Skip Header

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

P13020

- GELS_MOUSE

UniProt

P13020 - GELS_MOUSE

(max 400 entries)x

Your basket is currently empty.

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

Protein

Gelsolin

Gene

Gsn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi469 – 4691Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi470 – 4701Calcium 1By similarity
Metal bindingi500 – 5001Calcium 1By similarity
Metal bindingi549 – 5491Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi589 – 5891Calcium 2By similarity
Metal bindingi589 – 5891Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi590 – 5901Calcium 2By similarity
Metal bindingi612 – 6121Calcium 2By similarity
Metal bindingi694 – 6941Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi695 – 6951Calcium 3By similarity
Metal bindingi717 – 7171Calcium 3By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. actin filament polymerization Source: UniProtKB
  3. actin filament severing Source: UniProtKB
  4. aging Source: Ensembl
  5. apoptotic process Source: Ensembl
  6. cellular response to cadmium ion Source: Ensembl
  7. cilium morphogenesis Source: UniProtKB
  8. oligodendrocyte development Source: Ensembl
  9. phosphatidylinositol-mediated signaling Source: Ensembl
  10. regulation of cell adhesion Source: Ensembl
  11. response to ethanol Source: Ensembl
  12. response to folic acid Source: Ensembl
  13. tissue regeneration Source: Ensembl
  14. vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198563. Amyloids.
REACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Gelsolin
Alternative name(s):
Actin-depolymerizing factor
Short name:
ADF
Brevin
Gene namesi
Name:Gsn
Synonyms:Gsb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:95851. Gsn.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 780755GelsolinPRO_0000036387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841PhosphotyrosineBy similarity
Disulfide bondi213 ↔ 226In isoform 1By similarity
Modified residuei407 – 4071PhosphotyrosineBy similarity
Modified residuei463 – 4631PhosphotyrosineBy similarity
Modified residuei582 – 5821N6-acetyllysine1 Publication
Modified residuei601 – 6011PhosphotyrosineBy similarity
Modified residuei649 – 6491PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues in vitro.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP13020.
PaxDbiP13020.
PRIDEiP13020.

2D gel databases

REPRODUCTION-2DPAGEP13020.

PTM databases

PhosphoSiteiP13020.

Expressioni

Gene expression databases

BgeeiP13020.
CleanExiMM_GSN.
ExpressionAtlasiP13020. baseline and differential.
GenevestigatoriP13020.

Interactioni

Subunit structurei

Binds to actin and to fibronectin. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X By similarity. Interacts with the inactive form of EIF2AK2/PKR.By similarity1 Publication

Protein-protein interaction databases

BioGridi230683. 6 interactions.
IntActiP13020. 7 interactions.
MINTiMINT-1608422.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 593
Beta strandi62 – 7211
Beta strandi75 – 784
Helixi81 – 833
Beta strandi86 – 883
Beta strandi92 – 1009
Beta strandi106 – 1149
Helixi120 – 13617
Turni137 – 1393
Beta strandi141 – 1477
Helixi153 – 1564
Beta strandi164 – 1674
Beta strandi445 – 4517
Beta strandi454 – 4574
Helixi460 – 4623
Beta strandi465 – 4673
Beta strandi470 – 4778
Beta strandi486 – 4927
Helixi498 – 51417
Turni515 – 5173
Beta strandi519 – 5257
Helixi531 – 5355
Turni536 – 5394
Beta strandi542 – 5465
Beta strandi551 – 5533
Beta strandi560 – 5689
Beta strandi570 – 5723
Beta strandi574 – 5796
Helixi583 – 5853
Beta strandi590 – 5956
Beta strandi600 – 6045
Helixi610 – 62314
Beta strandi627 – 6315
Helixi637 – 6437
Helixi653 – 6564
Helixi660 – 6623
Beta strandi666 – 6716
Beta strandi674 – 6763
Beta strandi678 – 6814
Helixi688 – 6903
Beta strandi695 – 7006
Beta strandi705 – 7095
Helixi715 – 72915
Turni733 – 7353
Beta strandi742 – 7465
Helixi752 – 7554

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NPHX-ray3.00A439-767[»]
4CBUX-ray1.30G50-174[»]
4CBWX-ray2.50G50-174[»]
4CBXX-ray2.20G50-174[»]
ProteinModelPortaliP13020.
SMRiP13020. Positions 48-780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati74 – 12451Gelsolin-like 1Add
BLAST
Repeati196 – 23641Gelsolin-like 2Add
BLAST
Repeati312 – 35443Gelsolin-like 3Add
BLAST
Repeati451 – 50252Gelsolin-like 4Add
BLAST
Repeati574 – 61441Gelsolin-like 5Add
BLAST
Repeati677 – 71943Gelsolin-like 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 174124Actin-severingSequence AnalysisAdd
BLAST
Regioni121 – 1244Actin-actin interfilament contact point
Regioni160 – 1678Polyphosphoinositide bindingBy similarity
Regioni186 – 1949Polyphosphoinositide bindingBy similarity
Regioni432 – 780349Actin-binding, Ca-sensitiveSequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG304849.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP13020.
KOiK05768.
OMAiRIEKFDL.
OrthoDBiEOG7288RJ.
PhylomeDBiP13020.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P13020-1) [UniParc]FASTAAdd to Basket

