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Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) (C-Jun-binding protein) (JBP) (Casein kinase 2-interacting protein 1) (CK2-interacting protein 1) (CKIP-1) (Osteoclast maturation-associated gene 120 protein)

 PKHO1_HUMAN             Reviewed;         409 AA.
Q53GL0; Q336K5; Q8IZ51; Q9NRV3; Q9UL48;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
28-MAR-2018, entry version 108.
RecName: Full=Pleckstrin homology domain-containing family O member 1;
Short=PH domain-containing family O member 1;
AltName: Full=C-Jun-binding protein;
Short=JBP;
AltName: Full=Casein kinase 2-interacting protein 1;
Short=CK2-interacting protein 1;
Short=CKIP-1;
AltName: Full=Osteoclast maturation-associated gene 120 protein;
Name=PLEKHO1; Synonyms=CKIP1, OC120; ORFNames=HQ0024c;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymph node;
Kohchi C.;
"Identification of a protein that associates with TNF intracellular
domain.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yamane S., Toyosaki-Maeda T., Tsuruta Y., Suzuki R., Ochi T.;
"Differential screening of human osteoclast maturation associated
genes.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INTERACTION WITH CK2.
PubMed=10799509; DOI=10.1074/jbc.275.19.14295;
Bosc D.G., Graham K.C., Saulnier R.B., Zhang C., Prober D.,
Gietz R.D., Litchfield D.W.;
"Identification and characterization of CKIP-1, a novel pleckstrin
homology domain-containing protein that interacts with protein kinase
CK2.";
J. Biol. Chem. 275:14295-14306(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH JUN
AND JUND, CLEAVAGE BY CASPASE-3, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=15706351; DOI=10.1038/sj.emboj.7600532;
Zhang L., Xing G., Tie Y., Tang Y., Tian C., Li L., Sun L., Wei H.,
Zhu Y., He F.;
"Role for the pleckstrin homology domain-containing protein CKIP-1 in
AP-1 regulation and apoptosis.";
EMBO J. 24:766-778(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-409.
TISSUE=Fetal liver;
PubMed=11483580; DOI=10.1101/gr.175501;
Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C.,
Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C.,
He F.;
"Gene expression profiling in human fetal liver and identification of
tissue- and developmental-stage-specific genes through compiled
expression profiles and efficient cloning of full-length cDNAs.";
Genome Res. 11:1392-1403(2001).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH CK2.
PubMed=11827170; DOI=10.1023/A:1013188101465;
Litchfield D.W., Bosc D.G., Canton D.A., Saulnier R.B., Vilk G.,
Zhang C.;
"Functional specialization of CK2 isoforms and characterization of
isoform-specific binding partners.";
Mol. Cell. Biochem. 227:21-29(2001).
[11]
SUBCELLULAR LOCATION, INTERACTION WITH CK2, AND MUTAGENESIS OF LYS-42;
ARG-44 AND TRP-123.
PubMed=15254037; DOI=10.1074/jbc.M407628200;
Olsten M.E.K., Canton D.A., Zhang C., Walton P.A., Litchfield D.W.;
"The pleckstrin homology domain of CK2 interacting protein-1 is
required for interactions and recruitment of protein kinase CK2 to the
plasma membrane.";
J. Biol. Chem. 279:42114-42127(2004).
[12]
FUNCTION, INTERACTION WITH PHOSPHATIDYL INOSITOL 3-KINASE, SUBCELLULAR
LOCATION, AND INDUCTION.
PubMed=14729969; DOI=10.1128/MCB.24.3.1245-1255.2004;
Safi A., Vandromme M., Caussanel S., Valdacci L., Baas D., Vidal M.,
Brun G., Schaeffer L., Goillot E.;
"Role for the pleckstrin homology domain-containing protein CKIP-1 in
phosphatidylinositol 3-kinase-regulated muscle differentiation.";
Mol. Cell. Biol. 24:1245-1255(2004).
[13]
FUNCTION, INTERACTION WITH CK2 AND ACTIN CAPPING PROTEINS, SUBCELLULAR
LOCATION, AND SUBUNIT.
PubMed=15831458; DOI=10.1128/MCB.25.9.3519-3534.2005;
Canton D.A., Olsten M.E.K., Kim K., Doherty-Kirby A., Lajoie G.,
Cooper J.A., Litchfield D.W.;
"The pleckstrin homology domain-containing protein CKIP-1 is involved
in regulation of cell morphology and the actin cytoskeleton and
interaction with actin capping protein.";
Mol. Cell. Biol. 25:3519-3534(2005).
[14]
FUNCTION, INTERACTION WITH ATM, AND SUBCELLULAR LOCATION.
PubMed=16325375; DOI=10.1016/j.cellsig.2005.10.017;
Zhang L., Tie Y., Tian C., Xing G., Song Y., Zhu Y., Sun Z., He F.;
"CKIP-1 recruits nuclear ATM partially to the plasma membrane through
interaction with ATM.";
Cell. Signal. 18:1386-1395(2006).
[15]
FUNCTION, INTERACTION WITH ACTIN CAPPING PROTEINS, AND MUTAGENESIS OF
ARG-155 AND ARG-157.
PubMed=16987810; DOI=10.1074/jbc.M607595200;
Canton D.A., Olsten M.E.K., Niederstrasser H., Cooper J.A.,
Litchfield D.W.;
"The role of CKIP-1 in cell morphology depends on its interaction with
actin-capping protein.";
J. Biol. Chem. 281:36347-36359(2006).
[16]
FUNCTION, AND INTERACTION WITH PKB; PTDINS(3,5)P2; PTDINS(4,5)P2 AND
PTDINS(3,4,5)P2.
PubMed=17942896; DOI=10.1158/0008-5472.CAN-07-1050;
Tokuda E., Fujita N., Oh-hara T., Sato S., Kurata A., Katayama R.,
Itoh T., Takenawa T., Miyazono K., Tsuruo T.;
"Casein kinase 2-interacting protein-1, a novel Akt pleckstrin
homology domain-interacting protein, down-regulates PI3K/Akt signaling
and suppresses tumor growth in vivo.";
Cancer Res. 67:9666-9676(2007).
[17]
FUNCTION, INTERACTION WITH IFP35 AND NMI, INDUCTION BY IL2 AND IFNG,
TISSUE SPECIFICITY, AND SUBUNIT.
PubMed=17197158; DOI=10.1016/j.cellsig.2006.11.002;
Zhang L., Tang Y., Tie Y., Tian C., Wang J., Dong Y., Sun Z., He F.;
"The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is
involved in cytokine signaling.";
Cell. Signal. 19:932-944(2007).
-!- FUNCTION: 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. {ECO:0000269|PubMed:14729969,
ECO:0000269|PubMed:15706351, ECO:0000269|PubMed:15831458,
ECO:0000269|PubMed:16325375, ECO:0000269|PubMed:16987810,
ECO:0000269|PubMed:17197158, ECO:0000269|PubMed:17942896}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170,
ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15254037,
ECO:0000269|PubMed:15706351, ECO:0000269|PubMed:15831458,
ECO:0000269|PubMed:16325375, ECO:0000269|PubMed:16987810,
ECO:0000269|PubMed:17197158, ECO:0000269|PubMed:17942896}.
-!- INTERACTION:
P62195:PSMC5; NbExp=10; IntAct=EBI-949945, EBI-357745;
Q9HCE7:SMURF1; NbExp=2; IntAct=EBI-949945, EBI-976466;
Q9HCE7-2:SMURF1; NbExp=4; IntAct=EBI-949945, EBI-9845742;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10799509,
ECO:0000269|PubMed:11827170, ECO:0000269|PubMed:14729969,
ECO:0000269|PubMed:15254037, ECO:0000269|PubMed:16325375};
Peripheral membrane protein {ECO:0000305|PubMed:14729969}. Nucleus
{ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170,
ECO:0000269|PubMed:15706351}. Cytoplasm
{ECO:0000269|PubMed:15706351}. Note=Predominantly localized to the
plasma membrane through the binding to phosphatidylinositol 3-
phosphate (PubMed:14729969). In C2C12 cells, with the absence of
growth factor, it is found in the nucleus (PubMed:14729969). It
rapidly translocates to the plasma membrane after insulin
stimulation (PubMed:14729969). In response to TNF, it translocates
from the plasma membrane to the cytoplasm and then to the nucleus
accompanied by cleavage by caspase-3 (PubMed:15706351). However,
the subcellular location is highly dependent of the cell type, and
this explains why it is found exclusively at the plasma membrane,
in some type of cells (Probable). {ECO:0000269|PubMed:14729969,
ECO:0000269|PubMed:15706351, ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q53GL0-1; Sequence=Displayed;
Name=2;
IsoId=Q53GL0-2; Sequence=VSP_029282;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:17197158}.
