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Entry version 163 (18 Sep 2019)
Sequence version 2 (01 Oct 2001)
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Protein

Serine/threonine-protein kinase pak-1

Gene

pak-1

Organism
Caenorhabditis elegans
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

Required for hypodermal cell fusion, together with cdc-42 and ced-10, leading to embryonic body elongation, which involves dramatic cytoskeletal reorganization (PubMed:8824291). Plays a redundant role with max-2 in dorsal axonal guidance in ventral cord commissural motoneurons and in P neuroblast migration. Acts probably downstream of Rho GTPases mig-2 and ced-10 to regulate these 2 processes (PubMed:17050621). Involved in orientating axonal growth of HSN neurons (PubMed:18499456). During gonad morphogenesis and probably in association with pix-1 and git-1, involved in the migration of distal tip cell (DTC) and in maintaining their sharp tapering morphology. In addition, plays a redundant role with max-2 in DTC-mediated guidance of gonad elongation (PubMed:19023419, PubMed:19797046). May phosphorylate mlc-4 (PubMed:19675126).1 Publication5 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+1 Publication, Mn2+1 PublicationNote: Divalent cations such as magnesium or manganese.1 Publication

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 sitei324ATPPROSITE-ProRule annotationBy similarity1
<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 sitei414Proton acceptorPROSITE-ProRule annotationBy similarity1

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 bindingi301 – 309ATPPROSITE-ProRule annotationBy similarity9

<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 functionDevelopmental protein, Kinase, Serine/threonine-protein kinase, Transferase
Biological processNeurogenesis
LigandATP-binding, Magnesium, Manganese, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-389359 CD28 dependent Vav1 pathway
R-CEL-3928664 Ephrin signaling
R-CEL-399954 Sema3A PAK dependent Axon repulsion
R-CEL-5218920 VEGFR2 mediated vascular permeability
R-CEL-5621575 CD209 (DC-SIGN) signaling
R-CEL-5627123 RHO GTPases activate PAKs
R-CEL-5687128 MAPK6/MAPK4 signaling

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

More...
SignaLinki
Q17850

<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-1 (EC:2.7.11.11 Publication)
Alternative name(s):
CePAK
p21-activated kinase 1
Short name:
PAK1
<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:pak-1
ORF Names:C09B8.7
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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 X

Organism-specific databases

WormBase

More...
WormBasei
C09B8.7a ; CE27670 ; WBGene00003911 ; pak-1
C09B8.7b ; CE06792 ; WBGene00003911 ; pak-1
C09B8.7c ; CE33559 ; WBGene00003911 ; pak-1
C09B8.7e ; CE33561 ; WBGene00003911 ; pak-1

<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 membrane, Cell projection, Cytoplasm, Membrane

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

In pak-1 and pak-2 double mutants, defects in embryogenesis and L1 stage lethality. The few animals reaching adulthood have normal ventral cord commissural motoneuron axonal guidance and are relatively coordinated. In max-2 and pak-1 double mutants, DD and DC motoneuron axons fail to reach the dorsal cord (PubMed:17050621). Animals are also uncoordinated, defective in egg laying and in distal tip cell (DTC) migration, guidance and morphology, and exhibit ventral enclosure defects (PubMed:17050621, PubMed:19023419).2 Publications

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>Mutagenesisi68S → P: May prevent interaction with Rho GTPases. Defect in commissural axon guidance in ventral motoneurons in an RNAi-mediated max-2 knockdown background. Rescues anterior gonad morphology defects in pax-1 ok488 mutants. 1 Publication1
Mutagenesisi234 – 235RP → AA: May prevent interaction with pix-1. Fails to rescue distal tip cell migration defect in an RNAi-mediated max-2 knockdown background. 1 Publication2
Mutagenesisi324K → R: Probable loss of activity. Fails to rescue distal tip cell migration defect in an RNAi-mediated max-2 knockdown background. 1 Publication1

<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 ‘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_00000864631 – 572Serine/threonine-protein kinase pak-1Add BLAST572

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q17850

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

More...
PaxDbi
Q17850

PeptideAtlas

More...
PeptideAtlasi
Q17850

<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

Specifically colocalized with cdc-42 and ced-10 at all hypodermal cell boundaries during embryo elongation throughout the second phase of embryogenesis. Expressed mainly in pharyngeal muscles, the CAN neurons, motor neurons in the ventral nerve cord, several cells in the tail region (including the B and Y cells from L1 to adult, the hypodermal blast cell T in the L1 and some of its progeny in later stages), and the distal tip cells.4 Publications

<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

Highly expressed at the embryonic stage, with decreasing expression from L1 onwards.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00003911 Expressed in 8 organ(s), highest expression level in multi-cellular organism

<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

Interacts with cdc-42 (GTP-bound form) and cedd-10 (GTP-bound form).

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
45805, 2 interactors

Database of interacting proteins

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DIPi
DIP-26715N

Protein interaction database and analysis system

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IntActi
Q17850, 1 interactor

STRING: functional protein association networks

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STRINGi
6239.C09B8.7a

<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

3D structure databases

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

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SMRi
Q17850

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini67 – 80CRIBPROSITE-ProRule annotationAdd BLAST14
Domaini295 – 546Protein 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>Regioni81 – 294LinkerAdd BLAST214

<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
ENSGT00940000165560

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234202

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q17850

KEGG Orthology (KO)

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KOi
K04409

Identification of Orthologs from Complete Genome Data

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OMAi
PTIHCPT

Database of Orthologous Groups

More...
OrthoDBi
757766at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q17850

Family and domain databases

Conserved Domains Database

More...
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

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 (4)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.

This entry describes 4 <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
Isoform a1 Publication (identifier: Q17850-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MKAFSSYDEK PPAPPIRFSS SATRENQVVG LKPLPKEPEA TKKKKTMPNP
60 70 80 90 100
FMKKNKDKKE ASEKPVISRP SNFEHTIHVG YDPKTGEFTG MPEAWARLLT
110 120 130 140 150
DSQISKQEQQ QNPQAVLDAL KYYTQGESSG QKWLQYDMMF IDDAPSRTPS
160 170 180 190 200
YGLKPQPYST SSLPYHGNKI QDPRKMNPMT TSTSSAGYNS KQGVPPTTFS
210 220 230 240 250
VNENRSSMPP SYAPPPVPHG ETPADIVPPA IPDRPARTLS IYTKPKEEEE
260 270 280 290 300
KIPDLSKGQF GVQARGQKAK KKMTDAEVLT KLRTIVSIGN PDRKYRKVDK
310 320 330 340 350
IGSGASGSVY TAIEISTEAE VAIKQMNLKD QPKKELIINE ILVMRENKHA
360 370 380 390 400
NIVNYLDSYL VCDELWVVME YLAGGSLTDV VTECQMEDGI IAAVCREVLQ
410 420 430 440 450
ALEFLHSRHV IHRDIKSDNI LLGMDGSVKL TDFGFCAQLS PEQRKRTTMV
460 470 480 490 500
GTPYWMAPEV VTRKQYGPKV DVWSLGIMAI EMVEGEPPYL NENPLRAIYL
510 520 530 540 550
IATNGKPDFP GRDSMTLLFK DFVDSALEVQ VENRWSASQL LTHPFLRCAK
560 570
PLASLYYLIV AAKKSIAEAS NS
Length:572
Mass (Da):63,881
Last modified:October 1, 2001 - 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:iB8D74B0386343B78
GO
Isoform b1 Publication (identifier: Q17850-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-141: Missing.
     142-142: D → N

Show »
Length:569
Mass (Da):63,489
Checksum:i65058A2A38E33013
GO
Isoform c (identifier: Q17850-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.
     139-141: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:523
Mass (Da):58,392
Checksum:i0E4AFB6CF20FD29E
GO
Isoform e (identifier: Q17850-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-448: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:124
Mass (Da):13,879
Checksum:i0D9F0BEBD66E381F
GO

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 conflicti435F → L in AAC47308 (PubMed:8824291).Curated1

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_0515951 – 448Missing in isoform e. CuratedAdd BLAST448
Alternative sequenceiVSP_0515931 – 46Missing in isoform c. CuratedAdd BLAST46
Alternative sequenceiVSP_051596139 – 141Missing in isoform b and isoform c. 1 Publication3
Alternative sequenceiVSP_042128142D → N in isoform b. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U63744 mRNA Translation: AAC47308.1
D83215 mRNA Translation: BAA11844.1
FO080450 Genomic DNA Translation: CCD63804.1
FO080450 Genomic DNA Translation: CCD63805.1
FO080450 Genomic DNA Translation: CCD63806.1
FO080450 Genomic DNA Translation: CCD63807.1

