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Protein

Serine/threonine-protein kinase PAK 4

Gene

PAK4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei350 – 3501ATPPROSITE-ProRule annotation
Active sitei440 – 4401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi327 – 3359ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell cycle Source: UniProtKB-KW
  3. cell growth Source: UniProtKB
  4. cell migration Source: UniProtKB
  5. cell proliferation Source: UniProtKB
  6. cytoskeleton organization Source: UniProtKB
  7. intracellular signal transduction Source: GO_Central
  8. movement of cell or subcellular component Source: ProtInc
  9. signal transduction Source: UniProtKB
  10. 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

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_19226. Activation of Rac.
SignaLinkiO96013.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:16059. PAK4.

Subcellular locationi

Cytoplasm 1 Publication
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.

GO - Cellular componenti

  1. focal adhesion Source: UniProtKB
  2. Golgi apparatus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi445 – 4451S → N: Approximately 30-fold increased autophosphorylation (constitutively active mutant). 1 Publication
Mutagenesisi474 – 4741S → E: Approximately 3-fold increased autophosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA32920.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Serine/threonine-protein kinase PAK 4PRO_0000086474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine2 Publications
Modified residuei104 – 1041Phosphoserine2 Publications
Modified residuei148 – 1481Phosphoserine2 Publications
Modified residuei167 – 1671Phosphoserine2 Publications
Modified residuei181 – 1811Phosphoserine6 Publications
Modified residuei187 – 1871Phosphothreonine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication
Modified residuei258 – 2581Phosphoserine2 Publications
Modified residuei267 – 2671Phosphoserine1 Publication
Modified residuei291 – 2911Phosphoserine2 Publications
Modified residuei474 – 4741Phosphoserine; by autocatalysis8 Publications

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO96013.
PaxDbiO96013.
PRIDEiO96013.

PTM databases

PhosphoSiteiO96013.

Expressioni

Tissue specificityi

Highest expression in prostate, testis and colon.

Gene expression databases

BgeeiO96013.
CleanExiHS_PAK4.
ExpressionAtlasiO96013. baseline and differential.
GenevestigatoriO96013.

Organism-specific databases

HPAiCAB025747.
CAB044670.

Interactioni

Subunit structurei

Interacts with FGFR2 and GRB2 (By similarity). Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609532EBI-713738,EBI-81752

Protein-protein interaction databases

BioGridi115586. 32 interactions.
DIPiDIP-39742N.
IntActiO96013. 14 interactions.
MINTiMINT-1387795.
STRINGi9606.ENSP00000351049.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 2612Combined sources
Turni27 – 304Combined sources
Beta strandi31 – 344Combined sources
Helixi37 – 393Combined sources
Turni40 – 423Combined sources
Turni46 – 483Combined sources
Helixi301 – 31111Combined sources
Beta strandi312 – 3154Combined sources
Helixi317 – 3193Combined sources
Beta strandi321 – 3299Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi334 – 3407Combined sources
Turni341 – 3433Combined sources
Beta strandi346 – 3538Combined sources
Helixi354 – 3563Combined sources
Helixi360 – 3623Combined sources
Helixi363 – 3697Combined sources
Turni370 – 3723Combined sources
Beta strandi381 – 3877Combined sources
Beta strandi390 – 3956Combined sources
Helixi403 – 4097Combined sources
Helixi414 – 43320Combined sources
Helixi443 – 4453Combined sources
Beta strandi446 – 4483Combined sources
Beta strandi454 – 4563Combined sources
Helixi459 – 4613Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi475 – 4773Combined sources
Helixi479 – 4813Combined sources
Helixi484 – 4874Combined sources
Helixi495 – 51016Combined sources
Turni514 – 5174Combined sources
Helixi520 – 52910Combined sources
Helixi538 – 5403Combined sources
Helixi543 – 55210Combined sources
Turni557 – 5593Combined sources
Helixi563 – 5664Combined sources
Helixi570 – 5745Combined sources
Helixi578 – 5814Combined sources
Helixi582 – 5843Combined sources
Turni586 – 5883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BVAX-ray2.30A/B300-591[»]
2CDZX-ray2.30A291-591[»]
2J0IX-ray1.60A291-591[»]
2OV2X-ray2.10I/J/K/L/M/N/O/P10-44[»]
2Q0NX-ray1.75A291-591[»]
2X4ZX-ray2.10A297-591[»]
4APPX-ray2.20A300-591[»]
4FIEX-ray3.11A/B5-591[»]
4FIFX-ray2.60A/B286-591[»]
C/D49-56[»]
4FIGX-ray3.01A/B286-591[»]
4FIHX-ray1.97A286-591[»]
4FIIX-ray2.00A286-591[»]
B49-56[»]
4FIJX-ray2.30A286-591[»]
4JDHX-ray2.00A286-591[»]
4JDIX-ray1.85A286-591[»]
4JDJX-ray2.30A286-591[»]
4JDKX-ray2.40A286-591[»]
4L67X-ray2.80A300-591[»]
B36-60[»]
4NJDX-ray2.50A300-591[»]
4O0VX-ray2.80A300-591[»]
4O0XX-ray2.48A300-591[»]
4O0YX-ray2.20A300-591[»]
ProteinModelPortaliO96013.
SMRiO96013. Positions 10-44, 300-589.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96013.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 2414CRIBPROSITE-ProRule annotationAdd
BLAST
Domaini321 – 572252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 320296LinkerAdd
BLAST
Regioni298 – 32326GEF-interaction domain (GID)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi105 – 1084Poly-Pro
Compositional biasi242 – 2476Poly-Ser

