GSN
entrez
2934
canonical
uniprot
P06396
canonical
ensembl
ENSG00000148180
resolver
ensp
ENSP00000362914
resolver
ensp
ENSP00000362924
resolver
ensp
ENSP00000362929
resolver
ensp
ENSP00000377882
resolver
ensp
ENSP00000404226
resolver
ensp
ENSP00000409358
resolver
ensp
ENSP00000445823
resolver
ensp
ENSP00000514432
resolver
ensp
ENSP00000570581
resolver
ensp
ENSP00000570589
resolver
ensp
ENSP00000570590
resolver
ensp
ENSP00000570591
resolver
ensp
ENSP00000570592
resolver
ensp
ENSP00000570593
resolver
ensp
ENSP00000570595
resolver
ensp
ENSP00000570596
resolver
ensp
ENSP00000570603
resolver
ensp
ENSP00000570647
resolver
ensp
ENSP00000570652
resolver
ensp
ENSP00000587292
resolver
ensp
ENSP00000642640
resolver
enst
ENST00000394353
resolver
enst
ENST00000449733
resolver
enst
ENST00000699558
resolver
genesymbol
GSN
resolver
hgnc
HGNC:4620
resolver
uniprot
A0A0A0MS51
resolver
uniprot
A0A0A0MT01
resolver
uniprot
A0A384MEF1
resolver
uniprot
A0A8V8TND7
resolver
uniprot
A2A418
resolver
uniprot
A8MUD1
resolver
uniprot
A8MYN7
resolver
uniprot
B7Z373
resolver
uniprot
B7Z4U6
resolver
uniprot
B7Z5V1
resolver
uniprot
F5H1A8
resolver
uniprot
Q5T0I2
resolver
uniprot
Q8WVV7
resolver
uniprot_entry
A0A0A0MS51_HUMAN
resolver
uniprot_entry
A0A0A0MT01_HUMAN
resolver
uniprot_entry
A0A384MEF1_HUMAN
resolver
uniprot_entry
A0A8V8TND7_HUMAN
resolver
uniprot_entry
B7Z4U6_HUMAN
resolver
uniprot_entry
GELS_HUMAN
resolver
uniprot_sec
A2A418
resolver
uniprot_sec
A8MUD1
resolver
uniprot_sec
A8MYN7
resolver
uniprot_sec
B7Z373
resolver
uniprot_sec
B7Z5V1
resolver
uniprot_sec
F5H1A8
resolver
uniprot_sec
Q5T0I2
resolver
uniprot_sec
Q8WVV7
resolver
amino_acid_sequence
MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA
uniprot
proteins
disease_involvement
DISEASE: Amyloidosis, hereditary systemic 4, Finnish type (AMYLD4) [MIM:105120]: A form of hereditary systemic amyloidosis, a disorder characterized by amyloid deposition in multiple tissues resulting in a wide clinical spectrum. AMYLD4 is due to gelsolin amyloid deposition and is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure. AMYLD4 is usually inherited in an autosomal dominant pattern. However, homozygotes with a more severe phenotype have also been reported. {ECO:0000269|PubMed:1338910, ECO:0000269|PubMed:19666512, ECO:0000269|PubMed:2176481}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a role in ciliogenesis (PubMed:20393563). {ECO:0000269|PubMed:19666512, ECO:0000269|PubMed:20393563}.
uniprot
proteins
mass_dalton
85698
uniprot
proteins
mutagenesis
MUTAGEN 236; /note="E->Q: Does not result in actin depolymerization activity in absence of calcium. Has actin depolymerization activity in absence of calcium; when associated with N-214 and N-697 or N-214, N-697 and Q-719."; /evidence="ECO:0000269|PubMed:19666512"; MUTAGEN 697; /note="D->N: Does not result in actin depolymerization activity in absence of calcium. Has actin depolymerization activity in absence of calcium; when associated with N-214 and Q-236, N-214 and Q-719 or N-214, Q-236 and Q-719."; /evidence="ECO:0000269|PubMed:19666512"; MUTAGEN 719; /note="E->Q: Does not result in actin depolymerization activity in absence of calcium. Has actin depolymerization activity in absence of calcium; when associated with N-214 and N-697 or N-214, Q-236 and N-697."; /evidence="ECO:0000269|PubMed:19666512
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Tyr-86, Tyr-409, Tyr-465, Tyr-603 and Tyr-651 in vitro is induced in presence of phospholipids. {ECO:0000269|PubMed:10210201}.
uniprot
proteins
protein_family
Villin/gelsolin family
uniprot
proteins
pubmed
10210201
uniprot
proteins
pubmed
12460571
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
1338910
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16466744
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
19666512
uniprot
proteins
pubmed
20393563
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2153578
uniprot
proteins
pubmed
2157434
uniprot
proteins
pubmed
2176481
uniprot
proteins
pubmed
23009842
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
3020431
uniprot
proteins
pubmed
6092370
uniprot
proteins
pubmed
8395021
uniprot
proteins
pubmed
8599675
uniprot
proteins
pubmed
8703941
uniprot
proteins
pubmed
9003812
uniprot
proteins
sequence_length
782
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
uniprot
proteins