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Q61036

- PAK3_MOUSE

UniProt

Q61036 - PAK3_MOUSE

Protein

Serine/threonine-protein kinase PAK 3

Gene

Pak3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-436 and allows the kinase domain to adopt an active structure By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei312 – 3121ATPCurated
    Active sitei402 – 4021Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi289 – 2979ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: UniProtKB-KW
    6. Rho GTPase binding Source: BHF-UCL

    GO - Biological processi

    1. axonogenesis Source: UniProtKB
    2. dendrite development Source: UniProtKB
    3. regulation of actin filament polymerization Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.12. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PAK 3 (EC:2.7.11.1)
    Alternative name(s):
    Beta-PAK
    CDC42/RAC effector kinase PAK-B
    p21-activated kinase 3
    Short name:
    PAK-3
    Gene namesi
    Name:Pak3
    Synonyms:Pak-3, Pakb, Stk4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1339656. Pak3.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mice show significant abnormalities in synaptic plasticity as well as deficiencies in learning and memory. Pak1 and Pak3 double knockout mice display reduced brains characterized by simplified neuronal dendrites/axons and reduced synapse density.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671R → C: Decreases interaction of PAK3 with CDC42 but increases interaction with RAC1. 1 Publication
    Mutagenesisi312 – 3121K → A: Loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Serine/threonine-protein kinase PAK 3PRO_0000086470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501Phosphoserine; by autocatalysisBy similarity
    Modified residuei154 – 1541Phosphoserine; by autocatalysisBy similarity
    Modified residuei436 – 4361Phosphothreonine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated when activated by CDC42/p21.
    Neddylated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ61036.
    PaxDbiQ61036.
    PRIDEiQ61036.

    PTM databases

    PhosphoSiteiQ61036.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61036.
    BgeeiQ61036.
    CleanExiMM_PAK3.
    MM_STK4.
    GenevestigatoriQ61036.

    Interactioni

    Subunit structurei

    Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Shows highly specific binding to the SH3 domains of phospholipase C-gamma and of adapter protein NCK. Interacts with the C-terminal of APP. Interacts with ARHGEF6 and ARHGEF7 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC42P609533EBI-457317,EBI-81752From a different organism.

    Protein-protein interaction databases

    BioGridi202021. 3 interactions.
    DIPiDIP-447N.
    IntActiQ61036. 5 interactions.
    MINTiMINT-151864.

    Structurei

    Secondary structure

    1
    559
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi115 – 1184

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EESNMR-B63-123[»]
    ProteinModelPortaliQ61036.
    SMRiQ61036. Positions 65-156, 262-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61036.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini70 – 8314CRIBPROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 534252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 15086Autoregulatory regionBy similarityAdd
    BLAST
    Regioni65 – 12359GTPase-bindingBy similarityAdd
    BLAST
    Regioni84 – 282199LinkerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi187 – 19711Poly-GluAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CRIB domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00680000099789.
    HOGENOMiHOG000234202.
    HOVERGENiHBG108518.
    InParanoidiQ61036.
    KOiK05733.
    OMAiSANENDM.
    OrthoDBiEOG7CK36J.
    TreeFamiTF105351.

    Family and domain databases

    Gene3Di3.90.810.10. 1 hit.
    InterProiIPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00786. PBD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00285. PBD. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50108. CRIB. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q61036-1) [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

    MSDSLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS    50
    IFPGGGDKTN KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTPDLYGSQM 100
    CPGKLPEGIP EQWARLLQTS NITKLEQKKN PQAVLDVLKF YDSKETVNNQ 150
    KYMSFTSGDK SAHGYIAAHQ SNTKTASEPP LAPPVSEEED EEEEEEEDDN 200
    EPPPVIAPRP EHTKSIYTRS VVESIASPAA PNKEDIPPSA ENANSTTLYR 250
    NTDRQRKKSK MTDEEILEKL RSIVSVGDPK KKYTRFEKIG QGASGTVYTA 300
    LDIATGQEVA IKQMNLQQQP KKELIINEIL VMRENKNPNI VNYLDSYLVG 350
    DELWVVMEYL AGGSLTDVVT ETCMDEGQIA AVCRECLQAL DFLHSNQVIH 400
    RDIKSDNILL GMDGSVKLTD FGFCAQITPE QSKRSTMVGT PYWMAPEVVT 450
    RKAYGPKVDI WSLGIMAIEM VEGEPPYLNE NPLRALYLIA TNGTPELQNP 500
    ERLSAVFRDF LNRCLEMDVD RRGSAKELLQ HPFLKLAKPL SSLTPLIIAA 550
    KEAIKNSSR 559
    Length:559
    Mass (Da):62,398
    Last modified:May 10, 2004 - v2
    Checksum:i9AD07B0328F0B08C
    GO
    Isoform 2 (identifier: Q61036-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-107: Missing.

