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UniProtKB - Q13153 (PAK1_HUMAN)

Entry version 229 (02 Jun 2021)
Sequence version 2 (07 Mar 2006)
Previous versions | rss
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Protein

Serine/threonine-protein kinase PAK 1

Gene

PAK1

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phosphorylation of Thr-84 by OXSR1 inhibits activation (By similarity). Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, and enables activation by phosphorylation of Thr-423.By similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei299ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei389Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi276 – 284ATP9
Nucleotide bindingi345 – 347ATP3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Kinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Exocytosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.1, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q13153

Reactome - a knowledgebase of biological pathways and processes

More...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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q13153

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13153

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		Q13153, Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PAK1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:8590, PAK1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602590, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13153

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000149269.9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Chromosome, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Intellectual developmental disorder with macrocephaly, seizures, and speech delay (IDDMSSD)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurodevelopmental disorder characterized by impaired intellectual development, poor speech, postnatal macrocephaly, and seizures.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_081554131Y → C in IDDMSSD; gain of function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565638316EnsemblClinVar.1
Natural variantiVAR_081555429Y → C in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565583382EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi83H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-86. 2 Publications1
Mutagenesisi86H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-83. 2 Publications1
Mutagenesisi107L → F: Abolishes autoinhibition, leading to constitutive kinase activity. 1 Publication1
Mutagenesisi299K → R: Strongly decreases activity. Abolishes kinase activity; when associated with N-389. 1 Publication1
Mutagenesisi389D → N: Abolishes kinase activity; when associated with R-299. 1 Publication1
Mutagenesisi393D → A: Abolishes autophosphorylation at Thr-423. 1 Publication1
Mutagenesisi423T → A: Decreases CDC42-stimulated activity and autophosphorylation. 1 Publication1
Mutagenesisi423T → E: Constitutive kinase activity. 1 Publication1

Keywords - Diseasei

Disease variant, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET

More...DisGeNETi		5058

MalaCards human disease database

More...MalaCardsi		PAK1
MIMi618158, phenotype

Open Targets

More...OpenTargetsi		ENSG00000149269

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA32917

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q13153, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4600

Drug and drug target database

More...DrugBanki		DB12010, Fostamatinib

DrugCentral

More...DrugCentrali		Q13153

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2133

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PAK1

Domain mapping of disease mutations (DMDM)

More...DMDMi		90111767

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000864602 – 545Serine/threonine-protein kinase PAK 1Add BLAST544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei21Phosphoserine; by PKB and autocatalysis2 Publications1
Modified residuei57Phosphoserine; by autocatalysis1 Publication1
Modified residuei84Phosphothreonine; by OXSR1By similarity1
Modified residuei115PhosphoserineCombined sources1
Modified residuei131Phosphotyrosine1 Publication1
Modified residuei142Phosphotyrosine1 Publication1
Modified residuei144PhosphoserineCombined sources1
Modified residuei149PhosphoserineCombined sources1
Modified residuei153Phosphotyrosine; by JAK22 Publications1
Modified residuei174PhosphoserineCombined sources1 Publication1
Modified residuei185Phosphothreonine1 Publication1
Modified residuei199Phosphoserine; by autocatalysisBy similarity1
Modified residuei201Phosphotyrosine; by JAK21 Publication1
Modified residuei204PhosphoserineCombined sources1
Modified residuei212PhosphothreonineCombined sources2 Publications1
Modified residuei219PhosphothreonineCombined sources1
Modified residuei220PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1
Modified residuei225PhosphothreonineBy similarity1
Modified residuei229PhosphothreonineBy similarity1
Modified residuei230PhosphothreonineCombined sources1
Modified residuei285Phosphotyrosine; by JAK22 Publications1
Modified residuei423Phosphothreonine; by autocatalysis, BRSK2 and PDPK14 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1. Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites. Upon DNA damage, phosphorylated at Thr-212 and translocates to the nucleoplasm (PubMed:23260667). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).By similarity9 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q13153

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13153

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q13153

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13153

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q13153

PeptideAtlas

More...PeptideAtlasi		Q13153

PRoteomics IDEntifications database

More...PRIDEi		Q13153

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		59193 [Q13153-1]
59194 [Q13153-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q13153, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13153

