GSN

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	471	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	472	Calcium 1	1
Metal bindingⁱ	502	Calcium 1	1
Metal bindingⁱ	551	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	591	Calcium 2	1
Metal bindingⁱ	591	Calcium 2; via carbonyl oxygen	1
Metal bindingⁱ	592	Calcium 2	1
Metal bindingⁱ	614	Calcium 2	1
Metal bindingⁱ	696	Calcium 3; via carbonyl oxygen	1
Metal bindingⁱ	697	Calcium 3	1
Metal bindingⁱ	719	Calcium 3	1

GO - Molecular functionⁱ

actin binding
Source: UniProtKB
Inferred from direct assayⁱ
- "A new role for nuclear transport factor 2 and Ran: nuclear import of CapG."
  Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C., Vandekerckhove J., Gettemans J.
  Traffic 9:695-707(2008) [PubMed] [Europe PMC] [Abstract]
- "L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages."
  De Clercq S., Boucherie C., Vandekerckhove J., Gettemans J., Guillabert A.
  PLoS ONE 8:e78108-e78108(2013) [PubMed] [Europe PMC] [Abstract]
actin filament binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
calcium ion binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- "Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of finnish type."
  Huff M.E., Page L.J., Balch W.E., Kelly J.W.
  J. Mol. Biol. 334:119-127(2003) [PubMed] [Europe PMC] [Abstract]
myosin II binding
Source: UniProtKB
Inferred from physical interactionⁱ
- "Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions."
  Arora P.D., Wang Y., Bresnick A., Dawson J., Janmey P.A., McCulloch C.A.
  Mol. Biol. Cell 24:734-747(2013) [PubMed] [Europe PMC] [Abstract]
phosphatidylinositol-4,5-bisphosphate binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Actin capping, Actin-binding
Biological process	Cilium biogenesis/degradation
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

PathwayCommonsⁱ	P06396
Reactomeⁱ	R-HSA-264870, Caspase-mediated cleavage of cytoskeletal proteins R-HSA-6798695, Neutrophil degranulation R-HSA-977225, Amyloid fiber formation
SABIO-RKⁱ	P06396
SIGNORⁱ	P06396

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Gelsolin Alternative name(s): AGEL Actin-depolymerizing factor Short name: ADF Brevin
Gene namesⁱ	Name:GSN
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 9

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000148180.17
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4620, GSN
MIMⁱ	137350, gene
neXtProtⁱ	NX_P06396

Keywords - Cellular componentⁱ

Amyloid, Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Amyloidosis 5 (AMYL5)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_007718	214	D → N in AMYL5. 2 PublicationsCorresponds to variant dbSNP:rs121909715Ensembl.		1
Natural variantⁱVAR_007719	214	D → Y in AMYL5. 1 PublicationCorresponds to variant dbSNP:rs121909715Ensembl.		1

Keywords - Diseaseⁱ

Amyloidosis, Corneal dystrophy, Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2934
MalaCards human disease database More...MalaCardsⁱ	GSN
MIMⁱ	105120, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000148180
Orphanetⁱ	85448, AGel amyloidosis
PharmGKBⁱ	PA29011

Miscellaneous databases

Pharosⁱ	P06396, Tbio

Pharosⁱ

P06396, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL4295700
Drug and drug target database More...DrugBankⁱ	DB09130, Copper DB02621, Latrunculin A DB01593, Zinc DB14487, Zinc acetate

Polymorphism and mutation databases

BioMutaⁱ	GSN
DMDMⁱ	121116

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 27	Add BLAST		27
ChainⁱPRO_0000036385	28 – 782	GelsolinAdd BLAST		755

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	86	Phosphotyrosine; by SRC; in vitro1 Publication	1
Disulfide bondⁱ	215 ↔ 228	In isoform 12 Publications
Modified residueⁱ	409	Phosphotyrosine; by SRC; in vitro1 Publication	1
Modified residueⁱ	465	Phosphotyrosine; by SRC1 Publication	1
Modified residueⁱ	584	N6-acetyllysineBy similarity	1
Modified residueⁱ	603	Phosphotyrosine; by SRC; in vitro1 Publication	1
Modified residueⁱ	651	Phosphotyrosine; by SRC; in vitro1 Publication	1
Modified residueⁱ	742	PhosphothreonineCombined sources	1

