UniProtKB - Q13153 (PAK1_HUMAN)
Serine/threonine-protein kinase PAK 1
PAK1
Functioni
Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes (PubMed:11896197, PubMed:30290153).
Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (PubMed:25766321).
In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (PubMed:23260667).
In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization (By similarity).
In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity).
Along with GIT1, positively regulates microtubule nucleation during interphase (PubMed:27012601).
By similarity22 PublicationsCatalytic activityi
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 299 | ATP | 1 | |
Active sitei | 389 | Proton acceptor | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 276 – 284 | ATP | 9 | |
Nucleotide bindingi | 345 – 347 | ATP | 3 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- collagen binding Source: UniProtKB
- gamma-tubulin binding Source: UniProtKB
- identical protein binding Source: IntAct
- protein kinase activity Source: UniProtKB
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: UniProtKB
- protein serine kinase activity Source: RHEA
GO - Biological processi
- actin cytoskeleton reorganization Source: UniProtKB
- apoptotic process Source: UniProtKB-KW
- branching morphogenesis of an epithelial tube Source: UniProtKB
- cell migration Source: MGI
- cellular response to DNA damage stimulus Source: UniProtKB
- chromatin remodeling Source: UniProtKB
- ephrin receptor signaling pathway Source: Reactome
- exocytosis Source: UniProtKB-KW
- Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
- hepatocyte growth factor receptor signaling pathway Source: CAFA
- intracellular signal transduction Source: GO_Central
- negative regulation of cell proliferation involved in contact inhibition Source: UniProtKB
- neuron projection morphogenesis Source: UniProtKB
- phosphorylation Source: UniProtKB
- positive regulation of cell migration Source: UniProtKB
- positive regulation of cell population proliferation Source: BHF-UCL
- positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
- positive regulation of JUN kinase activity Source: UniProtKB
- positive regulation of microtubule nucleation Source: UniProtKB
- positive regulation of microtubule polymerization Source: CAFA
- positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of stress fiber assembly Source: UniProtKB
- protein autophosphorylation Source: UniProtKB
- protein phosphorylation Source: UniProtKB
- regulation of actin cytoskeleton organization Source: GO_Central
- regulation of axonogenesis Source: GO_Central
- regulation of MAPK cascade Source: GO_Central
- stimulatory C-type lectin receptor signaling pathway Source: Reactome
- wound healing Source: UniProtKB
Keywordsi
Molecular function | Allosteric enzyme, Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Apoptosis, Exocytosis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 2681 |
PathwayCommonsi | Q13153 |
Reactomei | R-HSA-202433, Generation of second messenger molecules R-HSA-2029482, Regulation of actin dynamics for phagocytic cup formation R-HSA-2871796, FCERI mediated MAPK activation R-HSA-376172, DSCAM interactions R-HSA-389359, CD28 dependent Vav1 pathway R-HSA-3928662, EPHB-mediated forward signaling R-HSA-3928664, Ephrin signaling R-HSA-399954, Sema3A PAK dependent Axon repulsion R-HSA-428540, Activation of RAC1 R-HSA-445144, Signal transduction by L1 R-HSA-445355, Smooth Muscle Contraction R-HSA-5218920, VEGFR2 mediated vascular permeability R-HSA-5621575, CD209 (DC-SIGN) signaling R-HSA-5625740, RHO GTPases activate PKNs R-HSA-5627117, RHO GTPases Activate ROCKs R-HSA-5627123, RHO GTPases activate PAKs R-HSA-5687128, MAPK6/MAPK4 signaling R-HSA-8964616, G beta:gamma signalling through CDC42 R-HSA-9013148, CDC42 GTPase cycle R-HSA-9013149, RAC1 GTPase cycle R-HSA-9013404, RAC2 GTPase cycle R-HSA-9013406, RHOQ GTPase cycle R-HSA-9013407, RHOH GTPase cycle R-HSA-9013409, RHOJ GTPase cycle R-HSA-9013420, RHOU GTPase cycle R-HSA-9013423, RAC3 GTPase cycle R-HSA-9013424, RHOV GTPase cycle |