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121858.
HOVERGENiHBG108518.
InParanoidiO96013.
KOiK05734.
OMAiHNVASNG.
OrthoDBiEOG73804D.
PhylomeDBiO96013.
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.
[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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O96013-1) [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
MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP
60 70 80 90 100
KPLVDPACIT SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL
110 120 130 140 150
RRDSPPPPAR ARQENGMPEE PATTARGGPG KAGSRGRFAG HSEAGGGSGD
160 170 180 190 200
RRRAGPEKRP KSSREGSGGP QESSRDKRPL SGPDVGTPQP AGLASGAKLA
210 220 230 240 250
AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAIP QSSSSSSRPP
260 270 280 290 300
TRARGAPSPG VLGPHASEPQ LAPPACTPAA PAVPGPPGPR SPQREPQRVS
310 320 330 340 350
HEQFRAALQL VVDPGDPRSY LDNFIKIGEG STGIVCIATV RSSGKLVAVK
360 370 380 390 400
KMDLRKQQRR ELLFNEVVIM RDYQHENVVE MYNSYLVGDE LWVVMEFLEG
410 420 430 440 450
GALTDIVTHT RMNEEQIAAV CLAVLQALSV LHAQGVIHRD IKSDSILLTH
460 470 480 490 500
DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY WMAPELISRL PYGPEVDIWS
510 520 530 540 550
LGIMVIEMVD GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK VSPSLKGFLD
560 570 580 590
RLLVRDPAQR ATAAELLKHP FLAKAGPPAS IVPLMRQNRT R
Length:591
Mass (Da):64,072
Last modified:April 30, 1999 - v1
Checksum:i04C2A5C0B06427D5
GO
Isoform 2 (identifier: O96013-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: E → K
     121-285: Missing.

Note: No experimental confirmation available.

Show »
Length:426
Mass (Da):47,924
Checksum:i505879690593E93A
GO
Isoform 3 (identifier: O96013-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-221: Missing.

Show »
Length:438
Mass (Da):48,268
Checksum:i4A596EBBCECE9883
GO
Isoform 4 (identifier: O96013-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-221: Missing.

Note: No experimental confirmation available.

Show »
Length:501
Mass (Da):54,940
Checksum:i6EE6240ECE65E79D
GO

Sequence cautioni

The sequence BAA86456.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC11166.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351R → Q.1 Publication
Corresponds to variant rs56099436 [ dbSNP | Ensembl ].
VAR_040970
Natural varianti139 – 1391A → T.1 Publication
Corresponds to variant rs35655056 [ dbSNP | Ensembl ].
VAR_040971

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 221153Missing in isoform 3. 3 PublicationsVSP_017572Add
BLAST
Alternative sequencei120 – 1201E → K in isoform 2. 1 PublicationVSP_004892
Alternative sequencei121 – 285165Missing in isoform 2. 1 PublicationVSP_004893Add
BLAST
Alternative sequencei132 – 22190Missing in isoform 4. 1 PublicationVSP_017573Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011855 mRNA. Translation: CAA09820.1.
AF005046 mRNA. Translation: AAD01210.1.
AB032968 mRNA. Translation: BAA86456.1. Different initiation.
AK074728 mRNA. Translation: BAC11166.1. Different initiation.
AK294586 mRNA. Translation: BAG57777.1.
AL834236 mRNA. Translation: CAD38914.2.
CH471126 Genomic DNA. Translation: EAW56861.1.
BC002921 mRNA. Translation: AAH02921.1.
BC011368 mRNA. Translation: AAH11368.1.
BC025282 mRNA. Translation: AAH25282.1.
BC034511 mRNA. Translation: AAH34511.1.
CCDSiCCDS12528.1. [O96013-1]
CCDS33019.1. [O96013-3]
RefSeqiNP_001014831.1. NM_001014831.2. [O96013-1]
NP_001014832.1. NM_001014832.1. [O96013-1]
NP_001014834.1. NM_001014834.2. [O96013-3]
NP_001014835.1. NM_001014835.1. [O96013-3]
NP_005875.1. NM_005884.3. [O96013-1]
XP_006723034.1. XM_006722971.1. [O96013-1]
XP_006723035.1. XM_006722972.1. [O96013-3]
UniGeneiHs.20447.

