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O75914

- PAK3_HUMAN

UniProt

O75914 - PAK3_HUMAN

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Protein
Serine/threonine-protein kinase PAK 3
Gene
PAK3, OPHN3
Organism
Homo sapiens (Human)
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, 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.1 Publication

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121ATP By similarity
Active sitei402 – 4021Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi289 – 2979ATP By similarity

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. receptor signaling protein serine/threonine kinase activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. MAPK cascade Source: GOC
  2. activation of MAPK activity Source: GOC
  3. axonogenesis Source: UniProtKB
  4. dendrite development Source: UniProtKB
  5. dendritic spine morphogenesis Source: UniProtKB
  6. regulation of actin filament polymerization Source: UniProtKB
  7. signal transduction by phosphorylation Source: GOC
  8. synapse organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_19226. Activation of Rac.
SignaLinkiO75914.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 3 (EC:2.7.11.1)
Alternative name(s):
Beta-PAK
Oligophrenin-3
p21-activated kinase 3
Short name:
PAK-3
Gene namesi
Name:PAK3
Synonyms:OPHN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8592. PAK3.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 30 (MRX30) [MIM:300558]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671R → C in MRX30. 1 Publication
VAR_023825
Natural varianti380 – 3801A → E in MRX30. 1 Publication
VAR_023826

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300558. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA32919.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Serine/threonine-protein kinase PAK 3
PRO_0000086469Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Autophosphorylated when activated by CDC42/p21.1 Publication
Neddylated.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO75914.
PRIDEiO75914.

PTM databases

PhosphoSiteiO75914.

Expressioni

Tissue specificityi

Restricted to the nervous system. Highly expressed in postmitotic neurons of the developing and postnatal cerebral cortex and hippocampus.1 Publication

Gene expression databases

ArrayExpressiO75914.
BgeeiO75914.
GenevestigatoriO75914.

Organism-specific databases

HPAiHPA044791.

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 By similarity. Interacts with ARHGEF6 and ARHGEF7.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P60953-22EBI-3389553,EBI-287394
RAC1P630002EBI-3389553,EBI-413628

Protein-protein interaction databases

BioGridi111099. 7 interactions.
IntActiO75914. 3 interactions.
MINTiMINT-3001915.

Structurei

3D structure databases

ProteinModelPortaliO75914.
SMRiO75914. Positions 65-156, 181-553.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 8314CRIB
Add
BLAST
Domaini283 – 534252Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 15086Autoregulatory region By similarity
Add
BLAST
Regioni65 – 12359GTPase-binding By similarity
Add
BLAST
Regioni84 – 282199Linker
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi187 – 20115Poly-Glu
Add
BLAST

Sequence similaritiesi

Contains 1 CRIB domain.

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000234202.
HOVERGENiHBG108518.
KOiK05733.
OMAiSANENDM.
OrthoDBiEOG7CK36J.
PhylomeDBiO75914.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75914-1) [UniParc]FASTAAdd to Basket

Also known as: PAK3b

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

MSDGLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS    50
IFPGGGDKTN KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTPDLYGSQM 100
CPGKLPEGIP EQWARLLQTS NITKLEQKKN PQAVLDVLKF YDSKETVNNQ 150
KYMSFTSGDK SAHGYIAAHP SSTKTASEPP LAPPVSEEED EEEEEEEDEN 200
EPPPVIAPRP EHTKSIYTRS VVESIASPAV PNKEVTPPSA ENANSSTLYR 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):62,310
Last modified:May 10, 2004 - v2
Checksum:iBC39AEC6F0A5478B
GO
Isoform 2 (identifier: O75914-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:544
Mass (Da):60,693
Checksum:i230AF6952CB049E2
GO
Isoform 3 (identifier: O75914-3) [UniParc]FASTAAdd to Basket

Also known as: PAK3cb

The sequence of this isoform differs from the canonical sequence as follows:
     92-92: T → TNSPFQTSRPVTVASSQSEGKM

Show »
Length:580
Mass (Da):64,530
Checksum:i9646E127F2F007A2
GO
Isoform 4 (identifier: O75914-4) [UniParc]FASTAAdd to Basket