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

The CPTAC Assay portal More...CPTACⁱ	non-CPTAC-1126 non-CPTAC-1127
EPDⁱ	P06396
jPOSTⁱ	P06396
MassIVEⁱ	P06396
PaxDbⁱ	P06396
PeptideAtlas More...PeptideAtlasⁱ	P06396
PRIDEⁱ	P06396
ProteomicsDBⁱ	12635 [P06396-3] 25596 51897 [P06396-1] 51898 [P06396-2] 51899 [P06396-3]

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	P06396

OGPⁱ

P06396

PTM databases

GlyGenⁱ	P06396, 8 sites, 3 O-linked glycans (8 sites)
iPTMnetⁱ	P06396
MetOSiteⁱ	P06396
PhosphoSitePlusⁱ	P06396
SwissPalmⁱ	P06396

Expressionⁱ

Tissue specificityⁱ

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

Gene expression databases

Bgeeⁱ	ENSG00000148180, Expressed in adipose tissue of abdominal region and 255 other tissues
ExpressionAtlasⁱ	P06396, baseline and differential
Genevisibleⁱ	P06396, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000148180, Low tissue specificity

HPAⁱ

ENSG00000148180, Low tissue specificity

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

Hide details

P06396

With	#Exp.	IntAct
AR [P10275]	2	EBI-351506,EBI-608057
ARRB1 [P49407]	3	EBI-351506,EBI-743313
ARRB2 [P32121]	3	EBI-351506,EBI-714559
act21 [P07830] from Dictyostelium discoideum.	4	EBI-351506,EBI-7195234
ACTA1 [P68135] from Oryctolagus cuniculus.	10	EBI-351506,EBI-367540

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	109189, 117 interactors
CORUMⁱ	P06396
Database of interacting proteins More...DIPⁱ	DIP-2196N
IntActⁱ	P06396, 92 interactors
Molecular INTeraction database More...MINTⁱ	P06396
STRINGⁱ	9606.ENSP00000362924