Genome annotation databases

EnsembliENST00000321944; ENSP00000326864; ENSG00000130669. [O96013-4]
ENST00000358301; ENSP00000351049; ENSG00000130669. [O96013-1]
ENST00000360442; ENSP00000353625; ENSG00000130669. [O96013-1]
ENST00000593690; ENSP00000469413; ENSG00000130669. [O96013-1]
ENST00000599386; ENSP00000471157; ENSG00000130669. [O96013-3]
ENST00000599470; ENSP00000470284; ENSG00000130669. [O96013-3]
GeneIDi10298.
KEGGihsa:10298.
UCSCiuc002okj.1. human. [O96013-1]
uc002okm.1. human. [O96013-3]
uc002okp.1. human. [O96013-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011855 mRNA. Translation: CAA09820.1.
AF005046 mRNA. Translation: AAD01210.1.
AB032968 mRNA. Translation: BAA86456.1. Different initiation.
AK074728 mRNA. Translation: BAC11166.1. Different initiation.
AK294586 mRNA. Translation: BAG57777.1.
AL834236 mRNA. Translation: CAD38914.2.
CH471126 Genomic DNA. Translation: EAW56861.1.
BC002921 mRNA. Translation: AAH02921.1.
BC011368 mRNA. Translation: AAH11368.1.
BC025282 mRNA. Translation: AAH25282.1.
BC034511 mRNA. Translation: AAH34511.1.
CCDSiCCDS12528.1. [O96013-1]
CCDS33019.1. [O96013-3]
RefSeqiNP_001014831.1. NM_001014831.2. [O96013-1]
NP_001014832.1. NM_001014832.1. [O96013-1]
NP_001014834.1. NM_001014834.2. [O96013-3]
NP_001014835.1. NM_001014835.1. [O96013-3]
NP_005875.1. NM_005884.3. [O96013-1]
XP_006723034.1. XM_006722971.1. [O96013-1]
XP_006723035.1. XM_006722972.1. [O96013-3]
UniGeneiHs.20447.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BVAX-ray2.30A/B300-591[»]
2CDZX-ray2.30A291-591[»]
2J0IX-ray1.60A291-591[»]
2OV2X-ray2.10I/J/K/L/M/N/O/P10-44[»]
2Q0NX-ray1.75A291-591[»]
2X4ZX-ray2.10A297-591[»]
4APPX-ray2.20A300-591[»]
4FIEX-ray3.11A/B5-591[»]
4FIFX-ray2.60A/B286-591[»]
C/D49-56[»]
4FIGX-ray3.01A/B286-591[»]
4FIHX-ray1.97A286-591[»]
4FIIX-ray2.00A286-591[»]
B49-56[»]
4FIJX-ray2.30A286-591[»]
4JDHX-ray2.00A286-591[»]
4JDIX-ray1.85A286-591[»]
4JDJX-ray2.30A286-591[»]
4JDKX-ray2.40A286-591[»]
4L67X-ray2.80A300-591[»]
B36-60[»]
4NJDX-ray2.50A300-591[»]
4O0VX-ray2.80A300-591[»]
4O0XX-ray2.48A300-591[»]
4O0YX-ray2.20A300-591[»]
ProteinModelPortaliO96013.
SMRiO96013. Positions 10-44, 300-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115586. 32 interactions.
DIPiDIP-39742N.
IntActiO96013. 14 interactions.
MINTiMINT-1387795.
STRINGi9606.ENSP00000351049.

Chemistry

BindingDBiO96013.
ChEMBLiCHEMBL4482.
GuidetoPHARMACOLOGYi2136.

PTM databases

PhosphoSiteiO96013.

Proteomic databases

MaxQBiO96013.
PaxDbiO96013.
PRIDEiO96013.

