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Entry version 199 (18 Sep 2019)
Sequence version 3 (15 Dec 1998)
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Protein

Serine/threonine-protein kinase PAK 1

Gene

Pak1

Organism
Rattus norvegicus (Rat)
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. 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. In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (By similarity).By similarity7 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-422.By similarity3 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 sitei298ATPPROSITE-ProRule annotation1
<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 sitei388Proton acceptorPROSITE-ProRule annotation1

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 bindingi275 – 283ATPPROSITE-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

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 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-202433 Generation of second messenger molecules
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-2871796 FCERI mediated MAPK activation
R-RNO-376172 DSCAM interactions
R-RNO-389359 CD28 dependent Vav1 pathway
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-3928664 Ephrin signaling
R-RNO-399954 Sema3A PAK dependent Axon repulsion
R-RNO-445144 Signal transduction by L1
R-RNO-445355 Smooth Muscle Contraction
R-RNO-5218920 VEGFR2 mediated vascular permeability
R-RNO-5621575 CD209 (DC-SIGN) signaling
R-RNO-5627123 RHO GTPases activate PAKs
R-RNO-5687128 MAPK6/MAPK4 signaling
R-RNO-8964616 G beta:gamma signalling through CDC42

<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 1Curated (EC:2.7.11.11 Publication)
Alternative name(s):
Alpha-PAKBy similarity
Protein kinase MUK21 Publication
p21-activated kinase 1By similarity
Short name:
PAK-1
p68-PAK1 Publication
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 1

Organism-specific databases

Rat genome database

More...
RGDi
3250 Pak1

<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

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. Reduces NMDA receptor-mediated synaptic currents; when associated with L-86 and R-299. 2 Publications1
Mutagenesisi84T → A: Constitutively active. 1 Publication1
Mutagenesisi84T → E: Inhibits activation by binding to CDC42. 1 Publication1
Mutagenesisi86H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-83. Reduces NMDA receptor-mediated synaptic currents; when associated with L-83 and R-299. 2 Publications1
Mutagenesisi107L → F: Abolishes autoinhibition, leading to constitutive kinase activation. 1 Publication1
Mutagenesisi144S → A: Decreases activity; when associated with A-149. 1 Publication1
Mutagenesisi149S → A: Decreases activity; when associated with A-144. 1 Publication1
Mutagenesisi298K → R: Reduces NMDA receptor-mediated synaptic currents; when associated with L-83 and L-86. 1 Publication1
Mutagenesisi404L → S: Decreases kinase activity. 1 Publication1
Mutagenesisi422T → A: Decreases activity. 3 Publications1
Mutagenesisi422T → E: Increases constitutive activity. 3 Publications1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3580528

<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 methionineiRemovedBy similarity
<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_00000864622 – 544Serine/threonine-protein kinase PAK 1Add BLAST543

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-acetylserineBy similarity1
Modified residuei21Phosphoserine; by PKB and autocatalysis1 Publication1
Modified residuei57Phosphoserine; by autocatalysis1 Publication1
Modified residuei84Phosphothreonine; by OXSR11 Publication1
Modified residuei115PhosphoserineBy similarity1
Modified residuei131PhosphotyrosineBy similarity1
Modified residuei142PhosphotyrosineBy similarity1
Modified residuei144Phosphoserine; by autocatalysis1 Publication1
Modified residuei149Phosphoserine; by autocatalysis1 Publication1
Modified residuei153Phosphotyrosine; by JAK2By similarity1
Modified residuei174PhosphoserineCombined sources1
Modified residuei184PhosphothreonineBy similarity1
Modified residuei198Phosphoserine; by autocatalysis1 Publication1
Modified residuei200Phosphotyrosine; by JAK2By similarity1
Modified residuei203Phosphoserine; by autocatalysis1 Publication1
Modified residuei211PhosphothreonineBy similarity1
Modified residuei218PhosphothreonineBy similarity1
Modified residuei219PhosphoserineBy similarity1
Modified residuei222PhosphoserineCombined sources1
Modified residuei224PhosphothreonineBy similarity1
Modified residuei228PhosphothreonineBy similarity1
Modified residuei229PhosphothreonineBy similarity1
Modified residuei284Phosphotyrosine; by JAK2By similarity1
Modified residuei422Phosphothreonine; by autocatalysis, BRSK2 and PDPK13 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-422 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-422 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 (By similarity). Activated by phosphorylation at Thr-422 by BRSK2. Upon DNA damage, phosphorylated at Thr-211 and translocates to the nucleoplasm (By similarity). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P35465

