81 items (Sus scrofa) - 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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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:
	COL8A2	Collagen type VIII alpha 2 chain. (707 aa)
	COL13A1	Collagen type XIII alpha 1 chain. (726 aa)
	COL21A1	Collagen type XXI alpha 1 chain. (957 aa)
	COL11A1	Collagen type XI alpha 1 chain. (1816 aa)
	AMELY	Amelogenin; Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family. (189 aa)
	MFAP5	Microfibril associated protein 5. (236 aa)
	COL8A1	Collagen type VIII alpha 1 chain. (759 aa)
	COL1A1	Collagen type I alpha 1 chain. (1477 aa)
	COL9A2	Uncharacterized protein. (709 aa)
	FBN2	Fibrillin 2. (2910 aa)
	COL14A1	Collagen alpha-1(XIV) chain isoform X1. (1796 aa)
	COL19A1	Collagen type XIX alpha 1 chain. (1132 aa)
	A0A5G2QPD6_PIG	ZP domain-containing protein. (665 aa)
	ENAM	142 kDa enamelin; Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation. (1142 aa)
	COL4A1	Collagen IV NC1 domain-containing protein. (461 aa)
	COL9A1	Collagen type IX alpha 1 chain. (922 aa)
	AMELX	Uncharacterized protein. (203 aa)
	A0A5G2QUL4_PIG	Uncharacterized protein. (536 aa)
	TECTA	Tectorin alpha. (2469 aa)
	EMILIN1	Elastin microfibril interfacer 1. (1292 aa)
	COL11A2	Collagen type XI alpha 2 chain. (1796 aa)
	COL6A5	Collagen type VI alpha 5 chain. (2337 aa)
	TBC1D31	TBC1 domain family member 31. (1066 aa)
	COL28A1	Collagen type XXVIII alpha 1 chain. (1236 aa)
	COL5A2	Collagen alpha-2(V) chain preproprotein. (1499 aa)
	LAMB4	Uncharacterized protein. (719 aa)
	PRELP	Proline and arginine rich end leucine rich repeat protein. (381 aa)
	COL4A4	Collagen type IV alpha 4 chain. (1691 aa)
	SCARA3	Scavenger receptor class A member 3 isoform X1. (606 aa)
	ELN	Elastin. (674 aa)
	LAMB2	Laminin subunit beta-2. (1881 aa)
	COL4A5	Collagen type IV alpha 5 chain. (1689 aa)
	FBLN1	Fibulin-1; Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. (819 aa)
	COL20A1	Uncharacterized protein. (1338 aa)
	COL9A3	Collagen type IX alpha 3 chain. (684 aa)
	LAMA2-2	Uncharacterized protein. (921 aa)
	LAMC1	Uncharacterized protein. (1607 aa)
	LAMA2	Uncharacterized protein. (2070 aa)
	COL2A1	Collagen type II alpha 1 chain. (1486 aa)
	DPT	Dermatopontin; Seems to mediate adhesion by cell surface integrin binding. May serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. Enhances TGFB1 activity. Inhibits cell proliferation (By similarity). Accelerates collagen fibril formation, and stabilizes collagen fibrils against low- temperature dissociation. (201 aa)
	COL16A1	Collagen alpha-1(XVI) chain isoform X2. (1624 aa)
	COL3A1	Collagen alpha-1(III) chain preproprotein. (1471 aa)
	IMPG2	Interphotoreceptor matrix proteoglycan 2. (1244 aa)
	COL18A1	Collagen type XVIII alpha 1 chain. (1755 aa)
	COL17A1	Collagen type XVII alpha 1 chain. (1506 aa)
	FBN3	Fibrillin 3. (2858 aa)
	PXDN	Peroxidasin. (1529 aa)
	UMODL1	Uromodulin like 1. (1360 aa)
	COLQ	Collagen like tail subunit of asymmetric acetylcholinesterase. (458 aa)
	MATN1	Matrilin 1. (496 aa)
	COL4A3	Collagen type IV alpha 3 chain. (1669 aa)
	C1QL2	Complement C1q like 2. (287 aa)
	LAMB3	Laminin subunit beta 3. (1172 aa)
	LAMB1	Laminin subunit beta 1. (1785 aa)
	COL1A2	Fibrillar collagen NC1 domain-containing protein. (1135 aa)
	OPTC	Opticin. (333 aa)
	COL23A1	Collagen type XXIII alpha 1 chain. (540 aa)
	COL5A3	Collagen type V alpha 3 chain. (1747 aa)
	LOC110257935	Uncharacterized protein. (1836 aa)
	COL4A6	Collagen type IV alpha 6 chain. (1547 aa)
	ZPLD1	Zona pellucida like domain containing 1. (452 aa)
	COL7A1	Uncharacterized protein. (2938 aa)
	TECTB	Tectorin beta. (333 aa)
	OIT3	Oncoprotein-induced transcript 3 protein. (546 aa)
	ZP4	Processed zona pellucida sperm-binding protein 4; Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor. (536 aa)
	COL4A2	Collagen type IV alpha 2 chain. (1712 aa)
	AMBN	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family. (421 aa)
	GP2	Pancreatic secretory granule membrane major glycoprotein GP2 isoform 1. (532 aa)
	UMOD	Uromodulin. (642 aa)
	ZP2	Processed zona pellucida sperm-binding protein 2; Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. Belongs to the ZP domain family. ZPA subfamily. (716 aa)
	ZP3	Processed zona pellucida sperm-binding protein 3; Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for zona matrix formation. May not have a sperm- binding activity by itself but may increase sperm-binding activity of ZPB. (421 aa)
	COL22A1	Collagen type XXII alpha 1 chain. (1602 aa)
	COL5A1	Fibrillar collagen NC1 domain-containing protein. (1918 aa)
	COL27A1	Collagen type XXVII alpha 1 chain. (1843 aa)
	COL15A1	Collagen type XV alpha 1 chain. (1359 aa)
	FBN1	Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...] (2871 aa)
	COL12A1	Collagen type XII alpha 1 chain. (3065 aa)
	COL10A1	Type X collagen. (675 aa)
	LAMA3	Laminin subunit alpha 3. (3345 aa)
	EMILIN2	Elastin microfibril interfacer 2. (1078 aa)
	DCN	Decorin; May affect the rate of fibrils formation. (359 aa)

