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Protein

Serine/threonine-protein kinase N1

Gene

PKN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 6441ATPPROSITE-ProRule annotation
Active sitei740 – 7401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi621 – 6299ATPPROSITE-ProRule annotation

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 kinase activity Source: ProtInc
  10. protein kinase C activity Source: UniProtKB-EC
  11. protein kinase C binding Source: UniProtKB
  12. protein serine/threonine kinase activity Source: UniProtKB
  13. 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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9405. PKN1.

Subcellular locationi

  1. Cytoplasm
  2. Nucleus
  3. Endosome
  4. Cell membrane; Peripheral membrane protein
  5. Cleavage furrow
  6. Midbody

  7. 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.

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.

Polymorphism and mutation databases

BioMutaiPKN1.
DMDMi259016304.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
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 – 3741PhosphoserineBy similarity
Modified residuei448 – 4481N6-acetyllysine1 Publication
Modified residuei533 – 5331Phosphoserine4 Publications
Modified residuei537 – 5371Phosphoserine4 Publications
Modified residuei559 – 5591Phosphoserine2 Publications
Modified residuei562 – 5621Phosphoserine5 Publications
Modified residuei774 – 7741Phosphothreonine; by PDPK11 Publication
Modified residuei778 – 7781Phosphothreonine1 Publication
Modified residuei914 – 9141Phosphothreonine1 Publication
Modified residuei916 – 9161Phosphoserine3 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.1 Publication

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

BgeeiQ16512.
CleanExiHS_PKN1.
ExpressionAtlasiQ16512. baseline and differential.
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.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC85BQ158342EBI-602382,EBI-739674
CDR2Q018503EBI-602382,EBI-1181367
CEP57L1Q8IYX8-23EBI-602382,EBI-10181988
GOLGA2Q083793EBI-602382,EBI-618309
HOMER3B2RA103EBI-602382,EBI-10175777
KRT15P190123EBI-602382,EBI-739566
KRT31Q153233EBI-602382,EBI-948001
MAPK12P537782EBI-602382,EBI-602406
MID1O153443EBI-602382,EBI-2340316
SSX2IPQ9Y2D83EBI-602382,EBI-2212028
VIMP086703EBI-602382,EBI-353844
ZAKQ9NYL2-12EBI-602382,EBI-687346

Protein-protein interaction databases

BioGridi111571. 57 interactions.
DIPiDIP-34240N.
IntActiQ16512. 23 interactions.
MINTiMINT-118694.
STRINGi9606.ENSP00000343325.

Structurei

Secondary structure

1
942
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 184Combined sources
Helixi29 – 6638Combined sources
Helixi71 – 9525Combined sources
Turni122 – 1243Combined sources
Helixi126 – 15126Combined sources
Turni157 – 1593Combined sources
Helixi160 – 18728Combined sources
Beta strandi194 – 1963Combined sources
Helixi612 – 6143Combined sources
Beta strandi615 – 62410Combined sources
Beta strandi627 – 6348Combined sources
Turni635 – 6373Combined sources
Beta strandi640 – 6478Combined sources
Helixi648 – 6536Combined sources
Helixi657 – 67115Combined sources
Turni672 – 6743Combined sources
Beta strandi681 – 6866Combined sources
Beta strandi688 – 6969Combined sources
Beta strandi700 – 7023Combined sources
Helixi703 – 7064Combined sources
Turni707 – 7093Combined sources
Helixi714 – 73320Combined sources
Helixi743 – 7453Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi750 – 7523Combined sources
Beta strandi754 – 7563Combined sources
Beta strandi763 – 7653Combined sources
Helixi779 – 7813Combined sources
Helixi784 – 7885Combined sources
Helixi794 – 81017Combined sources
Helixi820 – 82910Combined sources
Helixi840 – 84910Combined sources
Turni854 – 8563Combined sources
Turni862 – 8643Combined sources
Helixi865 – 8695Combined sources
Helixi872 – 8743Combined sources
Helixi879 – 8835Combined sources
Helixi906 – 9094Combined sources
Helixi926 – 9305Combined sources
Turni931 – 9344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXZX-ray2.20B13-98[»]
1URFNMR-A122-199[»]
2RMKNMR-B122-199[»]
4NKGX-ray2.90B/D122-199[»]
4OTDX-ray2.00A605-942[»]
4OTGX-ray2.60A605-942[»]
4OTHX-ray1.80A605-942[»]
4OTIX-ray1.93A605-942[»]
ProteinModelPortaliQ16512.
SMRiQ16512. Positions 13-98, 125-190, 581-940.
ModBaseiSearch...
MobiDBiSearch...