    Show »
    Length:544
    Mass (Da):60,781
    Checksum:i72E323575DC18E0F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761A → G in AAC52354. (PubMed:7559398)Curated
    Sequence conflicti286 – 2861F → L(PubMed:7559398)Curated
    Sequence conflicti286 – 2861F → L(PubMed:10352232)Curated
    Sequence conflicti376 – 3761E → V in AAC52354. (PubMed:7559398)Curated
    Sequence conflicti508 – 5081R → H in AAC52354. (PubMed:7559398)Curated
    Sequence conflicti540 – 5401L → M in AAC31969. (PubMed:10352232)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei93 – 10715Missing in isoform 2. 4 PublicationsVSP_010243Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39738 mRNA. Translation: AAC52354.1.
    AF082297 mRNA. Translation: AAC31969.1.
    AJ496262 mRNA. Translation: CAD42790.1.
    AJ496263 mRNA. Translation: CAD42791.1.
    AK031853 mRNA. Translation: BAC27580.1.
    BC053403 mRNA. Translation: AAH53403.1.
    CCDSiCCDS30454.1. [Q61036-2]
    CCDS57779.1. [Q61036-1]
    PIRiI49376.
    RefSeqiNP_001181977.1. NM_001195048.1. [Q61036-1]
    NP_001181978.1. NM_001195049.1. [Q61036-2]
    NP_032804.2. NM_008778.3. [Q61036-2]
    XP_006528814.1. XM_006528751.1. [Q61036-1]
    XP_006528815.1. XM_006528752.1. [Q61036-1]
    XP_006528816.1. XM_006528753.1. [Q61036-2]
    XP_006528817.1. XM_006528754.1. [Q61036-2]
    UniGeneiMm.40035.

    Genome annotation databases

    EnsembliENSMUST00000033640; ENSMUSP00000033640; ENSMUSG00000031284. [Q61036-1]
    ENSMUST00000112863; ENSMUSP00000108484; ENSMUSG00000031284. [Q61036-1]
    ENSMUST00000112864; ENSMUSP00000108485; ENSMUSG00000031284. [Q61036-2]
    ENSMUST00000112865; ENSMUSP00000108486; ENSMUSG00000031284. [Q61036-2]
    ENSMUST00000112868; ENSMUSP00000108489; ENSMUSG00000031284. [Q61036-2]
    ENSMUST00000172330; ENSMUSP00000126562; ENSMUSG00000031284. [Q61036-2]
    GeneIDi18481.
    KEGGimmu:18481.
    UCSCiuc009umg.2. mouse. [Q61036-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39738 mRNA. Translation: AAC52354.1 .
    AF082297 mRNA. Translation: AAC31969.1 .
    AJ496262 mRNA. Translation: CAD42790.1 .
    AJ496263 mRNA. Translation: CAD42791.1 .
    AK031853 mRNA. Translation: BAC27580.1 .
    BC053403 mRNA. Translation: AAH53403.1 .
    CCDSi CCDS30454.1. [Q61036-2 ]
    CCDS57779.1. [Q61036-1 ]
    PIRi I49376.
    RefSeqi NP_001181977.1. NM_001195048.1. [Q61036-1 ]
    NP_001181978.1. NM_001195049.1. [Q61036-2 ]
    NP_032804.2. NM_008778.3. [Q61036-2 ]
    XP_006528814.1. XM_006528751.1. [Q61036-1 ]
    XP_006528815.1. XM_006528752.1. [Q61036-1 ]
    XP_006528816.1. XM_006528753.1. [Q61036-2 ]
    XP_006528817.1. XM_006528754.1. [Q61036-2 ]
    UniGenei Mm.40035.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EES NMR - B 63-123 [» ]
    ProteinModelPortali Q61036.
    SMRi Q61036. Positions 65-156, 262-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202021. 3 interactions.
    DIPi DIP-447N.
    IntActi Q61036. 5 interactions.
    MINTi MINT-151864.

    PTM databases

    PhosphoSitei Q61036.

