PLEKHO2 protein (human) - STRING interaction network

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[Homology]

Score

PLEKHO2

Pleckstrin homology domain containing O2. (490 aa)

Predicted Functional Partners:

CAPZB

0.989

CAPZA1

0.975

FAM184A

0.666

TACC3

0.651

CAPZA2

0.641

MAP3K6

0.633

VEZT

0.614

FLAD1

0.580

THEMIS2

0.562

CENPJ

0.539

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CAPZA1	CAPZA2	ENSP00000263168	ENSP00000354947	F-actin-capping protein subunit alpha-1; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.	F-actin-capping protein subunit alpha-2; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	0.999
CAPZA1	CAPZB	ENSP00000263168	ENSP00000401010	F-actin-capping protein subunit alpha-1; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.	F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.	0.999
CAPZA1	PLEKHO2	ENSP00000263168	ENSP00000326706	F-actin-capping protein subunit alpha-1; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.	Pleckstrin homology domain containing O2.	0.975
CAPZA2	CAPZA1	ENSP00000354947	ENSP00000263168	F-actin-capping protein subunit alpha-2; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	F-actin-capping protein subunit alpha-1; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.	0.999
CAPZA2	CAPZB	ENSP00000354947	ENSP00000401010	F-actin-capping protein subunit alpha-2; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.	0.999
CAPZA2	PLEKHO2	ENSP00000354947	ENSP00000326706	F-actin-capping protein subunit alpha-2; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	Pleckstrin homology domain containing O2.	0.641
CAPZB	CAPZA1	ENSP00000401010	ENSP00000263168	F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.	F-actin-capping protein subunit alpha-1; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.	0.999
CAPZB	CAPZA2	ENSP00000401010	ENSP00000354947	F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.	F-actin-capping protein subunit alpha-2; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	0.999
CAPZB	PLEKHO2	ENSP00000401010	ENSP00000326706	F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.	Pleckstrin homology domain containing O2.	0.989
CENPJ	PLEKHO2	ENSP00000371308	ENSP00000326706	Centromere protein J; Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome. Involved in the regulation of slow processive growth of centriolar microtubules. Acts as microtubule plus-end tracking protein that stabilizes centriolar microtubules and inhibits microtubule polymerization and extension from the distal ends of centrioles. Required for centriole elongation and for STIL-mediated centriole amplification. Required for the recruitment of CEP295 to the proximal end of new-born [...]	Pleckstrin homology domain containing O2.	0.539
FAM184A	PLEKHO2	ENSP00000342604	ENSP00000326706	Protein FAM184A; Family with sequence similarity 184 member A.	Pleckstrin homology domain containing O2.	0.666
FLAD1	PLEKHO2	ENSP00000292180	ENSP00000326706	Molybdenum cofactor biosynthesis protein-like region; Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.	Pleckstrin homology domain containing O2.	0.580
MAP3K6	PLEKHO2	ENSP00000350195	ENSP00000326706	Mitogen-activated protein kinase kinase kinase 6; Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways.	Pleckstrin homology domain containing O2.	0.633
PLEKHO2	CAPZA1	ENSP00000326706	ENSP00000263168	Pleckstrin homology domain containing O2.	F-actin-capping protein subunit alpha-1; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.	0.975
PLEKHO2	CAPZA2	ENSP00000326706	ENSP00000354947	Pleckstrin homology domain containing O2.	F-actin-capping protein subunit alpha-2; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	0.641
PLEKHO2	CAPZB	ENSP00000326706	ENSP00000401010	Pleckstrin homology domain containing O2.	F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.	0.989
PLEKHO2	CENPJ	ENSP00000326706	ENSP00000371308	Pleckstrin homology domain containing O2.	Centromere protein J; Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome. Involved in the regulation of slow processive growth of centriolar microtubules. Acts as microtubule plus-end tracking protein that stabilizes centriolar microtubules and inhibits microtubule polymerization and extension from the distal ends of centrioles. Required for centriole elongation and for STIL-mediated centriole amplification. Required for the recruitment of CEP295 to the proximal end of new-born [...]	0.539
PLEKHO2	FAM184A	ENSP00000326706	ENSP00000342604	Pleckstrin homology domain containing O2.	Protein FAM184A; Family with sequence similarity 184 member A.	0.666
PLEKHO2	FLAD1	ENSP00000326706	ENSP00000292180	Pleckstrin homology domain containing O2.	Molybdenum cofactor biosynthesis protein-like region; Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.	0.580
PLEKHO2	MAP3K6	ENSP00000326706	ENSP00000350195	Pleckstrin homology domain containing O2.	Mitogen-activated protein kinase kinase kinase 6; Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways.	0.633