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Q8BTW9

- PAK4_MOUSE

UniProt

Q8BTW9 - PAK4_MOUSE

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Protein
Serine/threonine-protein kinase PAK 4
Gene
Pak4, Kiaa1142
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei352 – 3521ATP By similarity
Active sitei442 – 4421Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi329 – 3379ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. receptor signaling protein serine/threonine kinase activity Source: RefGenome

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. intracellular signal transduction Source: RefGenome
  4. signal transduction by phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 4 (EC:2.7.11.1)
Alternative name(s):
p21-activated kinase 4
Short name:
PAK-4
Gene namesi
Name:Pak4
Synonyms:Kiaa1142
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1917834. Pak4.

Subcellular locationi

Cytoplasm
Note: Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways By similarity.

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice die at embryonic day 11.5 probably due to a defect in the fetal heart. They show strong defects in neuronal development and axonal outgrowth. Spinal cord motor neurons and interneurons failed to differentiate and migrate to their proper position. Nervous system-specific conditional PAK4 deletion mice display growth retardation and die prematurely.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Serine/threonine-protein kinase PAK 4
PRO_0000086475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine By similarity
Modified residuei104 – 1041Phosphoserine By similarity
Modified residuei148 – 1481Phosphoserine By similarity
Modified residuei181 – 1811Phosphoserine2 Publications
Modified residuei187 – 1871Phosphothreonine By similarity
Modified residuei195 – 1951Phosphoserine By similarity
Modified residuei257 – 2571Phosphoserine By similarity
Modified residuei266 – 2661Phosphoserine By similarity
Modified residuei293 – 2931Phosphoserine By similarity
Modified residuei476 – 4761Phosphoserine; by autocatalysis3 Publications

Post-translational modificationi

Autophosphorylated on serine residues when activated by CDC42/p21 By similarity.1 Publication
Phosphorylated on tyrosine residues upon stimulation of FGFR2.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BTW9.
PaxDbiQ8BTW9.
PRIDEiQ8BTW9.

PTM databases

PhosphoSiteiQ8BTW9.

Expressioni

Gene expression databases

BgeeiQ8BTW9.
CleanExiMM_PAK4.
GenevestigatoriQ8BTW9.

Interactioni

Subunit structurei

Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1 By similarity. Interacts with FGFR2 and GRB2.1 Publication

Protein-protein interaction databases

BioGridi214149. 1 interaction.
IntActiQ8BTW9. 1 interaction.
MINTiMINT-4106515.
STRINGi10090.ENSMUSP00000103918.

Structurei

3D structure databases

ProteinModelPortaliQ8BTW9.
SMRiQ8BTW9. Positions 10-44, 300-593.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 2414CRIB
Add
BLAST
Domaini323 – 574252Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 322298Linker
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 74Poly-Lys
Compositional biasi105 – 1084Poly-Pro
Compositional biasi216 – 29883Pro-rich
Add
BLAST
Compositional biasi242 – 2465Poly-Ser

Sequence similaritiesi

Contains 1 CRIB domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00670000097939.
HOGENOMiHOG000234205.
HOVERGENiHBG108518.
InParanoidiQ8BTW9.
KOiK05734.
OMAiIDPACIT.
OrthoDBiEOG73804D.
PhylomeDBiQ8BTW9.
TreeFamiTF105352.

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.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BTW9-1 [UniParc]FASTAAdd to Basket

« Hide

MFGKKKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP    50
KPLIDPACIT SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL 100
RRESPPPPAR AHQENGMLEE RAAPARMAPD KAGSRARATG HSEAGSGSGD 150
RRRVGPEKRP KSSRDGPGGP QEASRDKRPL SGPDVSTPQP GSLTSGTKLA 200
AGRPFNTYPR ADTDHPPRGA QGEPHTMAPN GPSATGLAAP QSSSSSRPPT 250
RARGAPSPGV LGPHASEPQL APPARALAAP AVPPAPGPPG PRSPQREPQR 300
VSHEQFRAAL QLVVDPGDPR SYLDNFIKIG EGSTGIVCIA TVRSSGKLVA 350
VKKMDLRKQQ RRELLFNEVV IMRDYRHENV VEMYNSYLVG DELWVVMEFL 400
EGGALTDIVT HTRMNEEQIA AVCLAVLQAL AVLHAQGVIH RDIKSDSILL 450
THDGRVKLSD FGFCAQVSKE VPRRKSLVGT PYWMAPELIS RLPYGPEVDI 500
WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPRLKNL HKASPSLKGF 550
LDRLLVRDPA QRATAAELLK HPFLTKAGPP ASIVPLMRQH RTR 593
Length:593
Mass (Da):64,623
Last modified:March 1, 2003 - v1
Checksum:i4AFA91DD73D4C6D5
GO

