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P06396 (GELS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gelsolin
Alternative name(s):
AGEL
Actin-depolymerizing factor
Short name=ADF
Brevin
Gene names
Name:GSN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. Ref.13

Subunit structure

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. Ref.7 Ref.18

Subcellular location

Isoform 2: Cytoplasmcytoskeleton.

Isoform 1: Secreted.

Tissue specificity

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

Post-translational modification

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

Involvement in disease

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. Ref.8 Ref.9 Ref.19 Ref.20

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 6 gelsolin-like repeats.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentAmyloid
Cytoplasm
Cytoskeleton
Secreted
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseAmyloidosis
Corneal dystrophy
Disease mutation
   DomainRepeat
Signal
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionActin capping
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament polymerization

Inferred from direct assay Ref.1. Source: UniProtKB

actin filament severing

Inferred from direct assay Ref.1. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

barbed-end actin filament capping

Traceable author statement PubMed 1321812. Source: ProtInc

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

cilium morphogenesis

Inferred from mutant phenotype Ref.13. Source: UniProtKB

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Traceable author statement PubMed 1321812. Source: ProtInc

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytosol

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

lamellipodium

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Traceable author statement PubMed 1321812. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 17620599. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARRB1P494073EBI-351506,EBI-743313
ARRB2P321213EBI-351506,EBI-714559

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P06396-1)

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.
Isoform 2 (identifier: P06396-2)

Also known as: Cytoplasmic;

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
Isoform 3 (identifier: P06396-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEAR → MEKLFCCF
Isoform 4 (identifier: P06396-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEAR → MPLCT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 782755Gelsolin
PRO_0000036385

Regions

Repeat76 – 12651Gelsolin-like 1
Repeat198 – 23841Gelsolin-like 2
Repeat314 – 35643Gelsolin-like 3
Repeat453 – 50452Gelsolin-like 4
Repeat576 – 61641Gelsolin-like 5
Repeat679 – 72143Gelsolin-like 6
Region53 – 176124Actin-severing Potential
Region123 – 1264Actin-actin interfilament contact point
Region162 – 1698Polyphosphoinositide binding By similarity
Region188 – 1969Polyphosphoinositide binding By similarity
Region434 – 782349Actin-binding, Ca-sensitive Potential

Sites

Metal binding4711Calcium 1; via carbonyl oxygen
Metal binding4721Calcium 1
Metal binding5021Calcium 1
Metal binding5511Calcium 1; via carbonyl oxygen
Metal binding5911Calcium 2
Metal binding5911Calcium 2; via carbonyl oxygen
Metal binding5921Calcium 2
Metal binding6141Calcium 2
Metal binding6961Calcium 3; via carbonyl oxygen
Metal binding6971Calcium 3
Metal binding7191Calcium 3

Amino acid modifications

Modified residue861Phosphotyrosine; by SRC; in vitro Ref.12
Modified residue4091Phosphotyrosine; by SRC; in vitro Ref.12
Modified residue4651Phosphotyrosine; by SRC Ref.12
Modified residue5841N6-acetyllysine By similarity
Modified residue6031Phosphotyrosine; by SRC; in vitro Ref.12
Modified residue6511Phosphotyrosine; by SRC; in vitro Ref.12
Disulfide bond215 ↔ 228In isoform 1 Ref.10 Ref.11

Natural variations

Alternative sequence1 – 5151Missing in isoform 2.
VSP_018959
Alternative sequence1 – 4848MAPHR…VPEAR → MEKLFCCF in isoform 3.
VSP_042879
Alternative sequence1 – 4848MAPHR…VPEAR → MPLCT in isoform 4.
VSP_054791
Natural variant221S → L in a breast cancer sample; somatic mutation. Ref.21
VAR_036337
Natural variant1291A → T.
Corresponds to variant rs2230287 [ dbSNP | Ensembl ].
VAR_024690
Natural variant2011T → I in a breast cancer sample; somatic mutation. Ref.21
VAR_036338
Natural variant2141D → N in AMYL5. Ref.19 Ref.20
VAR_007718
Natural variant2141D → Y in AMYL5. Ref.20
VAR_007719
Natural variant2311N → D.
Corresponds to variant rs11550199 [ dbSNP | Ensembl ].
VAR_061982
Natural variant6111S → N in a breast cancer sample; somatic mutation. Ref.21
VAR_036339
Natural variant6681R → L.
Corresponds to variant rs9696578 [ dbSNP | Ensembl ].
VAR_033958

Experimental info

Sequence conflict2941N → D in BAH13037. Ref.2
Sequence conflict4191R → W in BAH13037. Ref.2
Sequence conflict6031Y → H in BAH13037. Ref.2

Secondary structure

.................................................................................................................................................... 782
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Secreted) (Plasma) [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 8CEBC52257A160F7