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

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PaxDbi
P35465

PRoteomics IDEntifications database

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PRIDEi
P35465

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35465

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

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PhosphoSitePlusi
P35465

SwissPalm database of S-palmitoylation events

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SwissPalmi
P35465

<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

Expressed predominantly in the brain, with higher expression in neuronal groups associated with motor function, and at lower levels in the spleen.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Found in the embryonic CNS with little expression elsewhere.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000029784 Expressed in 10 organ(s), highest expression level in brain

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35465 RN

<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 in its autoinhibited state. 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 (By similarity).

Interacts with ARHGEF7 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity).

Interacts with DSCAM (via cytoplasmic domain); the interaction is direct and enhanced in presence of RAC1.

Interacts with SCRIB (By similarity).

Interacts with PDPK1 (By similarity).

Interacts (via kinase domain) with RAF1 (By similarity).

Interacts with NCK1 and NCK2 (By similarity).

Interacts with TBCB (By similarity).

Interacts with CRIPAK (By similarity).

Interacts with BRSK2 (By similarity).

Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1 (PubMed:9032240).

Interacts with SNAI1 (By similarity).

Interacts with CIB1 (via N-terminal region); the interaction is direct, promotes PAK1 activity and occurs in a calcium-dependent manner.

Interacts with INPP5K (By similarity).

By similarity1 Publication

<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

WithEntry#Exp.IntActNotes
VimP201522EBI-444379,EBI-299269From Mus musculus.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
248078, 1 interactor

Database of interacting proteins

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DIPi
DIP-32990N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P35465

Protein interaction database and analysis system

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IntActi
P35465, 6 interactors

Molecular INTeraction database

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MINTi
P35465

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000045832

<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

1544
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

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SMRi
P35465

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P35465

<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
Domaini269 – 520Protein 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
Regioni70 – 105GTPase-bindingAdd BLAST36
Regioni132 – 269Interaction with CRIPAKBy similarityAdd BLAST138

<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

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eggNOGi
KOG0578 Eukaryota
ENOG410XP4K LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182988

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234202

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35465

KEGG Orthology (KO)

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KOi
K04409

Identification of Orthologs from Complete Genome Data

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OMAi
KELLQXS

Database of Orthologous Groups

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OrthoDBi
757766at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35465

TreeFam database of animal gene trees

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TreeFami
TF105351

Family and domain databases

Conserved Domains Database

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CDDi
cd01093 CRIB_PAK_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.90.810.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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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>Sequencei

<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.

P35465-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNNGLDVQD KPPAPPMRNT STMIGAGSKD PGTLNHGSKP LPPNPEEKKK
60 70 80 90 100
KDRFYRSILA GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP
110 120 130 140 150
EQWARLLQTS NITKSEQKKN PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA
160 170 180 190 200
EDYNSSNTLN VKTVSETPAV PPVSEDEDDD DDATPPPVIA PRPEHTKSVY
210 220 230 240 250
TRSVIEPLPV TPTRDVATSP ISPTENNTTP PDALTRNTEK QKKKPKMSDE
260 270 280 290 300
EILEKLRSIV SVGDPKKKYT RFEKIGQGAS GTVYTAMDVA TGQEVAIKQM
310 320 330 340 350
NLQQQPKKEL IINEILVMRE NKNPNIVNYL DSYLVGDELW VVMEYLAGGS
360 370 380 390 400
LTDVVTETCM DEGQIAAVCR ECLQALEFLH SNQVIHRDIK SDNILLGMDG
410 420 430 440 450
SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY GPKVDIWSLG
460 470 480 490 500
IMAIEMIEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS AIFRDFLNRC
510 520 530 540
LEMDVEKRGS AKELLQHQFL KIAKPLSSLT PLIAAAKEAT KNNH
Length:544
Mass (Da):60,578
Last modified:December 15, 1998 - 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:i93BE32D8222F5B7B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U23443 mRNA Translation: AAB95646.1
U49953 mRNA Translation: AAB61533.1

