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UniProtKB - Q53GL0 (PKHO1_HUMAN)

Entry version 115 (08 May 2019)
Sequence version 2 (13 Nov 2007)
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Protein

Pleckstrin homology domain-containing family O member 1

Gene

PLEKHO1

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

Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation.7 Publications

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 sitei155Capping protein1
Binding sitei157Capping protein1

<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 - Biological processi

Complete GO annotation on QuickGO ...

<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:
Pleckstrin homology domain-containing family O member 1
Short name:
PH domain-containing family O member 1
Alternative name(s):
C-Jun-binding protein
Short name:
JBP
Casein kinase 2-interacting protein 1
Short name:
CK2-interacting protein 1
Short name:
CKIP-1
Osteoclast maturation-associated gene 120 protein
<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:PLEKHO1
Synonyms:CKIP1, OC120
ORF Names:HQ0024c
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:24310 PLEKHO1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		608335 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q53GL0

<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

<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>Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, 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

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>Mutagenesisi42K → C: No effect on subcellular localization. No effect on subcellular localization; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-44 and W-123. 1 Publication1
Mutagenesisi44R → C: No effect on subcellular localization. No effect on subcellular localization; when associated with C-42. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and W-123. 1 Publication1
Mutagenesisi123W → A: Disruption of membrane localization and impaired interaction with CK2. Loss of phospholipid binding; when associated with C-42. Loss of phospholipid binding; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and C-44. 1 Publication1
Mutagenesisi133R → A: No effect on binding to capping proteins and loss of phospholipid binding; when associated with A-135 and A-137. 1
Mutagenesisi133R → E: No effect on binding to capping proteins; when associated with E-135. 1
Mutagenesisi135K → A: No effect on binding to capping proteins; when associated with A-133 and A-137. 1
Mutagenesisi135K → E: No effect on binding to capping proteins; when associated with E-133. 1
Mutagenesisi137R → A: No effect on binding to capping proteins; when associated with A-133 and A-135. 1
Mutagenesisi155R → A: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-157. Great loss of binding to capping proteins; when associated with A-157 and A-159. 1 Publication1
Mutagenesisi155R → E: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-157. 1 Publication1
Mutagenesisi157R → A: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-155. Great loss of binding to capping proteins; when associated with A-155 and A-159. 1 Publication1
Mutagenesisi157R → E: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-155. 1 Publication1
Mutagenesisi159K → A: Great loss of binding to capping proteins; when associated with A-155 and A-157. 1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		51177

Open Targets

More...OpenTargetsi		ENSG00000023902

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA142671167

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PLEKHO1

Domain mapping of disease mutations (DMDM)

More...DMDMi		160419242

<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_00003104231 – 409Pleckstrin homology domain-containing family O member 1Add BLAST409

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 residuei227PhosphoserineBy similarity1
Modified residuei271PhosphoserineBy similarity1
Modified residuei342PhosphoserineBy 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

C-terminal fragments could be released during apoptosis via caspase-3-dependent cleavage.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei310 – 311Cleavage; by caspase-3Sequence analysis2
Sitei345 – 346Cleavage; by caspase-3Sequence analysis2

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q53GL0

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q53GL0

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q53GL0

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

More...PaxDbi		Q53GL0

PeptideAtlas

More...PeptideAtlasi		Q53GL0

PRoteomics IDEntifications database

More...PRIDEi		Q53GL0

ProteomicsDB human proteome resource

More...ProteomicsDBi		62483
62484 [Q53GL0-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q53GL0

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

More...PhosphoSitePlusi		Q53GL0

<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

Abundantly expressed in skeletal muscle and heart, moderately in kidney, liver, brain and placenta and sparingly in the pancreas and lung. Easily detectable in cell lines such as MOLT-4, HEK293 and Jurkat.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by IFNG/IFN-gamma and IL2/interleukin-2 or in C2C12 cells.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000023902 Expressed in 201 organ(s), highest expression level in lower esophagus muscularis layer

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q53GL0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q53GL0 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA061018

<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

Heterodimer or homodimer. Interacts with CK2 and actin capping subunits (capping protein CP-alpha and CP-beta). CKIP1 and CK2 together inhibit the activity of actin capping protein at the barbed ends of actin filaments. Interacts with ATM, IFP35, JUN, JUND, NMI and PI3K. Interacts with AKT1, AKT2 and AKT3 (each isozyme of PKB), PtdIns(3,5)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P2.10 Publications

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		119355, 62 interactors

Database of interacting proteins

More...DIPi		DIP-46903N

Protein interaction database and analysis system

More...IntActi		Q53GL0, 43 interactors

Molecular INTeraction database

More...MINTi		Q53GL0

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000358120

<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

1409
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

More...SMRi		Q53GL0

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q53GL0

<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>Domaini21 – 132PHPROSITE-ProRule annotationAdd BLAST112

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>Regioni133 – 193Interaction with capping proteins (CPs)Add BLAST61
Regioni136 – 308Interaction with ATM, CKIP, IFP35 and NMI2 PublicationsAdd BLAST173
Regioni308 – 409Negative regulator of AP-1 activityAdd BLAST102

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IEJU Eukaryota
ENOG4110ACW LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063760

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000115563

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q53GL0

Identification of Orthologs from Complete Genome Data

More...OMAi		EIWKNRF

Database of Orthologous Groups

More...OrthoDBi		929437at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q53GL0

TreeFam database of animal gene trees

More...TreeFami		TF333115

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028452 CKIP-1
IPR011993 PH-like_dom_sf
IPR001849 PH_domain

The PANTHER Classification System

More...PANTHERi		PTHR15871:SF1 PTHR15871:SF1, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00169 PH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00233 PH, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50003 PH_DOMAIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q53GL0-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MMKKNNSAKR GPQDGNQQPA PPEKVGWVRK FCGKGIFREI WKNRYVVLKG 
        60         70         80         90        100
DQLYISEKEV KDEKNIQEVF DLSDYEKCEE LRKSKSRSKK NHSKFTLAHS 
       110        120        130        140        150
KQPGNTAPNL IFLAVSPEEK ESWINALNSA ITRAKNRILD EVTVEEDSYL 
       160        170        180        190        200
AHPTRDRAKI QHSRRPPTRG HLMAVASTST SDGMLTLDLI QEEDPSPEEP 
       210        220        230        240        250
TSCAESFRVD LDKSVAQLAG SRRRADSDRI QPSADRASSL SRPWEKTDKG 
       260        270        280        290        300
ATYTPQAPKK LTPTEKGRCA SLEEILSQRD AASARTLQLR AEEPPTPALP 
       310        320        330        340        350
NPGQLSRIQD LVARKLEETQ ELLAEVQGLG DGKRKAKDPP RSPPDSESEQ 
       360        370        380        390        400
LLLETERLLG EASSNWSQAK RVLQEVRELR DLYRQMDLQT PDSHLRQTTP 

HSQYRKSLM
Length:409
Mass (Da):46,237
Last modified:November 13, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5077D6B559EB9F78
GO
Isoform 2 (identifier: Q53GL0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-175: Missing.

Note: No experimental confirmation available.
Show »
Length:375
Mass (Da):42,330
Checksum:i65CC4D44156031EA
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T4P9Q5T4P9_HUMAN
Pleckstrin homology domain containi...
PLEKHO1 hCG_39382, RP11-458I7.3-002
226Annotation 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 AAF13461 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAQ13826 differs from that shown. Reason: Erroneous initiation.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 conflicti1 – 10MMKKNNSAKR → VRRCCRGWRSPVFTNPHVSP LSTAPAHWAPGRPAAGSLGL RVSPEPPPERGSLPPGERSP AASKPPSSPS in AAH23533 (PubMed:15489334).Curated10
Sequence conflicti285R → H in BAD96641 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03703421P → A. Corresponds to variant dbSNP:rs2306235Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_029282142 – 175Missing in isoform 2. CuratedAdd BLAST34

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF168676 mRNA Translation: AAF89644.1
AF192912 mRNA Translation: AAQ13826.1 Different initiation.
AF291105 mRNA Translation: AAK28027.1
AF217956 mRNA Translation: AAK71509.1
AK222921 mRNA Translation: BAD96641.1
AL358073 Genomic DNA Translation: CAI14264.1
CH471121 Genomic DNA Translation: EAW53580.1
BC010149 mRNA Translation: AAH10149.1
BC023533 mRNA Translation: AAH23533.2
AF073836 mRNA Translation: AAF13461.1 Different initiation.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS945.1 [Q53GL0-1]

NCBI Reference Sequences

More...RefSeqi		NP_001291651.1, NM_001304722.1
NP_001291652.1, NM_001304723.1
NP_001291653.1, NM_001304724.1
NP_057358.2, NM_016274.5 [Q53GL0-1]
XP_016856909.1, XM_017001420.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000369124; ENSP00000358120; ENSG00000023902 [Q53GL0-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		51177

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:51177

UCSC genome browser

More...UCSCi		uc001ett.4 human [Q53GL0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168676 mRNA Translation: AAF89644.1
AF192912 mRNA Translation: AAQ13826.1 Different initiation.
AF291105 mRNA Translation: AAK28027.1
AF217956 mRNA Translation: AAK71509.1
AK222921 mRNA Translation: BAD96641.1
AL358073 Genomic DNA Translation: CAI14264.1
CH471121 Genomic DNA Translation: EAW53580.1
BC010149 mRNA Translation: AAH10149.1
BC023533 mRNA Translation: AAH23533.2
AF073836 mRNA Translation: AAF13461.1 Different initiation.
CCDSiCCDS945.1 [Q53GL0-1]
RefSeqiNP_001291651.1, NM_001304722.1
NP_001291652.1, NM_001304723.1
NP_001291653.1, NM_001304724.1
NP_057358.2, NM_016274.5 [Q53GL0-1]
XP_016856909.1, XM_017001420.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AA1X-ray1.90C148-170[»]
SMRiQ53GL0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119355, 62 interactors
DIPiDIP-46903N
IntActiQ53GL0, 43 interactors
MINTiQ53GL0
STRINGi9606.ENSP00000358120

PTM databases

iPTMnetiQ53GL0
PhosphoSitePlusiQ53GL0

Polymorphism and mutation databases

BioMutaiPLEKHO1
DMDMi160419242

Proteomic databases

EPDiQ53GL0
jPOSTiQ53GL0
MaxQBiQ53GL0
PaxDbiQ53GL0
PeptideAtlasiQ53GL0
PRIDEiQ53GL0
ProteomicsDBi62483
62484 [Q53GL0-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		51177
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369124; ENSP00000358120; ENSG00000023902 [Q53GL0-1]
GeneIDi51177
KEGGihsa:51177
UCSCiuc001ett.4 human [Q53GL0-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		51177
DisGeNETi51177

GeneCards: human genes, protein and diseases

More...GeneCardsi		PLEKHO1
HGNCiHGNC:24310 PLEKHO1
HPAiHPA061018
MIMi608335 gene
neXtProtiNX_Q53GL0
OpenTargetsiENSG00000023902
PharmGKBiPA142671167

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IEJU Eukaryota
ENOG4110ACW LUCA
GeneTreeiENSGT00530000063760
HOGENOMiHOG000115563
InParanoidiQ53GL0
OMAiEIWKNRF
OrthoDBi929437at2759
PhylomeDBiQ53GL0
TreeFamiTF333115

Miscellaneous databases

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

More...ChiTaRSi		PLEKHO1 human
EvolutionaryTraceiQ53GL0

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PLEKHO1

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

More...GenomeRNAii		51177

Protein Ontology

More...PROi		PR:Q53GL0

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000023902 Expressed in 201 organ(s), highest expression level in lower esophagus muscularis layer
ExpressionAtlasiQ53GL0 baseline and differential
GenevisibleiQ53GL0 HS

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR028452 CKIP-1
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
PANTHERiPTHR15871:SF1 PTHR15871:SF1, 1 hit
PfamiView protein in Pfam
PF00169 PH, 1 hit
SMARTiView protein in SMART
SM00233 PH, 1 hit
PROSITEiView protein in PROSITE
PS50003 PH_DOMAIN, 1 hit

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 nameiPKHO1_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: Q53GL0
Secondary accession number(s): Q336K5
, Q8IZ51, Q9NRV3, Q9UL48
<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: November 13, 2007
Last sequence update: November 13, 2007
Last modified: May 8, 2019
This is version 115 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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