FASTA78285,698
        10         20         30         40         50         60 
MAPHRPAPAL LCALSLALCA LSLPVRAATA SRGASQAGAP QGRVPEARPN SMVVEHPEFL 

        70         80         90        100        110        120 
KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT VQLRNGNLQY DLHYWLGNEC 

       130        140        150        160        170        180 
SQDESGAAAI FTVQLDDYLN GRAVQHREVQ GFESATFLGY FKSGLKYKKG GVASGFKHVV 

       190        200        210        220        230        240 
PNEVVVQRLF QVKGRRVVRA TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA 

       250        260        270        280        290        300 
TQVSKGIRDN ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE DAANRKLAKL 

       310        320        330        340        350        360 
YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA NTEERKAALK 

       370        380        390        400        410        420 
TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD QTDGLGLSYL SSHIANVERV 

       430        440        450        460        470        480 
PFDAATLHTS TAMAAQHGMD DDGTGQKQIW RIEGSNKVPV DPATYGQFYG GDSYIILYNY 

       490        500        510        520        530        540 
RHGGRQGQII YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG 

       550        560        570        580        590        600 
GKPMIIYKGG TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS NDAFVLKTPS 

       610        620        630        640        650        660 
AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG FWEALGGKAA YRTSPRLKDK 

       670        680        690        700        710        720 
KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML LDTWDQVFVW VGKDSQEEEK 

       730        740        750        760        770        780 
TEALTSAKRY IETDPANRDR RTPITVVKQG FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL 


AA 

« Hide

Isoform 2 (Cytoplasmic) [UniParc].

Checksum: 0C5C30CE497A0684
Show »

FASTA73180,641
Isoform 3 [UniParc].

Checksum: CA633F2D7DFF84DA
Show »

FASTA74281,941
Isoform 4 [UniParc].

Checksum: 61A735296139EB27
Show »

FASTA73981,485

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Calcium ion exchange in crystalline gelsolin."
Chumnarnsilpa S., Loonchanta A., Xue B., Choe H., Urosev D., Wang H., Lindberg U., Burtnick L.D., Robinson R.C.
J. Mol. Biol. 357:773-782(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 439-782, CALCIUM-BINDING SITES.
[18]"Structural states and dynamics of the D-loop in actin."
Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W., Reisler E.
Biophys. J. 103:930-939(2012) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-22; ILE-201 AND ASN-611.
+Additional computationally mapped references.

Web resources

Wikipedia

Gelsolin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS48011.1. [P06396-3]
CCDS6828.1. [P06396-1]
CCDS6829.1. [P06396-2]
PIRFAHUP. A03011.
RefSeqNP_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]
UniGeneHs.522373.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP06396.
SMRP06396. Positions 50-782.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109189. 31 interactions.
DIPDIP-2196N.
IntActP06396. 14 interactions.
MINTMINT-5000481.
STRING9606.ENSP00000362924.

PTM databases

PhosphoSiteP06396.

Polymorphism databases

DMDM121116.

2D gel databases

OGPP06396.

Proteomic databases

MaxQBP06396.
PaxDbP06396.
PeptideAtlasP06396.
PRIDEP06396.

Protocols and materials databases

DNASU2934.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341272; 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.
GeneID2934.
KEGGhsa:2934.
UCSCuc004bld.1. human. [P06396-1]
uc010mvq.1. human. [P06396-3]

Organism-specific databases

CTD2934.
GeneCardsGC09P123971.
HGNCHGNC:4620. GSN.
HPACAB010823.
CAB016728.
CAB036009.
MIM105120. phenotype.
137350. gene.
neXtProtNX_P06396.
Orphanet85448. Familial amyloidosis, Finnish type.
PharmGKBPA29011.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304849.
HOGENOMHOG000233630.
HOVERGENHBG004183.
InParanoidP06396.
KOK05768.
OMARIEKFDL.
OrthoDBEOG7288RJ.
PhylomeDBP06396.
TreeFamTF313468.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP06396.
BgeeP06396.
CleanExHS_GSN.
GenevestigatorP06396.

Family and domain databases

Gene3D3.40.20.10. 6 hits.
InterProIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERPTHR11977. PTHR11977. 1 hit.
PfamPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSPR00597. GELSOLIN.
SMARTSM00262. GEL. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSN. human.
EvolutionaryTraceP06396.
GeneWikiGelsolin.
GenomeRNAi2934.
NextBio11625.
PMAP-CutDBP06396.
PROP06396.
SOURCESearch...

Entry information

Entry nameGELS_HUMAN
AccessionPrimary (citable) accession number: P06396
Secondary accession number(s): A2A418 expand/collapse secondary AC list , A8MUD1, A8MYN7, B7Z373, B7Z5V1, F5H1A8, Q5T0I2, Q8WVV7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 178 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM