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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-Experimental evidence at protein leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551Capping protein
Binding sitei157 – 1571Capping protein

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

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
Gene namesi
Name:PLEKHO1
Synonyms:CKIP1, OC120
ORF Names:HQ0024c
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24310. PLEKHO1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → 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 Publication
Mutagenesisi44 – 441R → 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 Publication
Mutagenesisi123 – 1231W → 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 Publication
Mutagenesisi133 – 1331R → A: No effect on binding to capping proteins and loss of phospholipid binding; when associated with A-135 and A-137.
Mutagenesisi133 – 1331R → E: No effect on binding to capping proteins; when associated with E-135.
Mutagenesisi135 – 1351K → A: No effect on binding to capping proteins; when associated with A-133 and A-137.
Mutagenesisi135 – 1351K → E: No effect on binding to capping proteins; when associated with E-133.
Mutagenesisi137 – 1371R → A: No effect on binding to capping proteins; when associated with A-133 and A-135.
Mutagenesisi155 – 1551R → 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 Publication
Mutagenesisi155 – 1551R → 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 Publication
Mutagenesisi157 – 1571R → 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 Publication
Mutagenesisi157 – 1571R → 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 Publication
Mutagenesisi159 – 1591K → A: Great loss of binding to capping proteins; when associated with A-155 and A-157.

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA142671167.

Polymorphism and mutation databases

BioMutaiPLEKHO1.
DMDMi160419242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Pleckstrin homology domain-containing family O member 1PRO_0000310423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271PhosphoserineBy similarity
Modified residuei271 – 2711PhosphoserineBy similarity
Modified residuei342 – 3421PhosphoserineBy similarity

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei310 – 3112Cleavage; by caspase-3Sequence analysis
Sitei345 – 3462Cleavage; by caspase-3Sequence analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ53GL0.
MaxQBiQ53GL0.
PaxDbiQ53GL0.
PeptideAtlasiQ53GL0.
PRIDEiQ53GL0.

PTM databases

iPTMnetiQ53GL0.
PhosphoSiteiQ53GL0.

Expressioni

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

Inductioni

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

Gene expression databases

BgeeiENSG00000023902.
CleanExiHS_PLEKHO1.
ExpressionAtlasiQ53GL0. baseline and differential.
GenevisibleiQ53GL0. HS.

Organism-specific databases

HPAiHPA061018.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMC5P6219510EBI-949945,EBI-357745
SMURF1Q9HCE72EBI-949945,EBI-976466
SMURF1Q9HCE7-24EBI-949945,EBI-9845742

Protein-protein interaction databases

BioGridi119355. 53 interactions.
DIPiDIP-46903N.
IntActiQ53GL0. 22 interactions.
MINTiMINT-2872992.
STRINGi9606.ENSP00000358120.

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi153 – 1553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AA1X-ray1.90C148-170[»]
ProteinModelPortaliQ53GL0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53GL0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 132112PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 19361Interaction with capping proteins (CPs)Add
BLAST
Regioni136 – 308173Interaction with ATM, CKIP, IFP35 and NMIAdd
BLAST
Regioni308 – 409102Negative regulator of AP-1 activityAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IEJU. Eukaryota.
ENOG4110ACW. LUCA.
GeneTreeiENSGT00530000063760.
HOGENOMiHOG000115563.
HOVERGENiHBG108259.
InParanoidiQ53GL0.
OMAiKRGPQDG.
OrthoDBiEOG091G0CAS.
PhylomeDBiQ53GL0.
TreeFamiTF333115.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR028452. CKIP-1.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR15871:SF1. PTHR15871:SF1. 1 hit.
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1010MMKKNNSAKR → VRRCCRGWRSPVFTNPHVSP LSTAPAHWAPGRPAAGSLGL RVSPEPPPERGSLPPGERSP AASKPPSSPS in AAH23533 (PubMed:15489334).Curated
Sequence conflicti285 – 2851R → H in BAD96641 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211P → A.
Corresponds to variant rs2306235 [ dbSNP | Ensembl ].
VAR_037034

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 17534Missing in isoform 2. CuratedVSP_029282Add
BLAST

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]
UniGeneiHs.438824.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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]
UniGeneiHs.438824.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AA1X-ray1.90C148-170[»]
ProteinModelPortaliQ53GL0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119355. 53 interactions.
DIPiDIP-46903N.
IntActiQ53GL0. 22 interactions.
MINTiMINT-2872992.
STRINGi9606.ENSP00000358120.

PTM databases

iPTMnetiQ53GL0.
PhosphoSiteiQ53GL0.

Polymorphism and mutation databases

BioMutaiPLEKHO1.
DMDMi160419242.

Proteomic databases

EPDiQ53GL0.
MaxQBiQ53GL0.
PaxDbiQ53GL0.
PeptideAtlasiQ53GL0.
PRIDEiQ53GL0.

Protocols and materials databases

DNASUi51177.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51177.
GeneCardsiPLEKHO1.
HGNCiHGNC:24310. PLEKHO1.
HPAiHPA061018.
MIMi608335. gene.
neXtProtiNX_Q53GL0.
PharmGKBiPA142671167.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEJU. Eukaryota.
ENOG4110ACW. LUCA.
GeneTreeiENSGT00530000063760.
HOGENOMiHOG000115563.
HOVERGENiHBG108259.
InParanoidiQ53GL0.
OMAiKRGPQDG.
OrthoDBiEOG091G0CAS.
PhylomeDBiQ53GL0.
TreeFamiTF333115.

Miscellaneous databases

ChiTaRSiPLEKHO1. human.
EvolutionaryTraceiQ53GL0.
GeneWikiiPLEKHO1.
GenomeRNAii51177.
PROiQ53GL0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000023902.
CleanExiHS_PLEKHO1.
ExpressionAtlasiQ53GL0. baseline and differential.
GenevisibleiQ53GL0. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR028452. CKIP-1.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR15871:SF1. PTHR15871:SF1. 1 hit.
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPKHO1_HUMAN
AccessioniPrimary (citable) accession number: Q53GL0
Secondary accession number(s): Q336K5
, Q8IZ51, Q9NRV3, Q9UL48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: September 7, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.