Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 215 (05 Jun 2019)
Sequence version 2 (07 Mar 2006)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
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: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).20 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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_section">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_section">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_section">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

GO - Biological processi

<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

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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Chromosome, Cytoplasm, 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 mutations 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 Publication1
Natural variantiVAR_081555429Y → C in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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
Mutagenesisi423T → A: Decreases CDC42-stimulated activity and autophosphorylation. 1 Publication1
Mutagenesisi423T → E: Constitutive kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
5058
MIMi618158 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000149269

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA32917

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4600

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2133

Polymorphism and mutation 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_processing_section">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.<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_processing_section">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

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 human proteome resource

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

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
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 203 organ(s), highest expression level in middle temporal gyrus

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
CAB005312
HPA003565

<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_section">'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_section">'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. Component of cytoplasmic complexes, which also contains PXN, ARHGEF6 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: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).By similarity20 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111095, 93 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, 65 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

<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

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

More...
SMRi
Q13153

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_and_domains_section">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>Regioni70 – 140Autoregulatory regionAdd BLAST71
Regioni75 – 105GTPase-bindingAdd BLAST31
Regioni132 – 270Interaction with CRIPAK1 PublicationAdd BLAST139

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0578 Eukaryota
ENOG410XP4K LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182988

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234202

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q13153

KEGG Orthology (KO)

More...
KOi
K04409

Identification of Orthologs from Complete Genome Data

More...
OMAi
KELLQXS

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

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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
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: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>
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
Serine/threonine-protein kinase PAK...
PAK1
106Annotation 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>
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 Publication1
Natural variantiVAR_081555429Y → C in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization. 1 Publication1
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 [Q13153-2]
XP_011543383.1, XM_011545081.2 [Q13153-2]
XP_011543384.1, XM_011545082.2 [Q13153-2]
XP_011543385.1, XM_011545083.2 [Q13153-2]
XP_011543386.1, XM_011545084.2 [Q13153-2]
XP_016873335.1, XM_017017846.1 [Q13153-1]
XP_016873336.1, XM_017017847.1 [Q13153-1]
XP_016873337.1, XM_017017848.1 [Q13153-1]
XP_016873338.1, XM_017017849.1 [Q13153-1]
XP_016873339.1, XM_017017850.1 [Q13153-1]

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, Polymorphism

<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_references_section">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 [Q13153-2]
XP_011543383.1, XM_011545081.2 [Q13153-2]
XP_011543384.1, XM_011545082.2 [Q13153-2]
XP_011543385.1, XM_011545083.2 [Q13153-2]
XP_011543386.1, XM_011545084.2 [Q13153-2]
XP_016873335.1, XM_017017846.1 [Q13153-1]
XP_016873336.1, XM_017017847.1 [Q13153-1]
XP_016873337.1, XM_017017848.1 [Q13153-1]
XP_016873338.1, XM_017017849.1 [Q13153-1]
XP_016873339.1, XM_017017850.1 [Q13153-1]

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[»]
SMRiQ13153
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111095, 93 interactors
CORUMiQ13153
DIPiDIP-31016N
ELMiQ13153
IntActiQ13153, 65 interactors
MINTiQ13153
STRINGi9606.ENSP00000278568

Chemistry databases

BindingDBiQ13153
ChEMBLiCHEMBL4600
GuidetoPHARMACOLOGYi2133

Protein family/group databases

MoonDBiQ13153 Predicted

PTM databases

iPTMnetiQ13153
PhosphoSitePlusiQ13153

Polymorphism and mutation databases

BioMutaiPAK1
DMDMi90111767

Proteomic databases

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

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5058
Structural Biology KnowledgebaseSearch...

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
HPAiCAB005312
HPA003565
MIMi602590 gene
618158 phenotype
neXtProtiNX_Q13153
OpenTargetsiENSG00000149269
PharmGKBiPA32917

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0578 Eukaryota
ENOG410XP4K LUCA
GeneTreeiENSGT00950000182988
HOGENOMiHOG000234202
InParanoidiQ13153
KOiK04409
OMAiKELLQXS
OrthoDBi757766at2759
PhylomeDBiQ13153
TreeFamiTF105351

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
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

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

Protein Ontology

More...
PROi
PR:Q13153

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000149269 Expressed in 203 organ(s), highest expression level in middle temporal gyrus
ExpressionAtlasiQ13153 baseline and differential
GenevisibleiQ13153 HS

Family and domain databases

CDDicd01093 CRIB_PAK_like, 1 hit
Gene3Di3.90.810.10, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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_and_isoforms">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 5, 2019
This is version 215 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again