Sequence cautioni

The sequence BAC98108.2 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → R in AAO61496. 1 Publication
Sequence conflicti248 – 2481P → L in AAO61496. 1 Publication
Sequence conflicti564 – 5641T → P in BAB30889. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY217016 mRNA. Translation: AAO61496.1.
AK129298 mRNA. Translation: BAC98108.2. Different initiation.
AK017713 mRNA. Translation: BAB30889.1.
AK088512 mRNA. Translation: BAC40396.1.
BC048238 mRNA. Translation: AAH48238.1.
CCDSiCCDS21049.1.
RefSeqiNP_081746.1. NM_027470.3.
XP_006540419.1. XM_006540356.1.
UniGeneiMm.21876.

Genome annotation databases

EnsembliENSMUST00000032823; ENSMUSP00000032823; ENSMUSG00000030602.
ENSMUST00000108283; ENSMUSP00000103918; ENSMUSG00000030602.
GeneIDi70584.
KEGGimmu:70584.
UCSCiuc009fzh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY217016 mRNA. Translation: AAO61496.1 .
AK129298 mRNA. Translation: BAC98108.2 . Different initiation.
AK017713 mRNA. Translation: BAB30889.1 .
AK088512 mRNA. Translation: BAC40396.1 .
BC048238 mRNA. Translation: AAH48238.1 .
CCDSi CCDS21049.1.
RefSeqi NP_081746.1. NM_027470.3.
XP_006540419.1. XM_006540356.1.
UniGenei Mm.21876.

3D structure databases

ProteinModelPortali Q8BTW9.
SMRi Q8BTW9. Positions 10-44, 300-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 214149. 1 interaction.
IntActi Q8BTW9. 1 interaction.
MINTi MINT-4106515.
STRINGi 10090.ENSMUSP00000103918.

PTM databases

PhosphoSitei Q8BTW9.

Proteomic databases

MaxQBi Q8BTW9.
PaxDbi Q8BTW9.
PRIDEi Q8BTW9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032823 ; ENSMUSP00000032823 ; ENSMUSG00000030602 .
ENSMUST00000108283 ; ENSMUSP00000103918 ; ENSMUSG00000030602 .
GeneIDi 70584.
KEGGi mmu:70584.
UCSCi uc009fzh.1. mouse.

Organism-specific databases

CTDi 10298.
MGIi MGI:1917834. Pak4.
Rougei Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00670000097939.
HOGENOMi HOG000234205.
HOVERGENi HBG108518.
InParanoidi Q8BTW9.
KOi K05734.
OMAi IDPACIT.
OrthoDBi EOG73804D.
PhylomeDBi Q8BTW9.
TreeFami TF105352.

Miscellaneous databases

ChiTaRSi PAK4. mouse.
NextBioi 331922.
PROi Q8BTW9.
SOURCEi Search...

Gene expression databases

Bgeei Q8BTW9.
CleanExi MM_PAK4.
Genevestigatori Q8BTW9.

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.
[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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "p21-activated protein kinase 4 (PAK4) interacts with the keratinocyte growth factor receptor and participates in keratinocyte growth factor-mediated inhibition of oxidant-induced cell death."
    Lu Y., Pan Z.-Z., Devaux Y., Ray P.
    J. Biol. Chem. 278:10374-10380(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR2 AND GRB2, PHOSPHORYLATION AT TYROSINE RESIDUES.
    Strain: BALB/c.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  3. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "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].
    Strain: NOD.
    Tissue: Embryo and Thymus.
  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].
    Strain: FVB/N.
    Tissue: Colon.
  6. "Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin."
    Dan C., Kelly A., Bernard O., Minden A.
    J. Biol. Chem. 276:32115-32121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LIMK1.
  7. "PAK4 kinase is essential for embryonic viability and for proper neuronal development."
    Qu J., Li X., Novitch B.G., Zheng Y., Kohn M., Xie J.M., Kozinn S., Bronson R., Beg A.A., Minden A.
    Mol. Cell. Biol. 23:7122-7133(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "PAK4 is required for regulation of the cell-cycle regulatory protein p21, and for control of cell-cycle progression."
    Nekrasova T., Minden A.
    J. Cell. Biochem. 112:1795-1806(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "A key role for Pak4 in proliferation and differentiation of neural progenitor cells."
    Tian Y., Lei L., Minden A.
    Dev. Biol. 353:206-216(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPAK4_MOUSE
AccessioniPrimary (citable) accession number: Q8BTW9
Secondary accession number(s): Q6ZPX0, Q80Z97, Q9CS71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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