SPTAN1 protein (Gallus gallus) - 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.

Node Color

colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

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.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

Your Input:

Neighborhood

Gene Fusion

Cooccurrence

Coexpression

Experiments

Databases

Textmining

[Homology]

Score

SPTAN1

Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization. (2497 aa)

Predicted Functional Partners:

SPTBN1

0.966

CASP3

0.932

SPTBN5

0.932

SPTBN4L

0.815

BDP1

0.724

SPTBN2

0.677

ENSGALP00000069115

0.670

LOC421441

0.656

ENSGALP00000061073

0.656

ENSGALP00000065294

0.656

Your Current Organism:

Gallus gallus

NCBI taxonomy Id: 9031
Other names: G. gallus, Gallus domesticus, Gallus gallus domesticus, bantam, chicken, chickens, dwarf Leghorn chickens, red junglefowl

Send network to Cytoscape

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

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

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
BDP1	SPTAN1	ENSGALP00000003837	ENSGALP00000066200	SANT domain-containing protein.	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	0.724
CASP3	SPTAN1	ENSGALP00000068843	ENSGALP00000066200	Caspase-3; Belongs to the peptidase C14A family.	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	0.932
ENSGALP00000061073	ENSGALP00000069115	ENSGALP00000061073	ENSGALP00000069115	PH_9 domain-containing protein.	Calponin-homology (CH) domain-containing protein.	0.899
ENSGALP00000061073	SPTAN1	ENSGALP00000061073	ENSGALP00000066200	PH_9 domain-containing protein.	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	0.656
ENSGALP00000061073	SPTBN4L	ENSGALP00000061073	ENSGALP00000066056	PH_9 domain-containing protein.	Calponin-homology (CH) domain-containing protein.	0.921
ENSGALP00000065294	SPTAN1	ENSGALP00000065294	ENSGALP00000066200	Uncharacterized protein.	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	0.656
ENSGALP00000065294	SPTBN2	ENSGALP00000065294	ENSGALP00000069859	Uncharacterized protein.	Uncharacterized protein.	0.735
ENSGALP00000065294	SPTBN4L	ENSGALP00000065294	ENSGALP00000066056	Uncharacterized protein.	Calponin-homology (CH) domain-containing protein.	0.726
ENSGALP00000069115	ENSGALP00000061073	ENSGALP00000069115	ENSGALP00000061073	Calponin-homology (CH) domain-containing protein.	PH_9 domain-containing protein.	0.899
ENSGALP00000069115	SPTAN1	ENSGALP00000069115	ENSGALP00000066200	Calponin-homology (CH) domain-containing protein.	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	0.670
ENSGALP00000069115	SPTBN2	ENSGALP00000069115	ENSGALP00000069859	Calponin-homology (CH) domain-containing protein.	Uncharacterized protein.	0.899
ENSGALP00000069115	SPTBN4L	ENSGALP00000069115	ENSGALP00000066056	Calponin-homology (CH) domain-containing protein.	Calponin-homology (CH) domain-containing protein.	0.884
LOC421441	SPTAN1	ENSGALP00000056703	ENSGALP00000066200	PH domain-containing protein.	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	0.656
SPTAN1	BDP1	ENSGALP00000066200	ENSGALP00000003837	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	SANT domain-containing protein.	0.724
SPTAN1	CASP3	ENSGALP00000066200	ENSGALP00000068843	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	Caspase-3; Belongs to the peptidase C14A family.	0.932
SPTAN1	ENSGALP00000061073	ENSGALP00000066200	ENSGALP00000061073	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	PH_9 domain-containing protein.	0.656
SPTAN1	ENSGALP00000065294	ENSGALP00000066200	ENSGALP00000065294	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	Uncharacterized protein.	0.656
SPTAN1	ENSGALP00000069115	ENSGALP00000066200	ENSGALP00000069115	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	Calponin-homology (CH) domain-containing protein.	0.670
SPTAN1	LOC421441	ENSGALP00000066200	ENSGALP00000056703	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	PH domain-containing protein.	0.656
SPTAN1	SPTBN1	ENSGALP00000066200	ENSGALP00000053130	Spectrin alpha chain, non-erythrocytic 1; Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.	Spectrin beta chain; Belongs to the spectrin family.	0.966

page 1 of 2

Server load: low (30%) [HD]

Permalink

Network

Fusion

Experiments

Cooccurrence

Databases

Coexpression

Textmining

Neighborhood

© STRING Consortium 2023

Credits

Access

Info

About