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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)DescriptionActionsGraphical viewLength
Binding sitei350ATPPROSITE-ProRule annotation1
Active sitei440Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi327 – 335ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein kinase activity Source: ProtInc
  • receptor signaling protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cell growth Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • cellular response to organic cyclic compound Source: Ensembl
  • cytoskeleton organization Source: UniProtKB
  • dendritic spine development Source: Ensembl
  • movement of cell or subcellular component Source: ProtInc
  • signal transduction Source: UniProtKB
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

BioCyciZFISH:HS05417-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-428540. Activation of Rac.
SignaLinkiO96013.
SIGNORiO96013.

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
Proteomesi
  • UP000005640 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

  • cell-cell adherens junction Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi445S → N: Approximately 30-fold increased autophosphorylation (constitutively active mutant). 1 Publication1
Mutagenesisi474S → E: Approximately 3-fold increased autophosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi10298.
OpenTargetsiENSG00000130669.
PharmGKBiPA32920.

Chemistry databases

ChEMBLiCHEMBL4482.
GuidetoPHARMACOLOGYi2136.

Polymorphism and mutation databases

BioMutaiPAK4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000864741 – 591Serine/threonine-protein kinase PAK 4Add BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41PhosphoserineCombined sources1
Modified residuei78N6-methyllysineCombined sources1
Modified residuei104PhosphoserineCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei167PhosphoserineCombined sources1
Modified residuei181PhosphoserineCombined sources1
Modified residuei187PhosphothreonineCombined sources1
Modified residuei195PhosphoserineCombined sources1
Modified residuei207PhosphothreonineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei267PhosphoserineCombined sources1
Modified residuei291PhosphoserineCombined sources1
Modified residuei474Phosphoserine; by autocatalysisCombined sources1 Publication1

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

Methylation, Phosphoprotein

Proteomic databases

EPDiO96013.
MaxQBiO96013.
PaxDbiO96013.
PeptideAtlasiO96013.
PRIDEiO96013.

PTM databases

iPTMnetiO96013.
PhosphoSitePlusiO96013.

Expressioni

Tissue specificityi

Highest expression in prostate, testis and colon.

Gene expression databases

BgeeiENSG00000130669.
CleanExiHS_PAK4.
ExpressionAtlasiO96013. baseline and differential.
GenevisibleiO96013. HS.

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
TERF1P542742EBI-713738,EBI-710997

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi115586. 49 interactors.
DIPiDIP-39742N.
IntActiO96013. 19 interactors.
MINTiMINT-1387795.
STRINGi9606.ENSP00000351049.

Chemistry databases

BindingDBiO96013.

Structurei

Secondary structure

1591
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 26Combined sources12
Turni27 – 30Combined sources4
Beta strandi31 – 34Combined sources4
Helixi37 – 39Combined sources3
Turni40 – 42Combined sources3
Turni46 – 48Combined sources3
Helixi301 – 311Combined sources11
Beta strandi312 – 315Combined sources4
Helixi317 – 319Combined sources3
Beta strandi321 – 329Combined sources9
Beta strandi331 – 333Combined sources3
Beta strandi334 – 340Combined sources7
Turni341 – 343Combined sources3
Beta strandi346 – 353Combined sources8
Helixi354 – 356Combined sources3
Helixi360 – 362Combined sources3
Helixi363 – 369Combined sources7
Turni370 – 372Combined sources3
Beta strandi381 – 387Combined sources7
Beta strandi390 – 395Combined sources6
Helixi403 – 409Combined sources7
Helixi414 – 433Combined sources20
Helixi443 – 445Combined sources3
Beta strandi446 – 448Combined sources3
Beta strandi454 – 456Combined sources3
Helixi459 – 461Combined sources3
Beta strandi467 – 469Combined sources3
Beta strandi475 – 477Combined sources3
Helixi479 – 481Combined sources3
Helixi484 – 487Combined sources4
Helixi495 – 510Combined sources16
Turni514 – 517Combined sources4
Helixi520 – 529Combined sources10
Helixi538 – 540Combined sources3
Helixi543 – 552Combined sources10
Turni557 – 559Combined sources3
Helixi563 – 566Combined sources4
Helixi570 – 574Combined sources5
Helixi578 – 581Combined sources4
Helixi582 – 584Combined sources3
Turni586 – 588Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XBRX-ray2.94A278-591[»]
4XBUX-ray2.06A286-591[»]
5BMSX-ray2.90A300-591[»]
ProteinModelPortaliO96013.
SMRiO96013.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96013.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 24CRIBPROSITE-ProRule annotationAdd BLAST14
Domaini321 – 572Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 320LinkerAdd BLAST296
Regioni298 – 323GEF-interaction domain (GID)Add BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi105 – 108Poly-Pro4
Compositional biasi242 – 247Poly-Ser6