    Proteomic databases

    MaxQBi Q61036.
    PaxDbi Q61036.
    PRIDEi Q61036.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033640 ; ENSMUSP00000033640 ; ENSMUSG00000031284 . [Q61036-1 ]
    ENSMUST00000112863 ; ENSMUSP00000108484 ; ENSMUSG00000031284 . [Q61036-1 ]
    ENSMUST00000112864 ; ENSMUSP00000108485 ; ENSMUSG00000031284 . [Q61036-2 ]
    ENSMUST00000112865 ; ENSMUSP00000108486 ; ENSMUSG00000031284 . [Q61036-2 ]
    ENSMUST00000112868 ; ENSMUSP00000108489 ; ENSMUSG00000031284 . [Q61036-2 ]
    ENSMUST00000172330 ; ENSMUSP00000126562 ; ENSMUSG00000031284 . [Q61036-2 ]
    GeneIDi 18481.
    KEGGi mmu:18481.
    UCSCi uc009umg.2. mouse. [Q61036-1 ]

    Organism-specific databases

    CTDi 5063.
    MGIi MGI:1339656. Pak3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00680000099789.
    HOGENOMi HOG000234202.
    HOVERGENi HBG108518.
    InParanoidi Q61036.
    KOi K05733.
    OMAi SANENDM.
    OrthoDBi EOG7CK36J.
    TreeFami TF105351.

    Enzyme and pathway databases

    BRENDAi 2.7.1.12. 3474.

    Miscellaneous databases

    EvolutionaryTracei Q61036.
    NextBioi 294190.
    PROi Q61036.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61036.
    Bgeei Q61036.
    CleanExi MM_PAK3.
    MM_STK4.
    Genevestigatori Q61036.

    Family and domain databases

    Gene3Di 3.90.810.10. 1 hit.
    InterProi IPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00786. PBD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00285. PBD. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50108. CRIB. 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

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fibroblast.
    2. Erratum
      Bagrodia S., Taylor S.J., Creasy C.L., Chernoff J., Cerione R.A.
      J. Biol. Chem. 271:1250-1250(1996)
    3. "Cloning, central nervous system expression and chromosomal mapping of the mouse PAK-1 and PAK-3 genes."
      Burbelo P.D., Kozak C.A., Finegold A.A., Hall A., Pirone D.M.
      Gene 232:209-215(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "A new constitutively active brain Pak3 isoform displays modified specificities towards Rac and Cdc42 GTPases."
      Rousseau V., Goupille O., Morin N., Barnier J.V.
      J. Biol. Chem. 278:3912-3920(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    5. "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.
      , 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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    6. "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: C3H/He.
      Tissue: Mesenchymal stem cell.
    7. "p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentially involving novel phosphorylation of troponin I."
      Buscemi N., Foster D.B., Neverova I., Van Eyk J.E.
      Circ. Res. 91:509-516(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TNNI3.
    8. "The mental retardation protein PAK3 contributes to synapse formation and plasticity in hippocampus."
      Boda B., Alberi S., Nikonenko I., Node-Langlois R., Jourdain P., Moosmayer M., Parisi-Jourdain L., Muller D.
      J. Neurosci. 24:10816-10825(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-312.
    9. "Abnormal long-lasting synaptic plasticity and cognition in mice lacking the mental retardation gene Pak3."
      Meng J., Meng Y., Hanna A., Janus C., Jia Z.
      J. Neurosci. 25:6641-6650(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "The p21-activated kinase 3 implicated in mental retardation regulates spine morphogenesis through a Cdc42-dependent pathway."
      Kreis P., Thevenot E., Rousseau V., Boda B., Muller D., Barnier J.V.
      J. Biol. Chem. 282:21497-21506(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-67.
    11. "Structural and kinetic effects of PAK3 phosphorylation mimic of cTnI(S151E) on the cTnC-cTnI interaction in the cardiac thin filament."
      Ouyang Y., Mamidi R., Jayasundar J.J., Chandra M., Dong W.J.
      J. Mol. Biol. 400:1036-1045(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TNNI3.
    12. "p21-Activated kinases 1 and 3 control brain size through coordinating neuronal complexity and synaptic properties."
      Huang W., Zhou Z., Asrar S., Henkelman M., Xie W., Jia Z.
      Mol. Cell. Biol. 31:388-403(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase."
      Gizachew D., Guo W., Chohan K.K., Sutcliffe M.J., Oswald R.E.
      Biochemistry 39:3963-3971(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 65-92 AND 108-123 IN COMPLEX WITH CDC42.

    Entry informationi

    Entry nameiPAK3_MOUSE
    AccessioniPrimary (citable) accession number: Q61036
    Secondary accession number(s): O88645, Q8K1R5, Q8K1R6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3