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Entry version 129 (23 Feb 2022)
Sequence version 1 (01 Jun 2001)
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Protein

Phosphatidylinositol 4-kinase type 2-alpha

Gene

Pi4k2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).

Curated1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=88 µM for ATP
  2. KM=45 µM for PtdIns

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei151ATPBy similarity1
Binding sitei345ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi130 – 136ATPBy similarity7
Nucleotide bindingi260 – 263ATPBy similarity4

<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
Biological processLipid metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1660499, Synthesis of PIPs at the plasma membrane
R-RNO-1660514, Synthesis of PIPs at the Golgi membrane
R-RNO-1660516, Synthesis of PIPs at the early endosome membrane

<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%5Fand%5Ftaxonomy%5Fsection">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:2.7.1.671 Publication)
Alternative name(s):
55 kDa type II phosphatidylinositol 4-kinase
Phosphatidylinositol 4-kinase type II-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
Synonyms:Pi4kii
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
620485, Pi4k2a

<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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi60L → A: Reduces targeting to synaptic vesicles and neurite tips; when associated with A-61. 1 Publication1
Mutagenesisi61L → A: Reduces targeting to synaptic vesicles and neurite tips; when associated with A-60. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002851601 – 478Phosphatidylinositol 4-kinase type 2-alphaAdd BLAST478

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-acetylmethionineBy similarity1
Modified residuei5PhosphoserineCombined sources1
Modified residuei9PhosphoserineCombined sources1
Modified residuei43PhosphoserineBy similarity1
Modified residuei46PhosphoserineCombined sources1
Modified residuei50PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Lipidationi173S-palmitoyl cysteineBy similarity1
Lipidationi174S-palmitoyl cysteineBy similarity1
Lipidationi176S-palmitoyl cysteineBy similarity1
Lipidationi177S-palmitoyl cysteineBy similarity1
Modified residuei461PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ubiquitinated by ITCH; this does not lead to proteasomal degradation.By similarity
Palmitoylated (PubMed:11244087). Palmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-dependent, and required for TGN localization (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q99M64

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

More...
PaxDbi
Q99M64

PRoteomics IDEntifications database

More...
PRIDEi
Q99M64

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q99M64

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

More...
PhosphoSitePlusi
Q99M64

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q99M64

<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

Detected in adult brain, especially in neurons in the cerebellum, brain cortex, dorsal root ganglion and spinal cord (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000014675, Expressed in cerebellum and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q99M64, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'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%5Fsection">'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 (By similarity).

Interacts with ATG9A (By similarity).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
250373, 1 interactor

Protein interaction database and analysis system

More...
IntActi
Q99M64, 3 interactors

Molecular INTeraction database

More...
MINTi
Q99M64

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000019874

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...
SMRi
Q99M64

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini123 – 452PI3K/PI4K catalyticPROSITE-ProRule annotationAdd BLAST330

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>Regioni1 – 57DisorderedSequence analysisAdd BLAST57
Regioni129 – 135G-loopPROSITE-ProRule annotation7
Regioni156 – 158Important for substrate bindingBy similarity3
Regioni164 – 177Important for interaction with membranesBy similarityAdd BLAST14
Regioni267 – 275Important for interaction with membranesBy similarity9
Regioni304 – 312Catalytic loopPROSITE-ProRule annotation9
Regioni343 – 363Activation loopPROSITE-ProRule annotationAdd BLAST21
Regioni358 – 367Important for interaction with membranesBy similarity10

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2381, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000010434

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_032516_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q99M64

Identification of Orthologs from Complete Genome Data

More...
OMAi
CLIPLNG

Database of Orthologous Groups

More...
OrthoDBi
1273723at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q99M64

TreeFam database of animal gene trees

More...
TreeFami
TF314740

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

More...
PANTHERi
PTHR12865, PTHR12865, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00454, PI3_PI4_kinase, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50290, PI3_4_KINASE_3, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q99M64-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDETSPLVSP ERAQPPEYTF PSVSGAHFPQ VPGGAVRVAA AGSGPSPPCS
60 70 80 90 100
PGHDRERQPL LDRARGAAAQ GQTHTVAAQA QALAAQAAVA VHAVQTHRER
110 120 130 140 150
NDFPEDPEFE VVVRQAEIAI ECSIYPERIY QGSSGSYFVK DSQGRIIAVF
160 170 180 190 200
KPKNEEPYGN LNPKWTKWLQ KLCCPCCFGR DCLVLNQGYL SEAGASLVDQ
210 220 230 240 250
KLELNIVPRT KVVYLASETF NYSAIDRVKS RGKRLALEKV PKVGQRFNRI
260 270 280 290 300
GLPPKVGSFQ LFVEGYKDAD YWLRRFEAEP LPENTNRQLL LQFERLVVLD
310 320 330 340 350
YIIRNTDRGN DNWLIKYDYP MDNPNCRDTD WVMVREPVIK VAAIDNGLAF
360 370 380 390 400
PLKHPDSWRA YPFYWAWLPQ AKVPFSQEIK DLILPKISDP NFVKDLEEDL
410 420 430 440 450
YELFKKDPGF DRGQFHKQIA VMRGQILNLT QALKDNKSPL HLVQMPPVIV
460 470
ETARSHQRSS SESYTQSFQS RKPFFSWW
Length:478
Mass (Da):54,305
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:iEBE4BFFB4574FD1F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY029199 mRNA Translation: AAK33002.1

NCBI Reference Sequences

More...
RefSeqi
NP_446187.1, NM_053735.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000019874; ENSRNOP00000019874; ENSRNOG00000014675

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
114554

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:114554

UCSC genome browser

More...
UCSCi
RGD:620485, rat

<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
AY029199 mRNA Translation: AAK33002.1
RefSeqiNP_446187.1, NM_053735.1

3D structure databases

SMRiQ99M64
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi250373, 1 interactor
IntActiQ99M64, 3 interactors
MINTiQ99M64
STRINGi10116.ENSRNOP00000019874

PTM databases

iPTMnetiQ99M64
PhosphoSitePlusiQ99M64
SwissPalmiQ99M64

Proteomic databases

jPOSTiQ99M64
PaxDbiQ99M64
PRIDEiQ99M64

Genome annotation databases

EnsembliENSRNOT00000019874; ENSRNOP00000019874; ENSRNOG00000014675
GeneIDi114554
KEGGirno:114554
UCSCiRGD:620485, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
55361
RGDi620485, Pi4k2a

Phylogenomic databases

eggNOGiKOG2381, Eukaryota
GeneTreeiENSGT00390000010434
HOGENOMiCLU_032516_2_0_1
InParanoidiQ99M64
OMAiCLIPLNG
OrthoDBi1273723at2759
PhylomeDBiQ99M64
TreeFamiTF314740

Enzyme and pathway databases

ReactomeiR-RNO-1660499, Synthesis of PIPs at the plasma membrane
R-RNO-1660514, Synthesis of PIPs at the Golgi membrane
R-RNO-1660516, Synthesis of PIPs at the early endosome membrane

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q99M64

Gene expression databases

BgeeiENSRNOG00000014675, Expressed in cerebellum and 20 other tissues
GenevisibleiQ99M64, RN

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
PROSITEiView protein in PROSITE
PS50290, PI3_4_KINASE_3, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiP4K2A_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q99M64
<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%5Fand%5Fisoforms">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: February 23, 2022
This is version 129 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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