Miscellaneous databases

RNActⁱ	P06396, protein

RNActⁱ

P06396, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	52 – 55	Combined sources	4
Helixⁱ	57 – 61	Combined sources	5
Beta strandⁱ	64 – 74	Combined sources	11
Beta strandⁱ	77 – 80	Combined sources	4
Helixⁱ	83 – 85	Combined sources	3
Beta strandⁱ	88 – 90	Combined sources	3
Beta strandⁱ	94 – 102	Combined sources	9
Turnⁱ	104 – 106	Combined sources	3
Beta strandⁱ	108 – 116	Combined sources	9
Helixⁱ	122 – 138	Combined sources	17
Turnⁱ	139 – 141	Combined sources	3
Beta strandⁱ	143 – 149	Combined sources	7
Beta strandⁱ	150 – 152	Combined sources	3
Helixⁱ	155 – 158	Combined sources	4
Beta strandⁱ	166 – 169	Combined sources	4
Turnⁱ	172 – 175	Combined sources	4
Turnⁱ	176 – 178	Combined sources	3
Beta strandⁱ	179 – 181	Combined sources	3
Helixⁱ	183 – 186	Combined sources	4
Beta strandⁱ	188 – 193	Combined sources	6
Beta strandⁱ	195 – 197	Combined sources	3
Beta strandⁱ	199 – 203	Combined sources	5
Helixⁱ	207 – 209	Combined sources	3
Beta strandⁱ	214 – 219	Combined sources	6
Beta strandⁱ	221 – 228	Combined sources	8
Beta strandⁱ	230 – 232	Combined sources	3
Helixⁱ	234 – 251	Combined sources	18
Beta strandⁱ	256 – 262	Combined sources	7
Turnⁱ	263 – 265	Combined sources	3
Helixⁱ	268 – 274	Combined sources	7
Helixⁱ	292 – 294	Combined sources	3
Beta strandⁱ	299 – 304	Combined sources	6
Beta strandⁱ	306 – 309	Combined sources	4
Beta strandⁱ	311 – 316	Combined sources	6
Beta strandⁱ	318 – 321	Combined sources	4
Helixⁱ	323 – 325	Combined sources	3
Beta strandⁱ	330 – 336	Combined sources	7
Helixⁱ	337 – 339	Combined sources	3
Beta strandⁱ	341 – 346	Combined sources	6
Helixⁱ	352 – 368	Combined sources	17
Beta strandⁱ	377 – 381	Combined sources	5
Helixⁱ	387 – 390	Combined sources	4
Beta strandⁱ	393 – 395	Combined sources	3
Beta strandⁱ	401 – 406	Combined sources	6
Helixⁱ	412 – 414	Combined sources	3
Helixⁱ	424 – 429	Combined sources	6
Helixⁱ	431 – 437	Combined sources	7
Beta strandⁱ	445 – 453	Combined sources	9
Beta strandⁱ	456 – 459	Combined sources	4
Helixⁱ	462 – 464	Combined sources	3
Beta strandⁱ	467 – 469	Combined sources	3
Beta strandⁱ	472 – 482	Combined sources	11
Beta strandⁱ	485 – 494	Combined sources	10
Helixⁱ	500 – 516	Combined sources	17
Turnⁱ	517 – 519	Combined sources	3
Beta strandⁱ	521 – 527	Combined sources	7
Helixⁱ	533 – 536	Combined sources	4
Helixⁱ	537 – 539	Combined sources	3
Beta strandⁱ	544 – 548	Combined sources	5
Turnⁱ	553 – 555	Combined sources	3
Beta strandⁱ	562 – 570	Combined sources	9
Beta strandⁱ	576 – 581	Combined sources	6
Helixⁱ	585 – 587	Combined sources	3
Beta strandⁱ	592 – 597	Combined sources	6
Beta strandⁱ	602 – 606	Combined sources	5
Helixⁱ	612 – 624	Combined sources	13
Beta strandⁱ	630 – 633	Combined sources	4
Helixⁱ	639 – 644	Combined sources	6
Beta strandⁱ	645 – 647	Combined sources	3
Helixⁱ	655 – 658	Combined sources	4
Helixⁱ	661 – 664	Combined sources	4
Beta strandⁱ	668 – 673	Combined sources	6
Beta strandⁱ	676 – 678	Combined sources	3
Beta strandⁱ	680 – 684	Combined sources	5
Helixⁱ	690 – 692	Combined sources	3
Beta strandⁱ	697 – 702	Combined sources	6
Beta strandⁱ	707 – 711	Combined sources	5
Helixⁱ	717 – 732	Combined sources	16
Turnⁱ	735 – 737	Combined sources	3
Beta strandⁱ	744 – 748	Combined sources	5
Helixⁱ	754 – 757	Combined sources	4
Beta strandⁱ	760 – 762	Combined sources	3
Helixⁱ	767 – 769	Combined sources	3
Helixⁱ	772 – 778	Combined sources	7

Show more details

3D structure databases

SMRⁱ	P06396
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P06396

EvolutionaryTraceⁱ

P06396

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	76 – 126	Gelsolin-like 1Add BLAST	51
Repeatⁱ	198 – 238	Gelsolin-like 2Add BLAST	41
Repeatⁱ	314 – 356	Gelsolin-like 3Add BLAST	43
Repeatⁱ	453 – 504	Gelsolin-like 4Add BLAST	52
Repeatⁱ	576 – 616	Gelsolin-like 5Add BLAST	41
Repeatⁱ	679 – 721	Gelsolin-like 6Add BLAST	43

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	53 – 176	Actin-severingSequence analysisAdd BLAST	124
Regionⁱ	123 – 126	Actin-actin interfilament contact point	4
Regionⁱ	162 – 169	Polyphosphoinositide bindingBy similarity	8
Regionⁱ	188 – 196	Polyphosphoinositide bindingBy similarity	9
Regionⁱ	434 – 782	Actin-binding, Ca-sensitiveSequence analysisAdd BLAST	349

Sequence similaritiesⁱ

Belongs to the villin/gelsolin family.Curated

Keywords - Domainⁱ

Repeat, Signal

Phylogenomic databases

eggNOGⁱ	KOG0443, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155591
HOGENOMⁱ	CLU_002568_3_2_1
InParanoidⁱ	P06396
KEGG Orthology (KO) More...KOⁱ	K05768
OMAⁱ	EWPQTPD
Database of Orthologous Groups More...OrthoDBⁱ	1376537at2759
PhylomeDBⁱ	P06396
TreeFamⁱ	TF313468

Family and domain databases

Gene3Dⁱ	3.40.20.10, 6 hits
IDEALⁱ	IID00265
InterProⁱ	View protein in InterPro IPR029006, ADF-H/Gelsolin-like_dom_sf IPR030004, Gelsolin IPR007123, Gelsolin-like_dom IPR007122, Villin/Gelsolin
PANTHERⁱ	PTHR11977, PTHR11977, 1 hit PTHR11977:SF29, PTHR11977:SF29, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00626, Gelsolin, 6 hits
PRINTSⁱ	PR00597, GELSOLIN
SMARTⁱ	View protein in SMART SM00262, GEL, 6 hits

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 Add to basket

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P06396-1) [UniParc]FASTA Add to basket

Also known as: Secreted, Plasma

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

« Hide

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

Length:782

Mass (Da):85,698

Last modified:January 1, 1988 - v1

Checksum:ⁱ8CEBC52257A160F7

GO

Isoform 2 (identifier: P06396-2) [UniParc]FASTA Add to basket

Also known as: Cytoplasmic

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

« Hide

        10         20         30         40         50
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PTNLYGDFFT GDAYVILKTV 
        60         70         80         90        100
QLRNGNLQYD LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG 
       110        120        130        140        150
FESATFLGYF KSGLKYKKGG VASGFKHVVP NEVVVQRLFQ VKGRRVVRAT 
       160        170        180        190        200
EVPVSWESFN NGDCFILDLG NNIHQWCGSN SNRYERLKAT QVSKGIRDNE 
       210        220        230        240        250
RSGRARVHVS EEGTEPEAML QVLGPKPALP AGTEDTAKED AANRKLAKLY 
       260        270        280        290        300
KVSNGAGTMS VSLVADENPF AQGALKSEDC FILDHGKDGK IFVWKGKQAN 
       310        320        330        340        350
TEERKAALKT ASDFITKMDY PKQTQVSVLP EGGETPLFKQ FFKNWRDPDQ 
       360        370        380        390        400
TDGLGLSYLS SHIANVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR 
       410        420        430        440        450
IEGSNKVPVD PATYGQFYGG DSYIILYNYR HGGRQGQIIY NWQGAQSTQD 
       460        470        480        490        500
EVAASAILTA QLDEELGGTP VQSRVVQGKE PAHLMSLFGG KPMIIYKGGT 
       510        520        530        540        550
SREGGQTAPA STRLFQVRAN SAGATRAVEV LPKAGALNSN DAFVLKTPSA 
       560        570        580        590        600
AYLWVGTGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDGF WEALGGKAAY 
       610        620        630        640        650
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGELMQE DLATDDVMLL 
       660        670        680        690        700
DTWDQVFVWV GKDSQEEEKT EALTSAKRYI ETDPANRDRR TPITVVKQGF 
       710        720        730 
EPPSFVGWFL GWDDDYWSVD PLDRAMAELA A

Show »

Length:731

Mass (Da):80,641

Checksum:ⁱ0C5C30CE497A0684

GO

Isoform 3 (identifier: P06396-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MEKLFCCFPN SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF 
        60         70         80         90        100
TGDAYVILKT VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN 
       110        120        130        140        150
GRAVQHREVQ GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVVVQRLF 
       160        170        180        190        200
QVKGRRVVRA TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA 
       210        220        230        240        250
TQVSKGIRDN ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE 
       260        270        280        290        300
DAANRKLAKL YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG 
       310        320        330        340        350
KIFVWKGKQA NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK 
       360        370        380        390        400
QFFKNWRDPD QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD 
       410        420        430        440        450
DDGTGQKQIW RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII 
       460        470        480        490        500
YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG 
       510        520        530        540        550
GKPMIIYKGG TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS 
       560        570        580        590        600
NDAFVLKTPS AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG 
       610        620        630        640        650
FWEALGGKAA YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ 
       660        670        680        690        700
EDLATDDVML LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR 
       710        720        730        740 
RTPITVVKQG FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL AA

Show »

Length:742

Mass (Da):81,941

Checksum:ⁱCA633F2D7DFF84DA

GO

Isoform 4 (identifier: P06396-4) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MPLCTPNSMV VEHPEFLKAG KEPGLQIWRV EKFDLVPVPT NLYGDFFTGD 
        60         70         80         90        100
AYVILKTVQL RNGNLQYDLH YWLGNECSQD ESGAAAIFTV QLDDYLNGRA 
       110        120        130        140        150
VQHREVQGFE SATFLGYFKS GLKYKKGGVA SGFKHVVPNE VVVQRLFQVK 
       160        170        180        190        200
GRRVVRATEV PVSWESFNNG DCFILDLGNN IHQWCGSNSN RYERLKATQV 
       210        220        230        240        250
SKGIRDNERS GRARVHVSEE GTEPEAMLQV LGPKPALPAG TEDTAKEDAA 
       260        270        280        290        300
NRKLAKLYKV SNGAGTMSVS LVADENPFAQ GALKSEDCFI LDHGKDGKIF 
       310        320        330        340        350
VWKGKQANTE ERKAALKTAS DFITKMDYPK QTQVSVLPEG GETPLFKQFF 
       360        370        380        390        400
KNWRDPDQTD GLGLSYLSSH IANVERVPFD AATLHTSTAM AAQHGMDDDG 
       410        420        430        440        450
TGQKQIWRIE GSNKVPVDPA TYGQFYGGDS YIILYNYRHG GRQGQIIYNW 
       460        470        480        490        500
QGAQSTQDEV AASAILTAQL DEELGGTPVQ SRVVQGKEPA HLMSLFGGKP 
       510        520        530        540        550
MIIYKGGTSR EGGQTAPAST RLFQVRANSA GATRAVEVLP KAGALNSNDA 
       560        570        580        590        600
FVLKTPSAAY LWVGTGASEA EKTGAQELLR VLRAQPVQVA EGSEPDGFWE 
       610        620        630        640        650
ALGGKAAYRT SPRLKDKKMD AHPPRLFACS NKIGRFVIEE VPGELMQEDL 
       660        670        680        690        700
ATDDVMLLDT WDQVFVWVGK DSQEEEKTEA LTSAKRYIET DPANRDRRTP 
       710        720        730 
ITVVKQGFEP PSFVGWFLGW DDDYWSVDPL DRAMAELAA

Show »

Length:739

Mass (Da):81,485

Checksum:ⁱ61A735296139EB27

GO

Computationally mapped potential isoform sequencesⁱ

There are 5 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0A0MS51	A0A0A0MS51_HUMAN	Actin-depolymerizing factor Actin-depolymerizing factor (Brevin) (Gelsolin)	GSN	748	Annotation score:
A0A0A0MT01	A0A0A0MT01_HUMAN	Actin-depolymerizing factor Actin-depolymerizing factor (Brevin) (Gelsolin)	GSN	767	Annotation score:
Q5T0I0	Q5T0I0_HUMAN	Actin-depolymerizing factor Actin-depolymerizing factor (Brevin) (Gelsolin)	GSN	260	Annotation score:
A0A0U1RQL8	A0A0U1RQL8_HUMAN	Actin-depolymerizing factor Actin-depolymerizing factor (Brevin) (Gelsolin)	GSN	232	Annotation score:
Q5T0H8	Q5T0H8_HUMAN	Actin-depolymerizing factor Actin-depolymerizing factor (Brevin) (Gelsolin)	GSN	67	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	294	N → D in BAH13037 (PubMed:14702039).Curated	1
Sequence conflictⁱ	419	R → W in BAH13037 (PubMed:14702039).Curated	1
Sequence conflictⁱ	603	Y → H in BAH13037 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_036337	22	S → L in a breast cancer sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_024690	129	A → T. Corresponds to variant dbSNP:rs2230287Ensembl.	1
Natural variantⁱVAR_036338	201	T → I in a breast cancer sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_007718	214	D → N in AMYL5. 2 PublicationsCorresponds to variant dbSNP:rs121909715Ensembl.	1
Natural variantⁱVAR_007719	214	D → Y in AMYL5. 1 PublicationCorresponds to variant dbSNP:rs121909715Ensembl.	1
Natural variantⁱVAR_061982	231	N → D. Corresponds to variant dbSNP:rs11550199Ensembl.	1
Natural variantⁱVAR_036339	611	S → N in a breast cancer sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_033958	668	R → L. Corresponds to variant dbSNP:rs9696578Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_018959	1 – 51	Missing in isoform 2. 2 PublicationsAdd BLAST	51
Alternative sequenceⁱVSP_042879	1 – 48	MAPHR…VPEAR → MEKLFCCF in isoform 3. 1 PublicationAdd BLAST	48
Alternative sequenceⁱVSP_054791	1 – 48	MAPHR…VPEAR → MPLCT in isoform 4. 1 PublicationAdd BLAST	48

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04412 mRNA Translation: CAA28000.1 AK096280 mRNA Translation: BAG53247.1 AK125819 mRNA Translation: BAG54252.1 AK295572 mRNA Translation: BAH12109.1 AK299453 mRNA Translation: BAH13037.1 AK315494 mRNA Translation: BAG37878.1 AL137068 Genomic DNA No translation available. AL513122 Genomic DNA No translation available. 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS48011.1 [P06396-3] CCDS65118.1 [P06396-4] CCDS6828.1 [P06396-1] CCDS6829.1 [P06396-2]
PIRⁱ	A03011, FAHUP
NCBI Reference Sequences More...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 XP_005252001.1, XM_005251944.1 [P06396-3] XP_005252002.1, XM_005251945.3 XP_006717142.1, XM_006717079.1 XP_011516888.1, XM_011518586.1 XP_011516889.1, XM_011518587.2 XP_011516890.1, XM_011518588.2 XP_011516891.1, XM_011518589.2 XP_011516892.1, XM_011518590.2 XP_011516893.1, XM_011518591.2 XP_011516894.1, XM_011518592.1 XP_011516895.1, XM_011518593.1 [P06396-2] XP_016870135.1, XM_017014646.1 XP_016870136.1, XM_017014647.1 XP_016870137.1, XM_017014648.1 [P06396-3]

Genome annotation databases

Ensemblⁱ	ENST00000373808; ENSP00000362914; ENSG00000148180 [P06396-3] ENST00000373818; ENSP00000362924; ENSG00000148180 [P06396-1] ENST00000373823; ENSP00000362929; ENSG00000148180 [P06396-2] ENST00000545652; ENSP00000445823; ENSG00000148180 [P06396-4]
GeneIDⁱ	2934
KEGGⁱ	hsa:2934
UCSC genome browser More...UCSCⁱ	uc004ble.1, human [P06396-1]

Keywords - Coding sequence diversityⁱ

Alternative initiation, Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P06396	Actin-depolymerizing factor		HUMAN		782	UniRef100_P06396
Isoform 2 of Gelsolin		HUMAN		731
Gelsolin exon 3 (Fragment)		HUMAN		48
Actin-depolymerizing factor (Fragment)		HUMAN		260
+1
P06396-3	Actin-depolymerizing factor (Fragment)		HUMAN		232	UniRef100_P06396-3

Protein	Similar proteins		Species	Score	Length	Source
P06396	Gelsolin	)	MOUSE		780	UniRef90_P06396
Gelsolin		RAT		780
Gelsolin (Fragment)		PIG		772
Gelsolin	)	HORSE		731
Gelsolin		BOVIN		731
+477