Also known as: PAK3c

The sequence of this isoform differs from the canonical sequence as follows:
     92-107: TPDLYGSQMCPGKLPE → TNSPFQTSRPVTVASSQSEGKM

Show »
Length:565
Mass (Da):62,913
Checksum:i6A0C2190BBBBDC1F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671R → C in MRX30. 1 Publication
VAR_023825
Natural varianti380 – 3801A → E in MRX30. 1 Publication
VAR_023826
Natural varianti440 – 4401T → S in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_046764

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei92 – 10716TPDLY…GKLPE → TNSPFQTSRPVTVASSQSEG KM in isoform 4.
VSP_041840Add
BLAST
Alternative sequencei92 – 921T → TNSPFQTSRPVTVASSQSEG KM in isoform 3.
VSP_041839
Alternative sequencei93 – 10715Missing in isoform 2.
VSP_010242Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321S → F in AAF67008. 1 Publication
Sequence conflicti36 – 361P → S in AAF67008. 1 Publication
Sequence conflicti73 – 731P → S in AAF67008. 1 Publication
Sequence conflicti106 – 1072PE → SL in AAF67008. 1 Publication
Sequence conflicti123 – 1231T → P in AAF67008. 1 Publication
Sequence conflicti127 – 1304QKKN → PEEE in AAF67008. 1 Publication
Sequence conflicti134 – 1374VLDV → CSRC in AAF67008. 1 Publication
Sequence conflicti146 – 1483TVN → PVT in AAF67008. 1 Publication
Sequence conflicti175 – 1751T → P in AAF67008. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068864 mRNA. Translation: AAC36097.1.
AF155651 mRNA. Translation: AAF67008.1.
AB102659 mRNA. Translation: BAC81128.1.
AB102251 Genomic DNA. Translation: BAC80750.1.
AB102252 Genomic DNA. Translation: BAC80751.1.
AB102253 Genomic DNA. Translation: BAC80752.1.
AB102254 Genomic DNA. Translation: BAC80753.1.
AB102255 Genomic DNA. Translation: BAC80754.1.
AB102256 Genomic DNA. Translation: BAC80755.1.
AB102257 Genomic DNA. Translation: BAC80756.1.
AB102258 Genomic DNA. Translation: BAC80757.1.
AB102259 Genomic DNA. Translation: BAC80758.1.
AB102260 Genomic DNA. Translation: BAC80759.1.
AB102261 Genomic DNA. Translation: BAC80760.1.
AB102262 Genomic DNA. Translation: BAC80761.1.
AB102263 Genomic DNA. Translation: BAC80762.1.
AB102264 Genomic DNA. Translation: BAC80763.1.
AB102265 Genomic DNA. Translation: BAC80764.1.
AB102266 Genomic DNA. Translation: BAC80765.1.
AB102267 Genomic DNA. Translation: BAC80766.1.
AB102268 Genomic DNA. Translation: BAC80767.1.
AB102269 Genomic DNA. Translation: BAC80768.1.
AB102270 Genomic DNA. Translation: BAC80769.1.
AB102281 Genomic DNA. Translation: BAC80780.1.
AB102282 Genomic DNA. Translation: BAC80781.1.
AB102283 Genomic DNA. Translation: BAC80782.1.
AB102284 Genomic DNA. Translation: BAC80783.1.
AB102285 Genomic DNA. Translation: BAC80784.1.
AB102286 Genomic DNA. Translation: BAC80785.1.
AB102287 Genomic DNA. Translation: BAC80786.1.
AB102288 Genomic DNA. Translation: BAC80787.1.
AB102289 Genomic DNA. Translation: BAC80788.1.
AB102290 Genomic DNA. Translation: BAC80789.1.
AB102291 Genomic DNA. Translation: BAC80790.1.
AB102292 Genomic DNA. Translation: BAC80791.1.
AB102293 Genomic DNA. Translation: BAC80792.1.
AB102294 Genomic DNA. Translation: BAC80793.1.
AB102295 Genomic DNA. Translation: BAC80794.1.
AB102296 Genomic DNA. Translation: BAC80795.1.
AB102297 Genomic DNA. Translation: BAC80796.1.
AB102298 Genomic DNA. Translation: BAC80797.1.
AB102299 Genomic DNA. Translation: BAC80798.1.
AB102300 Genomic DNA. Translation: BAC80799.1.
AM943850 mRNA. Translation: CAQ16016.1.
AM943851 mRNA. Translation: CAQ16017.1.
AM943852 mRNA. Translation: CAQ16018.1.
AK290504 mRNA. Translation: BAF83193.1.
AL356578 Genomic DNA. No translation available.
AL357774, AL031117, AL117326 Genomic DNA. Translation: CAI40843.1.
AL357774, AL031117, AL117326 Genomic DNA. Translation: CAI40844.1.
AL031117, AL117326, AL357774 Genomic DNA. Translation: CAI43157.1.
AL031117, AL117326, AL357774 Genomic DNA. Translation: CAI43158.1.
AL117326, AL031117, AL357774 Genomic DNA. Translation: CAI43167.1.
AL117326, AL031117, AL357774 Genomic DNA. Translation: CAI43168.1.
CH471120 Genomic DNA. Translation: EAX02654.1.
CCDSiCCDS14554.1. [O75914-2]
CCDS48151.1. [O75914-3]
CCDS48152.1. [O75914-4]
CCDS48153.1. [O75914-1]
RefSeqiNP_001121638.1. NM_001128166.1. [O75914-2]
NP_001121639.1. NM_001128167.1. [O75914-2]
NP_001121640.1. NM_001128168.1. [O75914-3]
NP_001121644.1. NM_001128172.1. [O75914-4]
NP_001121645.1. NM_001128173.1. [O75914-1]
NP_002569.1. NM_002578.3. [O75914-2]
XP_006724719.1. XM_006724656.1. [O75914-1]
UniGeneiHs.593599.
Hs.656789.

Genome annotation databases

EnsembliENST00000262836; ENSP00000262836; ENSG00000077264. [O75914-1]
ENST00000360648; ENSP00000353864; ENSG00000077264. [O75914-3]
ENST00000372007; ENSP00000361077; ENSG00000077264. [O75914-2]
ENST00000372010; ENSP00000361080; ENSG00000077264. [O75914-1]
ENST00000417227; ENSP00000389172; ENSG00000077264. [O75914-4]
ENST00000425146; ENSP00000401982; ENSG00000077264. [O75914-2]
ENST00000446737; ENSP00000410853; ENSG00000077264. [O75914-2]
ENST00000518291; ENSP00000428921; ENSG00000077264. [O75914-3]
ENST00000519681; ENSP00000429113; ENSG00000077264. [O75914-4]
GeneIDi5063.
KEGGihsa:5063.
UCSCiuc004eoz.2. human. [O75914-2]
uc004epa.2. human. [O75914-1]
uc010npv.1. human. [O75914-3]
uc010npw.1. human. [O75914-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068864 mRNA. Translation: AAC36097.1 .
AF155651 mRNA. Translation: AAF67008.1 .
AB102659 mRNA. Translation: BAC81128.1 .
AB102251 Genomic DNA. Translation: BAC80750.1 .
AB102252 Genomic DNA. Translation: BAC80751.1 .
AB102253 Genomic DNA. Translation: BAC80752.1 .
AB102254 Genomic DNA. Translation: BAC80753.1 .
AB102255 Genomic DNA. Translation: BAC80754.1 .
AB102256 Genomic DNA. Translation: BAC80755.1 .
AB102257 Genomic DNA. Translation: BAC80756.1 .
AB102258 Genomic DNA. Translation: BAC80757.1 .
AB102259 Genomic DNA. Translation: BAC80758.1 .
AB102260 Genomic DNA. Translation: BAC80759.1 .
AB102261 Genomic DNA. Translation: BAC80760.1 .
AB102262 Genomic DNA. Translation: BAC80761.1 .
AB102263 Genomic DNA. Translation: BAC80762.1 .
AB102264 Genomic DNA. Translation: BAC80763.1 .
AB102265 Genomic DNA. Translation: BAC80764.1 .
AB102266 Genomic DNA. Translation: BAC80765.1 .
AB102267 Genomic DNA. Translation: BAC80766.1 .
AB102268 Genomic DNA. Translation: BAC80767.1 .
AB102269 Genomic DNA. Translation: BAC80768.1 .
AB102270 Genomic DNA. Translation: BAC80769.1 .
AB102281 Genomic DNA. Translation: BAC80780.1 .
AB102282 Genomic DNA. Translation: BAC80781.1 .
AB102283 Genomic DNA. Translation: BAC80782.1 .
AB102284 Genomic DNA. Translation: BAC80783.1 .
AB102285 Genomic DNA. Translation: BAC80784.1 .
AB102286 Genomic DNA. Translation: BAC80785.1 .
