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Protein

Ribosomal protein S6 kinase alpha-1

Gene

RPS6KA1

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 acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (By similarity). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630).By similarity12 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

<p>This subsection of the ‘Function’ 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

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-573 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-380, allowing binding of PDPK1, which in turn phosphorylates Ser-221 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei94ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei187Proton acceptorBy similarity1
Binding sitei447ATPPROSITE-ProRule annotation1
Active sitei535Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi68 – 76ATPPROSITE-ProRule annotation9
Nucleotide bindingi424 – 432ATPPROSITE-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 functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Stress response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-198753 ERK/MAPK targets
R-HSA-199920 CREB phosphorylation
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-437239 Recycling pathway of L1
R-HSA-442742 CREB phosphorylation through the activation of Ras
R-HSA-444257 RSK activation
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q15418

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

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SignaLinki
Q15418

SIGNOR Signaling Network Open Resource

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SIGNORi
Q15418

<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:
Ribosomal protein S6 kinase alpha-1 (EC:2.7.11.1)
Short name:
S6K-alpha-1
Alternative name(s):
90 kDa ribosomal protein S6 kinase 1
Short name:
p90-RSK 1
Short name:
p90RSK1
Short name:
p90S6K
MAP kinase-activated protein kinase 1a
Short name:
MAPK-activated protein kinase 1a
Short name:
MAPKAP kinase 1a
Short name:
MAPKAPK-1a
Ribosomal S6 kinase 1
Short name:
RSK-1
<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:RPS6KA1
Synonyms:MAPKAPK1A, RSK1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000117676.13

Human Gene Nomenclature Database

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HGNCi
HGNC:10430 RPS6KA1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601684 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q15418

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

Organism-specific databases

DisGeNET

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DisGeNETi
6195

Open Targets

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OpenTargetsi
ENSG00000117676

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34845

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2553

Drug and drug target database

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DrugBanki
DB04751 Purvalanol A

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1527

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RPS6KA1

Domain mapping of disease mutations (DMDM)

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DMDMi
20178306

<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_00000861981 – 735Ribosomal protein S6 kinase alpha-1Add BLAST735

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 residuei54PhosphoserineCombined sources1
Modified residuei221Phosphoserine; by PDPK11 Publication1
Modified residuei307PhosphoserineCombined sources1
Modified residuei359PhosphothreonineCombined sources1 Publication1
Modified residuei363PhosphoserineCombined sources1 Publication1
Modified residuei369PhosphoserineCombined sources1
Modified residuei380Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei573Phosphothreonine1 Publication1
Modified residuei732Phosphoserine1 Publication1

<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

Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-380, as part of the activation process. May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.1 Publication
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q15418

MaxQB - The MaxQuant DataBase

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MaxQBi
Q15418

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

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PaxDbi
Q15418

PeptideAtlas

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PeptideAtlasi
Q15418

PRoteomics IDEntifications database

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PRIDEi
Q15418

ProteomicsDB human proteome resource

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ProteomicsDBi
60583
60584 [Q15418-2]
60585 [Q15418-3]

2D gel databases

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
Q15418

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q15418

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

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PhosphoSitePlusi
Q15418

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000117676 Expressed in 190 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_RPS6KA1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15418 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15418 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003852
HPA007981

<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

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation. Interacts with ETV1/ER81 and FGFR1.5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112109, 76 interactors

Database of interacting proteins

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DIPi
DIP-29987N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q15418

Protein interaction database and analysis system

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IntActi
Q15418, 34 interactors

Molecular INTeraction database

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MINTi
Q15418

STRING: functional protein association networks

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STRINGi
9606.ENSP00000435412

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q15418

<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

1735
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q15418

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

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SMRi
Q15418

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q15418

<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>Domaini62 – 321Protein kinase 1PROSITE-ProRule annotationAdd BLAST260
Domaini322 – 391AGC-kinase C-terminalAdd BLAST70
Domaini418 – 675Protein kinase 2PROSITE-ProRule annotationAdd BLAST258

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0598 Eukaryota
ENOG410XNPH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159314

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108317

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15418

KEGG Orthology (KO)

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KOi
K04373

Identification of Orthologs from Complete Genome Data

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OMAi
GGNWDTI

Database of Orthologous Groups

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OrthoDBi
EOG091G05Z7

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15418

TreeFam database of animal gene trees

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TreeFami
TF313438

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR017892 Pkinase_C
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR016239 Ribosomal_S6_kinase_II
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 2 hits
PF00433 Pkinase_C, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000606 Ribsml_S6_kin_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS00107 PROTEIN_KINASE_ATP, 2 hits
PS50011 PROTEIN_KINASE_DOM, 2 hits
PS00108 PROTEIN_KINASE_ST, 2 hits

<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>.<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

This entry has 4 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q15418-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV
60 70 80 90 100
KAGSEKADPS HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT
110 120 130 140 150
LKVRDRVRTK MERDILADVN HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF
160 170 180 190 200
TRLSKEVMFT EEDVKFYLAE LALGLDHLHS LGIIYRDLKP ENILLDEEGH
210 220 230 240 250
IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS HSADWWSYGV
260 270 280 290 300
LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN
310 320 330 340 350
PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREIKPPFKP AVAQPDDTFY
360 370 380 390 400
FDTEFTSRTP KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL
410 420 430 440 450
HSVVQQLHGK NLVFSDGYVV KETIGVGSYS ECKRCVHKAT NMEYAVKVID
460 470 480 490 500
KSKRDPSEEI EILLRYGQHP NIITLKDVYD DGKHVYLVTE LMRGGELLDK
510 520 530 540 550
ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN ILYVDESGNP
560 570 580 590 600
ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL
610 620 630 640 650
GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD
660 670 680 690 700
LVSKMLHVDP HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA
710 720 730
TYSALNSSKP TPQLKPIESS ILAQRRVRKL PSTTL
Length:735
Mass (Da):82,723
Last modified:April 16, 2002 - 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:i765731A4442A53DF
GO
Isoform 2 (identifier: Q15418-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MPLAQLKEPW...GEEAGLQPSK → MEQDPKPPRL...GPGSGPQRDS

Show »
Length:744
Mass (Da):83,932
Checksum:i3121E64369EBDBBF
GO
Isoform 3 (identifier: Q15418-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.

Note: No experimental confirmation available.
Show »
Length:643
Mass (Da):72,698
Checksum:iB8362021FCCC17B5
GO
Isoform 4Curated (identifier: Q15418-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPS → MQTPADFPRVERDLVPCPR

Show »
Length:719
Mass (Da):81,147
Checksum:iD47F7EC9609D5ACF
GO

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

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PGT3E9PGT3_HUMAN
Ribosomal protein S6 kinase
RPS6KA1
724Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SVM7Q5SVM7_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
115Annotation 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>
Q5SVM6Q5SVM6_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
166Annotation 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>
E9PAN7E9PAN7_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
204Annotation 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>
E9PMM7E9PMM7_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
112Annotation 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>
E9PPN6E9PPN6_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
52Annotation 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>
A6NND1A6NND1_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
111Annotation 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>
E9PPC1E9PPC1_HUMAN
Ribosomal protein S6 kinase alpha-1
RPS6KA1
56Annotation 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 conflicti609A → T in BAF85411 (PubMed:14702039).Curated1
Sequence conflicti619S → G in BAF85411 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_021864335K → T2 PublicationsCorresponds to variant dbSNP:rs2229712Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0415801 – 92Missing in isoform 3. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_0413801 – 36MPLAQ…LQPSK → MEQDPKPPRLRLWALIPWLP RKQRPRISQTSLPVPGPGSG PQRDS in isoform 2. 1 PublicationAdd BLAST36
Alternative sequenceiVSP_0574691 – 35MPLAQ…GLQPS → MQTPADFPRVERDLVPCPR in isoform 4. Add BLAST35

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
L07597 mRNA Translation: AAC82497.1
AK292722 mRNA Translation: BAF85411.1
AK299007 mRNA Translation: BAH12926.1
AK315730 mRNA Translation: BAG38085.1
AL109743 Genomic DNA Translation: CAC36348.1
AL627313 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07799.1
BC014966 mRNA Translation: AAH14966.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS284.1 [Q15418-1]
CCDS30649.1 [Q15418-2]
CCDS81286.1 [Q15418-4]

Protein sequence database of the Protein Information Resource

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PIRi
I51901

NCBI Reference Sequences

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RefSeqi
NP_001006666.1, NM_001006665.1 [Q15418-2]
NP_001317370.1, NM_001330441.1 [Q15418-4]
NP_002944.2, NM_002953.3 [Q15418-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.149957

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000374168; ENSP00000363283; ENSG00000117676 [Q15418-1]
ENST00000526792; ENSP00000431651; ENSG00000117676 [Q15418-3]
ENST00000530003; ENSP00000432281; ENSG00000117676 [Q15418-4]
ENST00000531382; ENSP00000435412; ENSG00000117676 [Q15418-2]
ENST00000628081; ENSP00000487553; ENSG00000281877 [Q15418-4]
ENST00000628256; ENSP00000487349; ENSG00000281877 [Q15418-2]
ENST00000629832; ENSP00000486881; ENSG00000281877 [Q15418-1]
ENST00000631108; ENSP00000487166; ENSG00000281877 [Q15418-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
6195

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:6195

UCSC genome browser

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UCSCi
uc001bmr.2 human [Q15418-1]
uc057dso.1 human

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07597 mRNA Translation: AAC82497.1
AK292722 mRNA Translation: BAF85411.1
AK299007 mRNA Translation: BAH12926.1
AK315730 mRNA Translation: BAG38085.1
AL109743 Genomic DNA Translation: CAC36348.1
AL627313 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07799.1
BC014966 mRNA Translation: AAH14966.1
CCDSiCCDS284.1 [Q15418-1]
CCDS30649.1 [Q15418-2]
CCDS81286.1 [Q15418-4]
PIRiI51901
RefSeqiNP_001006666.1, NM_001006665.1 [Q15418-2]
NP_001317370.1, NM_001330441.1 [Q15418-4]
NP_002944.2, NM_002953.3 [Q15418-1]
UniGeneiHs.149957

