HUMAN:GELS

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GSN
Protein Name(s)	Gelsolin AGEL Actin-depolymerizing factor ADF Brevin
External Links
UniProt	P06396
EMBL	X04412 AK096280 AK125819 AK295572 AK299453 AK315494 AL137068 AL513122 AL513122 CH471090 CH471090 CH471090 BC017491 BC026033
CCDS	CCDS48011.1 CCDS65118.1 CCDS6828.1 CCDS6829.1
PIR	A03011
RefSeq	NP_000168.1 NP_001121134.1 NP_001121135.2 NP_001121136.1 NP_001121137.1 NP_001121138.1 NP_001121139.1 NP_001244958.1 NP_001244959.1 NP_937895.1 XP_005252000.1 XP_005252001.1 XP_005252002.1 XP_006717139.1 XP_006717140.1 XP_006717141.1 XP_006717142.1
UniGene	Hs.522373
PDB	1C0F 1C0G 1D4X 1DEJ 1EQY 1ESV 1H1V 1KCQ 1MDU 1NLV 1NM1 1NMD 1P8X 1P8Z 1SOL 1T44 1YAG 1YVN 2FF3 2FF6 2FH1 2FH2 2FH3 2FH4 3A5L 3A5M 3A5N 3A5O 3CI5 3CIP 3CJB 3CJC 3FFK 3FFN 3TU5 4PKG 4PKH 4PKI
PDBsum	1C0F 1C0G 1D4X 1DEJ 1EQY 1ESV 1H1V 1KCQ 1MDU 1NLV 1NM1 1NMD 1P8X 1P8Z 1SOL 1T44 1YAG 1YVN 2FF3 2FF6 2FH1 2FH2 2FH3 2FH4 3A5L 3A5M 3A5N 3A5O 3CI5 3CIP 3CJB 3CJC 3FFK 3FFN 3TU5 4PKG 4PKH 4PKI
ProteinModelPortal	P06396
SMR	P06396
BioGrid	109189
DIP	DIP-2196N
IntAct	P06396
MINT	MINT-5000481
STRING	9606.ENSP00000362924
PhosphoSite	P06396
DMDM	121116
OGP	P06396
MaxQB	P06396
PaxDb	P06396
PeptideAtlas	P06396
PRIDE	P06396
DNASU	2934
Ensembl	ENST00000341272 ENST00000373808 ENST00000373818 ENST00000373823 ENST00000412819 ENST00000436847 ENST00000545652
GeneID	2934
KEGG	hsa:2934
UCSC	uc004bld.1 uc010mvq.1
CTD	2934
GeneCards	GC09P123971
HGNC	HGNC:4620
HPA	CAB010823 CAB016728 CAB036009
MIM	105120 137350
neXtProt	NX_P06396
Orphanet	85448
PharmGKB	PA29011
eggNOG	NOG304849
GeneTree	ENSGT00760000119111
HOGENOM	HOG000233630
HOVERGEN	HBG004183
InParanoid	P06396
KO	K05768
OMA	ANMEERK
OrthoDB	EOG7288RJ
PhylomeDB	P06396
TreeFam	TF313468
Reactome	REACT_13541 REACT_75925
ChiTaRS	GSN
EvolutionaryTrace	P06396
GeneWiki	Gelsolin
GenomeRNAi	2934
NextBio	11625
PMAP-CutDB	P06396
PRO	PR:P06396
Proteomes	UP000005640
Bgee	P06396
CleanEx	HS_GSN
ExpressionAtlas	P06396
Genevestigator	P06396
GO	GO:0015629 GO:0072562 GO:0005829 GO:0005576 GO:0070062 GO:0005925 GO:0030027 GO:0048471 GO:0043234 GO:0001726 GO:0005509 GO:0030041 GO:0051014 GO:0007568 GO:0006915 GO:0051016 GO:0006921 GO:0071276 GO:0060271 GO:0014003 GO:0048015 GO:0030155 GO:0045471 GO:0051593 GO:0042246 GO:0016192
Gene3D	3.40.20.10
InterPro	IPR029006 IPR030004 IPR007123 IPR007122
PANTHER	PTHR11977 PTHR11977:SF29
Pfam	PF00626
PRINTS	PR00597
SMART	SM00262

