P06396 (GELS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gelsolin

Alternative name(s):
AGEL
Actin-depolymerizing factor
Short name=ADF
Brevin

Gene names

Name:

GSN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	782 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.7 Ref.18
Subcellular location	Isoform 2: Cytoplasm › cytoskeleton. 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 process	Cilium biogenesis/degradation
Cellular component	Amyloid Cytoplasm Cytoskeleton Secreted
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Disease	Amyloidosis Corneal dystrophy Disease mutation
Domain	Repeat Signal
Ligand	Actin-binding Calcium Metal-binding
Molecular function	Actin capping
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin 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: Compara 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: Compara cilium morphogenesis Inferred from mutant phenotype Ref.13. Source: UniProtKB oligodendrocyte development Inferred from electronic annotation. Source: Compara phosphatidylinositol-mediated signaling Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to folic acid Inferred from electronic annotation. Source: Compara tissue regeneration Inferred from electronic annotation. Source: Compara vesicle-mediated transport Inferred from electronic annotation. Source: Compara
Cellular_component	actin cytoskeleton Traceable author statement PubMed 1321812. Source: ProtInc cytosol Inferred from direct assay Ref.1. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB lamellipodium Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara ruffle Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Traceable author statement PubMed 1321812. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	3	EBI-351506,EBI-743313
ARRB2	P32121	3	EBI-351506,EBI-714559

Alternative products

This entry describes 3 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.

Note: Initiator Met-1 may be either removed, or N-acetylated.

Isoform 3 (identifier: P06396-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Chain

28 – 782

755

Gelsolin

PRO_0000036385

Regions

Repeat

76 – 126

51

Gelsolin-like 1

Repeat

198 – 238

41

Gelsolin-like 2

Repeat

314 – 356

43

Gelsolin-like 3

Repeat

453 – 504

52

Gelsolin-like 4

Repeat

576 – 616

41

Gelsolin-like 5

Repeat

679 – 721

43

Gelsolin-like 6

Region

53 – 176

124

Actin-severing Potential

Region

123 – 126

4

Actin-actin interfilament contact point

Region

162 – 169

8

Polyphosphoinositide binding By similarity

Region

188 – 196

9

Polyphosphoinositide binding By similarity

Region

434 – 782

349

Actin-binding, Ca-sensitive Potential

Sites

Metal binding

471

1

Calcium 1; via carbonyl oxygen

Metal binding

472

1

Calcium 1

Metal binding

502

1

Calcium 1

Metal binding

551

1

Calcium 1; via carbonyl oxygen

Metal binding

591

1

Calcium 2

Metal binding

591

1

Calcium 2; via carbonyl oxygen

Metal binding

592

1

Calcium 2

Metal binding

614

1

Calcium 2

Metal binding

696

1

Calcium 3; via carbonyl oxygen

Metal binding

697

1

Calcium 3

Metal binding

719

1

Calcium 3

Amino acid modifications

Modified residue

86

1

Phosphotyrosine; by SRC; in vitro Ref.12

Modified residue

409

1

Phosphotyrosine; by SRC; in vitro Ref.12

Modified residue

465

1

Phosphotyrosine; by SRC Ref.12

Modified residue

603

1

Phosphotyrosine; by SRC; in vitro Ref.12

Modified residue

651

1

Phosphotyrosine; by SRC; in vitro Ref.12

Disulfide bond

215 ↔ 228

In isoform 1 Ref.10 Ref.11

Natural variations

Alternative sequence

1 – 51

51

Missing in isoform 2.

VSP_018959

Alternative sequence

1 – 48

48

MAPHR…VPEAR → MEKLFCCF in isoform 3.

VSP_042879

Natural variant

22

1

S → L in a breast cancer sample; somatic mutation. Ref.21

VAR_036337

Natural variant

129

1

A → T.
Corresponds to variant rs2230287 [ dbSNP | Ensembl ].

VAR_024690

Natural variant

201

1

T → I in a breast cancer sample; somatic mutation. Ref.21

VAR_036338

Natural variant

214

1

D → N in AMYL5. Ref.19 Ref.20

VAR_007718

Natural variant

214

1

D → Y in AMYL5. Ref.20

VAR_007719

Natural variant

231

1

N → D.
Corresponds to variant rs11550199 [ dbSNP | Ensembl ].

VAR_061982

Natural variant

611

1

S → N in a breast cancer sample; somatic mutation. Ref.21

VAR_036339

Natural variant

668

1

R → L.
Corresponds to variant rs9696578 [ dbSNP | Ensembl ].

VAR_033958

Secondary structure

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782

Helix Strand Turn

Details...

