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Entry version 151 (05 Jun 2019)
Sequence version 1 (01 Jun 2001)
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Protein

Phosphatidylinositol 4-kinase type 2-alpha

Gene

PI4K2A

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

Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).Curated6 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei152ATP2 Publications1
Binding sitei346ATP2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi131 – 137ATP2 Publications7
Nucleotide bindingi261 – 264ATP2 Publications4

<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, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS00573-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-1660514 Synthesis of PIPs at the Golgi membrane
R-HSA-1660516 Synthesis of PIPs at the early endosome membrane

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9BTU6

<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:
Phosphatidylinositol 4-kinase type 2-alpha (EC:2.7.1.674 Publications)
Alternative name(s):
Phosphatidylinositol 4-kinase type II-alpha
<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:PI4K2A
<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 10

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:30031 PI4K2A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609763 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9BTU6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Mitochondrion, Synapse, Synaptosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi129R → E: Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-275 and E-276. 1 Publication1
Mutagenesisi152K → A: Abolishes enzyme activity. 2 Publications1
Mutagenesisi157 – 159EPY → APA: Abolishes enzyme activity. 1 Publication3
Mutagenesisi163N → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi165 – 172KWTKWLQK → AAAAAAAA: Abolishes enzyme activity. 1 Publication8
Mutagenesisi165K → A: Abolishes enzyme activity; when associated with A-168 and A-172. 1 Publication1
Mutagenesisi166W → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi168K → A: Abolishes enzyme activity; when associated with A-165 and A-172. 1 Publication1
Mutagenesisi172K → A: Abolishes enzyme activity; when associated with A-165 and A-168. 1 Publication1
Mutagenesisi174 – 178CCPCC → FFPFF: No effect on membrane-association. 1 Publication5
Mutagenesisi174 – 178CCPCC → SSPSS: Abolishes palmitoylation and impairs membrane-association. 2 Publications5
Mutagenesisi184L → A: Abolishes enzyme activity; when associated with A-349. 1 Publication1
Mutagenesisi263F → A: Abolishes enzyme activity; when associated with A-345. 1 Publication1
Mutagenesisi269D → A: Reduces enzyme activity by half. 1 Publication1
Mutagenesisi275R → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi275R → E: Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-129 and E-276. 1 Publication1
Mutagenesisi276R → E: Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-129 and E-275. 1 Publication1
Mutagenesisi308D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi345I → A: Abolishes enzyme activity; when associated with A-263. 1 Publication1
Mutagenesisi349L → A: Abolishes enzyme activity; when associated with A-184. 1 Publication1
Mutagenesisi359W → A: Strongly reduced enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-365 and A-368. 1 Publication1
Mutagenesisi365Y → A: Reduces enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-368 and A-359. 1 Publication1
Mutagenesisi368W → A: Reduces enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-359 and A-365. 1 Publication1
Mutagenesisi445Q → A: Reduces enzyme activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
55361

Open Targets

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OpenTargetsi
ENSG00000155252

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA162399304

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2251

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2498

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PI4K2A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74752344

<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_00002851581 – 479Phosphatidylinositol 4-kinase type 2-alphaAdd BLAST479

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 residuei1N-acetylmethionineCombined sources1
Modified residuei5PhosphoserineCombined sources1
Modified residuei9PhosphoserineCombined sources1
Modified residuei44PhosphoserineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei51PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi174S-palmitoyl cysteine2 Publications1
Lipidationi175S-palmitoyl cysteine2 Publications1
Lipidationi177S-palmitoyl cysteine2 Publications1
Lipidationi178S-palmitoyl cysteine2 Publications1
Modified residuei462PhosphoserineBy similarity1

<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

Palmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-dependent, and required for TGN localization.1 Publication
Ubiquitinated by ITCH; this does not lead to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9BTU6

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9BTU6

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9BTU6

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

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PaxDbi
Q9BTU6

PeptideAtlas

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PeptideAtlasi
Q9BTU6

PRoteomics IDEntifications database

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PRIDEi
Q9BTU6

ProteomicsDB human proteome resource

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ProteomicsDBi
79011

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9BTU6

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

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PhosphoSitePlusi
Q9BTU6

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9BTU6

<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

Widely expressed. Highest expression is observed in kidney, brain, heart, skeletal muscle, and placenta and lowest expression is observed in colon, thymus, and small intestine.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000155252 Expressed in 212 organ(s), highest expression level in lower esophagus mucosa

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9BTU6 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB030649

<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

Associates with the BLOC-1 and the AP-3 complexes; the BLOC-1 complex is required for optimal binding of PI4K2A to the AP-3 complex. Interacts with BLOC1S5 and DTNBP1 (PubMed:21998198). Interacts with FOS; this interaction may enhance phosphatidylinositol phosphorylation activity (By similarity). Interacts with ITCH (PubMed:23146885).By similarity2 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

WithEntry#Exp.IntActNotes
ITCHQ96J025EBI-3239392,EBI-1564678

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
120639, 25 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9BTU6

Protein interaction database and analysis system

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IntActi
Q9BTU6, 7 interactors

Molecular INTeraction database

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MINTi
Q9BTU6

STRING: functional protein association networks

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STRINGi
9606.ENSP00000359665

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9BTU6

<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

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q9BTU6

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>Domaini133 – 438PI3K/PI4KAdd BLAST306

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni157 – 159Important for substrate binding1 Publication3
Regioni165 – 178Important for interaction with membranes2 PublicationsAdd BLAST14
Regioni268 – 276Important for interaction with membranes1 Publication9
Regioni359 – 368Important for interaction with membranes1 Publication10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi39 – 42Poly-Ala4
Compositional biasi65 – 97Ala-richAdd BLAST33

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2381 Eukaryota
ENOG410XP06 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000010434