SignaLinki | Q13153 |
SIGNORi | Q13153 |
Protein family/group databases
MoonDBi | Q13153, Predicted |
Names & Taxonomyi
Protein namesi | Recommended name: Serine/threonine-protein kinase PAK 11 Publication (EC:2.7.11.13 Publications)Alternative name(s): Alpha-PAK1 Publication p21-activated kinase 11 Publication Short name: PAK-1 p65-PAKBy similarity |
Gene namesi | Name:PAK1Imported |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:8590, PAK1 |
MIMi | 602590, gene |
neXtProti | NX_Q13153 |
VEuPathDBi | HostDB:ENSG00000149269 |
Subcellular locationi
Cytoskeleton
- centrosome 1 Publication
Cytoplasm and Cytosol
- Cytoplasm 3 Publications
Plasma membrane
- Cell membrane 1 Publication
- ruffle membrane 1 Publication
Nucleus
- nucleoplasm 1 Publication
Other locations
- focal adhesion 2 Publications
- lamellipodium 1 Publication
- invadopodium 1 Publication
- Chromosome 1 Publication
Note: Colocalizes with RUFY3, F-actin and other core migration components in invadopodia at the cell periphery (PubMed:25766321). Recruited to the cell membrane by interaction with CDC42 and RAC1. Recruited to focal adhesions upon activation. Colocalized with CIB1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Upon DNA damage, translocates to the nucleoplasm when phosphorylated at Thr-212 where is co-recruited with MORC2 on damaged chromatin (PubMed:23260667). Localization to the centrosome does not depend upon the presence of gamma-tubulin (PubMed:27012601). Localization of the active, but not inactive, protein to the adhesions and edge of lamellipodia is mediated by interaction with GIT1 (PubMed:11896197).By similarity4 Publications
Cytoskeleton
- actin filament Source: UniProtKB
- microtubule organizing center Source: UniProtKB-SubCell
Cytosol
- cytosol Source: HPA
Nucleus
- nuclear membrane Source: UniProtKB
- nucleoplasm Source: UniProtKB
Plasma Membrane
- plasma membrane Source: HGNC-UCL
- ruffle membrane Source: UniProtKB-SubCell
Other locations
- axon Source: UniProtKB
- cell-cell junction Source: UniProtKB
- chromosome Source: UniProtKB-SubCell
- cytoplasm Source: UniProtKB
- dendrite Source: UniProtKB
- focal adhesion Source: UniProtKB-SubCell
- intercalated disc Source: UniProtKB
- lamellipodium Source: UniProtKB-SubCell
- protein-containing complex Source: UniProtKB
- ruffle Source: UniProtKB
- Z disc Source: UniProtKB
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Chromosome, Cytoplasm, Cytoskeleton, Membrane, NucleusPathology & Biotechi
Involvement in diseasei
Intellectual developmental disorder with macrocephaly, seizures, and speech delay (IDDMSSD)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081554 | 131 | Y → C in IDDMSSD; gain of function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565638316EnsemblClinVar. | 1 | |
Natural variantiVAR_081555 | 429 | Y → C in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565583382EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 83 | H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-86. 2 Publications | 1 | |
Mutagenesisi | 86 | H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-83. 2 Publications | 1 | |
Mutagenesisi | 107 | L → F: Abolishes autoinhibition, leading to constitutive kinase activity. 1 Publication | 1 | |
Mutagenesisi | 299 | K → R: Strongly decreases activity. Abolishes kinase activity; when associated with N-389. 1 Publication | 1 | |
Mutagenesisi | 389 | D → N: Abolishes kinase activity; when associated with R-299. 1 Publication | 1 | |
Mutagenesisi | 393 | D → A: Abolishes autophosphorylation at Thr-423. 1 Publication | 1 | |
Mutagenesisi | 423 | T → A: Decreases CDC42-stimulated activity and autophosphorylation. 1 Publication | 1 | |
Mutagenesisi | 423 | T → E: Constitutive kinase activity. 1 Publication | 1 |
Keywords - Diseasei
Disease variant, Epilepsy, Mental retardationOrganism-specific databases
DisGeNETi | 5058 |
MalaCardsi | PAK1 |
