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Q16512

- PKN1_HUMAN

UniProt

Q16512 - PKN1_HUMAN

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Protein

Serine/threonine-protein kinase N1

Gene
PKN1, PAK1, PKN, PRK1, PRKCL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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. 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.10 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei108 – 1092Cleavage; by caspase-3
Sitei454 – 4552Cleavage; by caspase-3
Sitei558 – 5592Cleavage; by caspase-3
Binding sitei644 – 6441ATP By similarity
Active sitei740 – 7401Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi621 – 6299ATP By similarity

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. chromatin binding Source: UniProtKB
  4. GTP-Rho binding Source: UniProtKB
  5. histone binding Source: UniProtKB
  6. histone deacetylase binding Source: UniProtKB
  7. histone kinase activity (H3-T11 specific) Source: UniProtKB
  8. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  9. protein binding Source: UniProtKB
  10. protein kinase activity Source: ProtInc
  11. protein kinase C activity Source: UniProtKB-EC
  12. protein kinase C binding Source: UniProtKB
  13. protein serine/threonine kinase activity Source: UniProtKB
  14. Rac GTPase binding Source: UniProtKB

GO - Biological processi

  1. activation of JUN kinase activity Source: ProtInc
  2. epithelial cell migration Source: UniProtKB
  3. histone H3-T11 phosphorylation Source: UniProtKB
  4. hyperosmotic response Source: Ensembl
  5. protein phosphorylation Source: UniProtKB
  6. regulation of cell motility Source: UniProtKB
  7. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. signal transduction Source: ProtInc
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiQ16512.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase N1 (EC:2.7.11.13)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9405. PKN1.

Subcellular locationi

Cytoplasm. Nucleus. Endosome. Cell membrane; Peripheral membrane protein. Cleavage furrow. Midbody
Note: Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-374 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis.3 Publications

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic membrane-bounded vesicle Source: Ensembl
  4. endosome Source: UniProtKB
  5. midbody Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081D → A: Abolishes cleavage by caspase-3 and formation of AF1 fragment. 1 Publication
Mutagenesisi181 – 1811R → A: Abolishes interaction with bacterial SspH1. 1 Publication
Mutagenesisi181 – 1811R → K: Decreases interaction with bacterial SspH1. 1 Publication
Mutagenesisi185 – 1851R → A: Abolishes interaction with bacterial SspH1. 1 Publication
Mutagenesisi451 – 4511D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication
Mutagenesisi454 – 4541D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication
Mutagenesisi558 – 5581D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication
Mutagenesisi560 – 5601D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication
Mutagenesisi644 – 6441K → E: Abolishes Serine/threonine-protein kinase activity. 2 Publications
Mutagenesisi644 – 6441K → R: Substantial reduction of autophosphorylation. 2 Publications

Organism-specific databases

PharmGKBiPA33769.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 942941Serine/threonine-protein kinase N1PRO_0000055719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei205 – 2051Phosphoserine2 Publications
Modified residuei374 – 3741Phosphoserine By similarity
Modified residuei448 – 4481N6-acetyllysine1 Publication
Modified residuei533 – 5331Phosphoserine4 Publications
Modified residuei537 – 5371Phosphoserine4 Publications
Modified residuei774 – 7741Phosphothreonine; by PDPK11 Publication
Modified residuei778 – 7781Phosphothreonine1 Publication
Modified residuei914 – 9141Phosphothreonine1 Publication
Modified residuei916 – 9161Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16512.
PaxDbiQ16512.
PRIDEiQ16512.

PTM databases

PhosphoSiteiQ16512.

Miscellaneous databases

PMAP-CutDBQ16512.

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

ArrayExpressiQ16512.
BgeeiQ16512.
CleanExiHS_PKN1.
GenevestigatoriQ16512.

Organism-specific databases

HPAiCAB010278.
HPA003982.