Beta strand

52 – 55

4

Helix

57 – 61

5

Beta strand

64 – 74

11

Beta strand

77 – 80

4

Helix

83 – 85

3

Beta strand

88 – 90

3

Beta strand

94 – 102

9

Turn

104 – 106

3

Beta strand

108 – 116

9

Helix

122 – 138

17

Turn

139 – 141

3

Beta strand

143 – 149

7

Helix

155 – 158

4

Beta strand

166 – 169

4

Helix

172 – 174

3

Beta strand

179 – 181

3

Beta strand

188 – 203

16

Helix

207 – 209

3

Beta strand

214 – 219

6

Beta strand

221 – 228

8

Helix

234 – 250

17

Beta strand

256 – 262

7

Turn

263 – 265

3

Helix

268 – 274

7

Helix

288 – 294

7

Beta strand

299 – 304

6

Beta strand

306 – 309

4

Beta strand

311 – 321

11

Helix

323 – 325

3

Beta strand

330 – 336

7

Helix

337 – 339

3

Beta strand

341 – 346

6

Helix

352 – 368

17

Beta strand

376 – 381

6

Helix

387 – 390

4

Beta strand

393 – 395

3

Beta strand

402 – 406

5

Helix

412 – 414

3

Turn

424 – 426

3

Helix

427 – 429

3

Helix

431 – 437

7

Beta strand

445 – 453

9

Beta strand

456 – 459

4

Helix

462 – 464

3

Beta strand

467 – 469

3

Beta strand

472 – 482

11

Beta strand

485 – 494

10

Helix

500 – 516

17

Turn

517 – 519

3

Beta strand

521 – 527

7

Helix

533 – 536

4

Helix

537 – 539

3

Beta strand

544 – 548

5

Turn

553 – 555

3

Beta strand

562 – 570

9

Beta strand

576 – 581

6

Helix

585 – 587

3

Beta strand

592 – 597

6

Beta strand

602 – 606

5

Helix

612 – 624

13

Beta strand

630 – 633

4

Helix

639 – 644

6

Beta strand

645 – 647

3

Helix

655 – 658

4

Helix

661 – 664

4

Beta strand

668 – 673

6

Turn

675 – 677

3

Beta strand

680 – 684

5

Helix

690 – 692

3

Beta strand

697 – 702

6

Beta strand

707 – 711

5

Helix

717 – 732

16

Beta strand

744 – 748

5

Helix

754 – 757

4

Beta strand

760 – 762

3

Beta strand

765 – 767

3

Helix

772 – 778

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Secreted) (Plasma) [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 8CEBC52257A160F7	FASTA	782	85,698
	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
	Isoform 2 (Cytoplasmic) [UniParc]. Checksum: 0C5C30CE497A0684	FASTA	731	80,641
	10 20 30 40 50 60 MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PTNLYGDFFT GDAYVILKTV QLRNGNLQYD 70 80 90 100 110 120 LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG FESATFLGYF KSGLKYKKGG 130 140 150 160 170 180 VASGFKHVVP NEVVVQRLFQ VKGRRVVRAT EVPVSWESFN NGDCFILDLG NNIHQWCGSN 190 200 210 220 230 240 SNRYERLKAT QVSKGIRDNE RSGRARVHVS EEGTEPEAML QVLGPKPALP AGTEDTAKED 250 260 270 280 290 300 AANRKLAKLY KVSNGAGTMS VSLVADENPF AQGALKSEDC FILDHGKDGK IFVWKGKQAN 310 320 330 340 350 360 TEERKAALKT ASDFITKMDY PKQTQVSVLP EGGETPLFKQ FFKNWRDPDQ TDGLGLSYLS 370 380 390 400 410 420 SHIANVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR IEGSNKVPVD PATYGQFYGG 430 440 450 460 470 480 DSYIILYNYR HGGRQGQIIY NWQGAQSTQD EVAASAILTA QLDEELGGTP VQSRVVQGKE 490 500 510 520 530 540 PAHLMSLFGG KPMIIYKGGT SREGGQTAPA STRLFQVRAN SAGATRAVEV LPKAGALNSN 550 560 570 580 590 600 DAFVLKTPSA AYLWVGTGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDGF WEALGGKAAY 610 620 630 640 650 660 RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGELMQE DLATDDVMLL DTWDQVFVWV 670 680 690 700 710 720 GKDSQEEEKT EALTSAKRYI ETDPANRDRR TPITVVKQGF EPPSFVGWFL GWDDDYWSVD 730 PLDRAMAELA A
	Isoform 3 [UniParc]. Checksum: CA633F2D7DFF84DA	FASTA	742	81,941
	10 20 30 40 50 60 MEKLFCCFPN SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT 70 80 90 100 110 120 VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN GRAVQHREVQ GFESATFLGY 130 140 150 160 170 180 FKSGLKYKKG GVASGFKHVV PNEVVVQRLF QVKGRRVVRA TEVPVSWESF NNGDCFILDL 190 200 210 220 230 240 GNNIHQWCGS NSNRYERLKA TQVSKGIRDN ERSGRARVHV SEEGTEPEAM LQVLGPKPAL 250 260 270 280 290 300 PAGTEDTAKE DAANRKLAKL YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG 310 320 330 340 350 360 KIFVWKGKQA NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD 370 380 390 400 410 420 QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD DDGTGQKQIW RIEGSNKVPV 430 440 450 460 470 480 DPATYGQFYG GDSYIILYNY RHGGRQGQII YNWQGAQSTQ DEVAASAILT AQLDEELGGT 490 500 510 520 530 540 PVQSRVVQGK EPAHLMSLFG GKPMIIYKGG TSREGGQTAP ASTRLFQVRA NSAGATRAVE 550 560 570 580 590 600 VLPKAGALNS NDAFVLKTPS AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG 610 620 630 640 650 660 FWEALGGKAA YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML 670 680 690 700 710 720 LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR RTPITVVKQG FEPPSFVGWF 730 740 LGWDDDYWSV DPLDRAMAEL AA