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q13153

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q13153

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Overexpressed in gastric cancer cells and tissues (at protein level) (PubMed:25766321).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000149269, Expressed in middle temporal gyrus and 219 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13153, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13153, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000149269, Tissue enhanced (blood, brain)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details
Q13153
With#Exp.IntAct
ACP2 [P11117]3EBI-1307,EBI-2907070
ADD1 [P35611]3EBI-1307,EBI-2809187
ARHGEF6 [Q15052]4EBI-1307,EBI-1642523
ARHGEF7 [Q14155]12EBI-1307,EBI-717515
C11orf54 - isoform 3 [Q9H0W9-3]3EBI-1307,EBI-12108466
CDC42 [P60953]12EBI-1307,EBI-81752
CDK11B [P21127]4EBI-1307,EBI-1298
CRIPAK [Q8N1N5]6EBI-1307,EBI-1205846
DYNLL1 [P63167]4EBI-1307,EBI-349105
FAAP20 - isoform 4 [Q6NZ36-4]3EBI-1307,EBI-12013806
GIT1 [Q9Y2X7]5EBI-1307,EBI-466061
GIT2 [Q14161]3EBI-1307,EBI-1046878
GRB10 - isoform 4 [Q13322-4]3EBI-1307,EBI-12353035
KLHL20 [Q9Y2M5]3EBI-1307,EBI-714379
LASP1 - isoform 2 [Q14847-2]3EBI-1307,EBI-9088686
LIMK1 [P53667]5EBI-1307,EBI-444403
MAPK11 [Q15759]3EBI-1307,EBI-298304
NCK2 [O43639]10EBI-1307,EBI-713635
NOD1 [Q9Y239]3EBI-1307,EBI-1051262
OTX2 - isoform 2 [P32243-2]3EBI-1307,EBI-9087860
PCBP1 [Q15365]2EBI-1307,EBI-946095
PNKD - isoform 3 [Q8N490-3]3EBI-1307,EBI-25879276
RAC1 [P63000]25EBI-1307,EBI-413628
RAC1 - isoform A [P63000-1]3EBI-1307,EBI-7212896
RFFL - isoform 3 [Q8WZ73-3]3EBI-1307,EBI-25839575
RHOJ [Q9H4E5]3EBI-1307,EBI-6285694
RIT1 [Q92963]4EBI-1307,EBI-365845
SEMA4G - isoform 3 [Q9NTN9-3]3EBI-1307,EBI-9089805
SPSB1 [Q96BD6]3EBI-1307,EBI-2659201
STX11 [O75558]3EBI-1307,EBI-714135
SYNCRIP - isoform 4 [O60506-4]3EBI-1307,EBI-11123832
TCAP [O15273]3EBI-1307,EBI-954089
TCP10L [Q8TDR4]3EBI-1307,EBI-3923210
TEX12 [Q9BXU0]3EBI-1307,EBI-12090309
TIMM17B [O60830]3EBI-1307,EBI-2372529
TSACC [Q96A04]3EBI-1307,EBI-740411
TTC12 - isoform 2 [Q9H892-2]3EBI-1307,EBI-10274410
ZHX1-C8orf76 [Q96EF9]3EBI-1307,EBI-25830993
ZNF444 - isoform 2 [Q8N0Y2-2]3EBI-1307,EBI-12010736
Cdc42 [P60766] from Mus musculus.3EBI-1307,EBI-81763
Rac1 [P63001] from Mus musculus.3EBI-1307,EBI-413646
US3(L) [Q5PP90] from Suid alphaherpesvirus 1.2EBI-1307,EBI-15780451
PAK1 - isoform 1 [Q13153-1]
With#Exp.IntAct
itself2EBI-15628682,EBI-15628682
PCBP1 [Q15365]5EBI-15628682,EBI-946095
Isoform 2 [Q13153-2]
With#Exp.IntAct
RHOU [Q7L0Q8]2EBI-1019502,EBI-1638043

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111095, 168 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13153

Database of interacting proteins

More...DIPi		DIP-31016N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q13153

Protein interaction database and analysis system

More...IntActi		Q13153, 172 interactors

Molecular INTeraction database

More...MINTi		Q13153

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000278568

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q13153

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q13153, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1545
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q13153