MIMi | 618158, phenotype |
OpenTargetsi | ENSG00000149269 |
PharmGKBi | PA32917 |
Miscellaneous databases
Pharosi | Q13153, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4600 |
DrugBanki | DB12010, Fostamatinib |
DrugCentrali | Q13153 |
GuidetoPHARMACOLOGYi | 2133 |
Genetic variation databases
BioMutai | PAK1 |
DMDMi | 90111767 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000086460 | 2 – 545 | Serine/threonine-protein kinase PAK 1Add BLAST | 544 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 21 | Phosphoserine; by PKB and autocatalysis2 Publications | 1 | |
Modified residuei | 57 | Phosphoserine; by autocatalysis1 Publication | 1 | |
Modified residuei | 84 | Phosphothreonine; by OXSR1By similarity | 1 | |
Modified residuei | 115 | PhosphoserineCombined sources | 1 | |
Modified residuei | 131 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 142 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 144 | PhosphoserineCombined sources | 1 | |
Modified residuei | 149 | PhosphoserineCombined sources | 1 | |
Modified residuei | 153 | Phosphotyrosine; by JAK22 Publications | 1 | |
Modified residuei | 174 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 185 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 199 | Phosphoserine; by autocatalysisBy similarity | 1 | |
Modified residuei | 201 | Phosphotyrosine; by JAK21 Publication | 1 | |
Modified residuei | 204 | PhosphoserineCombined sources | 1 | |
Modified residuei | 212 | PhosphothreonineCombined sources2 Publications | 1 | |
Modified residuei | 219 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 220 | PhosphoserineCombined sources | 1 | |
Modified residuei | 223 | PhosphoserineCombined sources | 1 | |
Modified residuei | 225 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 229 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 230 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 285 | Phosphotyrosine; by JAK22 Publications | 1 | |
Modified residuei | 423 | Phosphothreonine; by autocatalysis, BRSK2 and PDPK14 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q13153 |
jPOSTi | Q13153 |
MassIVEi | Q13153 |
MaxQBi | Q13153 |
PaxDbi | Q13153 |
PeptideAtlasi | Q13153 |
PRIDEi | Q13153 |
ProteomicsDBi | 59193 [Q13153-1] 59194 [Q13153-2] |
PTM databases
GlyGeni | Q13153, 1 site |
iPTMneti | Q13153 |
MetOSitei | Q13153 |
PhosphoSitePlusi | Q13153 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000149269, Expressed in middle temporal gyrus and 219 other tissues |
ExpressionAtlasi | Q13153, baseline and differential |
Genevisiblei | Q13153, HS |
Organism-specific databases
HPAi | ENSG00000149269, Low tissue specificity |
Interactioni
Subunit structurei
Homodimer; homodimerization results in autoinhibition (PubMed:30290153). Active as monomer.
Interacts with GIT1 (PubMed:27012601).
Component of cytoplasmic complexes, which also contains PXN, ARHGEF7 and GIT1.
Interacts with NISCH (By similarity).
Interacts with DVL1; mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering (By similarity). Binds to the caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not the full-length proteins (PubMed:12624090).
Interacts with ARHGEF7 (PubMed:27012601, PubMed:16101281).
Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1.
Interacts with DSCAM (via cytoplasmic domain); the interaction is direct and enhanced in presence of RAC1 (PubMed:15169762).
Interacts with SCRIB (PubMed:18716323).
Interacts with PDPK1 (PubMed:10995762).
Interacts (via kinase domain) with RAF1 (PubMed:11733498).
Interacts with NCK1 and NCK2 (PubMed:10026169).
Interacts with TBCB (PubMed:15831477).
Interacts with CRIPAK (PubMed:16278681).
Interacts with BRSK2 (By similarity).
Interacts with SNAI1 (PubMed:15833848).
Interacts with CIB1 isoform 2 (PubMed:23503467).
Interacts with CIB1 (via N-terminal region); the interaction is direct, promotes PAK1 activity and occurs in a calcium-dependent manner.
Interacts with INPP5K (PubMed:26940976).
Interacts with gamma-tubulin (PubMed:27012601).