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000294076

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9BTU6

KEGG Orthology (KO)

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KOi
K13711

Identification of Orthologs from Complete Genome Data

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OMAi
VRDINYQ

Database of Orthologous Groups

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OrthoDBi
1273723at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9BTU6

TreeFam database of animal gene trees

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TreeFami
TF314740

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR039756 Lsb6/PI4K2
IPR000403 PI3/4_kinase_cat_dom

The PANTHER Classification System

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PANTHERi
PTHR12865 PTHR12865, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00454 PI3_PI4_kinase, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9BTU6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDETSPLVSP ERAQPPDYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPG
60 70 80 90 100
SPGHDRERQP LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE
110 120 130 140 150
RNEFPEDPEF EAVVRQAELA IERCIFPERI YQGSSGSYFV KDPQGRIIAV
160 170 180 190 200
FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG RDCLVLNQGY LSEAGASLVD
210 220 230 240 250
QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK VPKVGQRFNR
260 270 280 290 300
IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL
310 320 330 340 350
DYIIRNTDRG NDNWLIKYDC PMDSSSSRDT DWVVVKEPVI KVAAIDNGLA
360 370 380 390 400
FPLKHPDSWR AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED
410 420 430 440 450
LYELFKKDPG FDRGQFHKQI AVMRGQILNL TQALKDNKSP LHLVQMPPVI
460 470
VETARSHQRS SSESYTQSFQ SRKPFFSWW
Length:479
Mass (Da):54,022
Last modified:June 1, 2001 - 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:i9C9F4CE23F197BBD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AJ303098 mRNA Translation: CAC38065.1
BT007330 mRNA Translation: AAP35994.1
AL355315 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49906.1
CH471066 Genomic DNA Translation: EAW49907.1
BC003167 mRNA Translation: AAH03167.1
AL353952 mRNA Translation: CAB89254.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS7469.1

Protein sequence database of the Protein Information Resource

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PIRi
T48687

NCBI Reference Sequences

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RefSeqi
NP_060895.1, NM_018425.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000370631; ENSP00000359665; ENSG00000155252

Database of genes from NCBI RefSeq genomes

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GeneIDi
55361

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:55361

UCSC genome browser

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UCSCi
uc001kog.2 human

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303098 mRNA Translation: CAC38065.1
BT007330 mRNA Translation: AAP35994.1
AL355315 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49906.1
CH471066 Genomic DNA Translation: EAW49907.1
BC003167 mRNA Translation: AAH03167.1
AL353952 mRNA Translation: CAB89254.1
CCDSiCCDS7469.1
PIRiT48687
RefSeqiNP_060895.1, NM_018425.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HNDX-ray3.20A/B78-453[»]
4HNEX-ray2.95A/B78-453[»]
4PLAX-ray2.77A180-468[»]
4YC4X-ray2.58A180-468[»]
5EUTX-ray2.80A179-468[»]
5I0NX-ray2.28A180-468[»]
SMRiQ9BTU6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120639, 25 interactors
CORUMiQ9BTU6
IntActiQ9BTU6, 7 interactors
MINTiQ9BTU6
STRINGi9606.ENSP00000359665

Chemistry databases

BindingDBiQ9BTU6
ChEMBLiCHEMBL2251
GuidetoPHARMACOLOGYi2498

PTM databases

iPTMnetiQ9BTU6
PhosphoSitePlusiQ9BTU6
SwissPalmiQ9BTU6

Polymorphism and mutation databases

BioMutaiPI4K2A
DMDMi74752344

Proteomic databases

EPDiQ9BTU6
jPOSTiQ9BTU6
MaxQBiQ9BTU6
PaxDbiQ9BTU6
PeptideAtlasiQ9BTU6
PRIDEiQ9BTU6
ProteomicsDBi79011

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
55361
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370631; ENSP00000359665; ENSG00000155252
GeneIDi55361
KEGGihsa:55361
UCSCiuc001kog.2 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
55361
DisGeNETi55361

GeneCards: human genes, protein and diseases

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GeneCardsi
PI4K2A
HGNCiHGNC:30031 PI4K2A
HPAiCAB030649
MIMi609763 gene
neXtProtiNX_Q9BTU6
OpenTargetsiENSG00000155252
PharmGKBiPA162399304

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG2381 Eukaryota
ENOG410XP06 LUCA
GeneTreeiENSGT00390000010434
HOGENOMiHOG000294076
InParanoidiQ9BTU6
KOiK13711
OMAiVRDINYQ
OrthoDBi1273723at2759
PhylomeDBiQ9BTU6
TreeFamiTF314740

Enzyme and pathway databases

BioCyciMetaCyc:HS00573-MONOMER
ReactomeiR-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-1660514 Synthesis of PIPs at the Golgi membrane
R-HSA-1660516 Synthesis of PIPs at the early endosome membrane
SIGNORiQ9BTU6

Miscellaneous databases

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

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ChiTaRSi
PI4K2A human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PI4K2A

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

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GenomeRNAii
55361

Protein Ontology

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PROi
PR:Q9BTU6

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000155252 Expressed in 212 organ(s), highest expression level in lower esophagus mucosa
GenevisibleiQ9BTU6 HS

Family and domain databases

InterProiView protein in InterPro
IPR039756 Lsb6/PI4K2
IPR000403 PI3/4_kinase_cat_dom
PANTHERiPTHR12865 PTHR12865, 1 hit
PfamiView protein in Pfam
PF00454 PI3_PI4_kinase, 1 hit

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 nameiP4K2A_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: Q9BTU6
Secondary accession number(s): D3DR59, Q9NSG8
<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: May 1, 2007
Last sequence update: June 1, 2001
Last modified: June 5, 2019
This is version 151 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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