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Protein

Ribosomal protein S6 kinase alpha-3

Gene

RPS6KA3

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 and histone H3 at 'Ser-10', 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 preinitiation 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). 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. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630).By similarity8 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+By similarity

<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-577 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-227 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.

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 sitei100ATPPROSITE-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 sitei193Proton acceptorBy similarity1
Binding sitei451ATPPROSITE-ProRule annotation1
Active sitei539Proton 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 bindingi74 – 82ATPPROSITE-ProRule annotation9
Nucleotide bindingi428 – 436ATPPROSITE-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

  • ATP binding Source: UniProtKB-KW
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • kinase activity Source: Reactome
  • magnesium ion binding Source: InterPro
  • protein kinase activity Source: ProtInc
  • protein kinase binding Source: Ensembl
  • protein serine/threonine kinase activity Source: Reactome
  • ribosomal protein S6 kinase activity Source: GO_Central

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

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

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SignaLinki
P51812

SIGNOR Signaling Network Open Resource

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SIGNORi
P51812

<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-3 (EC:2.7.11.1)
Short name:
S6K-alpha-3
Alternative name(s):
90 kDa ribosomal protein S6 kinase 3
Short name:
p90-RSK 3
Short name:
p90RSK3
Insulin-stimulated protein kinase 1
Short name:
ISPK-1
MAP kinase-activated protein kinase 1b
Short name:
MAPK-activated protein kinase 1b
Short name:
MAPKAP kinase 1b
Short name:
MAPKAPK-1b
Ribosomal S6 kinase 2
Short name:
RSK-2
pp90RSK2
<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:RPS6KA3
Synonyms:ISPK1, MAPKAPK1B, RSK2
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000177189.12

Human Gene Nomenclature Database

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HGNCi
HGNC:10432 RPS6KA3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300075 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P51812

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Coffin-Lowry syndrome (CLS)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA X-linked mental retardation associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders.
See also OMIM:303600
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_00618975G → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454124EnsemblClinVar.1
Natural variantiVAR_00619082V → F in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454126EnsemblClinVar.1
Natural variantiVAR_006191114R → W in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454127EnsemblClinVar.1
Natural variantiVAR_006192127H → Q in CLS. 1 Publication1
Natural variantiVAR_006193154D → Y in CLS. 1 Publication1
Natural variantiVAR_065894189I → K in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454130EnsemblClinVar.1
Natural variantiVAR_006194225A → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs879027948Ensembl.1
Natural variantiVAR_006195227S → A in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454125EnsemblClinVar.1
Natural variantiVAR_065896268F → S in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454131EnsemblClinVar.1
Natural variantiVAR_006196431G → D in CLS. 1 Publication1
Natural variantiVAR_065898477Missing in CLS. 1 Publication1
Natural variantiVAR_006197729R → Q in CLS. 1 PublicationCorresponds to variant dbSNP:rs28935171EnsemblClinVar.1
Mental retardation, X-linked 19 (MRX19)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA non-syndromic form of mild to moderate mental retardation. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific X-linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation.
See also OMIM:300844
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065892115T → S in MRX19. 1 PublicationCorresponds to variant dbSNP:rs387906703EnsemblClinVar.1
Natural variantiVAR_065893152Missing in MRX19. 1 Publication1
Natural variantiVAR_065895202Missing in MRX19. 1 Publication1
Natural variantiVAR_065897383R → W in MRX19; kinase activity is decreased but not abolished. 1 PublicationCorresponds to variant dbSNP:rs122454129EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
6197

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
RPS6KA3

MalaCards human disease database

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MalaCardsi
RPS6KA3
MIMi300844 phenotype
303600 phenotype

Open Targets

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OpenTargetsi
ENSG00000177189

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
192 Coffin-Lowry syndrome
276630 Symptomatic form of Coffin-Lowry syndrome in female carriers
777 X-linked non-syndromic intellectual disability

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34847

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2345

Drug and drug target database

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DrugBanki
DB00945 Acetylsalicylic acid

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1528

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RPS6KA3

Domain mapping of disease mutations (DMDM)

