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P06396

- GELS_HUMAN

UniProt

P06396 - GELS_HUMAN

Protein

Gelsolin

Gene

GSN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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

    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

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 2727Add
    BLAST
    Chaini28 – 782755GelsolinPRO_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-acetyllysineBy 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.1 Publication

    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.By similarity

    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

    1
    782
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06396.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 176124Actin-severingSequence AnalysisAdd
    BLAST
    Regioni123 – 1264Actin-actin interfilament contact point
    Regioni162 – 1698Polyphosphoinositide bindingBy similarity
    Regioni188 – 1969Polyphosphoinositide bindingBy similarity
    Regioni434 – 782349Actin-binding, Ca-sensitiveSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941N → D in BAH13037. (PubMed:14702039)Curated
    Sequence conflicti419 – 4191R → W in BAH13037. (PubMed:14702039)Curated
    Sequence conflicti603 – 6031Y → H in BAH13037. (PubMed:14702039)Curated

    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. 2 PublicationsVSP_018959Add
    BLAST
    Alternative sequencei1 – 4848MAPHR…VPEAR → MEKLFCCF in isoform 3. 1 PublicationVSP_042879Add
    BLAST
    Alternative sequencei1 – 4848MAPHR…VPEAR → MPLCT in isoform 4. 1 PublicationVSP_054791Add
    BLAST

    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. [P06396-4]
    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 . [P06396-4 ]
    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

    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: October 1, 2014
    This is version 180 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