: BAF84819.1
    AK313886 mRNA Translation: BAG36611.1
    AC008569 Genomic DNA No translation available.
    BC040061 mRNA Translation: AAH40061.1
    BC094766 mRNA Translation: AAH94766.1
    CCDSiCCDS42513.1 [Q16512-1]
    CCDS42514.1 [Q16512-2]
    PIRiJC2129
    S51162
    RefSeqiNP_002732.3, NM_002741.3 [Q16512-1]
    NP_998725.1, NM_213560.1 [Q16512-2]
    UniGeneiHs.466044

    Genome annotation databases

    EnsembliENST00000242783; ENSP00000242783; ENSG00000123143 [Q16512-1]
    ENST00000342216; ENSP00000343325; ENSG00000123143 [Q16512-2]
    GeneIDi5585
    KEGGihsa:5585
    UCSCiuc002myp.4 human [Q16512-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiPKN1_HUMAN
    AccessioniPrimary (citable) accession number: Q16512
    Secondary accession number(s): A8K7W5
    , B2R9R4, B3KVN3, Q15143, Q504U4, Q8IUV5, Q9UD44
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 22, 2009
    Last modified: July 18, 2018
    This is version 210 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

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