Antimicrobial peptides (Homo sapiens)

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29, 5913, 6257, 6326, 66305, 7, 2540-4238, 61, 7165, 8520, 28, 5038, 61, 7123, 4449, 71, 73, 839, 15, 22, 31, 36...11785216, 18, 7437, 7940, 428, 8635, 456, 67, 8143, 552, 19, 753, 73, 8312, 144, 47, 548410, 52, 82808, 32, 51, 649, 15, 22, 31, 36...65, 851, 39, 648421, 46, 601, 3934, 7726, 66cell wallphagocytic vesicle lumencell wallhost cell cytosolDCD(63-110) CHGA-derivedpeptide:bacterialanionic lipidsHTN1,3,5:bacterialphospholipidsEPC:bacterialsurfaceAnionicphospholipids:microbial cell surfaceMicrobial cell surface PLA2G2A:Ca2+Zn2+ LCN2 DefensinsAnionic phospholipids RNASE6 GlcNac-(1-->4)MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 hC-EPPIN CAMP(134-170)GlcNAc(1-->4)MurNAc:L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 S100A7, S100A7A:Ca2+DCD(63-110)2.5DHBA Microbial cell surface DCD peptidesheptose REG3A(38-175) H+Anionic phospholipids REG3A(38-175) HTN3(20-43) PGLYRP1 PI3RNASE8 REG3A(38-175) Microbial cell surface BPIFB6 HTN3 HTN1 Microbial cell surface HTN1(31-57) Na+ CAMP(31-170)REG3A(38-175):anionic phospholipidsLTFPGLYRP2 dimerRNASE6 H+GlcNAc(1-->4)MurNAc:L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 BPIFB6 Fe3+RNASE8 CLU(23-227) HTN1(31-57) PGLYRP4 Ca2+ H2OBPIFA2 REG3Ahexamer:anionicphospholipidHTN3 Microbial cellsurfaceCAMP(134-170) REG3A(38-175) BPIFA1 hC239-SEMG1 BPIFB1 LYZLEAP2 ATOX1:Cu1+ELANE, CTSG, PRTN3BPIFA1 (GlcNAc+MurNac)nGNLY Zn2+LEAP2:bacterialphospholipidsPiLCN2:2,5DHBAREG3A(27-37) hC239-SEMG1 BPIFB4 hC-EPPIN PRTN3Anionic phospholipids RNASE3 PGLYRP3,4 dimersAnionic phospholipids Microbial cell surface CHGA(19-94) Microbial cell surface CAMP(134-170):microbial cell surfaceTrypsin 2, 3HTN3(20-43) S100A9 Ca2+ LPSBPIPGLYRP3,4dimer:peptidoglycanPGLYRP2 PLA2G2A:phospholipidsZn2+ PI3(61-117) Microbial cell surface LEAP2RNASE6 PI3(61-117) CLU(228-449) S100A8 Microbial cell surface LCN2:2,5DHBA:Fe3+RNASEs3,6,7,(8):LPS,PGNGlcNAc(1-->4)MurNAc:L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 BPIFA/BPIFBDCD(63-110) REG3G(27-37) ELANE,CTSG,PRTN3:microbialcell surfacePDZD11 PRSS3 Ca2+ PGLYRP2 H2OCa2+ CHGA(19-94) Ca2+ MurNAc:PeptidePGLYRP3 RNASE3,RNASE7,RNASE6,(RNASE8)Divalent metalstransported byNRAMP1Zn2+ Anionic phospholipids DCD(63-110) Mn2+ REG3A(27-37)/REG3G(27-37)heptose beta-D-galactofuranosyl 