-!- INDUCTION: Up-regulated by IFNG/IFN-gamma and IL2/interleukin-2 or
in C2C12 cells. {ECO:0000269|PubMed:14729969,
ECO:0000269|PubMed:17197158}.
-!- PTM: C-terminal fragments could be released during apoptosis via
caspase-3-dependent cleavage. {ECO:0000269|PubMed:15706351}.
-!- SEQUENCE CAUTION:
Sequence=AAF13461.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAQ13826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF168676; AAF89644.1; -; mRNA.
EMBL; AF192912; AAQ13826.1; ALT_INIT; mRNA.
EMBL; AF291105; AAK28027.1; -; mRNA.
EMBL; AF217956; AAK71509.1; -; mRNA.
EMBL; AK222921; BAD96641.1; -; mRNA.
EMBL; AL358073; CAI14264.1; -; Genomic_DNA.
EMBL; CH471121; EAW53580.1; -; Genomic_DNA.
EMBL; BC010149; AAH10149.1; -; mRNA.
EMBL; BC023533; AAH23533.2; -; mRNA.
EMBL; AF073836; AAF13461.1; ALT_INIT; mRNA.
CCDS; CCDS945.1; -. [Q53GL0-1]
RefSeq; NP_001291651.1; NM_001304722.1.
RefSeq; NP_001291652.1; NM_001304723.1.
RefSeq; NP_001291653.1; NM_001304724.1.
RefSeq; NP_057358.2; NM_016274.5. [Q53GL0-1]
RefSeq; XP_016856909.1; XM_017001420.1.
UniGene; Hs.438824; -.
PDB; 3AA1; X-ray; 1.90 A; C=148-170.
PDBsum; 3AA1; -.
ProteinModelPortal; Q53GL0; -.
SMR; Q53GL0; -.
BioGrid; 119355; 62.
DIP; DIP-46903N; -.
IntAct; Q53GL0; 23.
MINT; Q53GL0; -.
STRING; 9606.ENSP00000358120; -.
iPTMnet; Q53GL0; -.
PhosphoSitePlus; Q53GL0; -.
BioMuta; PLEKHO1; -.
DMDM; 160419242; -.
EPD; Q53GL0; -.
MaxQB; Q53GL0; -.
PaxDb; Q53GL0; -.
PeptideAtlas; Q53GL0; -.
PRIDE; Q53GL0; -.
DNASU; 51177; -.
Ensembl; ENST00000369124; ENSP00000358120; ENSG00000023902. [Q53GL0-1]
GeneID; 51177; -.
KEGG; hsa:51177; -.
UCSC; uc001ett.4; human. [Q53GL0-1]
CTD; 51177; -.
DisGeNET; 51177; -.
EuPathDB; HostDB:ENSG00000023902.13; -.
GeneCards; PLEKHO1; -.
HGNC; HGNC:24310; PLEKHO1.
HPA; HPA061018; -.
MIM; 608335; gene.
neXtProt; NX_Q53GL0; -.
OpenTargets; ENSG00000023902; -.
PharmGKB; PA142671167; -.
eggNOG; ENOG410IEJU; Eukaryota.
eggNOG; ENOG4110ACW; LUCA.
GeneTree; ENSGT00530000063760; -.
HOGENOM; HOG000115563; -.
HOVERGEN; HBG108259; -.
InParanoid; Q53GL0; -.
OMA; IFREIWK; -.
OrthoDB; EOG091G0CAS; -.
PhylomeDB; Q53GL0; -.
TreeFam; TF333115; -.
ChiTaRS; PLEKHO1; human.
EvolutionaryTrace; Q53GL0; -.
GeneWiki; PLEKHO1; -.
GenomeRNAi; 51177; -.
