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UniProtKB - Q13177 (PAK2_HUMAN)

Entry version 219 (10 Feb 2021)
Sequence version 3 (03 Apr 2007)
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Protein

Serine/threonine-protein kinase PAK 2

Gene

PAK2

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

Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation.8 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 <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

Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-402 and allows the kinase domain to adopt an active structure (By similarity). Following caspase cleavage, autophosphorylated PAK-2p34 is constitutively active.By similarity

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 sitei278ATPPROSITE-ProRule annotation1
<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 sitei367Proton acceptorPROSITE-ProRule annotation1

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 bindingi255 – 263ATPPROSITE-ProRule annotation9

<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, Growth regulation, Host-virus interaction
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		Q13177

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-164944, Nef and signal transduction
R-HSA-202433, Generation of second messenger molecules
R-HSA-211728, Regulation of PAK-2p34 activity by PS-GAP/RHG10
R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-211736, Stimulation of the cell death response by PAK-2p34
R-HSA-2871796, FCERI mediated MAPK activation
R-HSA-389359, CD28 dependent Vav1 pathway
R-HSA-3928664, Ephrin signaling
R-HSA-399954, Sema3A PAK dependent Axon repulsion
R-HSA-428540, Activation of RAC1
R-HSA-4420097, VEGFA-VEGFR2 Pathway
R-HSA-445355, Smooth Muscle Contraction
R-HSA-5218920, VEGFR2 mediated vascular permeability
R-HSA-5621575, CD209 (DC-SIGN) signaling
R-HSA-5627123, RHO GTPases activate PAKs
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-8950505, Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

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

More...SignaLinki		Q13177

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13177

<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 2 (EC:2.7.11.1)
Alternative name(s):
Gamma-PAK
PAK65
S6/H4 kinase
p21-activated kinase 2
Short name:
PAK-2
p58
Cleaved into the following 2 chains:
PAK-2p27
Short name:
p27
PAK-2p34
Short name:
p34
Alternative name(s):
C-t-PAK2
<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:PAK2
<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 3

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:8591, PAK2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605022, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13177

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000180370.10

<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

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

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>Mutagenesisi212D → N: Inhibits caspase-mediated cleavage. 1 Publication1
Mutagenesisi213G → A: Abolishes myristoylation of PAK-2p34 and membrane location. 1
Mutagenesisi239 – 243IVSIG → REGRS: Abolishes nuclear export. 1 Publication5
Mutagenesisi246 – 248KKK → MHE: Greatly inhibits nuclear localization. 1 Publication3
Mutagenesisi278K → R: Abolishes kinase activity and autophosphorylation. 1 Publication1
Mutagenesisi402T → A: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5062

Open Targets

More...OpenTargetsi		ENSG00000180370

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA32918

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q13177, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4487

Drug and drug target database

More...DrugBanki		DB12010, Fostamatinib

DrugCentral

More...DrugCentrali		Q13177

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2134

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PAK2

Domain mapping of disease mutations (DMDM)

More...DMDMi		143811432

<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_00000864652 – 524Serine/threonine-protein kinase PAK 2Add BLAST523
ChainiPRO_00003049222 – 212PAK-2p27Add BLAST211
ChainiPRO_0000304923213 – 524PAK-2p34Add BLAST312

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 residuei2PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei55PhosphoserineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei60PhosphothreonineCombined sources1
Modified residuei62N6-acetyllysineBy similarity1
Modified residuei64PhosphoserineCombined sources1
Modified residuei128N6-acetyllysineCombined sources1
Modified residuei134PhosphothreonineCombined sources1
Modified residuei139PhosphotyrosineCombined sources1
Modified residuei141PhosphoserineCombined sources1
Modified residuei143PhosphothreonineCombined sources1
Modified residuei152PhosphoserineBy similarity1
Modified residuei154PhosphothreonineCombined sources1
Modified residuei169PhosphothreonineCombined sources1
Modified residuei197PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi213N-myristoyl glycine; in form PAK-2p341 Publication1
Modified residuei402Phosphothreonine; by autocatalysisCurated1

<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

Full-length PAK2 is autophosphorylated when activated by CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, become highly autophosphorylated, with PAK-2p27 being phosphorylated on serine and PAK-2p34 on threonine residues, respectively. Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate.
During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34.
Ubiquitinated, leading to its proteasomal degradation.1 Publication
PAK-2p34 is myristoylated.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei212 – 213Cleavage; by caspase-3 or caspase-3-like proteases2 Publications2

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1628
CPTAC-1726

Encyclopedia of Proteome Dynamics

More...EPDi		Q13177

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13177

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q13177

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13177

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

More...PaxDbi		Q13177

PeptideAtlas

More...PeptideAtlasi		Q13177

PRoteomics IDEntifications database

More...PRIDEi		Q13177

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		59208

2D gel databases

USC-OGP 2-DE database

More...OGPi		Q13177

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q13177, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13177

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q13177

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

More...PhosphoSitePlusi		Q13177

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q13177

<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

Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000180370, Expressed in corpus callosum and 254 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13177, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13177, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000180370, Low tissue specificity

<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

Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1.

Interacts with SH3MD4.

Interacts with SCRIB.

Interacts with ARHGEF7 and GIT1. PAK-2p34 interacts with ARHGAP10 (PubMed:15471851, PubMed:16374509, PubMed:18716323, PubMed:19273597).

Interacts with RAC1 (PubMed:20696164).

5 Publications

(Microbial infection) Interacts with and activated by HIV-1 Nef.

1 Publication

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111098, 102 interactors

Database of interacting proteins

More...DIPi		DIP-38249N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q13177

Protein interaction database and analysis system

More...IntActi		Q13177, 62 interactors

Molecular INTeraction database

More...MINTi		Q13177

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000314067

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q13177

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q13177, 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

1524
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		Q13177

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		Q13177

<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>Domaini74 – 87CRIBPROSITE-ProRule annotationAdd BLAST14
Domaini249 – 499Protein kinasePROSITE-ProRule annotationAdd BLAST251

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>Regioni69 – 137Autoregulatory regionBy similarityAdd BLAST69
Regioni69 – 112GTPase-bindingBy similarityAdd BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi245 – 251Nuclear localization signal7

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_26_6_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13177

Identification of Orthologs from Complete Genome Data

More...OMAi		IMMMEMA

Database of Orthologous Groups

More...OrthoDBi		757766at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13177

TreeFam database of animal gene trees

More...TreeFami		TF105351

Family and domain databases

Conserved Domains Database

More...CDDi		cd01093, CRIB_PAK_like, 1 hit
cd06655, STKc_PAK2, 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		IID00244

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
IPR035065, PAK2
IPR033923, PAK_BD
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
IPR035064, STK_PAK2

The PANTHER Classification System

More...PANTHERi		PTHR45832:SF1, PTHR45832:SF1, 1 hit

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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q13177-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR 
        60         70         80         90        100
HKIISIFSGT EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE 
       110        120        130        140        150
QWARLLQTSN ITKLEQKKNP QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF 
       160        170        180        190        200
PSGTPALNAK GTEAPAVVTE EEDDDEETAP PVIAPRPDHT KSIYTRSVID 
       210        220        230        240        250
PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE EIMEKLRTIV SIGDPKKKYT 
       260        270        280        290        300
RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE 
       310        320        330        340        350
LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR 
       360        370        380        390        400
ECLQALEFLH ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR 
       410        420        430        440        450
STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMVEGE PPYLNENPLR 
       460        470        480        490        500
ALYLIATNGT PELQNPEKLS PIFRDFLNRC LEMDVEKRGS AKELLQHPFL 
       510        520 
KLAKPLSSLT PLIMAAKEAM KSNR
Length:524
Mass (Da):58,043
Last modified:April 3, 2007 - v3
<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:i00A7CD15F93D4180
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C1X3H7C1X3_HUMAN
Serine/threonine-protein kinase PAK...
PAK2
221Annotation 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 conflicti90A → T in AAA75468 (PubMed:7744004).Curated1
Sequence conflicti150F → L in AAA65442 (Ref. 1) Curated1
Sequence conflicti225T → P in AAA65442 (Ref. 1) Curated1
Sequence conflicti258G → R in AAH69613 (PubMed:15489334).Curated1
Sequence conflicti329G → R in AAA75468 (PubMed:7744004).Curated1
Sequence conflicti338T → TA in AAA65442 (Ref. 1) Curated1

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
U24153 mRNA Translation: AAA65442.1
BC069613 mRNA Translation: AAH69613.1
U25975 mRNA Translation: AAA75468.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3321.1

Protein sequence database of the Protein Information Resource

More...PIRi		S58682

NCBI Reference Sequences

More...RefSeqi		NP_002568.2, NM_002577.4
XP_011511172.1, XM_011512870.2
XP_016861990.1, XM_017006501.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000327134; ENSP00000314067; ENSG00000180370