Interactioni

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. In case of infection, interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region). Interacts (via C-terminus) with PDPK1.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC85BQ158342EBI-602382,EBI-739674
MAPK12P537782EBI-602382,EBI-602406
ZAKQ9NYL2-12EBI-602382,EBI-687346

Protein-protein interaction databases

BioGridi111571. 42 interactions.
DIPiDIP-34240N.
IntActiQ16512. 14 interactions.
MINTiMINT-118694.
STRINGi9606.ENSP00000343325.

Structurei

Secondary structure

1
942
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 184
Helixi29 – 6638
Helixi71 – 9525
Turni122 – 1243
Helixi126 – 15126
Turni157 – 1593
Helixi160 – 18728
Beta strandi194 – 1963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXZX-ray2.20B13-98[»]
1URFNMR-A122-199[»]
2RMKNMR-B122-199[»]
4NKGX-ray2.90B/D122-199[»]
ProteinModelPortaliQ16512.
SMRiQ16512. Positions 13-98, 125-190, 577-942.

Miscellaneous databases

EvolutionaryTraceiQ16512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 11077REM 1Add
BLAST
Repeati123 – 20987REM 2Add
BLAST
Repeati210 – 29182REM 3Add
BLAST
Domaini325 – 461137C2Add
BLAST
Domaini615 – 874260Protein kinaseAdd
BLAST
Domaini875 – 94268AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni181 – 1855Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination

Domaini

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

Sequence similaritiesi

Contains 1 C2 domain.
Contains 3 REM (Hr1) repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108317.
KOiK06071.
OMAiEFRSSGE.
OrthoDBiEOG7X9G6Q.
PhylomeDBiQ16512.
TreeFamiTF102005.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

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. Align

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

MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL    50
KLKEGAENLR RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL 100
PDPAATHDGP QSPGAGGPTC SATNLSRVAG LEKQLAIELK VKQGAENMIQ 150
TYSNGSTKDR KLLLTAQQML QDSKTKIDII RMQLRRALQA GQLENQAAPD 200
DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS AAKAPDRKAV 250
SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF 300
STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG 350
PGTPDSRPPF LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT 400
VVGQTSWKPC GPNAWDQSFT LELERARELE LAVFWRDQRG LCALKFLKLE 450
DFLDNERHEV QLDMEPQGCL VAEVTFRNPV IERIPRLRRQ KKIFSKQQGK 500
AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS EARTTGDISV 550
EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA 600
LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD 650
IVARDEVESL MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG 700
GDLMLHIHSD VFSEPRAIFY SACVVLGLQF LHEHKIVYRD LKLDNLLLDT 750
EGYVKIADFG LCKEGMGYGD RTSTFCGTPE FLAPEVLTDT SYTRAVDWWG 800
LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA EAIGIMRRLL 850
RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD 900
VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC 942
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851R → C in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042337
Natural varianti197 – 1971A → E.1 Publication
VAR_042338
Natural varianti436 – 4361R → W.1 Publication
Corresponds to variant rs35132656 [ dbSNP | Ensembl ].
VAR_042339
Natural varianti520 – 5201R → Q.1 Publication
Corresponds to variant rs56273055 [ dbSNP | Ensembl ].
VAR_042340
Natural varianti555 – 5551L → I.2 Publications
Corresponds to variant rs34309238 [ dbSNP | Ensembl ].
VAR_042341
Natural varianti635 – 6351R → Q.1 Publication
Corresponds to variant rs35416389 [ dbSNP | Ensembl ].
VAR_042342
Natural varianti718 – 7181I → V.2 Publications
Corresponds to variant rs2230539 [ dbSNP | Ensembl ].
VAR_042343
Natural varianti873 – 8731F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_042344
Natural varianti901 – 9011V → I.3 Publications
Corresponds to variant rs10846 [ dbSNP | Ensembl ].
VAR_014937
Natural varianti921 – 9211A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042345