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
2WNTX-ray2.40A/B413-719[»]
2Z7QX-ray2.00A33-353[»]
2Z7RX-ray2.00A33-353[»]
2Z7SX-ray2.10A33-353[»]
3RNYX-ray2.70A/B411-735[»]
3TEIX-ray2.40B712-735[»]
4H3PX-ray2.30B/E712-735[»]
4NIFX-ray2.15A/D411-735[»]
5CSFX-ray2.40C683-735[»]
5CSIX-ray2.13C689-735[»]
5CSJX-ray2.70C696-735[»]
5CSNX-ray2.95C683-720[»]
5N7DX-ray2.30C688-735[»]
5N7FX-ray2.30C688-735[»]
5N7GX-ray2.95C729-735[»]
5V61X-ray2.20I713-729[»]
5V62X-ray1.90I713-729[»]
ProteinModelPortaliQ15418
SMRiQ15418
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112109, 76 interactors
DIPiDIP-29987N
ELMiQ15418
IntActiQ15418, 34 interactors
MINTiQ15418
STRINGi9606.ENSP00000435412

Chemistry databases

BindingDBiQ15418
ChEMBLiCHEMBL2553
DrugBankiDB04751 Purvalanol A
GuidetoPHARMACOLOGYi1527

PTM databases

iPTMnetiQ15418
PhosphoSitePlusiQ15418

Polymorphism and mutation databases

BioMutaiRPS6KA1
DMDMi20178306

2D gel databases

UCD-2DPAGEiQ15418

Proteomic databases

EPDiQ15418
MaxQBiQ15418
PaxDbiQ15418
PeptideAtlasiQ15418
PRIDEiQ15418
ProteomicsDBi60583
60584 [Q15418-2]
60585 [Q15418-3]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
6195
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374168; ENSP00000363283; ENSG00000117676 [Q15418-1]
ENST00000526792; ENSP00000431651; ENSG00000117676 [Q15418-3]
ENST00000530003; ENSP00000432281; ENSG00000117676 [Q15418-4]
ENST00000531382; ENSP00000435412; ENSG00000117676 [Q15418-2]
ENST00000628081; ENSP00000487553; ENSG00000281877 [Q15418-4]
ENST00000628256; ENSP00000487349; ENSG00000281877 [Q15418-2]
ENST00000629832; ENSP00000486881; ENSG00000281877 [Q15418-1]
ENST00000631108; ENSP00000487166; ENSG00000281877 [Q15418-3]
GeneIDi6195
KEGGihsa:6195
UCSCiuc001bmr.2 human [Q15418-1]
uc057dso.1 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6195
DisGeNETi6195
EuPathDBiHostDB:ENSG00000117676.13

GeneCards: human genes, protein and diseases

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GeneCardsi
RPS6KA1
HGNCiHGNC:10430 RPS6KA1
HPAiCAB003852
HPA007981
MIMi601684 gene
neXtProtiNX_Q15418
OpenTargetsiENSG00000117676
PharmGKBiPA34845

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0598 Eukaryota
ENOG410XNPH LUCA
GeneTreeiENSGT00940000159314
HOVERGENiHBG108317
InParanoidiQ15418
KOiK04373
OMAiGGNWDTI
OrthoDBiEOG091G05Z7
PhylomeDBiQ15418
TreeFamiTF313438

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-198753 ERK/MAPK targets
R-HSA-199920 CREB phosphorylation
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-437239 Recycling pathway of L1
R-HSA-442742 CREB phosphorylation through the activation of Ras
R-HSA-444257 RSK activation
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK
SABIO-RKiQ15418
SignaLinkiQ15418
SIGNORiQ15418

Miscellaneous databases

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

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ChiTaRSi
RPS6KA1 human
EvolutionaryTraceiQ15418

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
RPS6KA1

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

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GenomeRNAii
6195

Protein Ontology

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PROi
PR:Q15418

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000117676 Expressed in 190 organ(s), highest expression level in blood
CleanExiHS_RPS6KA1
ExpressionAtlasiQ15418 baseline and differential
GenevisibleiQ15418 HS

Family and domain databases

InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR017892 Pkinase_C
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR016239 Ribosomal_S6_kinase_II
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 2 hits
PF00433 Pkinase_C, 1 hit
PIRSFiPIRSF000606 Ribsml_S6_kin_2, 1 hit
SMARTiView protein in SMART
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 2 hits
SUPFAMiSSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS00107 PROTEIN_KINASE_ATP, 2 hits
PS50011 PROTEIN_KINASE_DOM, 2 hits
PS00108 PROTEIN_KINASE_ST, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKS6A1_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: Q15418
Secondary accession number(s): A6NGG4
, A8K9K7, B2RDY8, B7Z5J0, E9PRI4, Q5SVM5, Q5SVM8, Q5SVM9, Q96C05, Q9BQK2
<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: December 15, 1998
Last sequence update: April 16, 2002
Last modified: December 5, 2018
This is version 202 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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