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5062

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5062

UCSC genome browser

More...UCSCi		uc003fwy.4, human

<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
U24153 mRNA Translation: AAA65442.1
BC069613 mRNA Translation: AAH69613.1
U25975 mRNA Translation: AAA75468.1
CCDSiCCDS3321.1
PIRiS58682
RefSeqiNP_002568.2, NM_002577.4
XP_011511172.1, XM_011512870.2
XP_016861990.1, XM_017006501.1

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
3PCSX-ray2.86E/F/G/H121-136[»]
SMRiQ13177
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111098, 102 interactors
DIPiDIP-38249N
ELMiQ13177
IntActiQ13177, 62 interactors
MINTiQ13177
STRINGi9606.ENSP00000314067

Chemistry databases

BindingDBiQ13177
ChEMBLiCHEMBL4487
DrugBankiDB12010, Fostamatinib
DrugCentraliQ13177
GuidetoPHARMACOLOGYi2134

PTM databases

GlyGeniQ13177, 1 site
iPTMnetiQ13177
MetOSiteiQ13177
PhosphoSitePlusiQ13177
SwissPalmiQ13177

Genetic variation databases

BioMutaiPAK2
DMDMi143811432

2D gel databases

OGPiQ13177

Proteomic databases

CPTACiCPTAC-1628
CPTAC-1726
EPDiQ13177
jPOSTiQ13177
MassIVEiQ13177
MaxQBiQ13177
PaxDbiQ13177
PeptideAtlasiQ13177
PRIDEiQ13177
ProteomicsDBi59208

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3583, 810 antibodies

The DNASU plasmid repository

More...DNASUi		5062

Genome annotation databases

EnsembliENST00000327134; ENSP00000314067; ENSG00000180370
GeneIDi5062
KEGGihsa:5062
UCSCiuc003fwy.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5062
DisGeNETi5062

GeneCards: human genes, protein and diseases

More...GeneCardsi		PAK2
HGNCiHGNC:8591, PAK2
HPAiENSG00000180370, Low tissue specificity
MIMi605022, gene
neXtProtiNX_Q13177
OpenTargetsiENSG00000180370
PharmGKBiPA32918
VEuPathDBiHostDB:ENSG00000180370.10

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0578, Eukaryota
GeneTreeiENSGT00950000182988
HOGENOMiCLU_000288_26_6_1
InParanoidiQ13177
OMAiIMMMEMA
OrthoDBi757766at2759
PhylomeDBiQ13177
TreeFamiTF105351

Enzyme and pathway databases

BRENDAi2.7.11.1, 2681
PathwayCommonsiQ13177
ReactomeiR-HSA-164944, Nef and signal transduction
R-HSA-202433, Generation of second messenger molecules
R-HSA-211728, Regulation of PAK-2p34 activity by PS-GAP/RHG10
R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-211736, Stimulation of the cell death response by PAK-2p34
R-HSA-2871796, FCERI mediated MAPK activation
R-HSA-389359, CD28 dependent Vav1 pathway
R-HSA-3928664, Ephrin signaling
R-HSA-399954, Sema3A PAK dependent Axon repulsion
R-HSA-428540, Activation of RAC1
R-HSA-4420097, VEGFA-VEGFR2 Pathway
R-HSA-445355, Smooth Muscle Contraction
R-HSA-5218920, VEGFR2 mediated vascular permeability
R-HSA-5621575, CD209 (DC-SIGN) signaling
R-HSA-5627123, RHO GTPases activate PAKs
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-8950505, Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
SignaLinkiQ13177
SIGNORiQ13177

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5062, 87 hits in 906 CRISPR screens

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

More...ChiTaRSi		PAK2, human
EvolutionaryTraceiQ13177

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PAK2

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

More...GenomeRNAii		5062
PharosiQ13177, Tchem

Protein Ontology

More...PROi		PR:Q13177
RNActiQ13177, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000180370, Expressed in corpus callosum and 254 other tissues
ExpressionAtlasiQ13177, baseline and differential
GenevisibleiQ13177, HS

Family and domain databases

CDDicd01093, CRIB_PAK_like, 1 hit
cd06655, STKc_PAK2, 1 hit
Gene3Di3.90.810.10, 1 hit
IDEALiIID00244
InterProiView protein in InterPro
IPR000095, CRIB_dom
IPR036936, CRIB_dom_sf
IPR011009, Kinase-like_dom_sf
IPR035065, PAK2
IPR033923, PAK_BD
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
IPR035064, STK_PAK2
PANTHERiPTHR45832:SF1, PTHR45832:SF1, 1 hit
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...

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 nameiPAK2_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: Q13177
Secondary accession number(s): Q13154, Q6ISC3
<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: April 3, 2007
Last modified: February 10, 2021
This is version 219 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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