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0005576	extracellular region	PMID:27068509^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0007318)	Seeded From UniProt	complete
NOT\|involved_in	GO:0022617	extracellular matrix disassembly	PMID:24236012^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030864	cortical actin cytoskeleton	PMID:24236012^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000235)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:14596804^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:14596804^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071801	regulation of podosome assembly	PMID:24236012^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000235)	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:24236012^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0002102	podosome	PMID:24236012^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000576)	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:18266911^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1903906	regulation of plasma membrane raft polarization	PMID:23575248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:1903903	regulation of establishment of T cell polarity	PMID:23575248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
part_of	GO:0030478	actin cap	PMID:23575248^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:23575248^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23575248^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0090527	actin filament reorganization	PMID:23575248^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P04578	P	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0046597	negative regulation of viral entry into host cell	PMID:23575248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0051014	actin filament severing	PMID:23575248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
colocalizes_with	GO:0030864	cortical actin cytoskeleton	PMID:23575248^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0051693	actin filament capping	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13020	P		Seeded From UniProt	complete
involved_in	GO:0006911	phagocytosis, engulfment	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13020	P	has_input:(GO:0005584)	Seeded From UniProt	complete
involved_in	GO:1903923	positive regulation of protein processing in phagocytic vesicle	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13020	P	has_input:(GO:0005584)	Seeded From UniProt	complete
enables	GO:0045159	myosin II binding	PMID:23325791^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8VDD5	F		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:19549824^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(UBERON:0002036)	Seeded From UniProt	complete
part_of	GO:0016528	sarcoplasm	PMID:19549824^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0014891	striated muscle atrophy	PMID:19549824^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:19549824^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0001969)\|part_of:(UBERON:0011895)	Seeded From UniProt	complete
involved_in	GO:0097017	renal protein absorption	PMID:24601799^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990000	amyloid fibril formation	PMID:24601799^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(UBERON:0000074)	Seeded From UniProt	complete
involved_in	GO:2001269	positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway	PMID:22952982^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42574)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:22952982^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O00220) has_regulation_target:(UniProtKB:O14763)	Seeded From UniProt	complete
involved_in	GO:0097284	hepatocyte apoptotic process	PMID:22952982^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000632)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22952982^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000182)	Seeded From UniProt	complete
involved_in	GO:1990000	amyloid fibril formation	PMID:19904968^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903909	regulation of receptor clustering	PMID:23575248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(CL:0000084) has_input:(UniProtKB:P01730) has_input:(UniProtKB:P61073)\|part_of(CL:0000084) has_input:(UniProtKB:P01730) has_input:(UniProtKB:P51681)	Seeded From UniProt	complete
involved_in	GO:0030041	actin filament polymerization	PMID:23729654^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902174	positive regulation of keratinocyte apoptotic process	PMID:23729654^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005634	nucleus	PMID:23729654^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051693	actin filament capping	PMID:19666531^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051127	positive regulation of actin nucleation	PMID:19666531^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042989	sequestering of actin monomers	PMID:19666531^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21362503^[19]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002367)	Seeded From UniProt	complete
involved_in	GO:0060271	cilium assembly	PMID:20393563^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051014	actin filament severing	PMID:3020431^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030041	actin filament polymerization	PMID:3020431^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:3020431^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:3020431^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:14718574^[22]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903923	positive regulation of protein processing in phagocytic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
involved_in	GO:0071346	cellular response to interferon-gamma	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
involved_in	GO:0051693	actin filament capping	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
involved_in	GO:0051014	actin filament severing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	C		Seeded From UniProt	complete
involved_in	GO:0030041	actin filament polymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	C		Seeded From UniProt	complete
involved_in	GO:0016192	vesicle-mediated transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
involved_in	GO:0006911	phagocytosis, engulfment	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13020 ensembl:ENSMUSP00000028239	C		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0051593	response to folic acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0051014	actin filament severing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	C		Seeded From UniProt	complete
involved_in	GO:0048015	phosphatidylinositol-mediated signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0045471	response to ethanol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
part_of	GO:0043209	myelin sheath	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	C		Seeded From UniProt	complete
involved_in	GO:0042246	tissue regeneration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	C		Seeded From UniProt	complete
involved_in	GO:0030155	regulation of cell adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	C		Seeded From UniProt	complete
involved_in	GO:0014003	oligodendrocyte development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0008154	actin polymerization or depolymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	F		Seeded From UniProt	complete
part_of	GO:0001726	ruffle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68FP1 ensembl:ENSRNOP00000025857	C		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030004	F		Seeded From UniProt	complete
involved_in	GO:0045010	actin nucleation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030004	P		Seeded From UniProt	complete
involved_in	GO:0051014	actin filament severing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030004	P		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007122	F		Seeded From UniProt	complete
involved_in	GO:0051016	barbed-end actin filament capping	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030004	P		Seeded From UniProt	complete
involved_in	GO:0051016	barbed-end actin filament capping	PMID:1321812^[23]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:1321812^[23]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:1321812^[23]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-201622	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-977136 Reactome:R-HSA-976734 Reactome:R-HSA-6800434 Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
involved_in	GO:0030030	cell projection organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0970	P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0009	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
involved_in	GO:0051693	actin filament capping	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0117	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 De Clercq, S et al. (2013) L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages. PLoS ONE 8 e78108 PubMed GONUTS page
↑ ^3.0 ^3.1 Huff, ME et al. (2003) Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of finnish type. J. Mol. Biol. 334 119-27 PubMed GONUTS page
↑ Van Impe, K et al. (2008) A new role for nuclear transport factor 2 and Ran: nuclear import of CapG. Traffic 9 695-707 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 ^5.9 García-Expósito, L et al. (2013) Gelsolin activity controls efficient early HIV-1 infection. Retrovirology 10 39 PubMed GONUTS page
↑ Arora, PD et al. (2013) Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions. Mol. Biol. Cell 24 734-47 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Page, LJ et al. (2009) Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins. Proc. Natl. Acad. Sci. U.S.A. 106 11125-30 PubMed GONUTS page
↑ ^8.0 ^8.1 Efebera, YA et al. (2014) Novel gelsolin variant as the cause of nephrotic syndrome and renal amyloidosis in a large kindred. Amyloid 21 110-2 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Mazumdar, B et al. (2012) N-terminal region of gelsolin induces apoptosis of activated hepatic stellate cells by a caspase-dependent mechanism. PLoS ONE 7 e44461 PubMed GONUTS page
↑ Solomon, JP et al. (2009) The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic. Biochemistry 48 11370-80 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Mileo, AM et al. (2013) The human papillomavirus-16 E7 oncoprotein exerts antiapoptotic effects via its physical interaction with the actin-binding protein gelsolin. Carcinogenesis 34 2424-33 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Chumnarnsilpa, S et al. (2009) The crystal structure of the C-terminus of adseverin reveals the actin-binding interface. Proc. Natl. Acad. Sci. U.S.A. 106 13719-24 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^18.0 ^18.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page
↑ Kim, J et al. (2010) Functional genomic screen for modulators of ciliogenesis and cilium length. Nature 464 1048-51 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 Kwiatkowski, DJ et al. () Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323 455-8 PubMed GONUTS page
↑ Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Yu, FX et al. (1992) Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267 14616-21 PubMed GONUTS page