AB102287 Genomic DNA. Translation: BAC80786.1 .
AB102288 Genomic DNA. Translation: BAC80787.1 .
AB102289 Genomic DNA. Translation: BAC80788.1 .
AB102290 Genomic DNA. Translation: BAC80789.1 .
AB102291 Genomic DNA. Translation: BAC80790.1 .
AB102292 Genomic DNA. Translation: BAC80791.1 .
AB102293 Genomic DNA. Translation: BAC80792.1 .
AB102294 Genomic DNA. Translation: BAC80793.1 .
AB102295 Genomic DNA. Translation: BAC80794.1 .
AB102296 Genomic DNA. Translation: BAC80795.1 .
AB102297 Genomic DNA. Translation: BAC80796.1 .
AB102298 Genomic DNA. Translation: BAC80797.1 .
AB102299 Genomic DNA. Translation: BAC80798.1 .
AB102300 Genomic DNA. Translation: BAC80799.1 .
AM943850 mRNA. Translation: CAQ16016.1 .
AM943851 mRNA. Translation: CAQ16017.1 .
AM943852 mRNA. Translation: CAQ16018.1 .
AK290504 mRNA. Translation: BAF83193.1 .
AL356578 Genomic DNA. No translation available.
AL357774 , AL031117 , AL117326 Genomic DNA. Translation: CAI40843.1 .
AL357774 , AL031117 , AL117326 Genomic DNA. Translation: CAI40844.1 .
AL031117 , AL117326 , AL357774 Genomic DNA. Translation: CAI43157.1 .
AL031117 , AL117326 , AL357774 Genomic DNA. Translation: CAI43158.1 .
AL117326 , AL031117 , AL357774 Genomic DNA. Translation: CAI43167.1 .
AL117326 , AL031117 , AL357774 Genomic DNA. Translation: CAI43168.1 .
CH471120 Genomic DNA. Translation: EAX02654.1 .
CCDSi CCDS14554.1. [O75914-2 ]
CCDS48151.1. [O75914-3 ]
CCDS48152.1. [O75914-4 ]
CCDS48153.1. [O75914-1 ]
RefSeqi NP_001121638.1. NM_001128166.1. [O75914-2 ]
NP_001121639.1. NM_001128167.1. [O75914-2 ]
NP_001121640.1. NM_001128168.1. [O75914-3 ]
NP_001121644.1. NM_001128172.1. [O75914-4 ]
NP_001121645.1. NM_001128173.1. [O75914-1 ]
NP_002569.1. NM_002578.3. [O75914-2 ]
XP_006724719.1. XM_006724656.1. [O75914-1 ]
UniGenei Hs.593599.
Hs.656789.

3D structure databases

ProteinModelPortali O75914.
SMRi O75914. Positions 65-156, 181-553.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111099. 7 interactions.
IntActi O75914. 3 interactions.
MINTi MINT-3001915.

Chemistry

BindingDBi O75914.
ChEMBLi CHEMBL2999.
GuidetoPHARMACOLOGYi 2135.

PTM databases

PhosphoSitei O75914.

Proteomic databases

PaxDbi O75914.
PRIDEi O75914.