By similarity21 PublicationsBinary interactionsi
Q13153
PAK1 - isoform 1 [Q13153-1]
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-15628682,EBI-15628682 |
PCBP1 [Q15365] | 5 | EBI-15628682,EBI-946095 |
Isoform 2 [Q13153-2]
With | #Exp. | IntAct |
---|---|---|
RHOU [Q7L0Q8] | 2 | EBI-1019502,EBI-1638043 |
GO - Molecular functioni
- gamma-tubulin binding Source: UniProtKB
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 111095, 174 interactors |
CORUMi | Q13153 |
DIPi | DIP-31016N |
ELMi | Q13153 |
IntActi | Q13153, 172 interactors |
MINTi | Q13153 |
STRINGi | 9606.ENSP00000278568 |
Chemistry databases
BindingDBi | Q13153 |
Miscellaneous databases
RNActi | Q13153, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | Q13153 |
SMRi | Q13153 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q13153 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 75 – 88 | CRIBPROSITE-ProRule annotationAdd BLAST | 14 | |
Domaini | 270 – 521 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 252 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 77 | DisorderedSequence analysisAdd BLAST | 77 | |
Regioni | 70 – 140 | Autoregulatory regionAdd BLAST | 71 | |
Regioni | 75 – 105 | GTPase-bindingAdd BLAST | 31 | |
Regioni | 132 – 270 | Interaction with CRIPAK1 PublicationAdd BLAST | 139 | |
Regioni | 159 – 198 | DisorderedSequence analysisAdd BLAST | 40 | |
Regioni | 211 – 251 | DisorderedSequence analysisAdd BLAST | 41 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 42 – 77 | Basic and acidic residuesSequence analysisAdd BLAST | 36 | |
Compositional biasi | 216 – 236 | Polar residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 237 – 251 | Basic and acidic residuesSequence analysisAdd BLAST | 15 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0578, Eukaryota |
GeneTreei | ENSGT00950000182988 |
InParanoidi | Q13153 |
OMAi | WYDASAT |
OrthoDBi | 757766at2759 |
PhylomeDBi | Q13153 |
TreeFami | TF105351 |
Family and domain databases
CDDi | cd01093, CRIB_PAK_like, 1 hit |
Gene3Di | 3.90.810.10, 1 hit |
IDEALi | IID00277 |
InterProi | View protein in InterPro IPR000095, CRIB_dom IPR036936, CRIB_dom_sf IPR011009, Kinase-like_dom_sf IPR033923, PAK_BD IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00786, PBD, 1 hit PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00285, PBD, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS50108, CRIB, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MSNNGLDIQD KPPAPPMRNT STMIGAGSKD AGTLNHGSKP LPPNPEEKKK
60 70 80 90 100
KDRFYRSILP GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP
110 120 130 140 150
EQWARLLQTS NITKSEQKKN PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA
160 170 180 190 200
EDYNSSNALN VKAVSETPAV PPVSEDEDDD DDDATPPPVI APRPEHTKSV
210 220 230 240 250
YTRSVIEPLP VTPTRDVATS PISPTENNTT PPDALTRNTE KQKKKPKMSD
260 270 280 290 300
EEILEKLRSI VSVGDPKKKY TRFEKIGQGA SGTVYTAMDV ATGQEVAIKQ
310 320 330 340 350
MNLQQQPKKE LIINEILVMR ENKNPNIVNY LDSYLVGDEL WVVMEYLAGG
360 370 380 390 400
SLTDVVTETC MDEGQIAAVC RECLQALEFL HSNQVIHRDI KSDNILLGMD
410 420 430 440 450
GSVKLTDFGF CAQITPEQSK RSTMVGTPYW MAPEVVTRKA YGPKVDIWSL
460 470 480 490 500
GIMAIEMIEG EPPYLNENPL RALYLIATNG TPELQNPEKL SAIFRDFLNR
510 520 530 540
CLEMDVEKRG SAKELLQHQF LKIAKPLSSL TPLIAAAKEA TKNNH