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 kinasePROSITE-ProRule annotationAdd
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 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 3 REM (Hr1) repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120523.
HOVERGENiHBG108317.
InParanoidiQ16512.
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.
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. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911G → D in AAB33345 (PubMed:7851406).Curated
Sequence conflicti191 – 1911G → D in AAC50209 (PubMed:7851406).Curated
Sequence conflicti562 – 5621S → P in BAG36611 (PubMed:14702039).Curated
Sequence conflicti736 – 7361I → T no nucleotide entry (PubMed:7988719).Curated
Sequence conflicti750 – 7501T → A no nucleotide entry (PubMed:7988719).Curated
Sequence conflicti800 – 8001G → A no nucleotide entry (PubMed:7988719).Curated
Sequence conflicti812 – 8121E → G in BAG36611 (PubMed:14702039).Curated
Sequence conflicti887 – 8871L → P in BAG53845 (PubMed:14702039).Curated

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. 1 PublicationVSP_038143
Alternative sequencei603 – 6031S → R in isoform 3. 1 PublicationVSP_039213
Alternative sequencei604 – 942339Missing in isoform 3. 1 PublicationVSP_039214Add
BLAST

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.3. human. [Q16512-1]
uc002myq.3. human. [Q16512-2]

Polymorphism and mutation databases

BioMutaiPKN1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXZX-ray2.20B13-98[»]
1URFNMR-A122-199[»]
2RMKNMR-B122-199[»]
4NKGX-ray2.90B/D122-199[»]
4OTDX-ray2.00A605-942[»]
4OTGX-ray2.60A605-942[»]
4OTHX-ray1.80A605-942[»]
4OTIX-ray1.93A605-942[»]
ProteinModelPortaliQ16512.
SMRiQ16512. Positions 13-98, 125-190, 581-940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111571. 57 interactions.
DIPiDIP-34240N.
IntActiQ16512. 23 interactions.
MINTiMINT-118694.
STRINGi9606.ENSP00000343325.

Chemistry

BindingDBiQ16512.
ChEMBLiCHEMBL3384.
GuidetoPHARMACOLOGYi1520.

PTM databases

PhosphoSiteiQ16512.

Polymorphism and mutation databases

BioMutaiPKN1.
DMDMi259016304.

Proteomic databases

MaxQBiQ16512.
PaxDbiQ16512.
PRIDEiQ16512.

Protocols and materials databases

DNASUi5585.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5585.
GeneCardsiGC19P014544.
H-InvDBHIX0027472.
HGNCiHGNC:9405. PKN1.
HPAiCAB010278.
HPA003982.
MIMi601032. gene.
neXtProtiNX_Q16512.
PharmGKBiPA33769.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120523.
HOVERGENiHBG108317.
InParanoidiQ16512.
KOiK06071.
OMAiEFRSSGE.
OrthoDBiEOG7X9G6Q.
PhylomeDBiQ16512.
TreeFamiTF102005.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiQ16512.

Miscellaneous databases

ChiTaRSiPKN1. human.
EvolutionaryTraceiQ16512.
GeneWikiiProtein_kinase_N1.
GenomeRNAii5585.
NextBioi21660.
PMAP-CutDBQ16512.
PROiQ16512.
SOURCEiSearch...

Gene expression databases

BgeeiQ16512.
CleanExiHS_PKN1.
ExpressionAtlasiQ16512. baseline and differential.
GenevestigatoriQ16512.

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.
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]
ProtoNetiSearch...

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 AND SER-562, 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; SER-559; SER-562 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; SER-559; SER-562; 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; SER-537 AND SER-562, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  33. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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: April 29, 2015
This is version 174 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.