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00860000133680.
HOVERGENiHBG108518.
InParanoidiO96013.
KOiK05734.
OMAiCQASHSS.
OrthoDBiEOG091G0OT5.
PhylomeDBiO96013.
TreeFamiTF105352.

Family and domain databases

CDDicd01093. CRIB_PAK_like. 1 hit.
Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR033923. PAK_BD.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 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:May 1, 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 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAC11166 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040970135R → Q.1 PublicationCorresponds to variant rs56099436dbSNPEnsembl.1
Natural variantiVAR_040971139A → T.1 PublicationCorresponds to variant rs35655056dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01757269 – 221Missing in isoform 3. 3 PublicationsAdd BLAST153
Alternative sequenceiVSP_004892120E → K in isoform 2. 1 Publication1
Alternative sequenceiVSP_004893121 – 285Missing in isoform 2. 1 PublicationAdd BLAST165
Alternative sequenceiVSP_017573132 – 221Missing in isoform 4. 1 PublicationAdd BLAST90

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_011524618.1. XM_011526316.1. [O96013-1]
XP_011524619.1. XM_011526317.2. [O96013-1]
XP_011524620.1. XM_011526318.2. [O96013-1]
XP_011524621.1. XM_011526319.2. [O96013-1]
XP_011524622.1. XM_011526320.1. [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.2. human. [O96013-1]

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_011524618.1. XM_011526316.1. [O96013-1]
XP_011524619.1. XM_011526317.2. [O96013-1]
XP_011524620.1. XM_011526318.2. [O96013-1]
XP_011524621.1. XM_011526319.2. [O96013-1]
XP_011524622.1. XM_011526320.1. [O96013-3]
UniGeneiHs.20447.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XBRX-ray2.94A278-591[»]
4XBUX-ray2.06A286-591[»]
5BMSX-ray2.90A300-591[»]
ProteinModelPortaliO96013.
SMRiO96013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115586. 49 interactors.
DIPiDIP-39742N.
IntActiO96013. 19 interactors.
MINTiMINT-1387795.
STRINGi9606.ENSP00000351049.

Chemistry databases

BindingDBiO96013.
ChEMBLiCHEMBL4482.
GuidetoPHARMACOLOGYi2136.

PTM databases

iPTMnetiO96013.
PhosphoSitePlusiO96013.

Polymorphism and mutation databases

BioMutaiPAK4.

Proteomic databases

EPDiO96013.
MaxQBiO96013.
PaxDbiO96013.
PeptideAtlasiO96013.
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.2. human. [O96013-1]

Organism-specific databases

CTDi10298.
DisGeNETi10298.
GeneCardsiPAK4.
HGNCiHGNC:16059. PAK4.
HPAiCAB025747.
CAB044670.
MIMi605451. gene.
neXtProtiNX_O96013.
OpenTargetsiENSG00000130669.
PharmGKBiPA32920.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00860000133680.
HOVERGENiHBG108518.
InParanoidiO96013.
KOiK05734.
OMAiCQASHSS.
OrthoDBiEOG091G0OT5.
PhylomeDBiO96013.
TreeFamiTF105352.

Enzyme and pathway databases

BioCyciZFISH:HS05417-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-428540. Activation of Rac.
SignaLinkiO96013.
SIGNORiO96013.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000130669.
CleanExiHS_PAK4.
ExpressionAtlasiO96013. baseline and differential.
GenevisibleiO96013. HS.

Family and domain databases

CDDicd01093. CRIB_PAK_like. 1 hit.
Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR033923. PAK_BD.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 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...

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 24, 2001
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 179 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

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 one 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.