cbwd1 protein (Anolis carolinensis) - 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.

Knowledge-based Evidence

from curated databases

textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Input:

Neighborhood

Gene fusion

Co-occurrence

Co-expression

Experiments

Databases

Textmining

[Homology]

Score

cbwd1

Uncharacterized protein. (386 aa)

Predicted Functional Partners:

METAP1

0.919

fam72a

0.877

RSAD1

0.658

MRPS14

0.655

TCERG1

0.649

NUP42

0.568

pa2g4

0.540

METAP2

0.540

G1KIT6_ANOCA

0.535

mamdc4

0.535

Your Current Organism:

Anolis carolinensis

NCBI taxonomy Id: 28377
Other names: A. carolinensis, Carolina anole, UCMZ 53793, green anole

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 proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
G1KIT6_ANOCA	cbwd1	ENSACAP00000009169	ENSACAP00000001807	Uncharacterized protein.	Uncharacterized protein.	0.535
G1KIT6_ANOCA	mamdc4	ENSACAP00000009169	ENSACAP00000021155	Uncharacterized protein.	Uncharacterized protein.	0.897
METAP1	METAP2	ENSACAP00000014015	ENSACAP00000013935	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	0.982
METAP1	MRPS14	ENSACAP00000014015	ENSACAP00000019554	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	Mitochondrial ribosomal protein S14.	0.702
METAP1	RSAD1	ENSACAP00000014015	ENSACAP00000005051	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	0.714
METAP1	cbwd1	ENSACAP00000014015	ENSACAP00000001807	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	Uncharacterized protein.	0.919
METAP2	METAP1	ENSACAP00000013935	ENSACAP00000014015	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.982
METAP2	MRPS14	ENSACAP00000013935	ENSACAP00000019554	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	Mitochondrial ribosomal protein S14.	0.702
METAP2	RSAD1	ENSACAP00000013935	ENSACAP00000005051	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	0.702
METAP2	cbwd1	ENSACAP00000013935	ENSACAP00000001807	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	Uncharacterized protein.	0.540
MRPS14	METAP1	ENSACAP00000019554	ENSACAP00000014015	Mitochondrial ribosomal protein S14.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.702
MRPS14	METAP2	ENSACAP00000019554	ENSACAP00000013935	Mitochondrial ribosomal protein S14.	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	0.702
MRPS14	cbwd1	ENSACAP00000019554	ENSACAP00000001807	Mitochondrial ribosomal protein S14.	Uncharacterized protein.	0.655
MRPS14	pa2g4	ENSACAP00000019554	ENSACAP00000004955	Mitochondrial ribosomal protein S14.	Peptidase_M24 domain-containing protein.	0.702
NUP42	cbwd1	ENSACAP00000013474	ENSACAP00000001807	Nucleoporin 42.	Uncharacterized protein.	0.568
RSAD1	METAP1	ENSACAP00000005051	ENSACAP00000014015	Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val).	0.714
RSAD1	METAP2	ENSACAP00000005051	ENSACAP00000013935	Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.	0.702
RSAD1	cbwd1	ENSACAP00000005051	ENSACAP00000001807	Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	Uncharacterized protein.	0.658
RSAD1	pa2g4	ENSACAP00000005051	ENSACAP00000004955	Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	Peptidase_M24 domain-containing protein.	0.735
TCERG1	cbwd1	ENSACAP00000013971	ENSACAP00000001807	Transcription elongation regulator 1.	Uncharacterized protein.	0.649