SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06396

- GELS_HUMAN

UniProt

P06396 - GELS_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Gelsolin
Gene
GSN
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi471 – 4711Calcium 1; via carbonyl oxygen
Metal bindingi472 – 4721Calcium 1
Metal bindingi502 – 5021Calcium 1
Metal bindingi551 – 5511Calcium 1; via carbonyl oxygen
Metal bindingi591 – 5911Calcium 2
Metal bindingi591 – 5911Calcium 2; via carbonyl oxygen
Metal bindingi592 – 5921Calcium 2
Metal bindingi614 – 6141Calcium 2
Metal bindingi696 – 6961Calcium 3; via carbonyl oxygen
Metal bindingi697 – 6971Calcium 3
Metal bindingi719 – 7191Calcium 3

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. protein binding Source: IntAct

GO - Biological processi

  1. actin filament polymerization Source: UniProtKB
  2. actin filament severing Source: UniProtKB
  3. aging Source: Ensembl
  4. apoptotic process Source: Reactome
  5. barbed-end actin filament capping Source: ProtInc
  6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  7. cellular response to cadmium ion Source: Ensembl
  8. cilium morphogenesis Source: UniProtKB
  9. oligodendrocyte development Source: Ensembl
  10. phosphatidylinositol-mediated signaling Source: Ensembl
  11. regulation of cell adhesion Source: Ensembl
  12. response to ethanol Source: Ensembl
  13. response to folic acid Source: Ensembl
  14. tissue regeneration Source: Ensembl
  15. vesicle-mediated transport Source: Ensembl
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

ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_75925. Amyloids.

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:4620. GSN.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. blood microparticle Source: UniProt
  3. cytosol Source: UniProtKB
  4. extracellular region Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. lamellipodium Source: Ensembl
  7. perinuclear region of cytoplasm Source: Ensembl
  8. protein complex Source: Ensembl
  9. ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechi

Involvement in diseasei

Amyloidosis 5 (AMYL5) [MIM:105120]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141D → N in AMYL5. 2 Publications
VAR_007718
Natural varianti214 – 2141D → Y in AMYL5. 1 Publication
VAR_007719

Keywords - Diseasei

Amyloidosis, Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi105120. phenotype.
Orphaneti85448. Familial amyloidosis, Finnish type.
PharmGKBiPA29011.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727
Add
BLAST
Chaini28 – 782755Gelsolin
PRO_0000036385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861Phosphotyrosine; by SRC; in vitro1 Publication
Disulfide bondi215 ↔ 228In isoform 12 Publications
Modified residuei409 – 4091Phosphotyrosine; by SRC; in vitro1 Publication
Modified residuei465 – 4651Phosphotyrosine; by SRC1 Publication
Modified residuei584 – 5841N6-acetyllysine By similarity
Modified residuei603 – 6031Phosphotyrosine; by SRC; in vitro1 Publication
Modified residuei651 – 6511Phosphotyrosine; by SRC; in vitro1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP06396.
PaxDbiP06396.
PeptideAtlasiP06396.
PRIDEiP06396.

2D gel databases

OGPiP06396.

PTM databases

PhosphoSiteiP06396.

Miscellaneous databases

PMAP-CutDBP06396.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP06396.
BgeeiP06396.
CleanExiHS_GSN.
GenevestigatoriP06396.

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.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109189. 31 interactions.
DIPiDIP-2196N.
IntActiP06396. 14 interactions.
MINTiMINT-5000481.
STRINGi9606.ENSP00000362924.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 554
Helixi57 – 615
Beta strandi64 – 7411
Beta strandi77 – 804
Helixi83 – 853
Beta strandi88 – 903
Beta strandi94 – 1029
Turni104 – 1063
Beta strandi108 – 1169
Helixi122 – 13817
Turni139 – 1413
Beta strandi143 – 1497
Helixi155 – 1584
Beta strandi166 – 1694
Helixi172 – 1743
Beta strandi179 – 1813
Beta strandi188 – 20316
Helixi207 – 2093
Beta strandi214 – 2196
Beta strandi221 – 2288
Helixi234 – 25017
Beta strandi256 – 2627
Turni263 – 2653
Helixi268 – 2747
Helixi288 – 2947
Beta strandi299 – 3046
Beta strandi306 – 3094
Beta strandi311 – 32111
Helixi323 – 3253
Beta strandi330 – 3367
Helixi337 – 3393
Beta strandi341 – 3466
Helixi352 – 36817
Beta strandi376 – 3816
Helixi387 – 3904
Beta strandi393 – 3953
Beta strandi402 – 4065
Helixi412 – 4143
Turni424 – 4263
Helixi427 – 4293
Helixi431 – 4377
Beta strandi445 – 4539
Beta strandi456 – 4594
Helixi462 – 4643
Beta strandi467 – 4693
Beta strandi472 – 48211
Beta strandi485 – 49410
Helixi500 – 51617
Turni517 – 5193
Beta strandi521 – 5277
Helixi533 – 5364
Helixi537 – 5393
Beta strandi544 – 5485
Turni553 – 5553
Beta strandi562 – 5709
Beta strandi576 – 5816
Helixi585 – 5873
Beta strandi592 – 5976
Beta strandi602 – 6065
Helixi612 – 62413
Beta strandi630 – 6334
Helixi639 – 6446
Beta strandi645 – 6473
Helixi655 – 6584
Helixi661 – 6644
Beta strandi668 – 6736
Turni675 – 6773
Beta strandi680 – 6845
Helixi690 – 6923
Beta strandi697 – 7026
Beta strandi707 – 7115
Helixi717 – 73216
Beta strandi744 – 7485
Helixi754 – 7574
Beta strandi760 – 7623
Beta strandi765 – 7673
Helixi772 – 7787

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP06396.
SMRiP06396. Positions 50-782.

Miscellaneous databases

EvolutionaryTraceiP06396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati76 – 12651Gelsolin-like 1
Add
BLAST
Repeati198 – 23841Gelsolin-like 2
Add
BLAST
Repeati314 – 35643Gelsolin-like 3
Add
BLAST
Repeati453 – 50452Gelsolin-like 4
Add
BLAST
Repeati576 – 61641Gelsolin-like 5
Add
BLAST
Repeati679 – 72143Gelsolin-like 6
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 176124Actin-severing Reviewed prediction
Add
BLAST
Regioni123 – 1264Actin-actin interfilament contact point
Regioni162 – 1698Polyphosphoinositide binding By similarity
Regioni188 – 1969Polyphosphoinositide binding By similarity
Regioni434 – 782349Actin-binding, Ca-sensitive Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the villin/gelsolin family.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG304849.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP06396.
KOiK05768.
OMAiRIEKFDL.
OrthoDBiEOG7288RJ.
PhylomeDBiP06396.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 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. Align

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

MAPHRPAPAL LCALSLALCA LSLPVRAATA SRGASQAGAP QGRVPEARPN    50
SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT 100
VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN GRAVQHREVQ 150
GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVVVQRLF QVKGRRVVRA 200
TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA TQVSKGIRDN 250
ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE DAANRKLAKL 300
YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA 350
NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD 400
QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD DDGTGQKQIW 450
RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII YNWQGAQSTQ 500
DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG GKPMIIYKGG 550
TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS NDAFVLKTPS 600
AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG FWEALGGKAA 650
YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML 700
LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR RTPITVVKQG 750
FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL AA 782
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221S → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036337
Natural varianti129 – 1291A → T.
Corresponds to variant rs2230287 [ dbSNP | Ensembl ].
VAR_024690
Natural varianti201 – 2011T → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_036338
Natural varianti214 – 2141D → N in AMYL5. 2 Publications
VAR_007718
Natural varianti214 – 2141D → Y in AMYL5. 1 Publication
VAR_007719
Natural varianti231 – 2311N → D.
Corresponds to variant rs11550199 [ dbSNP | Ensembl ].
VAR_061982
Natural varianti611 – 6111S → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036339
Natural varianti668 – 6681R → L.
Corresponds to variant rs9696578 [ dbSNP | Ensembl ].
VAR_033958

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform 2.
VSP_018959Add
BLAST
Alternative sequencei1 – 4848MAPHR…VPEAR → MEKLFCCF in isoform 3.
VSP_042879Add
BLAST
Alternative sequencei1 – 4848MAPHR…VPEAR → MPLCT in isoform 4.
VSP_054791Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941N → D in BAH13037. 1 Publication
Sequence conflicti419 – 4191R → W in BAH13037. 1 Publication
Sequence conflicti603 – 6031Y → H in BAH13037. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005251945.2. [P06396-2]
XP_006717139.1. XM_006717076.1. [P06396-3]
XP_006717140.1. XM_006717077.1. [P06396-3]
XP_006717141.1. XM_006717078.1. [P06396-3]
XP_006717142.1. XM_006717079.1. [P06396-3]
UniGeneiHs.522373.

