ARAP1 protein (Pongo abelii) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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query proteins and first shell of interactors

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second shell of interactors

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proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

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Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Knowledge-based Evidence

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Assay-based Predictions

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co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

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Your Current Organism:

Pongo abelii

NCBI taxonomy Id: 9601
Other names: Orang-utan, Orangutan, P. abelii, Pongo pygmaeus abeli, Pongo pygmaeus abelii, Sumatran orangutan, orang utan

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a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ARAP1	CAPZA2	ENSPPYP00000004176	ENSPPYP00000020107	ARAP1 isoform 1.	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 (By similarity).	0.721
ARAP1	CAPZB	ENSPPYP00000004176	ENSPPYP00000002072	ARAP1 isoform 1.	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 (By similarity).	0.716
ARAP1	CDC42	ENSPPYP00000004176	ENSPPYP00000002031	ARAP1 isoform 1.	Cell division cycle 42.	0.583
ARAP1	CRK	ENSPPYP00000004176	ENSPPYP00000008754	ARAP1 isoform 1.	CRK isoform 1.	0.544
ARAP1	FYN	ENSPPYP00000004176	ENSPPYP00000018952	ARAP1 isoform 1.	Tyrosine-protein kinase.	0.572
ARAP1	GRB2	ENSPPYP00000004176	ENSPPYP00000009686	ARAP1 isoform 1.	Growth factor receptor-bound protein 2; Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway. Belongs to the GRB2/sem-5/DRK family.	0.810
ARAP1	PDE2A	ENSPPYP00000004176	ENSPPYP00000004175	ARAP1 isoform 1.	Phosphodiesterase.	0.532
ARAP1	PTK6	ENSPPYP00000004176	ENSPPYP00000012555	ARAP1 isoform 1.	Tyrosine-protein kinase.	0.839
ARAP1	SH3KBP1	ENSPPYP00000004176	ENSPPYP00000022571	ARAP1 isoform 1.	SH3KBP1 isoform 1.	0.925
ARAP1	SRMS	ENSPPYP00000004176	ENSPPYP00000012556	ARAP1 isoform 1.	Tyrosine-protein kinase.	0.572
CAPZA2	ARAP1	ENSPPYP00000020107	ENSPPYP00000004176	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 (By similarity).	ARAP1 isoform 1.	0.721
CAPZA2	CAPZB	ENSPPYP00000020107	ENSPPYP00000002072	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 (By similarity).	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 (By similarity).	0.999
CAPZA2	CDC42	ENSPPYP00000020107	ENSPPYP00000002031	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 (By similarity).	Cell division cycle 42.	0.422
CAPZA2	SH3KBP1	ENSPPYP00000020107	ENSPPYP00000022571	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 (By similarity).	SH3KBP1 isoform 1.	0.824
CAPZB	ARAP1	ENSPPYP00000002072	ENSPPYP00000004176	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 (By similarity).	ARAP1 isoform 1.	0.716
CAPZB	CAPZA2	ENSPPYP00000002072	ENSPPYP00000020107	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 (By similarity).	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 (By similarity).	0.999
CAPZB	CDC42	ENSPPYP00000002072	ENSPPYP00000002031	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 (By similarity).	Cell division cycle 42.	0.457
CAPZB	SH3KBP1	ENSPPYP00000002072	ENSPPYP00000022571	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 (By similarity).	SH3KBP1 isoform 1.	0.817
CDC42	ARAP1	ENSPPYP00000002031	ENSPPYP00000004176	Cell division cycle 42.	ARAP1 isoform 1.	0.583
CDC42	CAPZA2	ENSPPYP00000002031	ENSPPYP00000020107	Cell division cycle 42.	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 (By similarity).	0.422