2.5DHBA PGLYRP1 dimerS100A7,S100A7A:Ca2+:Zn2+LCN2 CTSG HTN1 Anionic phospholipids RNASE7 REG3A(27-175)/REG3G(27-175)Microbial cell surface GNLY:bacterialanionic lipidsDCD(20-62)Microbial cell surface GlcNAc(1-->4)MurNAc:L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 DCD(20-110)LTF S100A9 CLU(23-227) Microbial cell surface Mn2+ DCD:anionicphospholipidunknown peptidaseHTN3 LPS CO3(2-) PGLYRP4 Microbial cell surface Anionic phospholipids Fe3+ Anionicphospholipids:microbial cell surfaceLTF HTN3 GNLY:bacterialanionic lipidsCa2+ HTN1 PI3(23-117) REG3A(27-175) HTN3(20-43) peptidoglycan-NHAc Ca2+ SSA2 Anionic phospholipids GNLYDCDhexamer:Zn(2+):anionic phospholipidsDivalent metalstransported byNRAMP1ITLN1 S100A7 KDO ELANE ADPLTF:2xFe3+:2xCO3(2-)REG3G(38-175) INTL1:bacterialglycanFe3+ ATPZn2+BPI RNASE3 Cu1+Microbial cell surface S100A8 EPPIN:SEMG1:LTF:CLUH2OPLA2G2A REG3G(38-175) PGLYRP3 L-Ala-gamma-D-Glu-L-Lys-D-Alapeptidoglycan-NHAc Zn2+ REG3G(27-175) INTL1 ligandsRNASEs3,6,7,(8):anionicphospholipidsAnionic phospholipids GlcNac-(1-->4)MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2SSA1 BPI:LPSCLU(228-449) Microbial cell surface PRTN3 PGLYRP1dimer:peptidoglycanFe2+ LYZ HTN5,(HTN1, HTN3)ATP7A:PDZD11S100A8:S100A9:Ca2+:Zn2+Mn2+HTN1,3,5S100A7A ATP7A GNLYDCD(63-110):anionicphospholipidCHGA fragmentsCTSG betaGlcNAcAnionic phospholipids Fe3+HTN1 PRSS2(24-247) S100A8:S100A9:Ca2+:Mn2+:Na+CO3(2-)BPIFA2 REG3A(38-175)PGLYRP2:peptidoglycanRNASE8 ITLN1 trimer:Ca2+ITLN1 Zn2+ BPIFB2 CHGA(370-390) DCD(63-109) Microbial cell surface S100A7A HTN3(20-43) RNASE3 Microbial cell surface PI3(23-117) ATOX1Anionic phospholipids Microbial cell surface DCD(63-110) DCD(63-109) HTN5, (HTN1,HTN3):SSA1,SSA2RNASE7 LYZ:PGNREG3A(38-175),REG3G(38-175):peptidoglycanCu1+ Anionic phospholipids LPS ELANE S100A8 SLC11A1LPSCHGA(370-390) PLA2G2A BPIFB4 MurNAc Anionic phospholipids RNASE7 Ca2+ BPIFB1 DCD(63-109)Zn2+PRTN3 REG3A(38-175),REG3G(38-175)LPS, PGNLPS SSA1,SSA2PI3:LPSLTF Na+SSA1 beta-D-galactofuranosyl GlcNac-(1-->4)MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2S100A9 SSA2 Microbial cell surface ATOX1 Ca2+ S100A7 LPS Fe2+ Anionic phospholipids GNLY KDO PGLYRP1 Peptide Mn2+ BPIFA/BPIFB:bacterial cellBPIFB2 S100A8:S100A9:Ca2+32, 51312427845573, 8312122451125, 733703149, 835310, 17, 56, 7658685, 7, 2584586410, 52, 5649, 69, 8317, 52, 56, 76