Computationally mapped potential isoform sequencesi
There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB3KNX7 | B3KNX7_HUMAN | Non-specific serine/threonine prote... | PAK1 | 522 | Annotation score: | ||
E9PM17 | E9PM17_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 455 | Annotation score: | ||
E9PKH9 | E9PKH9_HUMAN | Non-specific serine/threonine prote... | PAK1 | 106 | Annotation score: | ||
E9PQW5 | E9PQW5_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 99 | Annotation score: | ||
E9PMP2 | E9PMP2_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 89 | Annotation score: | ||
H0YCM0 | H0YCM0_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 167 | Annotation score: | ||
E9PRP6 | E9PRP6_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 63 | Annotation score: | ||
H0YCG5 | H0YCG5_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 244 | Annotation score: | ||
E9PJF8 | E9PJF8_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 26 | Annotation score: | ||
H0YF55 | H0YF55_HUMAN | Serine/threonine-protein kinase PAK... | PAK1 | 18 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 26 | A → V in AAA65441 (PubMed:9395435).Curated | 1 | |
Sequence conflicti | 26 | A → V in AAC24716 (Ref. 3) Curated | 1 | |
Sequence conflicti | 237 | R → L in AAC50590 (PubMed:8805275).Curated | 1 | |
Sequence conflicti | 379 | F → S in AAC50590 (PubMed:8805275).Curated | 1 | |
Sequence conflicti | 503 | E → D in AAA65441 (PubMed:9395435).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081554 | 131 | Y → C in IDDMSSD; gain of function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565638316EnsemblClinVar. | 1 | |
Natural variantiVAR_081555 | 429 | Y → C in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565583382EnsemblClinVar. | 1 | |
Natural variantiVAR_051654 | 515 | L → V. Corresponds to variant dbSNP:rs35345144Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_017507 | 518 – 545 | HQFLK…TKNNH → VRKLRFQVFSNFSMIAASIP EDCQAPLQPHSTDCCS in isoform 2. 1 PublicationAdd BLAST | 28 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51120 mRNA Translation: AAC50590.1 U24152 mRNA Translation: AAA65441.1 AF071884 mRNA Translation: AAC24716.1 AP000486 Genomic DNA No translation available. AP003680 Genomic DNA No translation available. BC109299 mRNA Translation: AAI09300.1 |
CCDSi | CCDS44687.1 [Q13153-2] CCDS8250.1 [Q13153-1] |
PIRi | G01773 |
RefSeqi | NP_001122092.1, NM_001128620.1 [Q13153-2] NP_002567.3, NM_002576.4 [Q13153-1] XP_011543382.1, XM_011545080.2 XP_011543383.1, XM_011545081.2 XP_011543384.1, XM_011545082.2 [Q13153-2] XP_011543385.1, XM_011545083.2 XP_011543386.1, XM_011545084.2 [Q13153-2] XP_016873335.1, XM_017017846.1 [Q13153-1] XP_016873336.1, XM_017017847.1 XP_016873337.1, XM_017017848.1 XP_016873338.1, XM_017017849.1 XP_016873339.1, XM_017017850.1 |
Genome annotation databases
Ensembli | ENST00000278568; ENSP00000278568; ENSG00000149269 [Q13153-2] ENST00000356341; ENSP00000348696; ENSG00000149269 |
GeneIDi | 5058 |
KEGGi | hsa:5058 |
MANE-Selecti | ENST00000356341.8; ENSP00000348696.4; NM_002576.5; NP_002567.3 |
UCSCi | uc001oyg.5, human [Q13153-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51120 mRNA Translation: AAC50590.1 U24152 mRNA Translation: AAA65441.1 AF071884 mRNA Translation: AAC24716.1 AP000486 Genomic DNA No translation available. AP003680 Genomic DNA No translation available. BC109299 mRNA Translation: AAI09300.1 |
