15 items (Penicillium roqueforti) - STRING interaction network

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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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second shell of interactors

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proteins of unknown 3D structure

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Predicted Interactions

gene neighborhood

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Your Input:
	W6PR70_PENRF	Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins; Belongs to the NMT family. (501 aa)
	W6QRY5_PENRF	Uncharacterized protein. (537 aa)
	W6QQX1_PENRF	Zn(2)-C6 fungal-type DNA-binding domain. (581 aa)
	ncs1	Calcium-binding protein NCS-1. (190 aa)
	W6QNB6_PENRF	Zn(2)-C6 fungal-type DNA-binding domain. (569 aa)
	W6QN73_PENRF	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). (433 aa)
	W6QG29_PENRF	Zn(2)-C6 fungal-type DNA-binding domain. (454 aa)
	W6QET0_PENRF	Zn(2)-C6 fungal-type DNA-binding domain. (532 aa)
	W6QAJ7_PENRF	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). (374 aa)
	W6Q6R6_PENRF	Genomic scaffold, ProqFM164S02. (63 aa)
	W6Q2L3_PENRF	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). (407 aa)
	W6Q1N4_PENRF	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). (382 aa)
	W6Q121_PENRF	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). (439 aa)
	W6PYL2_PENRF	Zn(2)-C6 fungal-type DNA-binding domain. (426 aa)
	W6PY25_PENRF	Zn(2)-C6 fungal-type DNA-binding domain. (602 aa)

Your Current Organism:

Penicillium roqueforti

NCBI taxonomy Id: 1365484
Other names: P. roqueforti FM164, Penicillium roqueforti FM164

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
W6PR70_PENRF	W6Q1N4_PENRF	W6PR70	W6Q1N4	Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins; Belongs to the NMT 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).	0.447
W6PR70_PENRF	W6QAJ7_PENRF	W6PR70	W6QAJ7	Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins; Belongs to the NMT 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).	0.447
W6PY25_PENRF	W6Q121_PENRF	W6PY25	W6Q121	Zn(2)-C6 fungal-type DNA-binding domain.	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).	0.592
W6PY25_PENRF	W6Q2L3_PENRF	W6PY25	W6Q2L3	Zn(2)-C6 fungal-type DNA-binding domain.	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).	0.592
W6PY25_PENRF	W6QN73_PENRF	W6PY25	W6QN73	Zn(2)-C6 fungal-type DNA-binding domain.	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).	0.592
W6PYL2_PENRF	W6Q121_PENRF	W6PYL2	W6Q121	Zn(2)-C6 fungal-type DNA-binding domain.	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).	0.592
W6PYL2_PENRF	W6Q2L3_PENRF	W6PYL2	W6Q2L3	Zn(2)-C6 fungal-type DNA-binding domain.	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).	0.592
W6PYL2_PENRF	W6QN73_PENRF	W6PYL2	W6QN73	Zn(2)-C6 fungal-type DNA-binding domain.	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).	0.592
W6Q121_PENRF	W6PY25_PENRF	W6Q121	W6PY25	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).	Zn(2)-C6 fungal-type DNA-binding domain.	0.592
W6Q121_PENRF	W6PYL2_PENRF	W6Q121	W6PYL2	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).	Zn(2)-C6 fungal-type DNA-binding domain.	0.592
W6Q121_PENRF	W6Q1N4_PENRF	W6Q121	W6Q1N4	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).	0.863
W6Q121_PENRF	W6QAJ7_PENRF	W6Q121	W6QAJ7	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).	0.863
W6Q121_PENRF	W6QNB6_PENRF	W6Q121	W6QNB6	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).	Zn(2)-C6 fungal-type DNA-binding domain.	0.592
W6Q121_PENRF	W6QQX1_PENRF	W6Q121	W6QQX1	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).	Zn(2)-C6 fungal-type DNA-binding domain.	0.592
W6Q121_PENRF	W6QRY5_PENRF	W6Q121	W6QRY5	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.	0.592
W6Q1N4_PENRF	W6PR70_PENRF	W6Q1N4	W6PR70	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).	Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins; Belongs to the NMT family.	0.447
W6Q1N4_PENRF	W6Q121_PENRF	W6Q1N4	W6Q121	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).	0.863
W6Q1N4_PENRF	W6Q2L3_PENRF	W6Q1N4	W6Q2L3	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).	0.777
W6Q1N4_PENRF	W6QN73_PENRF	W6Q1N4	W6QN73	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).	0.777
W6Q2L3_PENRF	W6PY25_PENRF	W6Q2L3	W6PY25	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).	Zn(2)-C6 fungal-type DNA-binding domain.	0.592