Protein	Similar proteins		Species	Score	Length	Source
P06396	Gelsolin		RAT		780	UniRef50_P06396
Gelsolin	)	MOUSE		780
Gelsolin (Fragment)		PIG		772
Gelsolin	)	HORSE		731
Gelsolin		BOVIN		731
+1359

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

Gelsolin entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04412 mRNA Translation: CAA28000.1 AK096280 mRNA Translation: BAG53247.1 AK125819 mRNA Translation: BAG54252.1 AK295572 mRNA Translation: BAH12109.1 AK299453 mRNA Translation: BAH13037.1 AK315494 mRNA Translation: BAG37878.1 AL137068 Genomic DNA No translation available. AL513122 Genomic DNA No translation available. 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 XP_005252001.1, XM_005251944.1 [P06396-3] XP_005252002.1, XM_005251945.3 XP_006717142.1, XM_006717079.1 XP_011516888.1, XM_011518586.1 XP_011516889.1, XM_011518587.2 XP_011516890.1, XM_011518588.2 XP_011516891.1, XM_011518589.2 XP_011516892.1, XM_011518590.2 XP_011516893.1, XM_011518591.2 XP_011516894.1, XM_011518592.1 XP_011516895.1, XM_011518593.1 [P06396-2] XP_016870135.1, XM_017014646.1 XP_016870136.1, XM_017014647.1 XP_016870137.1, XM_017014648.1 [P06396-3]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4PKG	X-ray	1.80	G	52-176	[»]
	4PKH	X-ray	2.15	B/E/G/J	52-176	[»]
				B/E/G/J	196-260	[»]
	4PKI	X-ray	2.30	G	52-176	[»]
	4S10	X-ray	2.61	C/D	186-288	[»]
	4Z94	X-ray	2.40	G	52-176	[»]
	5DD2	X-ray	2.60	A/G	55-188	[»]
	5FAE	X-ray	1.70	A	178-293	[»]
	5FAF	X-ray	1.05	A	178-293	[»]
	5H3M	NMR	-	A	55-187	[»]
	5H3N	NMR	-	A	55-187	[»]
	5O2Z	X-ray	1.70	A/B	178-293	[»]
	5UBO	X-ray	2.39	S	52-178	[»]
	5ZZ0	X-ray	2.63	A/G	55-188	[»]
	6H1F	X-ray	1.90	B	178-293	[»]
	6JCO	X-ray	2.88	A/B	56-782	[»]
	6JEG	X-ray	2.98	A/B	54-782	[»]
	6JEH	X-ray	2.95	A/B	56-782	[»]
	6LJE	X-ray	1.40	A/B	297-397	[»]
	6LJF	X-ray	1.50	A/B	297-397	[»]
	6Q9R	X-ray	2.73	A/B	28-782	[»]
	6Q9Z	X-ray	3.80	A/B	28-782	[»]
	6QBF	X-ray	3.50	A/B	28-782	[»]
	6QW3	X-ray	1.30	A	178-293	[»]
SMRⁱ	P06396
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	109189, 117 interactors
CORUMⁱ	P06396
DIPⁱ	DIP-2196N
IntActⁱ	P06396, 92 interactors
MINTⁱ	P06396
STRINGⁱ	9606.ENSP00000362924

Chemistry databases

ChEMBLⁱ	CHEMBL4295700
DrugBankⁱ	DB09130, Copper DB02621, Latrunculin A DB01593, Zinc DB14487, Zinc acetate

PTM databases

GlyGenⁱ	P06396, 8 sites, 3 O-linked glycans (8 sites)
iPTMnetⁱ	P06396
MetOSiteⁱ	P06396
PhosphoSitePlusⁱ	P06396
SwissPalmⁱ	P06396

Polymorphism and mutation databases

BioMutaⁱ	GSN
DMDMⁱ	121116

2D gel databases

OGPⁱ	P06396

OGPⁱ

P06396

Proteomic databases

CPTACⁱ	non-CPTAC-1126 non-CPTAC-1127
EPDⁱ	P06396
jPOSTⁱ	P06396
MassIVEⁱ	P06396
PaxDbⁱ	P06396
PeptideAtlasⁱ	P06396
PRIDEⁱ	P06396
ProteomicsDBⁱ	12635 [P06396-3] 25596 51897 [P06396-1] 51898 [P06396-2] 51899 [P06396-3]

