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Q8BWW9 (PKN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase N2

EC=2.7.11.13
Alternative name(s):
PKN gamma
Protein kinase C-like 2
Protein-kinase C-related kinase 2
Gene names
Name:Pkn2
Synonyms:Prk2, Prkcl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length983 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Ref.3 Ref.7 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Kinase activity is activated upon binding to GTP-bound Rho1/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-815 (activation loop of the kinase domain) and Thr-957 (turn motif), need to be phosphorylated for its full activation By similarity. Ref.7

Subunit structure

Interacts with RHOA (GTP-bound form preferentially) and RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation. Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity. Interacts (via C-terminus domain) with AKT1; the interaction occurs with the C-terminus cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with NCK1, NCK2 and RHOC By similarity. Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially). Interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially). Interacts with NCK1 (via SH3 domains). Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity. Interacts with CD44. Ref.3 Ref.5 Ref.7 Ref.10

Subcellular location

Cytoplasm. Nucleus By similarity. Membrane. Cell projectionlamellipodium By similarity. Cytoplasmcytoskeleton By similarity. Cleavage furrow By similarity. Midbody By similarity. Cell junction By similarity. Note: Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells By similarity. Ref.4

Tissue specificity

Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous. Ref.3 Ref.4 Ref.6 Ref.7

Domain

The N-terminus region interferes with the interaction between AKT1 and the C-terminus region of PKN2 By similarity.

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

The apoptotic C-terminus cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations By similarity.

Post-translational modification

Phosphorylated during mitosis By similarity. Autophosphorylated. Phosphorylated.

Activated by limited proteolysis with trypsin By similarity. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death By similarity.

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 1 protein kinase domain.

Contains 3 REM (Hr1) repeats.

Ontologies

Keywords
   Biological processApoptosis
Cell adhesion
Cell cycle
Cell division
Transcription
Transcription regulation
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapical junction assembly

Inferred from direct assay Ref.10. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell motility

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical junction complex

Inferred from direct assay Ref.10. Source: UniProtKB

cleavage furrow

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12783890. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12783890. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone deacetylase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BWW9-1)

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.
Isoform 2 (identifier: Q8BWW9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     35-45: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8BWW9-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 983983Serine/threonine-protein kinase N2
PRO_0000055723

Regions

Repeat44 – 11976REM 1
Repeat133 – 21381REM 2
Repeat214 – 29582REM 3
Domain329 – 462134C2
Domain656 – 915260Protein kinase
Domain916 – 98368AGC-kinase C-terminal
Nucleotide binding662 – 6709ATP By similarity
Region381 – 46282Necessary to rescue apical junction formation
Region916 – 97661Necessary for the catalytic activity By similarity
Region977 – 9837Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA By similarity

Sites

Active site7811Proton acceptor By similarity
Binding site6851ATP By similarity
Site117 – 1182Cleavage; by caspase-3 By similarity
Site699 – 7002Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue771N6-acetyllysine Ref.11
Modified residue1101Phosphoserine By similarity
Modified residue1211Phosphothreonine By similarity
Modified residue1241Phosphothreonine By similarity
Modified residue3011Phosphoserine By similarity
Modified residue3051Phosphoserine By similarity
Modified residue3591Phosphoserine By similarity
Modified residue3611Phosphoserine By similarity
Modified residue5341Phosphoserine By similarity
Modified residue5821Phosphoserine By similarity
Modified residue6301Phosphoserine By similarity
Modified residue8151Phosphothreonine; by PDPK1 By similarity
Modified residue9571Phosphothreonine Probable

Natural variations

Alternative sequence35 – 4511Missing in isoform 2.
VSP_012042
Alternative sequence781 – 7877DLKLDNL → NTIFSSI in isoform 3.
VSP_042185
Alternative sequence788 – 983196Missing in isoform 3.
VSP_042186

Experimental info

Mutagenesis661A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155. Ref.10
Mutagenesis1551A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60. Ref.10
Mutagenesis6851K → M: Prevents apical junction formation. Ref.10
Mutagenesis7811D → A: Prevents apical junction formation. Ref.10
Sequence conflict321Q → H in BAC32655. Ref.1
Sequence conflict841N → H in BAC33888. Ref.1
Sequence conflict3951V → D in BAC38910. Ref.1
Sequence conflict5691L → F in BAC32655. Ref.1
Sequence conflict7041E → K in BAC33888. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 3961FD79D2718609

FASTA983111,607
        10         20         30         40         50         60 
MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 

        70         80         90        100        110        120 
KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDSTDCPR 

       130        140        150        160        170        180 
TPDTPNSDSR SSTSNNRLMA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 

       190        200        210        220        230        240 
QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM 

       250        260        270        280        290        300 
KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA 

       310        320        330        340        350        360 
SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA TSVALPGWSP 

       370        380        390        400        410        420 
SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN TVVGQTSWKP ISNQSWDQKF 

       430        440        450        460        470        480 
TLELDRSREL EISVYWRDWR SLCAVKFLRL EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP 

       490        500        510        520        530        540 
VIERRPKLQR QKKIFSKQQG KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP 

       550        560        570        580        590        600 
ATVPVVDARI PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ 

       610        620        630        640        650        660 
GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ FSLQDFRCCA 

       670        680        690        700        710        720 
VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS LMCEKRIFET VNSVRHPFLV 

       730        740        750        760        770        780 
NLFACFQTKE HVCFVMEYAA GGDLMMHIHT DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR 

       790        800        810        820        830        840 
DLKLDNLLLD TEGFVKIADF GLCKEGMGYG DRTSTFCGTP EFLAPEVLTE TSYTRAVDWW 

       850        860        870        880        890        900 
GLGVLIYEML VGESPFPGDD EEEVFDSIVN DEVRYPRFLS TEAISIMRRL LRRNPERRLG 

       910        920        930        940        950        960 
AGEKDAEDVK KHPFFRLTDW SALMDKKVKP PFVPTIRGRE DVSNFDDEFT SEAPILTPPR 

       970        980 
EPRILLEEEQ EMFHDFDYVA DWC 

« Hide

Isoform 2 [UniParc].

Checksum: D2806BCD710C1B29
Show »

FASTA972110,313
Isoform 3 [UniParc].

Checksum: 6B762C942B96D5EF
Show »

FASTA78788,961

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Corpora quadrigemina, Spinal cord and Testis.
[2]"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] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[3]"Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling."
Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.
J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NCK1, TISSUE SPECIFICITY.
[4]"The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
Vincent S., Settleman J.
Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase."
Sun W., Vincent S., Settleman J., Johnson G.L.
J. Biol. Chem. 275:24421-24428(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K2.
[6]"Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion."
Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P.
J. Cell Biol. 156:137-148(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN PHOSPHORYLATION OF CTTN, ENZYME REGULATION, INTERACTION WITH CD44 AND RAC1, TISSUE SPECIFICITY.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
Wallace S.W., Magalhaes A., Hall A.
Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAC1 AND RHOA, MUTAGENESIS OF ALA-66; ALA-155; LYS-685 AND ASP-781.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK046248 mRNA. Translation: BAC32655.1.
AK133298 mRNA. Translation: BAE21599.1.
AK171092 mRNA. Translation: BAE42244.1.
AK049713 mRNA. Translation: BAC33888.1.
AK083425 mRNA. Translation: BAC38910.1.
BC052073 mRNA. Translation: AAH52073.1.
RefSeqNP_848769.2. NM_178654.4.
UniGeneMm.244236.

3D structure databases

ProteinModelPortalQ8BWW9.
SMRQ8BWW9. Positions 56-107, 132-203, 613-982.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BWW9.

Proteomic databases

PaxDbQ8BWW9.
PRIDEQ8BWW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591. [Q8BWW9-1]
GeneID109333.
KEGGmmu:109333.
UCSCuc008rpe.2. mouse. [Q8BWW9-1]

Organism-specific databases

CTD5586.
MGIMGI:109211. Pkn2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117322.
HOGENOMHOG000233032.
HOVERGENHBG108317.
InParanoidQ3TBR3.
KOK06071.
OMARSQQMFQ.
OrthoDBEOG7X9G6Q.
TreeFamTF102005.

Gene expression databases

BgeeQ8BWW9.
CleanExMM_PKN2.
GenevestigatorQ8BWW9.

Family and domain databases

Gene3D1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
InterProIPR000961. 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]
PfamPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSPKN2. mouse.
NextBio361929.
PROQ8BWW9.
SOURCESearch...

Entry information

Entry namePKN2_MOUSE
AccessionPrimary (citable) accession number: Q8BWW9
Secondary accession number(s): Q3TBR3 expand/collapse secondary AC list , Q80WS2, Q8BJL7, Q8BL62
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot