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Protein

Gelsolin

Gene

GSN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Plays a role in ciliogenesis.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi471Calcium 1; via carbonyl oxygen1
Metal bindingi472Calcium 11
Metal bindingi502Calcium 11
Metal bindingi551Calcium 1; via carbonyl oxygen1
Metal bindingi591Calcium 21
Metal bindingi591Calcium 2; via carbonyl oxygen1
Metal bindingi592Calcium 21
Metal bindingi614Calcium 21
Metal bindingi696Calcium 3; via carbonyl oxygen1
Metal bindingi697Calcium 31
Metal bindingi719Calcium 31

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • myosin II binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

  • actin filament capping Source: UniProtKB
  • actin filament polymerization Source: UniProtKB
  • actin filament reorganization Source: UniProtKB
  • actin filament severing Source: UniProtKB
  • actin nucleation Source: InterPro
  • amyloid fibril formation Source: UniProtKB
  • barbed-end actin filament capping Source: ProtInc
  • cellular protein metabolic process Source: Reactome
  • cilium morphogenesis Source: UniProtKB
  • hepatocyte apoptotic process Source: UniProtKB
  • negative regulation of viral entry into host cell Source: UniProtKB
  • phagocytosis, engulfment Source: UniProtKB
  • positive regulation of actin nucleation Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of keratinocyte apoptotic process Source: UniProtKB
  • positive regulation of protein processing in phagocytic vesicle Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • regulation of establishment of T cell polarity Source: UniProtKB
  • regulation of plasma membrane raft polarization Source: UniProtKB
  • regulation of podosome assembly Source: UniProtKB
  • regulation of receptor clustering Source: UniProtKB
  • regulation of wound healing, spreading of epidermal cells Source: UniProtKB
  • renal protein absorption Source: UniProtKB
  • sequestering of actin monomers Source: UniProtKB
  • striated muscle atrophy Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148180-MONOMER.
ReactomeiR-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP06396.

Names & Taxonomyi

Protein namesi
Recommended name:
Gelsolin
Alternative name(s):
AGEL
Actin-depolymerizing factor
Short name:
ADF
Brevin
Gene namesi
Name:GSN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:4620. GSN.

Subcellular locationi

GO - Cellular componenti

  • actin cap Source: UniProtKB
  • actin cytoskeleton Source: ProtInc
  • blood microparticle Source: UniProtKB
  • cortical actin cytoskeleton Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • podosome Source: UniProtKB
  • sarcoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechi

Involvement in diseasei

Amyloidosis 5 (AMYL5)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary generalized amyloidosis due to gelsolin amyloid deposition. It 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.
See also OMIM:105120
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007718214D → N in AMYL5. 2 PublicationsCorresponds to variant rs121909715dbSNPEnsembl.1
Natural variantiVAR_007719214D → Y in AMYL5. 1 PublicationCorresponds to variant rs121909715dbSNPEnsembl.1

Keywords - Diseasei

Amyloidosis, Corneal dystrophy, Disease mutation

Organism-specific databases

DisGeNETi2934.
MalaCardsiGSN.
MIMi105120. phenotype.
OpenTargetsiENSG00000148180.
ENSG00000283430.
Orphaneti85448. Familial amyloidosis, Finnish type.
PharmGKBiPA29011.

Polymorphism and mutation databases

BioMutaiGSN.
DMDMi121116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000003638528 – 782GelsolinAdd BLAST755

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei86Phosphotyrosine; by SRC; in vitro1 Publication1
Disulfide bondi215 ↔ 228In isoform 12 Publications
Modified residuei409Phosphotyrosine; by SRC; in vitro1 Publication1
Modified residuei465Phosphotyrosine; by SRC1 Publication1
Modified residuei584N6-acetyllysineBy similarity1
Modified residuei603Phosphotyrosine; by SRC; in vitro1 Publication1
Modified residuei651Phosphotyrosine; by SRC; in vitro1 Publication1
Modified residuei742PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation on Tyr-86, Tyr-409, Tyr-465, Tyr-603 and Tyr-651 in vitro is induced in presence of phospholipids.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP06396.
PaxDbiP06396.
PeptideAtlasiP06396.
PRIDEiP06396.