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DMDMi
1730070

<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_00000862031 – 740Ribosomal protein S6 kinase alpha-3Add BLAST740

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 residuei227Phosphoserine; by PDPK1By similarityCurated1
Modified residuei365PhosphothreonineCombined sources1
Modified residuei369PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1
Modified residuei386Phosphoserine; by autocatalysis and MAPKAPK2Combined sources1
Modified residuei415PhosphoserineCombined sources1
Modified residuei529Phosphotyrosine; by FGFR3By similarity1
Modified residuei556PhosphoserineCombined sources1
Modified residuei715PhosphoserineCombined sources1

<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-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.
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
P51812

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P51812

MaxQB - The MaxQuant DataBase

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MaxQBi
P51812

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

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PaxDbi
P51812

PeptideAtlas

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PeptideAtlasi
P51812

PRoteomics IDEntifications database

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PRIDEi
P51812

ProteomicsDB human proteome resource

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ProteomicsDBi
56408

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P51812

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

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PhosphoSitePlusi
P51812

<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 in many tissues, highest levels in skeletal muscle.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000177189 Expressed in 222 organ(s), highest expression level in biceps brachii

CleanEx database of gene expression profiles

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CleanExi
HS_RPS6KA3

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P51812 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51812 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003853
CAB013520
HPA003221

<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 (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1.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
MAPK1P284823EBI-1046616,EBI-959949

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112111, 64 interactors

Database of interacting proteins

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DIPi
DIP-38247N

Protein interaction database and analysis system

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IntActi
P51812, 22 interactors

Molecular INTeraction database

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MINTi
P51812

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368884

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P51812

<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

1740
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
4D9TX-ray2.40A399-740[»]
4D9UX-ray2.40A399-740[»]
4JG6X-ray2.60A399-740[»]
4JG7X-ray3.00A399-740[»]
4JG8X-ray3.10A399-740[»]
4NUSX-ray2.39A39-359[»]
4NW5X-ray1.94A39-359[»]
4NW6X-ray1.74A39-359[»]
5D9KX-ray2.55A/B39-366[»]
5D9LX-ray2.15A39-359[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P51812

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

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SMRi
P51812

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...

<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>Domaini68 – 327Protein kinase 1PROSITE-ProRule annotationAdd BLAST260
Domaini328 – 397AGC-kinase C-terminalAdd BLAST70
Domaini422 – 679Protein 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
ENSGT00940000159370

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233033

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108317

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P51812

KEGG Orthology (KO)

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KOi
K04373

Identification of Orthologs from Complete Genome Data

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OMAi
TGMEYAV

Database of Orthologous Groups

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OrthoDBi
1132245at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P51812

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>Sequence (1+)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 has 1 described isoform and 7 potential isoforms that are computationally mapped.Show allAlign All

P51812-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEVSIKEI
60 70 80 90 100
AITHHVKEGH EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK
110 120 130 140 150
VLKKATLKVR DRVRTKMERD ILVEVNHPFI VKLHYAFQTE GKLYLILDFL
160 170 180 190 200
RGGDLFTRLS KEVMFTEEDV KFYLAELALA LDHLHSLGII YRDLKPENIL
210 220 230 240 250
LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV NRRGHTQSAD
260 270 280 290 300
WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
310 320 330 340 350
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR
360 370 380 390 400
PEDTFYFDPE FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ
410 420 430 440 450
TVGVHSIVQQ LHRNSIQFTD GYEVKEDIGV GSYSVCKRCI HKATNMEFAV
460 470 480 490 500
KIIDKSKRDP TEEIEILLRY GQHPNIITLK DVYDDGKYVY VVTELMKGGE
510 520 530 540 550
LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL KPSNILYVDE
560 570 580 590 600
SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
610 620 630 640 650
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD
660 670 680 690 700
TAKDLVSKML HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK
710 720 730 740
GAMAATYSAL NRNQSPVLEP VGRSTLAQRR GIKKITSTAL
Length:740
Mass (Da):83,736
Last modified:October 1, 1996 - v1
<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:i486AE8357CEAB6C8
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 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DG22B4DG22_HUMAN
Non-specific serine/threonine prote...
RPS6KA3
711Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B7ZB17B7ZB17_HUMAN
Non-specific serine/threonine prote...
RPS6KA3
712Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B1AXG1B1AXG1_HUMAN
Non-specific serine/threonine prote...
RPS6KA3
711Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B1AXG2B1AXG2_HUMAN
Ribosomal protein S6 kinase alpha-3
RPS6KA3
65Annotation 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>
A0A2R8Y7S9A0A2R8Y7S9_HUMAN
Ribosomal protein S6 kinase alpha-3
RPS6KA3
144Annotation 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>
A0A2R8Y603A0A2R8Y603_HUMAN
Ribosomal protein S6 kinase alpha-3
RPS6KA3
282Annotation 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>
A0A2R8YGB7A0A2R8YGB7_HUMAN
Ribosomal protein S6 kinase alpha-3
RPS6KA3
81Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAD92170 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti89S → L in AAH96303 (PubMed:15489334).Curated1
Sequence conflicti410Missing in BAD92170 (Ref. 3) Curated1
Sequence conflicti424V → L in AAC82495 (PubMed:8141249).Curated1
Sequence conflicti480K → N in AAC82495 (PubMed:8141249).Curated1
Sequence conflicti494Missing in AAC82495 (PubMed:8141249).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00618838I → S2 PublicationsCorresponds to variant dbSNP:rs56218010EnsemblClinVar.1
Natural variantiVAR_00618975G → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454124EnsemblClinVar.1
Natural variantiVAR_00619082V → F in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454126EnsemblClinVar.1
Natural variantiVAR_006191114R → W in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454127EnsemblClinVar.1
Natural variantiVAR_065892115T → S in MRX19. 1 PublicationCorresponds to variant dbSNP:rs387906703EnsemblClinVar.1
Natural variantiVAR_006192127H → Q in CLS. 1 Publication1
Natural variantiVAR_065893152Missing in MRX19. 1 Publication1
Natural variantiVAR_006193154D → Y in CLS. 1 Publication1
Natural variantiVAR_065894189I → K in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454130EnsemblClinVar.1
Natural variantiVAR_065895202Missing in MRX19. 1 Publication1
Natural variantiVAR_006194225A → V in CLS. 1 PublicationCorresponds to variant dbSNP:rs879027948Ensembl.1
Natural variantiVAR_006195227S → A in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454125EnsemblClinVar.1
Natural variantiVAR_065896268F → S in CLS. 1 PublicationCorresponds to variant dbSNP:rs122454131EnsemblClinVar.1
Natural variantiVAR_065897383R → W in MRX19; kinase activity is decreased but not abolished. 1 PublicationCorresponds to variant dbSNP:rs122454129EnsemblClinVar.1
Natural variantiVAR_035627416I → V in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs148050184Ensembl.1
Natural variantiVAR_006196431G → D in CLS. 1 Publication1
Natural variantiVAR_065898477Missing in CLS. 1 Publication1
Natural variantiVAR_040629483Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1271090915Ensembl.1
Natural variantiVAR_040630608L → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_040631723R → C1 PublicationCorresponds to variant dbSNP:rs35026425Ensembl.1
Natural variantiVAR_006197729R → Q in CLS. 1 PublicationCorresponds to variant dbSNP:rs28935171EnsemblClinVar.1

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

More...
DDBJi
Links Updated
U08316 mRNA Translation: AAA81952.1
AK313932 mRNA Translation: BAG36651.1
AB208933 mRNA Translation: BAD92170.1 Different initiation.
AL732366 Genomic DNA No translation available.
AL807772 Genomic DNA No translation available.
BC096301 mRNA Translation: AAH96301.1
BC096302 mRNA Translation: AAH96302.1
BC096303 mRNA Translation: AAH96303.1
L07599 mRNA Translation: AAC82495.1
AB102662 mRNA Translation: BAC81131.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS14197.1

Protein sequence database of the Protein Information Resource

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PIRi
I38556

NCBI Reference Sequences

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RefSeqi
NP_004577.1, NM_004586.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.445387