Description

Antimicrobial peptides (AMPs) are small molecular weight proteins with broad spectrum of antimicrobial activity against bacteria, viruses, and fungi (Zasloff M 2002; Radek K & Gallo R 2007). The majority of known AMPs are cationic peptides with common structural characteristics where domains of hydrophobic and cationic amino acids are spatially arranged into an amphipathic design, which facilitates their interaction with bacterial membranes (Shai Y 2002; Yeaman MR & Yount NY 2003; Brown KL & Hancock RE 2006; Dennison SR et al. 2005; Zelezetsky I & Tossi A 2006). It is generally excepted that the electrostatic interaction facilitates the initial binding of the positively charged peptides to the negatively charged bacterial membrane. Moreover, the structural amphiphilicity of AMPs is thought to promote their integration into lipid bilayers of pathogenic cells, leading to membrane disintegration and finally to the microbial cell death. In addition to cationic AMPs a few anionic antimicrobial peptides have been found in humans, however their mechanism of action remains to be clarified (Lai Y et al. 2007; Harris F et al. 2009; Paulmann M et al. 2012). Besides the direct neutralizing effects on bacteria AMPs may modulate cells of the adaptive immunity (neutrophils, T-cells, macrophages) to control inflammation and/or to increase bacterial clearance.

AMPs have also been referred to as cationic host defense peptides, anionic antimicrobial peptides/proteins, cationic amphipathic peptides, cationic AMPs, host defense peptides and alpha-helical antimicrobial peptides (Brown KL & Hancock RE 2006; Harris F et al. 2009; Groenink J et al. 1999; Bradshaw J 2003; Riedl S et al. 2011; Huang Y et al. 2010).<p>The Reactome module describes the interaction events of various types of human AMPs, such as cathelicidin, histatins and neutrophil serine proteases, with conserved patterns of microbial membranes at the host-pathogen interface. The module includes also proteolytic processing events for dermcidin (DCD) and cathelicidin (CAMP) that become functional upon cleavage. In addition, the module highlights an AMP-associated ability of the host to control metal quota at inflammation sites to influence host-pathogen interactions. View original pathway at:Reactome.</div>

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 6803157
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: Shamovsky, Veronica

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Bibliography

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History

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CompareRevisionActionTimeUserComment
101534view11:40, 1 November 2018ReactomeTeamreactome version 66
101069view21:22, 31 October 2018ReactomeTeamreactome version 65
100599view19:56, 31 October 2018ReactomeTeamreactome version 64
100149view16:41, 31 October 2018ReactomeTeamreactome version 63
99699view15:10, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99284view12:46, 31 October 2018ReactomeTeamreactome version 62
93538view11:26, 9 August 2017ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
(GlcNAc+MurNac)nR-ALL-6799970 (Reactome)
2.5DHBA MetaboliteCHEBI:17189 (ChEBI)
ADPMetaboliteCHEBI:16761 (ChEBI)
ATOX1 ProteinO00244 (Uniprot-TrEMBL)
ATOX1:Cu1+ComplexR-HSA-3697875 (Reactome)
ATOX1ProteinO00244 (Uniprot-TrEMBL)
ATP7A ProteinQ04656 (Uniprot-TrEMBL)
ATP7A:PDZD11ComplexR-HSA-6803541 (Reactome)
ATPMetaboliteCHEBI:15422 (ChEBI)
Anionic phospholipids:microbial cell surfaceComplexR-ALL-8931784 (Reactome)
Anionic phospholipids MetaboliteCHEBI:62643 (ChEBI)
BPI ProteinP17213 (Uniprot-TrEMBL)
BPI:LPSComplexR-HSA-6807590 (Reactome)
BPIFA/BPIFB:bacterial cellComplexR-HSA-6809519 (Reactome)
BPIFA/BPIFBComplexR-HSA-6809283 (Reactome)
BPIFA1 ProteinQ9NP55 (Uniprot-TrEMBL)
BPIFA2 ProteinQ96DR5 (Uniprot-TrEMBL)
BPIFB1 ProteinQ8TDL5 (Uniprot-TrEMBL)
BPIFB2 ProteinQ8N4F0 (Uniprot-TrEMBL)
BPIFB4 ProteinP59827 (Uniprot-TrEMBL)
BPIFB6 ProteinQ8NFQ5 (Uniprot-TrEMBL)
BPIProteinP17213 (Uniprot-TrEMBL)
CAMP(134-170) ProteinP49913 (Uniprot-TrEMBL)
CAMP(134-170):microbial cell surfaceComplexR-HSA-8879163 (Reactome)
CAMP(134-170)ProteinP49913 (Uniprot-TrEMBL)
CAMP(31-170)ProteinP49913 (Uniprot-TrEMBL)
CHGA fragmentsComplexR-HSA-6808534 (Reactome)
CHGA(19-94) ProteinP10645 (Uniprot-TrEMBL)
CHGA(370-390) ProteinP10645 (Uniprot-TrEMBL)
CHGA-derived