Genome annotation databases

EnsembliENST00000341272; ENSP00000340888; ENSG00000148180. [P06396-2]
ENST00000373808; ENSP00000362914; ENSG00000148180. [P06396-2]
ENST00000373818; ENSP00000362924; ENSG00000148180. [P06396-1]
ENST00000373823; ENSP00000362929; ENSG00000148180. [P06396-2]
ENST00000394353; ENSP00000377882; ENSG00000148180. [P06396-3]
ENST00000412819; ENSP00000416586; ENSG00000148180. [P06396-2]
ENST00000436847; ENSP00000411293; ENSG00000148180. [P06396-3]
ENST00000449733; ENSP00000409358; ENSG00000148180. [P06396-2]
ENST00000545652; ENSP00000445823; ENSG00000148180.
GeneIDi2934.
KEGGihsa:2934.
UCSCiuc004bld.1. human. [P06396-1]
uc010mvq.1. human. [P06396-3]

Polymorphism databases

DMDMi121116.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Gelsolin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS48011.1. [P06396-3 ]
CCDS65118.1. [P06396-4 ]
CCDS6828.1. [P06396-1 ]
CCDS6829.1. [P06396-2 ]
PIRi A03011. FAHUP.
RefSeqi NP_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_005251945.2. [P06396-2 ]
XP_006717139.1. XM_006717076.1. [P06396-3 ]
XP_006717140.1. XM_006717077.1. [P06396-3 ]
XP_006717141.1. XM_006717078.1. [P06396-3 ]
XP_006717142.1. XM_006717079.1. [P06396-3 ]
UniGenei Hs.522373.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C0F X-ray 2.40 S 53-176 [» ]
1C0G X-ray 2.00 S 53-176 [» ]
1D4X X-ray 1.75 G 52-177 [» ]
1DEJ X-ray 2.40 S 53-176 [» ]
1EQY X-ray 2.30 S 52-176 [» ]
1ESV X-ray 2.00 S 52-176 [» ]
1H1V X-ray 3.00 G 439-769 [» ]
1KCQ X-ray 1.65 A 185-288 [» ]
1MDU X-ray 2.20 A/D 52-176 [» ]
1NLV X-ray 1.80 G 52-176 [» ]
1NM1 X-ray 1.80 G 52-176 [» ]
1NMD X-ray 1.90 G 52-176 [» ]
1P8X X-ray 2.00 A/B/C 439-782 [» ]
1P8Z X-ray 2.60 G 52-187 [» ]
1SOL NMR - A 177-196 [» ]
1T44 X-ray 2.00 G 55-179 [» ]
1YAG X-ray 1.90 G 52-176 [» ]
1YVN X-ray 2.10 G 52-176 [» ]
2FF3 X-ray 2.00 A 52-179 [» ]
2FF6 X-ray 2.05 G 52-179 [» ]
2FH1 X-ray 1.55 A/B/C 439-782 [» ]
2FH2 X-ray 2.50 A/B/C 439-782 [» ]
2FH3 X-ray 2.87 A/B/C 439-782 [» ]
2FH4 X-ray 3.00 A/B/C 439-782 [» ]
3A5L X-ray 2.40 S 53-176 [» ]
3A5M X-ray 2.40 S 53-176 [» ]
3A5N X-ray 2.36 S 53-176 [» ]
3A5O X-ray 2.40 S 53-176 [» ]
3CI5 X-ray 1.70 G 52-176 [» ]
3CIP X-ray 1.60 G 52-176 [» ]
3CJB X-ray 3.21 G 52-176 [» ]
3CJC X-ray 3.90 G 52-176 [» ]
3FFK X-ray 3.00 A/D 52-426 [» ]
3FFN X-ray 3.00 A/B 1-782 [» ]
3TU5 X-ray 3.00 B 53-174 [» ]
ProteinModelPortali P06396.
SMRi P06396. Positions 50-782.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109189. 31 interactions.
DIPi DIP-2196N.
IntActi P06396. 14 interactions.
MINTi MINT-5000481.
STRINGi 9606.ENSP00000362924.

PTM databases

PhosphoSitei P06396.

Polymorphism databases

DMDMi 121116.

2D gel databases

OGPi P06396.

Proteomic databases

MaxQBi P06396.
PaxDbi P06396.
PeptideAtlasi P06396.
PRIDEi P06396.