References

	« Hide 'large scale' referencesShow '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. , 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 AND 3). 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]	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. , 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. , 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

GeneReviews

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.
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.

IPI

IPI00026314.
IPI00646773.
IPI00647556.

PIR

FAHUP. A03011.

RefSeq

NP_000168.1. NM_000177.4.
NP_001121134.1. NM_001127662.1.
NP_001121135.2. NM_001127663.1.
NP_001121136.1. NM_001127664.1.
NP_001121137.1. NM_001127665.1.
NP_001121138.1. NM_001127666.1.
NP_001121139.1. NM_001127667.1.
NP_001244958.1. NM_001258029.1.
NP_001244959.1. NM_001258030.1.
NP_937895.1. NM_198252.2.

UniGene

Hs.522373.

3D structure databases

PDBe
RCSB PDB
PDBj

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	51-179	[»]
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	[»]

ProteinModelPortal

P06396.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2196N.

IntAct

P06396. 12 interactions.

MINT

MINT-5000481.

STRING

9606.ENSP00000362924.

PTM databases

PhosphoSite

P06396.

Polymorphism databases

DMDM

121116.

2D gel databases

OGP

P06396.

Proteomic databases

PaxDb

P06396.

PeptideAtlas

P06396.

PRIDE

P06396.

Protocols and materials databases

DNASU

2934.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341272; ENSP00000340888; ENSG00000148180.
ENST00000373808; ENSP00000362914; ENSG00000148180.
ENST00000373818; ENSP00000362924; ENSG00000148180.
ENST00000373823; ENSP00000362929; ENSG00000148180.
ENST00000394353; ENSP00000377882; ENSG00000148180.
ENST00000412819; ENSP00000416586; ENSG00000148180.
ENST00000436847; ENSP00000411293; ENSG00000148180.
ENST00000449733; ENSP00000409358; ENSG00000148180.

GeneID

2934.

KEGG

hsa:2934.

UCSC

uc004bld.1. human.

Organism-specific databases

CTD

2934.

GeneCards

GC09P123971.

HGNC

HGNC:4620. GSN.

HPA

CAB010823.
CAB016728.
CAB036009.

MIM

105120. phenotype.
137350. gene.

neXtProt

NX_P06396.

Orphanet

85448. Familial amyloidosis, Finnish type.

PharmGKB

PA29011.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG304849.

HOGENOM

HOG000233630.

HOVERGEN

HBG004183.

InParanoid

P06396.

KO

K05768.

OMA

PKHTQVQ.

PhylomeDB

P06396.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
ar_pathway. Coregulation of Androgen receptor activity.
faspathway. FAS signaling pathway (CD95).
avb3_opn_pathway. Osteopontin-mediated events.

Reactome

REACT_116125. Disease.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P06396.

Bgee

P06396.

CleanEx

HS_GSN.

Genevestigator

P06396.

GermOnline

ENSG00000148180. Homo sapiens.

Family and domain databases

InterPro

IPR007123. Gelsolin_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]

PANTHER

PTHR11977. PTHR11977. 1 hit.

Pfam

PF00626. Gelsolin. 6 hits.
[Graphical view]

PRINTS

PR00597. GELSOLIN.

SMART

SM00262. GEL. 6 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GSN. human.

EvolutionaryTrace

P06396.

GenomeRNAi

2934.

NextBio

11625.

PMAP-CutDB

P06396.

SOURCE

Search...

Entry information

Entry name

GELS_HUMAN

Accession

Primary (citable) accession number: P06396
Secondary accession number(s): A2A418 , A8MUD1, A8MYN7, B7Z373, Q5T0I2, Q8WVV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 166 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.