peptide:bacterial

anionic lipids
ComplexR-HSA-6808558 (Reactome)
CLU(228-449) ProteinP10909 (Uniprot-TrEMBL)
CLU(23-227) ProteinP10909 (Uniprot-TrEMBL)
CO3(2-) MetaboliteCHEBI:41609 (ChEBI)
CO3(2-)MetaboliteCHEBI:41609 (ChEBI)
CTSG ProteinP08311 (Uniprot-TrEMBL) After secretion Cathepsin G is extracellular and associated with the plasma membrane.
Ca2+ MetaboliteCHEBI:29108 (ChEBI)
Cu1+ MetaboliteCHEBI:49552 (ChEBI)
Cu1+MetaboliteCHEBI:49552 (ChEBI)
DCD hexamer:Zn(2+):anionic phospholipidsComplexR-HSA-6803105 (Reactome)
DCD peptidesComplexR-HSA-6803037 (Reactome)
DCD(20-110)ProteinP81605 (Uniprot-TrEMBL)
DCD(20-62)ProteinP81605 (Uniprot-TrEMBL)
DCD(63-109) ProteinP81605 (Uniprot-TrEMBL)
DCD(63-109)ProteinP81605 (Uniprot-TrEMBL)
DCD(63-110) ProteinP81605 (Uniprot-TrEMBL)
DCD(63-110):anionic phospholipidComplexR-HSA-6803024 (Reactome)
DCD(63-110)ProteinP81605 (Uniprot-TrEMBL)
DCD:anionic phospholipidComplexR-HSA-6803066 (Reactome)
DefensinsPathwayR-HSA-1461973 (Reactome) The defensins are a family of antimicrobial cationic peptide molecules which in mammals have a characteristic beta-sheet-rich fold and framework of six disulphide-linked cysteines (Selsted & Ouellette 2005, Ganz 2003). Human defensin peptides have two subfamilies, alpha- and beta-defensins, differing in the length of peptide chain between the six cysteines and the order of disulphide bond pairing between them. A third subfamily, the theta defensins, is derived from alpha-defensins prematurely truncated by a stop codon between the third and fourth cysteine residues. The translated products are shortened to nonapeptides, covalently dimerized by disulfide linkages, and cyclized via new peptide bonds between the first and ninth residues. Humans have one pseudogene but no translated representatives of the theta class.
In solution most alpha and beta defensins are monomers but can form dimers and higher order structures.

The primary cellular sources of defensins are neutrophils, epithelial cells and intestinal Paneth cells.Those expressed in neutrophils and the gut are predominantly constitutive, while those in epithelial tissues such as skin are often inducible by proinflammatory stimuli such as LPS or TNF-alpha.

Defensins are translated as precursor polypeptides that include a typical signal peptide or prepiece that is cleaved in the Golgi body, and a propiece, cleaved by differing mechanisms to produce the mature defensin. Mature defensin peptides can be further processed by removal of individual N-terminal residues (Yang et al. 2004). This may be a mechanism to broaden the activity profile of defensins (Ghosh et al. 2002).

Defensins have direct antimicrobial effects and kill a wide range of Gram-positive and negative bacteria, fungi and some viruses. The primary antimicrobial action of defensins is permeabilization of microbial target membranes but several additional mechanisms have been suggested (Brogden 2005, Wilmes et al. 2011). Defensins and related antimicrobial peptides such as cathelicidin bridge the innate and acquired immune responses. In addition to their antimicrobial properties, cathelicidin and several defensins show receptor-mediated chemotactic activity for immune cells such as monocytes, T cells or immature DCs, induce cytokine production by monocytes and epithelial cells, modulate angiogenesis and stimulate wound healing (Yang et al. 1999, 2000, 2004, Rehaume & Hancock 2008, Yeung et al. 2011).
Divalent metals

transported by

NRAMP1
ComplexR-ALL-445829 (Reactome)
Divalent metals

transported by

NRAMP1
ComplexR-ALL-445832 (Reactome)
ELANE ProteinP08246 (Uniprot-TrEMBL)
ELANE, CTSG, PRTN3ComplexR-HSA-6813639 (Reactome)
ELANE,CTSG,