CCDSi | CCDS44687.1 [Q13153-2] CCDS8250.1 [Q13153-1] |
PIRi | G01773 |
RefSeqi | NP_001122092.1, NM_001128620.1 [Q13153-2] NP_002567.3, NM_002576.4 [Q13153-1] XP_011543382.1, XM_011545080.2 XP_011543383.1, XM_011545081.2 XP_011543384.1, XM_011545082.2 [Q13153-2] XP_011543385.1, XM_011545083.2 XP_011543386.1, XM_011545084.2 [Q13153-2] XP_016873335.1, XM_017017846.1 [Q13153-1] XP_016873336.1, XM_017017847.1 XP_016873337.1, XM_017017848.1 XP_016873338.1, XM_017017849.1 XP_016873339.1, XM_017017850.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1F3M | X-ray | 2.30 | A/B | 70-149 | [»] | |
C/D | 249-545 | [»] | ||||
1YHV | X-ray | 1.80 | A | 249-545 | [»] | |
1YHW | X-ray | 1.80 | A | 249-545 | [»] | |
1ZSG | NMR | - | B | 183-204 | [»] | |
2HY8 | X-ray | 2.00 | 1 | 249-545 | [»] | |
2QME | X-ray | 1.75 | I | 74-109 | [»] | |
3DVP | X-ray | 2.50 | C/D | 212-221 | [»] | |
3FXZ | X-ray | 1.64 | A | 249-545 | [»] | |
3FY0 | X-ray | 2.35 | A | 249-545 | [»] | |
3Q4Z | X-ray | 1.89 | A/B | 248-545 | [»] | |
3Q52 | X-ray | 1.80 | A | 248-545 | [»] | |
3Q53 | X-ray | 2.09 | A | 248-545 | [»] | |
4DAW | X-ray | 2.00 | A | 249-545 | [»] | |
4EQC | X-ray | 2.01 | A | 249-545 | [»] | |
4O0R | X-ray | 2.40 | A/B | 249-545 | [»] | |
4O0T | X-ray | 2.60 | A/B | 249-545 | [»] | |
4P90 | X-ray | 2.49 | A/B | 249-545 | [»] | |
4ZJI | X-ray | 1.99 | A/B/C/D | 249-545 | [»] | |
4ZJJ | X-ray | 2.20 | A/B/C/D | 249-545 | [»] | |
4ZLO | X-ray | 2.50 | A/B | 249-545 | [»] | |
4ZY4 | X-ray | 2.60 | A/B | 249-545 | [»] | |
4ZY5 | X-ray | 2.35 | A/B | 249-545 | [»] | |
4ZY6 | X-ray | 2.15 | A/B | 249-545 | [»] | |
5DEW | X-ray | 1.90 | A/B | 249-545 | [»] | |
5DEY | X-ray | 2.10 | A/B | 249-545 | [»] | |
5DFP | X-ray | 2.20 | A | 249-545 | [»] | |
5IME | X-ray | 2.22 | A/B | 249-545 | [»] | |
5KBQ | X-ray | 2.58 | A/B | 254-542 | [»] | |
5KBR | X-ray | 2.36 | A/B | 254-542 | [»] | |
6B16 | X-ray | 2.29 | A/B | 249-545 | [»] | |
BMRBi | Q13153 | |||||
SMRi | Q13153 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111095, 174 interactors |
CORUMi | Q13153 |
DIPi | DIP-31016N |
ELMi | Q13153 |
IntActi | Q13153, 172 interactors |
MINTi | Q13153 |
STRINGi | 9606.ENSP00000278568 |
Chemistry databases
BindingDBi | Q13153 |
ChEMBLi | CHEMBL4600 |
DrugBanki | DB12010, Fostamatinib |
DrugCentrali | Q13153 |
GuidetoPHARMACOLOGYi | 2133 |
Protein family/group databases
MoonDBi | Q13153, Predicted |
PTM databases
GlyGeni | Q13153, 1 site |
iPTMneti | Q13153 |
MetOSitei | Q13153 |
PhosphoSitePlusi | Q13153 |
Genetic variation databases
BioMutai | PAK1 |
DMDMi | 90111767 |
Proteomic databases
EPDi | Q13153 |
jPOSTi | Q13153 |
MassIVEi | Q13153 |
MaxQBi | Q13153 |
PaxDbi | Q13153 |
PeptideAtlasi | Q13153 |
PRIDEi | Q13153 |
ProteomicsDBi | 59193 [Q13153-1] 59194 [Q13153-2] |
Protocols and materials databases
Antibodypediai | 1132, 1432 antibodies from 50 providers |
DNASUi | 5058 |
Genome annotation databases
Ensembli | ENST00000278568; ENSP00000278568; ENSG00000149269 [Q13153-2] ENST00000356341; ENSP00000348696; ENSG00000149269 |
GeneIDi | 5058 |
KEGGi | hsa:5058 |