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000379565; ENSP00000368884; ENSG00000177189
ENST00000645845; ENSP00000494131; ENSG00000177189

Database of genes from NCBI RefSeq genomes

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GeneIDi
6197

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6197

UCSC genome browser

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UCSCi
uc004czu.4 human

Keywords - Coding sequence diversityi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08316 mRNA Translation: AAA81952.1
AK313932 mRNA Translation: BAG36651.1
AB208933 mRNA Translation: BAD92170.1 Different initiation.
AL732366 Genomic DNA No translation available.
AL807772 Genomic DNA No translation available.
BC096301 mRNA Translation: AAH96301.1
BC096302 mRNA Translation: AAH96302.1
BC096303 mRNA Translation: AAH96303.1
L07599 mRNA Translation: AAC82495.1
AB102662 mRNA Translation: BAC81131.1
CCDSiCCDS14197.1
PIRiI38556
RefSeqiNP_004577.1, NM_004586.2
UniGeneiHs.445387

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D9TX-ray2.40A399-740[»]
4D9UX-ray2.40A399-740[»]
4JG6X-ray2.60A399-740[»]
4JG7X-ray3.00A399-740[»]
4JG8X-ray3.10A399-740[»]
4NUSX-ray2.39A39-359[»]
4NW5X-ray1.94A39-359[»]
4NW6X-ray1.74A39-359[»]
5D9KX-ray2.55A/B39-366[»]
5D9LX-ray2.15A39-359[»]
ProteinModelPortaliP51812
SMRiP51812
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112111, 64 interactors
DIPiDIP-38247N
IntActiP51812, 22 interactors
MINTiP51812
STRINGi9606.ENSP00000368884

Chemistry databases

BindingDBiP51812
ChEMBLiCHEMBL2345
DrugBankiDB00945 Acetylsalicylic acid
GuidetoPHARMACOLOGYi1528

PTM databases

iPTMnetiP51812
PhosphoSitePlusiP51812

Polymorphism and mutation databases

BioMutaiRPS6KA3
DMDMi1730070

Proteomic databases

EPDiP51812
jPOSTiP51812
MaxQBiP51812
PaxDbiP51812
PeptideAtlasiP51812
PRIDEiP51812
ProteomicsDBi56408

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6197
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379565; ENSP00000368884; ENSG00000177189
ENST00000645845; ENSP00000494131; ENSG00000177189
GeneIDi6197
KEGGihsa:6197
UCSCiuc004czu.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6197
DisGeNETi6197
EuPathDBiHostDB:ENSG00000177189.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RPS6KA3
GeneReviewsiRPS6KA3
HGNCiHGNC:10432 RPS6KA3
HPAiCAB003853
CAB013520
HPA003221
MalaCardsiRPS6KA3
MIMi300075 gene
300844 phenotype
303600 phenotype
neXtProtiNX_P51812
OpenTargetsiENSG00000177189
Orphaneti192 Coffin-Lowry syndrome
276630 Symptomatic form of Coffin-Lowry syndrome in female carriers
777 X-linked non-syndromic intellectual disability
PharmGKBiPA34847

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0598 Eukaryota
ENOG410XNPH LUCA
GeneTreeiENSGT00940000159370
HOGENOMiHOG000233033
HOVERGENiHBG108317
InParanoidiP51812
KOiK04373
OMAiTGMEYAV
OrthoDBi1132245at2759
PhylomeDBiP51812
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
SignaLinkiP51812
SIGNORiP51812

Miscellaneous databases

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

More...
ChiTaRSi
RPS6KA3 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RPS6KA3

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

More...
GenomeRNAii
6197

Protein Ontology

More...
PROi
PR:P51812

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000177189 Expressed in 222 organ(s), highest expression level in biceps brachii
CleanExiHS_RPS6KA3
ExpressionAtlasiP51812 baseline and differential
GenevisibleiP51812 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

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKS6A3_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: P51812
Secondary accession number(s): B2R9V4
, Q4VAP3, Q59H26, Q5JPK8, Q7Z3Z7
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 16, 2019
This is version 198 of the entry and version 1 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 and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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