PRTN3:microbial

cell surface
ComplexR-HSA-6813664 (Reactome)
EPC:bacterial surfaceComplexR-HSA-6810673 (Reactome)
EPPIN:SEMG1:LTF:CLUComplexR-HSA-6810613 (Reactome)
Fe2+ MetaboliteCHEBI:18248 (ChEBI)
Fe3+ MetaboliteCHEBI:29034 (ChEBI)
Fe3+MetaboliteCHEBI:29034 (ChEBI)
GNLY ProteinP22749 (Uniprot-TrEMBL)
GNLY:bacterial anionic lipidsComplexR-HSA-6806759 (Reactome)
GNLY:bacterial anionic lipidsComplexR-HSA-8858201 (Reactome)
GNLYProteinP22749 (Uniprot-TrEMBL)
GlcNAc(1-->4)MurNAc:L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 R-ALL-6788957 (Reactome)
GlcNac-(1-->4)MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 MetaboliteCHEBI:55424 (ChEBI) In Staphylococcus aureus, the pentapeptide coming off the N-acetyl muramic acid is composed of the amino acids L-alanine, D-glutamine, L-lysine, and two D-alanines.
GlcNac-(1-->4)MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2MetaboliteCHEBI:55424 (ChEBI) In Staphylococcus aureus, the pentapeptide coming off the N-acetyl muramic acid is composed of the amino acids L-alanine, D-glutamine, L-lysine, and two D-alanines.
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HTN1 ProteinP15515 (Uniprot-TrEMBL)
HTN1(31-57) ProteinP15515 (Uniprot-TrEMBL)
HTN1,3,5:bacterial phospholipidsComplexR-HSA-6807169 (Reactome)
HTN1,3,5ComplexR-HSA-6807193 (Reactome)
HTN3 ProteinP15516 (Uniprot-TrEMBL)
HTN3(20-43) ProteinP15516 (Uniprot-TrEMBL)
HTN5, (HTN1, HTN3):SSA1,SSA2ComplexR-HSA-6807587 (Reactome)
HTN5,(HTN1, HTN3)ComplexR-HSA-6807573 (Reactome)
INTL1 ligandsComplexR-ALL-6804535 (Reactome)
INTL1:bacterial glycanComplexR-HSA-6804513 (Reactome)
ITLN1 ProteinQ8WWA0 (Uniprot-TrEMBL)
ITLN1 trimer:Ca2+ComplexR-HSA-6804509 (Reactome)
KDO MetaboliteCHEBI:85986 (ChEBI)
L-Ala-gamma-D-Glu-L-Lys-D-AlaMetaboliteCHEBI:61626 (ChEBI)
LCN2 ProteinP80188 (Uniprot-TrEMBL)
LCN2:2,5DHBA:Fe3+ComplexR-HSA-5229238 (Reactome)
LCN2:2,5DHBAComplexR-HSA-5229290 (Reactome)
LEAP2 ProteinQ969E1 (Uniprot-TrEMBL)
LEAP2:bacterial phospholipidsComplexR-HSA-6813633 (Reactome)
LEAP2ProteinQ969E1 (Uniprot-TrEMBL)
LPS MetaboliteCHEBI:16412 (ChEBI)
LPS, PGNComplexR-ALL-6803074 (Reactome)
LPSMetaboliteCHEBI:16412 (ChEBI)
LTF ProteinP02788 (Uniprot-TrEMBL)
LTF:2xFe3+:2xCO3(2-)ComplexR-HSA-1222432 (Reactome)
LTFProteinP02788 (Uniprot-TrEMBL)
LYZ ProteinP61626 (Uniprot-TrEMBL)
LYZ:PGNComplexR-HSA-8862293 (Reactome)
LYZProteinP61626 (Uniprot-TrEMBL)
Microbial cell surfaceR-ALL-8879165 (Reactome) This entity is intended to represent any molecule that might be at the outer cell surface of a microbial cell
Microbial cell surface R-ALL-8879165 (Reactome) This entity is intended to represent any molecule that might be at the outer cell surface of a microbial cell
Mn2+ MetaboliteCHEBI:29035 (ChEBI)
Mn2+MetaboliteCHEBI:29035 (ChEBI)
MurNAc MetaboliteCHEBI:21615 (ChEBI)
MurNAc:PeptideComplexR-ALL-6788991 (Reactome)
Na+ MetaboliteCHEBI:29101 (ChEBI)
Na+MetaboliteCHEBI:29101 (ChEBI)
PDZD11 ProteinQ5EBL8 (Uniprot-TrEMBL)
PGLYRP1 ProteinO75594 (Uniprot-TrEMBL)
PGLYRP1 dimerComplexR-HSA-6789200 (Reactome)
PGLYRP1dimer:peptidoglycanComplexR-HSA-6789175 (Reactome)
PGLYRP2 ProteinQ96PD5 (Uniprot-TrEMBL)
PGLYRP2 dimerComplexR-HSA-8933468 (Reactome)
PGLYRP2:peptidoglycanComplexR-HSA-6799988 (Reactome)
PGLYRP3 ProteinQ96LB9 (Uniprot-TrEMBL)
PGLYRP3,4 dimer:peptidoglycanComplexR-HSA-6799966 (Reactome)
PGLYRP3,4 dimersComplexR-HSA-6799960 (Reactome)
PGLYRP4 ProteinQ96LB8 (Uniprot-TrEMBL)
PI3(23-117) ProteinP19957 (Uniprot-TrEMBL)
PI3(61-117) ProteinP19957 (Uniprot-TrEMBL)
PI3:LPSComplexR-HSA-6810759 (Reactome)
PI3ComplexR-HSA-6810794 (Reactome)
PLA2G2A ProteinP14555 (Uniprot-TrEMBL)
PLA2G2A:Ca2+ComplexR-HSA-1602363 (Reactome)
PLA2G2A:phospholipidsComplexR-HSA-8862769 (Reactome)
PRSS2(24-247) ProteinP07478 (Uniprot-TrEMBL)
PRSS3 ProteinP35030 (Uniprot-TrEMBL)
PRTN3 ProteinP24158 (Uniprot-TrEMBL)
PRTN3ProteinP24158 (Uniprot-TrEMBL)
Peptide MetaboliteCHEBI:16670 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
REG3A