MANE-Selecti | ENST00000356341.8; ENSP00000348696.4; NM_002576.5; NP_002567.3 |
UCSCi | uc001oyg.5, human [Q13153-1] |
Organism-specific databases
CTDi | 5058 |
DisGeNETi | 5058 |
GeneCardsi | PAK1 |
HGNCi | HGNC:8590, PAK1 |
HPAi | ENSG00000149269, Low tissue specificity |
MalaCardsi | PAK1 |
MIMi | 602590, gene 618158, phenotype |
neXtProti | NX_Q13153 |
OpenTargetsi | ENSG00000149269 |
PharmGKBi | PA32917 |
VEuPathDBi | HostDB:ENSG00000149269 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0578, Eukaryota |
GeneTreei | ENSGT00950000182988 |
InParanoidi | Q13153 |
OMAi | WYDASAT |
OrthoDBi | 757766at2759 |
PhylomeDBi | Q13153 |
TreeFami | TF105351 |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 2681 |
PathwayCommonsi | Q13153 |
Reactomei | R-HSA-202433, Generation of second messenger molecules R-HSA-2029482, Regulation of actin dynamics for phagocytic cup formation R-HSA-2871796, FCERI mediated MAPK activation R-HSA-376172, DSCAM interactions R-HSA-389359, CD28 dependent Vav1 pathway R-HSA-3928662, EPHB-mediated forward signaling R-HSA-3928664, Ephrin signaling R-HSA-399954, Sema3A PAK dependent Axon repulsion R-HSA-428540, Activation of RAC1 R-HSA-445144, Signal transduction by L1 R-HSA-445355, Smooth Muscle Contraction R-HSA-5218920, VEGFR2 mediated vascular permeability R-HSA-5621575, CD209 (DC-SIGN) signaling R-HSA-5625740, RHO GTPases activate PKNs R-HSA-5627117, RHO GTPases Activate ROCKs R-HSA-5627123, RHO GTPases activate PAKs R-HSA-5687128, MAPK6/MAPK4 signaling R-HSA-8964616, G beta:gamma signalling through CDC42 R-HSA-9013148, CDC42 GTPase cycle R-HSA-9013149, RAC1 GTPase cycle R-HSA-9013404, RAC2 GTPase cycle R-HSA-9013406, RHOQ GTPase cycle R-HSA-9013407, RHOH GTPase cycle R-HSA-9013409, RHOJ GTPase cycle R-HSA-9013420, RHOU GTPase cycle R-HSA-9013423, RAC3 GTPase cycle R-HSA-9013424, RHOV GTPase cycle |
SignaLinki | Q13153 |
SIGNORi | Q13153 |
Miscellaneous databases
BioGRID-ORCSi | 5058, 16 hits in 1079 CRISPR screens |
ChiTaRSi | PAK1, human |
EvolutionaryTracei | Q13153 |
GeneWikii | PAK1 |
GenomeRNAii | 5058 |
Pharosi | Q13153, Tchem |
PROi | PR:Q13153 |
RNActi | Q13153, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000149269, Expressed in middle temporal gyrus and 219 other tissues |
ExpressionAtlasi | Q13153, baseline and differential |
Genevisiblei | Q13153, HS |
Family and domain databases
CDDi | cd01093, CRIB_PAK_like, 1 hit |
Gene3Di | 3.90.810.10, 1 hit |
IDEALi | IID00277 |
InterProi | View protein in InterPro IPR000095, CRIB_dom IPR036936, CRIB_dom_sf IPR011009, Kinase-like_dom_sf IPR033923, PAK_BD IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00786, PBD, 1 hit PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00285, PBD, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS50108, CRIB, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PAK1_HUMAN | |
Accessioni | Q13153Primary (citable) accession number: Q13153 Secondary accession number(s): O75561 Q86W79 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | March 7, 2006 | |
Last modified: | February 23, 2022 | |
This is version 231 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human and mouse protein kinases
Human and mouse protein kinases: classification and index - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families