Protocols and materials databases

DNASUi10298.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321944; ENSP00000326864; ENSG00000130669. [O96013-4]
ENST00000358301; ENSP00000351049; ENSG00000130669. [O96013-1]
ENST00000360442; ENSP00000353625; ENSG00000130669. [O96013-1]
ENST00000593690; ENSP00000469413; ENSG00000130669. [O96013-1]
ENST00000599386; ENSP00000471157; ENSG00000130669. [O96013-3]
ENST00000599470; ENSP00000470284; ENSG00000130669. [O96013-3]
GeneIDi10298.
KEGGihsa:10298.
UCSCiuc002okj.1. human. [O96013-1]
uc002okm.1. human. [O96013-3]
uc002okp.1. human. [O96013-4]

Organism-specific databases

CTDi10298.
GeneCardsiGC19P039616.
HGNCiHGNC:16059. PAK4.
HPAiCAB025747.
CAB044670.
MIMi605451. gene.
neXtProtiNX_O96013.
PharmGKBiPA32920.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121858.
HOVERGENiHBG108518.
InParanoidiO96013.
KOiK05734.
OMAiHNVASNG.
OrthoDBiEOG73804D.
PhylomeDBiO96013.
TreeFamiTF105352.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_19226. Activation of Rac.
SignaLinkiO96013.

Miscellaneous databases

ChiTaRSiPAK4. human.
EvolutionaryTraceiO96013.
GeneWikiiPAK4.
GenomeRNAii10298.
NextBioi39028.
PROiO96013.
SOURCEiSearch...

Gene expression databases

BgeeiO96013.
CleanExiHS_PAK4.
ExpressionAtlasiO96013. baseline and differential.
GenevestigatoriO96013.

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.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia."
    Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A.
    EMBO J. 17:6527-6540(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphoma.
  2. Melnick M.B.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Neuroblastoma.
  3. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1).
    Tissue: Brain and Teratocarcinoma.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
    Tissue: Eye, Pancreas and Placenta.
  8. "The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis."
    Gnesutta N., Qu J., Minden A.
    J. Biol. Chem. 276:14414-14419(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
  9. "Activated PAK4 regulates cell adhesion and anchorage-independent growth."
    Qu J., Cammarano M.S., Shi Q., Ha K.C., de Lanerolle P., Minden A.
    Mol. Cell. Biol. 21:3523-3533(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-445 AND SER-474.
  10. "P21-activated kinase 4 interacts with integrin alpha v beta 5 and regulates alpha v beta 5-mediated cell migration."
    Zhang H., Li Z., Viklund E.K., Stromblad S.
    J. Cell Biol. 158:1287-1297(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Death receptor-induced activation of initiator caspase 8 is antagonized by serine/threonine kinase PAK4."
    Gnesutta N., Minden A.
    Mol. Cell. Biol. 23:7838-7848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
    Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
    EMBO J. 24:473-486(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "PAK4 mediates morphological changes through the regulation of GEF-H1."
    Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.
    J. Cell Sci. 118:1861-1872(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF2.
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; SER-258; SER-267; SER-291 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; THR-187; SER-195; SER-258; SER-291 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "p21-activated kinase 4 phosphorylation of integrin beta5 Ser-759 and Ser-762 regulates cell migration."
    Li Z., Zhang H., Lundin L., Thullberg M., Liu Y., Wang Y., Claesson-Welsh L., Stromblad S.
    J. Biol. Chem. 285:23699-23710(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ITGB5.
  20. "Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis."
    Bompard G., Rabeharivelo G., Frank M., Cau J., Delsert C., Morin N.
    J. Cell Biol. 190:807-822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RAN.
  21. "Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B."
    Wallace S.W., Durgan J., Jin D., Hall A.
    Mol. Biol. Cell 21:2996-3006(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "p21-activated kinases: three more join the Pak."
    Jaffer Z.M., Chernoff J.
    Int. J. Biochem. Cell Biol. 34:713-717(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  23. "The emerging importance of group II PAKs."
    Wells C.M., Jones G.E.
    Biochem. J. 425:465-473(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  24. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  28. "Crystal structure of the human p21-activated kinase 4."
    Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S., Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F., Knapp S.
    Submitted (JUN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, PHOSPHORYLATION AT SER-474.
  29. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-135 AND THR-139.

Entry informationi

Entry nameiPAK4_HUMAN
AccessioniPrimary (citable) accession number: O96013
Secondary accession number(s): B4DGG6
, Q8N4E1, Q8NCH5, Q8NDE3, Q9BU33, Q9ULS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2001
Last sequence update: April 30, 1999
Last modified: March 3, 2015
This is version 160 of the entry and version 1 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.