DCAR_005465 protein (Daucus carota) - 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

DCAR_005465

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). (389 aa)

Predicted Functional Partners:

DCAR_023951

0.963

DCAR_024228

0.901

EIF6

0.872

DCAR_008547

0.868

DCAR_030077

0.868

DCAR_012725

0.858

DCAR_000378

0.858

DCAR_025822

0.851

DCAR_017890

0.851

DCAR_014576

0.841

Your Current Organism:

Daucus carota

NCBI taxonomy Id: 79200
Other names: D. carota subsp. sativus, Daucus carota subsp. sativus, Daucus carota subsp. sativus (Hoffm.) Arcang., Daucus carota var. sativus

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
DCAR_000378	DCAR_005465	A0A175Y907	A0A166D1Q5	KOW domain-containing protein.	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).	0.858
DCAR_000378	DCAR_008547	A0A175Y907	A0A166FF60	KOW domain-containing protein.	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).	0.858
DCAR_000378	DCAR_014576	A0A175Y907	A0A162A9I5	KOW domain-containing protein.	Uncharacterized protein.	0.998
DCAR_000378	DCAR_017890	A0A175Y907	A0A164YKE7	KOW domain-containing protein.	Ribosomal_L23eN domain-containing protein; Belongs to the universal ribosomal protein uL23 family.	0.998
DCAR_000378	DCAR_023951	A0A175Y907	A0A164SY24	KOW domain-containing protein.	Ribosomal_L18_c domain-containing protein.	0.999
DCAR_000378	DCAR_024228	A0A175Y907	A0A164T5R7	KOW domain-containing protein.	Uncharacterized protein; Belongs to the universal ribosomal protein uS19 family.	0.999
DCAR_000378	DCAR_025822	A0A175Y907	A0A164UDG0	KOW domain-containing protein.	Uncharacterized protein.	0.998
DCAR_000378	DCAR_030077	A0A175Y907	A0A175YH74	KOW domain-containing protein.	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). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.858
DCAR_000378	EIF6	A0A175Y907	A0A166EBT4	KOW domain-containing protein.	Eukaryotic translation initiation factor 6; Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May also be involved in ribosome biogenesis.	0.979
DCAR_005465	DCAR_000378	A0A166D1Q5	A0A175Y907	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).	KOW domain-containing protein.	0.858
DCAR_005465	DCAR_008547	A0A166D1Q5	A0A166FF60	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).	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).	0.868
DCAR_005465	DCAR_012725	A0A166D1Q5	A0A165ZDQ9	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).	KOW domain-containing protein; Belongs to the universal ribosomal protein uL24 family.	0.858
DCAR_005465	DCAR_014576	A0A166D1Q5	A0A162A9I5	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).	Uncharacterized protein.	0.841
DCAR_005465	DCAR_017890	A0A166D1Q5	A0A164YKE7	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).	Ribosomal_L23eN domain-containing protein; Belongs to the universal ribosomal protein uL23 family.	0.851
DCAR_005465	DCAR_023951	A0A166D1Q5	A0A164SY24	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).	Ribosomal_L18_c domain-containing protein.	0.963
DCAR_005465	DCAR_024228	A0A166D1Q5	A0A164T5R7	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).	Uncharacterized protein; Belongs to the universal ribosomal protein uS19 family.	0.901
DCAR_005465	DCAR_025822	A0A166D1Q5	A0A164UDG0	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).	Uncharacterized protein.	0.851
DCAR_005465	DCAR_030077	A0A166D1Q5	A0A175YH74	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).	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). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.868
DCAR_005465	EIF6	A0A166D1Q5	A0A166EBT4	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).	Eukaryotic translation initiation factor 6; Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May also be involved in ribosome biogenesis.	0.872
DCAR_008547	DCAR_000378	A0A166FF60	A0A175Y907	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).	KOW domain-containing protein.	0.858

page 1 of 6

Server load: low (26%) [HD]

Permalink

Network

Neighborhood

Experiments

Cooccurrence

Databases

Coexpression

Textmining

Fusion

© STRING Consortium 2023

Credits

Access

Info

About