2D gel databases

OGPiP06396.

PTM databases

iPTMnetiP06396.
PhosphoSitePlusiP06396.
SwissPalmiP06396.

Miscellaneous databases

PMAP-CutDBP06396.

Expressioni

Tissue specificityi

Phagocytic cells, platelets, fibroblasts, nonmuscle cells, smooth and skeletal muscle cells.

Gene expression databases

BgeeiENSG00000148180.
CleanExiHS_GSN.
ExpressionAtlasiP06396. baseline and differential.
GenevisibleiP06396. HS.

Organism-specific databases

HPAiCAB010823.
CAB016728.
CAB036009.

Interactioni

Subunit structurei

Binds to actin and to fibronectin. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X. Interacts with the inactive form of EIF2AK2/PKR (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494073EBI-351506,EBI-743313
ARRB2P321213EBI-351506,EBI-714559

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • myosin II binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109189. 84 interactors.
DIPiDIP-2196N.
IntActiP06396. 49 interactors.
MINTiMINT-5000481.
STRINGi9606.ENSP00000362924.

Structurei

Secondary structure

1782
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 55Combined sources4
Helixi57 – 61Combined sources5
Beta strandi64 – 74Combined sources11
Beta strandi77 – 80Combined sources4
Helixi83 – 85Combined sources3
Beta strandi88 – 90Combined sources3
Beta strandi94 – 102Combined sources9
Turni104 – 106Combined sources3
Beta strandi108 – 116Combined sources9
Helixi122 – 138Combined sources17
Turni139 – 141Combined sources3
Beta strandi143 – 149Combined sources7
Helixi155 – 158Combined sources4
Beta strandi166 – 169Combined sources4
Helixi172 – 174Combined sources3
Beta strandi179 – 181Combined sources3
Beta strandi188 – 203Combined sources16
Helixi207 – 209Combined sources3
Beta strandi214 – 219Combined sources6
Beta strandi221 – 228Combined sources8
Helixi234 – 250Combined sources17
Beta strandi256 – 262Combined sources7
Turni263 – 265Combined sources3
Helixi268 – 274Combined sources7
Helixi288 – 294Combined sources7
Beta strandi299 – 304Combined sources6
Beta strandi306 – 309Combined sources4
Beta strandi311 – 321Combined sources11
Helixi323 – 325Combined sources3
Beta strandi330 – 336Combined sources7
Helixi337 – 339Combined sources3
Beta strandi341 – 346Combined sources6
Helixi352 – 368Combined sources17
Beta strandi376 – 381Combined sources6
Helixi387 – 390Combined sources4
Beta strandi393 – 395Combined sources3
Beta strandi402 – 406Combined sources5
Helixi412 – 414Combined sources3
Turni424 – 426Combined sources3
Helixi427 – 429Combined sources3
Helixi431 – 437Combined sources7
Beta strandi445 – 453Combined sources9
Beta strandi456 – 459Combined sources4
Helixi462 – 464Combined sources3
Beta strandi467 – 469Combined sources3
Beta strandi472 – 482Combined sources11
Beta strandi485 – 494Combined sources10
Helixi500 – 516Combined sources17
Turni517 – 519Combined sources3
Beta strandi521 – 527Combined sources7
Helixi533 – 536Combined sources4
Helixi537 – 539Combined sources3
Beta strandi544 – 548Combined sources5
Turni553 – 555Combined sources3
Beta strandi562 – 570Combined sources9
Beta strandi576 – 581Combined sources6
Helixi585 – 587Combined sources3
Beta strandi592 – 597Combined sources6
Beta strandi602 – 606Combined sources5
Helixi612 – 624Combined sources13
Beta strandi630 – 633Combined sources4
Helixi639 – 644Combined sources6
Beta strandi645 – 647Combined sources3
Helixi655 – 658Combined sources4
Helixi661 – 664Combined sources4
Beta strandi668 – 673Combined sources6
Turni675 – 677Combined sources3
Beta strandi680 – 684Combined sources5
Helixi690 – 692Combined sources3
Beta strandi697 – 702Combined sources6
Beta strandi707 – 711Combined sources5
Helixi717 – 732Combined sources16
Turni735 – 737Combined sources3
Beta strandi744 – 748Combined sources5
Helixi754 – 757Combined sources4
Beta strandi760 – 762Combined sources3
Beta strandi765 – 767Combined sources3
Helixi772 – 778Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C0FX-ray2.40S53-176[»]
1C0GX-ray2.00S53-176[»]
1D4XX-ray1.75G52-177[»]
1DEJX-ray2.40S53-176[»]
1EQYX-ray2.30S52-176[»]
1ESVX-ray2.00S52-176[»]
1H1VX-ray3.00G439-769[»]
1KCQX-ray1.65A185-288[»]
1MDUX-ray2.20A/D52-176[»]
1NLVX-ray1.80G52-176[»]
1NM1X-ray1.80G52-176[»]
1NMDX-ray1.90G52-176[»]
1P8XX-ray2.00A/B/C439-782[»]
1P8ZX-ray2.60G52-187[»]
1SOLNMR-A177-196[»]
1T44X-ray2.00G55-179[»]
1YAGX-ray1.90G52-176[»]
1YVNX-ray2.10G52-176[»]
2FF3X-ray2.00A52-179[»]
2FF6X-ray2.05G52-179[»]
2FH1X-ray1.55A/B/C439-782[»]
2FH2X-ray2.50A/B/C439-782[»]
2FH3X-ray2.87A/B/C439-782[»]
2FH4X-ray3.00A/B/C439-782[»]
3A5LX-ray2.40S53-176[»]
3A5MX-ray2.40S53-176[»]
3A5NX-ray2.36S53-176[»]
3A5OX-ray2.40S53-176[»]
3CI5X-ray1.70G52-176[»]
3CIPX-ray1.60G52-176[»]
3CJBX-ray3.21G52-176[»]
3CJCX-ray3.90G52-176[»]
3FFKX-ray3.00A/D52-426[»]
3FFNX-ray3.00A/B1-782[»]
3TU5X-ray3.00B53-174[»]
4PKGX-ray1.80G52-176[»]
4PKHX-ray2.15B/E/G/J52-176[»]
B/E/G/J196-260[»]
4PKIX-ray2.30G52-176[»]
4S10X-ray2.61C/D186-288[»]
4Z94X-ray2.40G52-176[»]
5DD2X-ray2.60A/G55-188[»]
5FAEX-ray1.70A178-293[»]
5FAFX-ray1.05A178-293[»]
ProteinModelPortaliP06396.
SMRiP06396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati76 – 126Gelsolin-like 1Add BLAST51
Repeati198 – 238Gelsolin-like 2Add BLAST41
Repeati314 – 356Gelsolin-like 3Add BLAST43
Repeati453 – 504Gelsolin-like 4Add BLAST52
Repeati576 – 616Gelsolin-like 5Add BLAST41
Repeati679 – 721Gelsolin-like 6Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 176Actin-severingSequence analysisAdd BLAST124
Regioni123 – 126Actin-actin interfilament contact point4
Regioni162 – 169Polyphosphoinositide bindingBy similarity8
Regioni188 – 196Polyphosphoinositide bindingBy similarity9
Regioni434 – 782Actin-binding, Ca-sensitiveSequence analysisAdd BLAST349

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 6 gelsolin-like repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP06396.
KOiK05768.
OMAiANMEERK.
OrthoDBiEOG091G05SC.
PhylomeDBiP06396.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR030004. Gelsolin.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF29. PTHR11977:SF29. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P06396-1) [UniParc]FASTAAdd to basket
Also known as: Secreted, Plasma

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPHRPAPAL LCALSLALCA LSLPVRAATA SRGASQAGAP QGRVPEARPN
60 70 80 90 100
SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT
110 120 130 140 150
VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN GRAVQHREVQ
160 170 180 190 200
GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVVVQRLF QVKGRRVVRA
210 220 230 240 250
TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA TQVSKGIRDN
260 270 280 290 300
ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE DAANRKLAKL
310 320 330 340 350
YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA
360 370 380 390 400
NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD
410 420 430 440 450
QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD DDGTGQKQIW
460 470 480 490 500
RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII YNWQGAQSTQ
510 520 530 540 550
DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG GKPMIIYKGG
560 570 580 590 600
TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS NDAFVLKTPS
610 620 630 640 650
AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG FWEALGGKAA
660 670 680 690 700
YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML
710 720 730 740 750
LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR RTPITVVKQG
760 770 780
FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL AA
Length:782
Mass (Da):85,698
Last modified:January 1, 1988 - v1
Checksum:i8CEBC52257A160F7
GO
Isoform 2 (identifier: P06396-2) [UniParc]FASTAAdd to basket
Also known as: Cytoplasmic

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Show »
Length:731
Mass (Da):80,641
Checksum:i0C5C30CE497A0684
GO
Isoform 3 (identifier: P06396-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEAR → MEKLFCCF

Show »
Length:742
Mass (Da):81,941
Checksum:iCA633F2D7DFF84DA
GO
Isoform 4 (identifier: P06396-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEAR → MPLCT

Note: No experimental confirmation available.
Show »
Length:739
Mass (Da):81,485
Checksum:i61A735296139EB27
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti294N → D in BAH13037 (PubMed:14702039).Curated1
Sequence conflicti419R → W in BAH13037 (PubMed:14702039).Curated1
Sequence conflicti603Y → H in BAH13037 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03633722S → L in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_024690129A → T.Corresponds to variant rs2230287dbSNPEnsembl.1
Natural variantiVAR_036338201T → I in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_007718214D → N in AMYL5. 2 PublicationsCorresponds to variant rs121909715dbSNPEnsembl.1
Natural variantiVAR_007719214D → Y in AMYL5. 1 PublicationCorresponds to variant rs121909715dbSNPEnsembl.1
Natural variantiVAR_061982231N → D.Corresponds to variant rs11550199dbSNPEnsembl.1
Natural variantiVAR_036339611S → N in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_033958668R → L.Corresponds to variant rs9696578dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189591 – 51Missing in isoform 2. 2 PublicationsAdd BLAST51
Alternative sequenceiVSP_0428791 – 48MAPHR…VPEAR → MEKLFCCF in isoform 3. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_0547911 – 48MAPHR…VPEAR → MPLCT in isoform 4. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04412 mRNA. Translation: CAA28000.1.
AK096280 mRNA. Translation: BAG53247.1.
AK125819 mRNA. Translation: BAG54252.1.
AK295572 mRNA. Translation: BAH12109.1.
AK299453 mRNA. Translation: BAH13037.1.
AK315494 mRNA. Translation: BAG37878.1.
AL137068 Genomic DNA. No translation available.
AL513122 Genomic DNA. Translation: CAI14413.1.
AL513122 Genomic DNA. Translation: CAM20459.1.
CH471090 Genomic DNA. Translation: EAW87489.1.
CH471090 Genomic DNA. Translation: EAW87490.1.
CH471090 Genomic DNA. Translation: EAW87491.1.
BC017491 mRNA. Translation: AAH17491.1.
BC026033 mRNA. Translation: AAH26033.1.
CCDSiCCDS48011.1. [P06396-3]
CCDS65118.1. [P06396-4]
CCDS6828.1. [P06396-1]
CCDS6829.1. [P06396-2]
PIRiA03011. FAHUP.
RefSeqiNP_000168.1. NM_000177.4. [P06396-1]
NP_001121134.1. NM_001127662.1. [P06396-2]
NP_001121135.2. NM_001127663.1.
NP_001121136.1. NM_001127664.1. [P06396-2]
NP_001121137.1. NM_001127665.1. [P06396-2]
NP_001121138.1. NM_001127666.1. [P06396-3]
NP_001121139.1. NM_001127667.1. [P06396-3]
NP_001244958.1. NM_001258029.1.
NP_001244959.1. NM_001258030.1. [P06396-4]
NP_937895.1. NM_198252.2. [P06396-2]
XP_005252000.1. XM_005251943.1. [P06396-3]
XP_005252001.1. XM_005251944.1. [P06396-3]
XP_005252002.1. XM_005251945.3. [P06396-2]
XP_006717142.1. XM_006717079.1. [P06396-3]
XP_011516888.1. XM_011518586.1. [P06396-3]
XP_011516889.1. XM_011518587.2. [P06396-3]
XP_011516890.1. XM_011518588.2. [P06396-3]
XP_011516891.1. XM_011518589.2. [P06396-3]
XP_011516892.1. XM_011518590.2. [P06396-3]
XP_011516893.1. XM_011518591.2. [P06396-2]
XP_011516894.1. XM_011518592.1. [P06396-2]
XP_011516895.1. XM_011518593.1. [P06396-2]
XP_016870135.1. XM_017014646.1. [P06396-3]
XP_016870136.1. XM_017014647.1. [P06396-3]
XP_016870137.1. XM_017014648.1. [P06396-3]
UniGeneiHs.522373.