[PMID:27068509-1] Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page

[PMID:24236012-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 De Clercq, S et al. (2013) L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages. PLoS ONE 8 e78108 PubMed GONUTS page

[PMID:14596804-3] 3.0 ^3.1 Huff, ME et al. (2003) Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of finnish type. J. Mol. Biol. 334 119-27 PubMed GONUTS page

[PMID:18266911-4] Van Impe, K et al. (2008) A new role for nuclear transport factor 2 and Ran: nuclear import of CapG. Traffic 9 695-707 PubMed GONUTS page

[PMID:23575248-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 ^5.9 García-Expósito, L et al. (2013) Gelsolin activity controls efficient early HIV-1 infection. Retrovirology 10 39 PubMed GONUTS page

[PMID:23325791-6] Arora, PD et al. (2013) Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions. Mol. Biol. Cell 24 734-47 PubMed GONUTS page

[PMID:19549824-7] 7.0 ^7.1 ^7.2 ^7.3 Page, LJ et al. (2009) Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins. Proc. Natl. Acad. Sci. U.S.A. 106 11125-30 PubMed GONUTS page

[PMID:24601799-8] 8.0 ^8.1 Efebera, YA et al. (2014) Novel gelsolin variant as the cause of nephrotic syndrome and renal amyloidosis in a large kindred. Amyloid 21 110-2 PubMed GONUTS page

[PMID:22952982-9] 9.0 ^9.1 ^9.2 ^9.3 Mazumdar, B et al. (2012) N-terminal region of gelsolin induces apoptosis of activated hepatic stellate cells by a caspase-dependent mechanism. PLoS ONE 7 e44461 PubMed GONUTS page

[PMID:19904968-10] Solomon, JP et al. (2009) The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic. Biochemistry 48 11370-80 PubMed GONUTS page

[PMID:23729654-11] 11.0 ^11.1 ^11.2 Mileo, AM et al. (2013) The human papillomavirus-16 E7 oncoprotein exerts antiapoptotic effects via its physical interaction with the actin-binding protein gelsolin. Carcinogenesis 34 2424-33 PubMed GONUTS page

[PMID:19666531-12] 12.0 ^12.1 ^12.2 Chumnarnsilpa, S et al. (2009) The crystal structure of the C-terminus of adseverin reveals the actin-binding interface. Proc. Natl. Acad. Sci. U.S.A. 106 13719-24 PubMed GONUTS page

[PMID:23533145-13] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:21423176-14] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:22516433-15] Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page

[PMID:19199708-16] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:19056867-17] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-18] 18.0 ^18.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:21362503-19] Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page

[PMID:20393563-20] Kim, J et al. (2010) Functional genomic screen for modulators of ciliogenesis and cilium length. Nature 464 1048-51 PubMed GONUTS page

[PMID:3020431-21] 21.0 ^21.1 ^21.2 ^21.3 Kwiatkowski, DJ et al. () Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323 455-8 PubMed GONUTS page

[PMID:14718574-22] Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page

[PMID:1321812-23] 23.0 ^23.1 ^23.2 Yu, FX et al. (1992) Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267 14616-21 PubMed GONUTS page

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