Protocols and materials databases

DNASUi 2934.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341272 ; ENSP00000340888 ; ENSG00000148180 . [P06396-2 ]
ENST00000373808 ; ENSP00000362914 ; ENSG00000148180 . [P06396-2 ]
ENST00000373818 ; ENSP00000362924 ; ENSG00000148180 . [P06396-1 ]
ENST00000373823 ; ENSP00000362929 ; ENSG00000148180 . [P06396-2 ]
ENST00000394353 ; ENSP00000377882 ; ENSG00000148180 . [P06396-3 ]
ENST00000412819 ; ENSP00000416586 ; ENSG00000148180 . [P06396-2 ]
ENST00000436847 ; ENSP00000411293 ; ENSG00000148180 . [P06396-3 ]
ENST00000449733 ; ENSP00000409358 ; ENSG00000148180 . [P06396-2 ]
ENST00000545652 ; ENSP00000445823 ; ENSG00000148180 .
GeneIDi 2934.
KEGGi hsa:2934.
UCSCi uc004bld.1. human. [P06396-1 ]
uc010mvq.1. human. [P06396-3 ]

Organism-specific databases

CTDi 2934.
GeneCardsi GC09P123971.
HGNCi HGNC:4620. GSN.
HPAi CAB010823.
CAB016728.
CAB036009.
MIMi 105120. phenotype.
137350. gene.
neXtProti NX_P06396.
Orphaneti 85448. Familial amyloidosis, Finnish type.
PharmGKBi PA29011.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304849.
HOGENOMi HOG000233630.
HOVERGENi HBG004183.
InParanoidi P06396.
KOi K05768.
OMAi RIEKFDL.
OrthoDBi EOG7288RJ.
PhylomeDBi P06396.
TreeFami TF313468.

Enzyme and pathway databases

Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSi GSN. human.
EvolutionaryTracei P06396.
GeneWikii Gelsolin.
GenomeRNAii 2934.
NextBioi 11625.
PMAP-CutDB P06396.
PROi P06396.
SOURCEi Search...

Gene expression databases

ArrayExpressi P06396.
Bgeei P06396.
CleanExi HS_GSN.
Genevestigatori P06396.

Family and domain databases

Gene3Di 3.40.20.10. 6 hits.
InterProi IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view ]
PANTHERi PTHR11977. PTHR11977. 1 hit.
Pfami PF00626. Gelsolin. 6 hits.
[Graphical view ]
PRINTSi PR00597. GELSOLIN.
SMARTi SM00262. GEL. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain."
    Kwiatkowski D.J., Stossel T.P., Orkin S.H., Mole J.E., Colten H.R., Yin H.L.
    Nature 323:455-458(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Hippocampus, Testis and Tongue.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon and Pancreas.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 53-72 (ISOFORM 2).
    Tissue: Platelet.
  7. "Human plasma gelsolin binds to fibronectin."
    Lind S.E., Janmey P.A.
    J. Biol. Chem. 259:13262-13266(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FIBRONECTIN.
  8. "Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein."
    Haltia M., Prelli F., Ghiso J., Kiuru S., Sommer H., Palo J., Frangione B.
    Biochem. Biophys. Res. Commun. 167:927-932(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF AMYL5 AMYLOID PROTEIN WITH GELSOLIN.
  9. "Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline."
    Maury C.P.J., Alli K., Baumann M.
    FEBS Lett. 260:85-87(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF AMYL5 AMYLOID PROTEIN WITH GELSOLIN.
  10. "The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure."
    Wen D., Corina K., Chow E.P., Miller S., Janmey P.A., Pepinsky R.B.
    Biochemistry 35:9700-9709(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  11. "Functional consequences of disulfide bond formation in gelsolin."
    Allen P.G.
    FEBS Lett. 401:89-94(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  12. "Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: a mass spectrometric approach."
    De Corte V., Demol H., Goethals M., Van Damme J., Gettemans J., Vandekerckhove J.
    Protein Sci. 8:234-241(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-86; TYR-409; TYR-465; TYR-603 AND TYR-651.
  13. "Functional genomic screen for modulators of ciliogenesis and cilium length."
    Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
    Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structure of gelsolin segment 1-actin complex and the mechanism of filament severing."
    McLaughlin P.J., Gooch J.T., Mannherz H.-G., Weeds A.G.
    Nature 364:685-692(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-503.
  16. "Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles."
    Xian W., Vegners R., Janmey P.A., Braunlin W.H.
    Biophys. J. 69:2695-2702(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 177-196.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 439-782, CALCIUM-BINDING SITES.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 53-174 IN COMPLEX WITH ACTA1; COBL AND TMSB4X, SUBUNIT.
  19. "Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type."
    Ghiso J., Haltia M., Prelli F., Novello J., Frangione B.
    Biochem. J. 272:827-830(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AMYL5 ASN-214.
  20. "Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187."
    de la Chapelle A., Tolvanen R., Boysen G., Santavy J., Bleeker-Wagemakers L., Maury C.P.J., Kere J.
    Nat. Genet. 2:157-160(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AMYL5 ASN-214 AND TYR-214.
  21. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-22; ILE-201 AND ASN-611.

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: September 3, 2014
This is version 179 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

External Data

Dasty 3

Similar proteinsi