Genome annotation databases

EnsembliENST00000373818; ENSP00000362924; ENSG00000148180. [P06396-1]
ENST00000373823; ENSP00000362929; ENSG00000148180. [P06396-2]
ENST00000545652; ENSP00000445823; ENSG00000148180. [P06396-4]
GeneIDi2934.
KEGGihsa:2934.
UCSCiuc004ble.1. human. [P06396-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Gelsolin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04412 mRNA. Translation: CAA28000.1.
AK096280 mRNA. Translation: BAG53247.1.
AK125819 mRNA. Translation: BAG54252.1.
AK295572 mRNA. Translation: BAH12109.1.
AK299453 mRNA. Translation: BAH13037.1.
AK315494 mRNA. Translation: BAG37878.1.
AL137068 Genomic DNA. No translation available.
AL513122 Genomic DNA. Translation: CAI14413.1.
AL513122 Genomic DNA. Translation: CAM20459.1.
CH471090 Genomic DNA. Translation: EAW87489.1.
CH471090 Genomic DNA. Translation: EAW87490.1.
CH471090 Genomic DNA. Translation: EAW87491.1.
BC017491 mRNA. Translation: AAH17491.1.
BC026033 mRNA. Translation: AAH26033.1.
CCDSiCCDS48011.1. [P06396-3]
CCDS65118.1. [P06396-4]
CCDS6828.1. [P06396-1]
CCDS6829.1. [P06396-2]
PIRiA03011. FAHUP.
RefSeqiNP_000168.1. NM_000177.4. [P06396-1]
NP_001121134.1. NM_001127662.1. [P06396-2]
NP_001121135.2. NM_001127663.1.
NP_001121136.1. NM_001127664.1. [P06396-2]
NP_001121137.1. NM_001127665.1. [P06396-2]
NP_001121138.1. NM_001127666.1. [P06396-3]
NP_001121139.1. NM_001127667.1. [P06396-3]
NP_001244958.1. NM_001258029.1.
NP_001244959.1. NM_001258030.1. [P06396-4]
NP_937895.1. NM_198252.2. [P06396-2]
XP_005252000.1. XM_005251943.1. [P06396-3]
XP_005252001.1. XM_005251944.1. [P06396-3]
XP_005252002.1. XM_005251945.3. [P06396-2]
XP_006717142.1. XM_006717079.1. [P06396-3]
XP_011516888.1. XM_011518586.1. [P06396-3]
XP_011516889.1. XM_011518587.2. [P06396-3]
XP_011516890.1. XM_011518588.2. [P06396-3]
XP_011516891.1. XM_011518589.2. [P06396-3]
XP_011516892.1. XM_011518590.2. [P06396-3]
XP_011516893.1. XM_011518591.2. [P06396-2]
XP_011516894.1. XM_011518592.1. [P06396-2]
XP_011516895.1. XM_011518593.1. [P06396-2]
XP_016870135.1. XM_017014646.1. [P06396-3]
XP_016870136.1. XM_017014647.1. [P06396-3]
XP_016870137.1. XM_017014648.1. [P06396-3]
UniGeneiHs.522373.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C0FX-ray2.40S53-176[»]
1C0GX-ray2.00S53-176[»]
1D4XX-ray1.75G52-177[»]
1DEJX-ray2.40S53-176[»]
1EQYX-ray2.30S52-176[»]
1ESVX-ray2.00S52-176[»]
1H1VX-ray3.00G439-769[»]
1KCQX-ray1.65A185-288[»]
1MDUX-ray2.20A/D52-176[»]
1NLVX-ray1.80G52-176[»]
1NM1X-ray1.80G52-176[»]
1NMDX-ray1.90G52-176[»]
1P8XX-ray2.00A/B/C439-782[»]
1P8ZX-ray2.60G52-187[»]
1SOLNMR-A177-196[»]
1T44X-ray2.00G55-179[»]
1YAGX-ray1.90G52-176[»]
1YVNX-ray2.10G52-176[»]
2FF3X-ray2.00A52-179[»]
2FF6X-ray2.05G52-179[»]
2FH1X-ray1.55A/B/C439-782[»]
2FH2X-ray2.50A/B/C439-782[»]
2FH3X-ray2.87A/B/C439-782[»]
2FH4X-ray3.00A/B/C439-782[»]
3A5LX-ray2.40S53-176[»]
3A5MX-ray2.40S53-176[»]
3A5NX-ray2.36S53-176[»]
3A5OX-ray2.40S53-176[»]
3CI5X-ray1.70G52-176[»]
3CIPX-ray1.60G52-176[»]
3CJBX-ray3.21G52-176[»]
3CJCX-ray3.90G52-176[»]
3FFKX-ray3.00A/D52-426[»]
3FFNX-ray3.00A/B1-782[»]
3TU5X-ray3.00B53-174[»]
4PKGX-ray1.80G52-176[»]
4PKHX-ray2.15B/E/G/J52-176[»]
B/E/G/J196-260[»]
4PKIX-ray2.30G52-176[»]
4S10X-ray2.61C/D186-288[»]
4Z94X-ray2.40G52-176[»]
5DD2X-ray2.60A/G55-188[»]
5FAEX-ray1.70A178-293[»]
5FAFX-ray1.05A178-293[»]
ProteinModelPortaliP06396.
SMRiP06396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109189. 84 interactors.
DIPiDIP-2196N.
IntActiP06396. 49 interactors.
MINTiMINT-5000481.
STRINGi9606.ENSP00000362924.