Protein sequence database of the Protein Information Resource

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PIRi
S40482

NCBI Reference Sequences

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RefSeqi
NP_058894.1, NM_017198.1
XP_006229814.1, XM_006229752.2
XP_006229815.1, XM_006229753.2
XP_006229816.1, XM_006229754.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000049321; ENSRNOP00000045832; ENSRNOG00000029784
ENSRNOT00000091952; ENSRNOP00000073036; ENSRNOG00000029784

Database of genes from NCBI RefSeq genomes

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GeneIDi
29431

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:29431

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23443 mRNA Translation: AAB95646.1
U49953 mRNA Translation: AAB61533.1
PIRiS40482
RefSeqiNP_058894.1, NM_017198.1
XP_006229814.1, XM_006229752.2
XP_006229815.1, XM_006229753.2
XP_006229816.1, XM_006229754.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E0ANMR-B75-118[»]
SMRiP35465
ModBaseiSearch...

Protein-protein interaction databases

BioGridi248078, 1 interactor
DIPiDIP-32990N
ELMiP35465
IntActiP35465, 6 interactors
MINTiP35465
STRINGi10116.ENSRNOP00000045832

Chemistry databases

ChEMBLiCHEMBL3580528

PTM databases

iPTMnetiP35465
PhosphoSitePlusiP35465
SwissPalmiP35465

Proteomic databases

jPOSTiP35465
PaxDbiP35465
PRIDEiP35465

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000049321; ENSRNOP00000045832; ENSRNOG00000029784
ENSRNOT00000091952; ENSRNOP00000073036; ENSRNOG00000029784
GeneIDi29431
KEGGirno:29431

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5058
RGDi3250 Pak1

Phylogenomic databases

eggNOGiKOG0578 Eukaryota
ENOG410XP4K LUCA
GeneTreeiENSGT00950000182988
HOGENOMiHOG000234202
InParanoidiP35465
KOiK04409
OMAiKELLQXS
OrthoDBi757766at2759
PhylomeDBiP35465
TreeFamiTF105351

Enzyme and pathway databases

BRENDAi2.7.11.1 5301
ReactomeiR-RNO-202433 Generation of second messenger molecules
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-2871796 FCERI mediated MAPK activation
R-RNO-376172 DSCAM interactions
R-RNO-389359 CD28 dependent Vav1 pathway
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-3928664 Ephrin signaling
R-RNO-399954 Sema3A PAK dependent Axon repulsion
R-RNO-445144 Signal transduction by L1
R-RNO-445355 Smooth Muscle Contraction
R-RNO-5218920 VEGFR2 mediated vascular permeability
R-RNO-5621575 CD209 (DC-SIGN) signaling
R-RNO-5627123 RHO GTPases activate PAKs
R-RNO-5687128 MAPK6/MAPK4 signaling
R-RNO-8964616 G beta:gamma signalling through CDC42

Miscellaneous databases

EvolutionaryTraceiP35465

Protein Ontology

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PROi
PR:P35465

Gene expression databases

BgeeiENSRNOG00000029784 Expressed in 10 organ(s), highest expression level in brain
GenevisibleiP35465 RN

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAK1_RAT
<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: P35465
Secondary accession number(s): Q62934
<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: June 1, 1994
Last sequence update: December 15, 1998
Last modified: September 18, 2019
This is version 199 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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