PRO; PR:Q53GL0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000023902; -.
CleanEx; HS_PLEKHO1; -.
ExpressionAtlas; Q53GL0; baseline and differential.
Genevisible; Q53GL0; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0036195; C:muscle cell projection membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
GO; GO:0051451; P:myoblast migration; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR028452; CKIP-1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR15871:SF1; PTHR15871:SF1; 1.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Tumor suppressor.
CHAIN 1 409 Pleckstrin homology domain-containing
family O member 1.
/FTId=PRO_0000310423.
DOMAIN 21 132 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 133 193 Interaction with capping proteins (CPs).
REGION 136 308 Interaction with ATM, CKIP, IFP35 and
NMI. {ECO:0000269|PubMed:16325375,
ECO:0000269|PubMed:17197158}.
REGION 308 409 Negative regulator of AP-1 activity.
BINDING 155 155 Capping protein.
BINDING 157 157 Capping protein.
SITE 310 311 Cleavage; by caspase-3. {ECO:0000255}.
SITE 345 346 Cleavage; by caspase-3. {ECO:0000255}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JIY0}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JIY0}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BJM5}.
VAR_SEQ 142 175 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_029282.
VARIANT 21 21 P -> A (in dbSNP:rs2306235).
/FTId=VAR_037034.
MUTAGEN 42 42 K->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.
{ECO:0000269|PubMed:15254037}.
MUTAGEN 44 44 R->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.
{ECO:0000269|PubMed:15254037}.
MUTAGEN 123 123 W->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.
{ECO:0000269|PubMed:15254037}.
MUTAGEN 133 133 R->A: No effect on binding to capping
proteins and loss of phospholipid
binding; when associated with A-135 and
A-137.
MUTAGEN 133 133 R->E: No effect on binding to capping
proteins; when associated with E-135.
MUTAGEN 135 135 K->A: No effect on binding to capping
proteins; when associated with A-133 and
A-137.
MUTAGEN 135 135 K->E: No effect on binding to capping
proteins; when associated with E-133.
MUTAGEN 137 137 R->A: No effect on binding to capping
proteins; when associated with A-133 and
A-135.
MUTAGEN 155 155 R->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. {ECO:0000269|PubMed:16987810}.
MUTAGEN 155 155 R->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.
{ECO:0000269|PubMed:16987810}.
MUTAGEN 157 157 R->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. {ECO:0000269|PubMed:16987810}.
MUTAGEN 157 157 R->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.
{ECO:0000269|PubMed:16987810}.
MUTAGEN 159 159 K->A: Great loss of binding to capping
proteins; when associated with A-155 and
A-157.
CONFLICT 1 10 MMKKNNSAKR -> VRRCCRGWRSPVFTNPHVSPLSTAPAH
WAPGRPAAGSLGLRVSPEPPPERGSLPPGERSPAASKPPSS
PS (in Ref. 8; AAH23533). {ECO:0000305}.
CONFLICT 285 285 R -> H (in Ref. 5; BAD96641).
{ECO:0000305}.
HELIX 153 155 {ECO:0000244|PDB:3AA1}.
SEQUENCE 409 AA; 46237 MW; 5077D6B559EB9F78 CRC64;
MMKKNNSAKR GPQDGNQQPA PPEKVGWVRK FCGKGIFREI WKNRYVVLKG DQLYISEKEV
KDEKNIQEVF DLSDYEKCEE LRKSKSRSKK NHSKFTLAHS KQPGNTAPNL IFLAVSPEEK
ESWINALNSA ITRAKNRILD EVTVEEDSYL AHPTRDRAKI QHSRRPPTRG HLMAVASTST
SDGMLTLDLI QEEDPSPEEP TSCAESFRVD LDKSVAQLAG SRRRADSDRI QPSADRASSL
SRPWEKTDKG ATYTPQAPKK LTPTEKGRCA SLEEILSQRD AASARTLQLR AEEPPTPALP
NPGQLSRIQD LVARKLEETQ ELLAEVQGLG DGKRKAKDPP RSPPDSESEQ LLLETERLLG
EASSNWSQAK RVLQEVRELR DLYRQMDLQT PDSHLRQTTP HSQYRKSLM


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