Protocols and materials databases

DNASUi 5063.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262836 ; ENSP00000262836 ; ENSG00000077264 . [O75914-1 ]
ENST00000360648 ; ENSP00000353864 ; ENSG00000077264 . [O75914-3 ]
ENST00000372007 ; ENSP00000361077 ; ENSG00000077264 . [O75914-2 ]
ENST00000372010 ; ENSP00000361080 ; ENSG00000077264 . [O75914-1 ]
ENST00000417227 ; ENSP00000389172 ; ENSG00000077264 . [O75914-4 ]
ENST00000425146 ; ENSP00000401982 ; ENSG00000077264 . [O75914-2 ]
ENST00000446737 ; ENSP00000410853 ; ENSG00000077264 . [O75914-2 ]
ENST00000518291 ; ENSP00000428921 ; ENSG00000077264 . [O75914-3 ]
ENST00000519681 ; ENSP00000429113 ; ENSG00000077264 . [O75914-4 ]
GeneIDi 5063.
KEGGi hsa:5063.
UCSCi uc004eoz.2. human. [O75914-2 ]
uc004epa.2. human. [O75914-1 ]
uc010npv.1. human. [O75914-3 ]
uc010npw.1. human. [O75914-4 ]

Organism-specific databases

CTDi 5063.
GeneCardsi GC0XP110226.
HGNCi HGNC:8592. PAK3.
HPAi HPA044791.
MIMi 300142. gene.
300558. phenotype.
neXtProti NX_O75914.
Orphaneti 777. X-linked non-syndromic intellectual disability.
PharmGKBi PA32919.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000234202.
HOVERGENi HBG108518.
KOi K05733.
OMAi SANENDM.
OrthoDBi EOG7CK36J.
PhylomeDBi O75914.
TreeFami TF105351.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_19226. Activation of Rac.
SignaLinki O75914.

Miscellaneous databases

GeneWikii PAK3.
GenomeRNAii 5063.
NextBioi 19502.
PROi O75914.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75914.
Bgeei O75914.
Genevestigatori O75914.

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

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  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN MRX30.
  2. "A novel gene expressed in the human adrenal gland."
    Jiang C., Gu J., Fu S., Ren S., Gu Y., Huang Q., Dong H., Yu Y., Fu G., Wang Y., Chen Z., Han Z.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Adrenal gland.
  3. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
    Kitano T., Schwarz C., Nickel B., Paeaebo S.
    Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The four mammalian splice variants encoded by the p21-activated kinase 3 gene have different biological properties."
    Kreis P., Rousseau V., Thevenot E., Combeau G., Barnier J.V.
    J. Neurochem. 106:1184-1197(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Brain.
  5. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  6. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity."
    Chong C., Tan L., Lim L., Manser E.
    J. Biol. Chem. 276:17347-17353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  9. "Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases."
    Feng Q., Albeck J.G., Cerione R.A., Yang W.
    J. Biol. Chem. 277:5644-5650(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF6 AND ARHGEF7.
  10. "DNA synthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3."
    McPhie D.L., Coopersmith R., Hines-Peralta A., Chen Y., Ivins K.J., Manly S.P., Kozlowski M.R., Neve K.A., Neve R.L.
    J. Neurosci. 23:6914-6927(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
    Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
    PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION.
  12. "Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein kinase 5 signaling pathway."
    Deleris P., Trost M., Topisirovic I., Tanguay P.L., Borden K.L., Thibault P., Meloche S.
    J. Biol. Chem. 286:6470-6478(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK4 AND MAPK6.
  13. "PAK signalling in neuronal physiology."
    Kreis P., Barnier J.V.
    Cell. Signal. 21:384-393(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  14. Cited for: VARIANT MRX30 CYS-67.
  15. "X-linked mild non-syndromic mental retardation with neuropsychiatric problems and the missense mutation A365E in PAK3."
    Gedeon A.K., Nelson J., Gecz J., Mulley J.C.
    Am. J. Med. Genet. A 120:509-517(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MRX30 GLU-380.
  16. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-440.

Entry informationi

Entry nameiPAK3_HUMAN
AccessioniPrimary (citable) accession number: O75914
Secondary accession number(s): A8K389
, B1GX77, B1GX78, B1GX79, Q5JWX1, Q5JWX2, Q7Z2D6, Q7Z2E4, Q7Z3Z8, Q8WWK5, Q8WX23, Q9P0J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 10, 2004
Last modified: September 3, 2014
This is version 151 of the entry and version 2 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

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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