Protein sequence database of the Protein Information Resource

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PIRi
T15467

NCBI Reference Sequences

More...
RefSeqi
NP_001024377.1, NM_001029206.2 [Q17850-1]
NP_001024378.1, NM_001029207.2 [Q17850-2]
NP_001024379.1, NM_001029208.3
NP_001024380.1, NM_001029209.3 [Q17850-5]

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
C09B8.7a.1; C09B8.7a.1; WBGene00003911 [Q17850-1]
C09B8.7b.1; C09B8.7b.1; WBGene00003911 [Q17850-2]
C09B8.7c.1; C09B8.7c.1; WBGene00003911
C09B8.7e.1; C09B8.7e.1; WBGene00003911 [Q17850-5]

Database of genes from NCBI RefSeq genomes

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GeneIDi
180873

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C09B8.7

UCSC genome browser

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UCSCi
C09B8.7e.2 c. elegans [Q17850-1]

Keywords - Coding sequence diversityi

Alternative splicing

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63744 mRNA Translation: AAC47308.1
D83215 mRNA Translation: BAA11844.1
FO080450 Genomic DNA Translation: CCD63804.1
FO080450 Genomic DNA Translation: CCD63805.1
FO080450 Genomic DNA Translation: CCD63806.1
FO080450 Genomic DNA Translation: CCD63807.1
PIRiT15467
RefSeqiNP_001024377.1, NM_001029206.2 [Q17850-1]
NP_001024378.1, NM_001029207.2 [Q17850-2]
NP_001024379.1, NM_001029208.3
NP_001024380.1, NM_001029209.3 [Q17850-5]

3D structure databases

SMRiQ17850
ModBaseiSearch...

Protein-protein interaction databases

BioGridi45805, 2 interactors
DIPiDIP-26715N
IntActiQ17850, 1 interactor
STRINGi6239.C09B8.7a

Proteomic databases

EPDiQ17850
PaxDbiQ17850
PeptideAtlasiQ17850

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC09B8.7a.1; C09B8.7a.1; WBGene00003911 [Q17850-1]
C09B8.7b.1; C09B8.7b.1; WBGene00003911 [Q17850-2]
C09B8.7c.1; C09B8.7c.1; WBGene00003911
C09B8.7e.1; C09B8.7e.1; WBGene00003911 [Q17850-5]
GeneIDi180873
KEGGicel:CELE_C09B8.7
UCSCiC09B8.7e.2 c. elegans [Q17850-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
180873
WormBaseiC09B8.7a ; CE27670 ; WBGene00003911 ; pak-1
C09B8.7b ; CE06792 ; WBGene00003911 ; pak-1
C09B8.7c ; CE33559 ; WBGene00003911 ; pak-1
C09B8.7e ; CE33561 ; WBGene00003911 ; pak-1

Phylogenomic databases

eggNOGiKOG0578 Eukaryota
ENOG410XP4K LUCA
GeneTreeiENSGT00940000165560
HOGENOMiHOG000234202
InParanoidiQ17850
KOiK04409
OMAiPTIHCPT
OrthoDBi757766at2759
PhylomeDBiQ17850

Enzyme and pathway databases

ReactomeiR-CEL-389359 CD28 dependent Vav1 pathway
R-CEL-3928664 Ephrin signaling
R-CEL-399954 Sema3A PAK dependent Axon repulsion
R-CEL-5218920 VEGFR2 mediated vascular permeability
R-CEL-5621575 CD209 (DC-SIGN) signaling
R-CEL-5627123 RHO GTPases activate PAKs
R-CEL-5687128 MAPK6/MAPK4 signaling
SignaLinkiQ17850

Miscellaneous databases

Protein Ontology

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PROi
PR:Q17850

Gene expression databases

BgeeiWBGene00003911 Expressed in 8 organ(s), highest expression level in multi-cellular organism

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
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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 nameiPK1_CAEEL
<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: Q17850
Secondary accession number(s): Q22041
, Q86GT8, Q86GT9, Q86GU0, Q94133
<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: August 31, 2004
Last sequence update: October 1, 2001
Last modified: September 18, 2019
This is version 163 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 programCaenorhabditis annotation project

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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