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 77MASDAVQ → MAEANNPSEQELE in isoform 2. VSP_038143
Alternative sequencei603 – 6031S → R in isoform 3. VSP_039213
Alternative sequencei604 – 942339Missing in isoform 3. VSP_039214Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911G → D in AAB33345. 1 Publication
Sequence conflicti191 – 1911G → D in AAC50209. 1 Publication
Sequence conflicti562 – 5621S → P in BAG36611. 1 Publication
Sequence conflicti736 – 7361I → T no nucleotide entry 1 Publication
Sequence conflicti750 – 7501T → A no nucleotide entry 1 Publication
Sequence conflicti800 – 8001G → A no nucleotide entry 1 Publication
Sequence conflicti812 – 8121E → G in BAG36611. 1 Publication
Sequence conflicti887 – 8871L → P in BAG53845. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [Q16512-1]
uc002myq.3. human. [Q16512-2]

Polymorphism databases

DMDMi259016304.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS42513.1. [Q16512-1 ]
CCDS42514.1. [Q16512-2 ]
PIRi JC2129.
S51162.
RefSeqi NP_002732.3. NM_002741.3. [Q16512-1 ]
NP_998725.1. NM_213560.1. [Q16512-2 ]
UniGenei Hs.466044.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CXZ X-ray 2.20 B 13-98 [» ]
1URF NMR - A 122-199 [» ]
2RMK NMR - B 122-199 [» ]
4NKG X-ray 2.90 B/D 122-199 [» ]
ProteinModelPortali Q16512.
SMRi Q16512. Positions 13-98, 125-190, 577-942.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111571. 42 interactions.
DIPi DIP-34240N.
IntActi Q16512. 14 interactions.
MINTi MINT-118694.
STRINGi 9606.ENSP00000343325.

Chemistry

BindingDBi Q16512.
ChEMBLi CHEMBL3384.
GuidetoPHARMACOLOGYi 1520.

PTM databases

PhosphoSitei Q16512.

Polymorphism databases

DMDMi 259016304.

Proteomic databases

MaxQBi Q16512.
PaxDbi Q16512.
PRIDEi Q16512.

Protocols and materials databases

DNASUi 5585.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000242783 ; ENSP00000242783 ; ENSG00000123143 . [Q16512-1 ]
ENST00000342216 ; ENSP00000343325 ; ENSG00000123143 . [Q16512-2 ]
GeneIDi 5585.
KEGGi hsa:5585.
UCSCi uc002myp.3. human. [Q16512-1 ]
uc002myq.3. human. [Q16512-2 ]

Organism-specific databases

CTDi 5585.
GeneCardsi GC19P014544.
H-InvDB HIX0027472.
HGNCi HGNC:9405. PKN1.
HPAi CAB010278.
HPA003982.
MIMi 601032. gene.
neXtProti NX_Q16512.
PharmGKBi PA33769.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108317.
KOi K06071.
OMAi EFRSSGE.
OrthoDBi EOG7X9G6Q.
PhylomeDBi Q16512.
TreeFami TF102005.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
SignaLinki Q16512.

Miscellaneous databases

ChiTaRSi PKN1. human.
EvolutionaryTracei Q16512.
GeneWikii Protein_kinase_N1.
GenomeRNAii 5585.
NextBioi 21660.
PMAP-CutDB Q16512.
PROi Q16512.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16512.
Bgeei Q16512.
CleanExi HS_PKN1.
Genevestigatori Q16512.

Family and domain databases

Gene3Di 1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
InterProi IPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C."
    Mukai H., Ono Y.
    Biochem. Biophys. Res. Commun. 199:897-904(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-644.
    Tissue: Hippocampus.
  2. "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family."
    Palmer R.H., Ridden J., Parker P.J.
    Eur. J. Biochem. 227:344-351(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ILE-555 AND ILE-901.
    Tissue: Kidney, Synovium and Thymus.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT ILE-901.
    Tissue: Brain and Placenta.
  6. "Identification of multiple, novel, protein kinase C-related gene products."
    Palmer R.H., Ridden J., Parker P.J.
    FEBS Lett. 356:5-8(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 700-800 (ISOFORMS 1/2), VARIANT VAL-718.
  7. "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163."
    Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T., Parker P.J.
    FEBS Lett. 378:281-285(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MARCKS.
  8. "PKN associates and phosphorylates the head-rod domain of neurofilament protein."
    Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M., Miyahara M., Sunakawa H., Ono Y.
    J. Biol. Chem. 271:9816-9822(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NEFH; NEFL AND NEFM.
  9. "Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho."
    Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N., Mukai H., Ono Y., Kakizuka A., Narumiya S.
    Science 271:645-648(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH RHOA.
  10. "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN."
    Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.
    Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GFAP AND VIM.
  11. "PRK1 is targeted to endosomes by the small GTPase, RhoB."
    Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.
    J. Biol. Chem. 273:4811-4814(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHOB.
  12. "Proteolytic activation of PKN by caspase-3 or related protease during apoptosis."
    Takahashi M., Mukai H., Toshimori M., Miyamoto M., Ono Y.
    Proc. Natl. Acad. Sci. U.S.A. 95:11566-11571(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-108; ASP-451; ASP-454; ASP-558 AND ASP-560.
  13. "Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton."
    Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.
    Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-774 BY PDPK1, INTERACTION WITH PDPK1.
  14. Cited for: FUNCTION, INTERACTION WITH MAPT.
  15. "A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer."
    Metzger E., Muller J.M., Ferrari S., Buettner R., Schule R.
    EMBO J. 22:270-280(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ANDR.
  16. "A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1."
    Haraga A., Miller S.I.
    Cell. Microbiol. 8:837-846(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S.TYPHIMURIUM SSPH1.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis."
    Schmidt A., Durgan J., Magalhaes A., Hall A.
    EMBO J. 26:1624-1636(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation."
    Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R.
    Nat. Cell Biol. 10:53-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-644.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537 AND SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537; THR-914 AND SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases."
    Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A.
    FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH HDAC5; HDAC7 AND HDAC9.
  27. Cited for: INTERACTION WITH PRKCB.
  28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration."
    Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S., Collazos A., Parker P.J.
    PLoS ONE 6:E21732-E21732(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, TISSUE SPECIFICITY.
  31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1."
    Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K., Hakoshima T.
    Mol. Cell 4:793-803(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98 IN COMPLEX WITH RHOA.
  34. "Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
    Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
    J. Struct. Biol. 126:166-170(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
  35. "Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)."
    Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y., Parker P.J., Blundell T.L., Mott H.R.
    J. Biol. Chem. 278:50578-50587(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 116-199 IN COMPLEX WITH RAC1.
  36. "The Rac1 polybasic region is required for interaction with its effector PRK1."
    Modha R., Campbell L.J., Nietlispach D., Buhecha H.R., Owen D., Mott H.R.
    J. Biol. Chem. 283:1492-1500(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 122-199 IN COMPLEX WITH RAC1.
  37. "Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase."
    Keszei A.F., Tang X., McCormick C., Zeqiraj E., Rohde J.R., Tyers M., Sicheri F.
    Mol. Cell. Biol. 34:362-373(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 122-199 IN COMPLEX WITH SALMONELLA SSPH1, UBIQUITINATION, MUTAGENESIS OF ARG-181 AND ARG-185, FUNCTION AS ANDROGEN RECEPTOR COACTIVATOR.
  38. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-185; GLU-197; TRP-436; GLN-520; ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.

Entry informationi

Entry nameiPKN1_HUMAN
AccessioniPrimary (citable) accession number: Q16512
Secondary accession number(s): A8K7W5
, B2R9R4, B3KVN3, Q15143, Q504U4, Q8IUV5, Q9UD44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 167 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

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