hexamer:anionic

phospholipid
ComplexR-HSA-6801795 (Reactome)
REG3A(27-175) ProteinQ06141 (Uniprot-TrEMBL)
REG3A(27-175)/REG3G(27-175)ComplexR-HSA-6801779 (Reactome)
REG3A(27-37) ProteinQ06141 (Uniprot-TrEMBL)
REG3A(27-37)/REG3G(27-37)ComplexR-HSA-6801797 (Reactome)
REG3A(38-175) ProteinQ06141 (Uniprot-TrEMBL)
REG3A(38-175), REG3G(38-175):peptidoglycanComplexR-HSA-6801809 (Reactome)
REG3A(38-175), REG3G(38-175)ComplexR-HSA-6801794 (Reactome)
REG3A(38-175):anionic phospholipidsComplexR-HSA-6801804 (Reactome)
REG3A(38-175)ProteinQ06141 (Uniprot-TrEMBL)
REG3G(27-175) ProteinQ6UW15 (Uniprot-TrEMBL)
REG3G(27-37) ProteinQ6UW15 (Uniprot-TrEMBL)
REG3G(38-175) ProteinQ6UW15 (Uniprot-TrEMBL)
RNASE3 ProteinP12724 (Uniprot-TrEMBL)
RNASE3,RNASE7,RNASE6,(RNASE8)ComplexR-HSA-6803116 (Reactome)
RNASE6 ProteinQ93091 (Uniprot-TrEMBL)
RNASE7 ProteinQ9H1E1 (Uniprot-TrEMBL)
RNASE8 ProteinQ8TDE3 (Uniprot-TrEMBL)
RNASEs 3,6,7,(8):LPS,PGNComplexR-HSA-6803051 (Reactome)
RNASEs

3,6,7,(8):anionic

phospholipids
ComplexR-HSA-8948028 (Reactome)
S100A7 ProteinP31151 (Uniprot-TrEMBL)
S100A7, S100A7A:Ca2+:Zn2+ComplexR-HSA-6798500 (Reactome)
S100A7, S100A7A:Ca2+ComplexR-HSA-6798557 (Reactome)
S100A7A ProteinQ86SG5 (Uniprot-TrEMBL)
S100A8 ProteinP05109 (Uniprot-TrEMBL)
S100A8:S100A9:Ca2+:Mn2+:Na+ComplexR-HSA-6798411 (Reactome)
S100A8:S100A9:Ca2+:Zn2+ComplexR-HSA-8944189 (Reactome)
S100A8:S100A9:Ca2+ComplexR-HSA-8944198 (Reactome)
S100A9 ProteinP06702 (Uniprot-TrEMBL)
SLC11A1ProteinP49279 (Uniprot-TrEMBL)
SSA1 ProteinP41797 (Uniprot-TrEMBL)
SSA1,SSA2ComplexR-CAL-6807575 (Reactome)
SSA2 ProteinP46587 (Uniprot-TrEMBL)
Trypsin 2, 3ComplexR-HSA-1460242 (Reactome)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
Zn2+MetaboliteCHEBI:29105 (ChEBI)
beta-D-galactofuranosyl MetaboliteCHEBI:59496 (ChEBI)
betaGlcNAcMetaboliteCHEBI:28009 (ChEBI)
hC-EPPIN ProteinO95925 (Uniprot-TrEMBL)
hC239-SEMG1 ProteinP04279 (Uniprot-TrEMBL)
heptose MetaboliteCHEBI:42976 (ChEBI)
peptidoglycan-NHAc CHEBI:8005 (ChEBI)
unknown peptidaseR-HSA-3076903 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
(GlcNAc+MurNac)nArrowR-HSA-6799977 (Reactome)
ADPArrowR-HSA-6803545 (Reactome)
ATOX1:Cu1+R-HSA-6803545 (Reactome)
ATOX1ArrowR-HSA-6803545 (Reactome)
ATP7A:PDZD11mim-catalysisR-HSA-6803545 (Reactome)
ATPR-HSA-6