Protocols and materials databases

ABCDⁱ	P06396, 5 sequenced antibodies
Antibodypediaⁱ	3387, 685 antibodies
The DNASU plasmid repository More...DNASUⁱ	2934

Genome annotation databases

Ensemblⁱ	ENST00000373808; ENSP00000362914; ENSG00000148180 [P06396-3] ENST00000373818; ENSP00000362924; ENSG00000148180 [P06396-1] ENST00000373823; ENSP00000362929; ENSG00000148180 [P06396-2] ENST00000545652; ENSP00000445823; ENSG00000148180 [P06396-4]
GeneIDⁱ	2934
KEGGⁱ	hsa:2934
UCSCⁱ	uc004ble.1, human [P06396-1]

Organism-specific databases

CTDⁱ	2934
DisGeNETⁱ	2934
EuPathDBⁱ	HostDB:ENSG00000148180.17
GeneCardsⁱ	GSN
HGNCⁱ	HGNC:4620, GSN
HPAⁱ	ENSG00000148180, Low tissue specificity
MalaCardsⁱ	GSN
MIMⁱ	105120, phenotype 137350, gene
neXtProtⁱ	NX_P06396
OpenTargetsⁱ	ENSG00000148180
Orphanetⁱ	85448, AGel amyloidosis
PharmGKBⁱ	PA29011
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0443, Eukaryota
GeneTreeⁱ	ENSGT00940000155591
HOGENOMⁱ	CLU_002568_3_2_1
InParanoidⁱ	P06396
KOⁱ	K05768
OMAⁱ	EWPQTPD
OrthoDBⁱ	1376537at2759
PhylomeDBⁱ	P06396
TreeFamⁱ	TF313468

Enzyme and pathway databases

PathwayCommonsⁱ	P06396
Reactomeⁱ	R-HSA-264870, Caspase-mediated cleavage of cytoskeletal proteins R-HSA-6798695, Neutrophil degranulation R-HSA-977225, Amyloid fiber formation
SABIO-RKⁱ	P06396
SIGNORⁱ	P06396

Miscellaneous databases

BioGRID-ORCSⁱ	2934, 4 hits in 868 CRISPR screens
ChiTaRSⁱ	GSN, human
EvolutionaryTraceⁱ	P06396
GeneWikiⁱ	Gelsolin
GenomeRNAiⁱ	2934
Pharosⁱ	P06396, Tbio
Protein Ontology More...PROⁱ	PR:P06396
RNActⁱ	P06396, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000148180, Expressed in adipose tissue of abdominal region and 255 other tissues
ExpressionAtlasⁱ	P06396, baseline and differential
Genevisibleⁱ	P06396, HS

Family and domain databases

Gene3Dⁱ	3.40.20.10, 6 hits
IDEALⁱ	IID00265
InterProⁱ	View protein in InterPro IPR029006, ADF-H/Gelsolin-like_dom_sf IPR030004, Gelsolin IPR007123, Gelsolin-like_dom IPR007122, Villin/Gelsolin
PANTHERⁱ	PTHR11977, PTHR11977, 1 hit PTHR11977:SF29, PTHR11977:SF29, 1 hit
Pfamⁱ	View protein in Pfam PF00626, Gelsolin, 6 hits
PRINTSⁱ	PR00597, GELSOLIN
SMARTⁱ	View protein in SMART SM00262, GEL, 6 hits
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GELS_HUMAN
Accessionⁱ	P06396Primary (citable) accession number: P06396 Secondary accession number(s): A2A418 Q8WVV7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
	Last sequence update:	January 1, 1988
	Last modified:	August 12, 2020
	This is version 240 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

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

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UniProtKB - P06396 (GELS_HUMAN)

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Gelsolin

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Extracellular region or secreted

Cytoskeleton

Cytosol

Extracellular region or secreted

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P06396

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