SERPINB11 protein (human) - 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.

Knowledge-based Evidence

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textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man

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

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

... functional annotations:

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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
CBWD3	SERPINB11	ENSP00000353295	ENSP00000485532	COBW domain containing 3.	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.603
CPE	SERPINB11	ENSP00000386104	ENSP00000485532	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.633
DNLZ	SERPINB11	ENSP00000360803	ENSP00000485532	DNL-type zinc finger protein; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation.	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.693
GPC3	SERPINB11	ENSP00000377836	ENSP00000485532	Glypican-3 alpha subunit; Cell surface proteoglycan that bears heparan sulfate. Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligand [...]	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.465
ITPA	SERPINB11	ENSP00000369456	ENSP00000485532	Inosine triphosphate pyrophosphatase; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions; Belongs to the HAM1 NTPase family.	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.568
KLK14	SERPINB11	ENSP00000375678	ENSP00000485532	Kallikrein-14; Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression incl [...]	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.483
SERPINB11	CBWD3	ENSP00000485532	ENSP00000353295	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	COBW domain containing 3.	0.603
SERPINB11	CPE	ENSP00000485532	ENSP00000386104	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	0.633
SERPINB11	DNLZ	ENSP00000485532	ENSP00000360803	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	DNL-type zinc finger protein; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation.	0.693
SERPINB11	GPC3	ENSP00000485532	ENSP00000377836	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	Glypican-3 alpha subunit; Cell surface proteoglycan that bears heparan sulfate. Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligand [...]	0.465
SERPINB11	ITPA	ENSP00000485532	ENSP00000369456	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	Inosine triphosphate pyrophosphatase; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions; Belongs to the HAM1 NTPase family.	0.568
SERPINB11	KLK14	ENSP00000485532	ENSP00000375678	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	Kallikrein-14; Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression incl [...]	0.483
SERPINB11	ZC2HC1C	ENSP00000485532	ENSP00000435550	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	Zinc finger C2HC-type containing 1C; Belongs to the ZC2HC1 family.	0.422
ZC2HC1C	SERPINB11	ENSP00000435550	ENSP00000485532	Zinc finger C2HC-type containing 1C; Belongs to the ZC2HC1 family.	Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change.	0.422