PTM databases

iPTMnetiP06396.
PhosphoSitePlusiP06396.
SwissPalmiP06396.

Polymorphism and mutation databases

BioMutaiGSN.
DMDMi121116.

2D gel databases

OGPiP06396.

Proteomic databases

EPDiP06396.
PaxDbiP06396.
PeptideAtlasiP06396.
PRIDEiP06396.

Protocols and materials databases

DNASUi2934.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373818; ENSP00000362924; ENSG00000148180. [P06396-1]
ENST00000373823; ENSP00000362929; ENSG00000148180. [P06396-2]
ENST00000545652; ENSP00000445823; ENSG00000148180. [P06396-4]
GeneIDi2934.
KEGGihsa:2934.
UCSCiuc004ble.1. human. [P06396-1]

Organism-specific databases

CTDi2934.
DisGeNETi2934.
GeneCardsiGSN.
HGNCiHGNC:4620. GSN.
HPAiCAB010823.
CAB016728.
CAB036009.
MalaCardsiGSN.
MIMi105120. phenotype.
137350. gene.
neXtProtiNX_P06396.
OpenTargetsiENSG00000148180.
ENSG00000283430.
Orphaneti85448. Familial amyloidosis, Finnish type.
PharmGKBiPA29011.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP06396.
KOiK05768.
OMAiANMEERK.
OrthoDBiEOG091G05SC.
PhylomeDBiP06396.
TreeFamiTF313468.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148180-MONOMER.
ReactomeiR-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP06396.

Miscellaneous databases

ChiTaRSiGSN. human.
EvolutionaryTraceiP06396.
GeneWikiiGelsolin.
GenomeRNAii2934.
PMAP-CutDBP06396.
PROiP06396.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000148180.
CleanExiHS_GSN.
ExpressionAtlasiP06396. baseline and differential.
GenevisibleiP06396. HS.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR030004. Gelsolin.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF29. PTHR11977:SF29. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGELS_HUMAN
AccessioniPrimary (citable) accession number: P06396
Secondary accession number(s): A2A418
, A8MUD1, A8MYN7, B7Z373, B7Z5V1, F5H1A8, Q5T0I2, Q8WVV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 30, 2016
This is version 204 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.