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q13153

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q13153

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini75 – 88CRIBPROSITE-ProRule annotationAdd BLAST14
Domaini270 – 521Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 77DisorderedSequence analysisAdd BLAST77
Regioni70 – 140Autoregulatory regionAdd BLAST71
Regioni75 – 105GTPase-bindingAdd BLAST31
Regioni132 – 270Interaction with CRIPAK1 PublicationAdd BLAST139
Regioni159 – 198DisorderedSequence analysisAdd BLAST40
Regioni211 – 251DisorderedSequence analysisAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi42 – 77Basic and acidic residuesSequence analysisAdd BLAST36
Compositional biasi216 – 236Polar residuesSequence analysisAdd BLAST21
Compositional biasi237 – 251Basic and acidic residuesSequence analysisAdd BLAST15

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0578, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182988

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13153

Identification of Orthologs from Complete Genome Data

More...OMAi		TKMVGVV

Database of Orthologous Groups

More...OrthoDBi		757766at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13153

TreeFam database of animal gene trees

More...TreeFami		TF105351

Family and domain databases

Conserved Domains Database

More...CDDi		cd01093, CRIB_PAK_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.810.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00277

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00786, PBD, 1 hit
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00285, PBD, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13153-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
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
Length:545
Mass (Da):60,647
Last modified:March 7, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1A95CD5F2195CD7B
GO
Isoform 2 (identifier: Q13153-2) [UniParc]FASTAAdd to basket
Also known as: PAK1B

The sequence of this isoform differs from the canonical sequence as follows:
     518-545: HQFLKIAKPLSSLTPLIAAAKEATKNNH → VRKLRFQVFSNFSMIAASIPEDCQAPLQPHSTDCCS

Show »
Length:553
Mass (Da):61,632
Checksum:i6A3BB134DD2A82A8
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B3KNX7B3KNX7_HUMAN
Non-specific serine/threonine prote...
PAK1
522Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PM17E9PM17_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
455Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKH9E9PKH9_HUMAN
Non-specific serine/threonine prote...
PAK1
106Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PQW5E9PQW5_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
99Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PMP2E9PMP2_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
89Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YCM0H0YCM0_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
167Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PRP6E9PRP6_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
63Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YCG5H0YCG5_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
244Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PJF8E9PJF8_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
26Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YF55H0YF55_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
18Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26A → V in AAA65441 (PubMed:9395435).Curated1
Sequence conflicti26A → V in AAC24716 (Ref. 3) Curated1
Sequence conflicti237R → L in AAC50590 (PubMed:8805275).Curated1
Sequence conflicti379F → S in AAC50590 (PubMed:8805275).Curated1
Sequence conflicti503E → D in AAA65441 (PubMed:9395435).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081554131Y → C in IDDMSSD; gain of function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565638316EnsemblClinVar.1
Natural variantiVAR_081555429Y → C in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1565583382EnsemblClinVar.1
Natural variantiVAR_051654515L → V. Corresponds to variant dbSNP:rs35345144Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_017507518 – 545HQFLK…TKNNH → VRKLRFQVFSNFSMIAASIP EDCQAPLQPHSTDCCS in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44687.1 [Q13153-2]
CCDS8250.1 [Q13153-1]

Protein sequence database of the Protein Information Resource

More...PIRi		G01773

NCBI Reference Sequences

More...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

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000278568; ENSP00000278568; ENSG00000149269 [Q13153-2]
ENST00000356341; ENSP00000348696; ENSG00000149269 [Q13153-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5058