Your Current Organism:

Sus scrofa

NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A0A5G2QUL4_PIG	COL4A2	ENSSSCP00000061856	ENSSSCP00000010191	Uncharacterized protein.	Collagen type IV alpha 2 chain.	0.998
A0A5G2QUL4_PIG	COL4A6	ENSSSCP00000061856	ENSSSCP00000013368	Uncharacterized protein.	Collagen type IV alpha 6 chain.	0.547
A0A5G2QUL4_PIG	COL5A3	ENSSSCP00000061856	ENSSSCP00000014530	Uncharacterized protein.	Collagen type V alpha 3 chain.	0.438
A0A5G2QUL4_PIG	FBN1	ENSSSCP00000061856	ENSSSCP00000005017	Uncharacterized protein.	Fibrillin-1; [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus [...]	0.536
A0A5G2QUL4_PIG	LAMA2	ENSSSCP00000061856	ENSSSCP00000037113	Uncharacterized protein.	Uncharacterized protein.	0.496
A0A5G2QUL4_PIG	LAMB1	ENSSSCP00000061856	ENSSSCP00000016375	Uncharacterized protein.	Laminin subunit beta 1.	0.610
A0A5G2QUL4_PIG	LAMC1	ENSSSCP00000061856	ENSSSCP00000037158	Uncharacterized protein.	Uncharacterized protein.	0.570
AMBN	AMELX	ENSSSCP00000009536	ENSSSCP00000062033	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	Uncharacterized protein.	0.892
AMBN	AMELY	ENSSSCP00000009536	ENSSSCP00000072463	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	Amelogenin; Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family.	0.978
AMBN	COL1A1	ENSSSCP00000009536	ENSSSCP00000066291	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	Collagen type I alpha 1 chain.	0.418
AMBN	COL22A1	ENSSSCP00000009536	ENSSSCP00000006349	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	Collagen type XXII alpha 1 chain.	0.409
AMBN	ENAM	ENSSSCP00000009536	ENSSSCP00000063311	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	142 kDa enamelin; Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation.	0.969
AMELX	AMBN	ENSSSCP00000062033	ENSSSCP00000009536	Uncharacterized protein.	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	0.892
AMELX	ENAM	ENSSSCP00000062033	ENSSSCP00000063311	Uncharacterized protein.	142 kDa enamelin; Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation.	0.874
AMELX	OPTC	ENSSSCP00000062033	ENSSSCP00000016195	Uncharacterized protein.	Opticin.	0.905
AMELX	PXDN	ENSSSCP00000062033	ENSSSCP00000022033	Uncharacterized protein.	Peroxidasin.	0.403
AMELY	AMBN	ENSSSCP00000072463	ENSSSCP00000009536	Amelogenin; Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family.	Ameloblastin; Involved in the mineralization and structural organization of enamel; Belongs to the ameloblastin family.	0.978
AMELY	ENAM	ENSSSCP00000072463	ENSSSCP00000063311	Amelogenin; Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family.	142 kDa enamelin; Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation.	0.970
AMELY	OPTC	ENSSSCP00000072463	ENSSSCP00000016195	Amelogenin; Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family.	Opticin.	0.805
COL10A1	COL11A1	ENSSSCP00000004785	ENSSSCP00000072487	Type X collagen.	Collagen type XI alpha 1 chain.	0.568