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5058

UCSC genome browser

More...UCSCi		uc001oyg.5, human [Q13153-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
CCDSiCCDS44687.1 [Q13153-2]
CCDS8250.1 [Q13153-1]
PIRiG01773
RefSeqiNP_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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F3MX-ray2.30A/B70-149[»]
C/D249-545[»]
1YHVX-ray1.80A249-545[»]
1YHWX-ray1.80A249-545[»]
1ZSGNMR-B183-204[»]
2HY8X-ray2.001249-545[»]
2QMEX-ray1.75I74-109[»]
3DVPX-ray2.50C/D212-221[»]
3FXZX-ray1.64A249-545[»]
3FY0X-ray2.35A249-545[»]
3Q4ZX-ray1.89A/B248-545[»]
3Q52X-ray1.80A248-545[»]
3Q53X-ray2.09A248-545[»]
4DAWX-ray2.00A249-545[»]
4EQCX-ray2.01A249-545[»]
4O0RX-ray2.40A/B249-545[»]
4O0TX-ray2.60A/B249-545[»]
4P90X-ray2.49A/B249-545[»]
4ZJIX-ray1.99A/B/C/D249-545[»]
4ZJJX-ray2.20A/B/C/D249-545[»]
4ZLOX-ray2.50A/B249-545[»]
4ZY4X-ray2.60A/B249-545[»]
4ZY5X-ray2.35A/B249-545[»]
4ZY6X-ray2.15A/B249-545[»]
5DEWX-ray1.90A/B249-545[»]
5DEYX-ray2.10A/B249-545[»]
5DFPX-ray2.20A249-545[»]
5IMEX-ray2.22A/B249-545[»]
5KBQX-ray2.58A/B254-542[»]
5KBRX-ray2.36A/B254-542[»]
6B16X-ray2.29A/B249-545[»]
BMRBiQ13153
SMRiQ13153
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111095, 168 interactors
CORUMiQ13153
DIPiDIP-31016N
ELMiQ13153
IntActiQ13153, 172 interactors
MINTiQ13153
STRINGi9606.ENSP00000278568

Chemistry databases

BindingDBiQ13153
ChEMBLiCHEMBL4600
DrugBankiDB12010, Fostamatinib
DrugCentraliQ13153
GuidetoPHARMACOLOGYi2133

Protein family/group databases

MoonDBiQ13153, Predicted

PTM databases

GlyGeniQ13153, 1 site
iPTMnetiQ13153
MetOSiteiQ13153
PhosphoSitePlusiQ13153

Genetic variation databases

BioMutaiPAK1
DMDMi90111767

Proteomic databases

EPDiQ13153
jPOSTiQ13153
MassIVEiQ13153
MaxQBiQ13153
PaxDbiQ13153
PeptideAtlasiQ13153
PRIDEiQ13153
ProteomicsDBi59193 [Q13153-1]
59194 [Q13153-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1132, 1400 antibodies

The DNASU plasmid repository

More...DNASUi		5058

Genome annotation databases

EnsembliENST00000278568; ENSP00000278568; ENSG00000149269 [Q13153-2]
ENST00000356341; ENSP00000348696; ENSG00000149269 [Q13153-1]
GeneIDi5058
KEGGihsa:5058
UCSCiuc001oyg.5, human [Q13153-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5058
DisGeNETi5058

GeneCards: human genes, protein and diseases

More...GeneCardsi		PAK1
HGNCiHGNC:8590, PAK1
HPAiENSG00000149269, Tissue enhanced (blood, brain)
MalaCardsiPAK1
MIMi602590, gene
618158, phenotype
neXtProtiNX_Q13153
OpenTargetsiENSG00000149269
PharmGKBiPA32917
VEuPathDBiHostDB:ENSG00000149269.9

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0578, Eukaryota
GeneTreeiENSGT00950000182988
InParanoidiQ13153
OMAiTKMVGVV
OrthoDBi757766at2759
PhylomeDBiQ13153
TreeFamiTF105351

Enzyme and pathway databases

BRENDAi2.7.11.1, 2681
PathwayCommonsiQ13153
ReactomeiR-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
SignaLinkiQ13153
SIGNORiQ13153

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5058, 15 hits in 1026 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PAK1, human
EvolutionaryTraceiQ13153

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PAK1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5058
PharosiQ13153, Tchem

Protein Ontology

More...PROi		PR:Q13153
RNActiQ13153, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000149269, Expressed in middle temporal gyrus and 219 other tissues
ExpressionAtlasiQ13153, baseline and differential
GenevisibleiQ13153, HS

Family and domain databases

CDDicd01093, CRIB_PAK_like, 1 hit
Gene3Di3.90.810.10, 1 hit
IDEALiIID00277
InterProiView 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
PfamiView protein in Pfam
PF00786, PBD, 1 hit
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM00285, PBD, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView 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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAK1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13153
Secondary accession number(s): O75561
, Q13567, Q32M53, Q32M54, Q86W79
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: June 2, 2021
This is version 229 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human entries with genetic variants
    List of human entries with genetic variants
  4. Human variants curated from literature reports
    Index of human variants curated from literature reports
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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