Also known as: Secreted, Plasma

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

« Hide

        10         20         30         40         50
MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM
60 70 80 90 100
VVEHPEFLKA GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ
110 120 130 140 150
LRNGNLQYDL HYWLGNECSQ DESGAAAIFT VQLDDYLNGR AVQHREVQGF
160 170 180 190 200
ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN EVVVQRLFQV KGRRVVRATE
210 220 230 240 250
VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ VSKGIRDNER
260 270 280 290 300
SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK
310 320 330 340 350
VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM
360 370 380 390 400
EERKAALKTA SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT
410 420 430 440 450
DGPGLGYLSS HIANVERVPF DAATLHTSTA MAAQHGMDDD GTGQKQIWRI
460 470 480 490 500
EGSNKVPVDP ATYGQFYGGD SYIILYNYRH GGRQGQIIYN WQGAQSTQDE
510 520 530 540 550
VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK PMIIYKGGTS
560 570 580 590 600
RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA
610 620 630 640 650
YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW EALGGKTAYR
660 670 680 690 700
TSPRLKDKKM DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD
710 720 730 740 750
TWDQVFVWVG KDSQEEEKTE ALTSAKRYIE TDPANRDRRT PITVVRQGFE
760 770 780
PPSFVGWFLG WDDNYWSVDP LDRALAELAA
Length:780
Mass (Da):85,942
Last modified:February 12, 2003 - v3
Checksum:iAE94297BE457FF2D
GO
Isoform 2 (identifier: P13020-2) [UniParc]FASTAAdd to Basket

Also known as: Cytoplasmic

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Note: Initiator Met-1 is removed or contains a N-acetylalanine at position 1.

Show »
Length:731
Mass (Da):80,763
Checksum:i56F6A4964DF1CB04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2632GG → ET in AAA37677. (PubMed:2546951)Curated
Sequence conflicti274 – 2741P → H in BAC41004. (PubMed:16141072)Curated
Sequence conflicti294 – 2941R → K in AAA37677. (PubMed:2546951)Curated
Sequence conflicti316 – 3161E → K in BAC41004. (PubMed:16141072)Curated
Sequence conflicti323 – 3231A → P in AAA37677. (PubMed:2546951)Curated
Sequence conflicti423 – 4231A → G in AAA37677. (PubMed:2546951)Curated
Sequence conflicti615 – 6151G → A in AAA37677. (PubMed:2546951)Curated
Sequence conflicti638 – 6381A → G in AAA37677. (PubMed:2546951)Curated
Sequence conflicti648 – 6481A → S in AAA37677. (PubMed:2546951)Curated
Sequence conflicti763 – 7631D → N in AAA37677. (PubMed:2546951)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949Missing in isoform 2. 2 PublicationsVSP_018960Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04953 mRNA. Translation: AAA37677.1.
AK076156 mRNA. Translation: BAC36223.1.
AK089934 mRNA. Translation: BAC41004.1.
AK143664 mRNA. Translation: BAE25485.1.
BC023143 mRNA. Translation: AAH23143.2.
CCDSiCCDS15960.1. [P13020-1]
RefSeqiNP_666232.2. NM_146120.4. [P13020-1]
UniGeneiMm.21109.

Genome annotation databases

EnsembliENSMUST00000028239; ENSMUSP00000028239; ENSMUSG00000026879. [P13020-1]
GeneIDi227753.
KEGGimmu:227753.
UCSCiuc008jkc.2. mouse. [P13020-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04953 mRNA. Translation: AAA37677.1 .
AK076156 mRNA. Translation: BAC36223.1 .
AK089934 mRNA. Translation: BAC41004.1 .
AK143664 mRNA. Translation: BAE25485.1 .
BC023143 mRNA. Translation: AAH23143.2 .
CCDSi CCDS15960.1. [P13020-1 ]
RefSeqi NP_666232.2. NM_146120.4. [P13020-1 ]
UniGenei Mm.21109.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NPH X-ray 3.00 A 439-767 [» ]
4CBU X-ray 1.30 G 50-174 [» ]
4CBW X-ray 2.50 G 50-174 [» ]
4CBX X-ray 2.20 G 50-174 [» ]
ProteinModelPortali P13020.
SMRi P13020. Positions 48-780.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230683. 6 interactions.
IntActi P13020. 7 interactions.
MINTi MINT-1608422.

PTM databases

PhosphoSitei P13020.

2D gel databases

REPRODUCTION-2DPAGE P13020.

Proteomic databases

MaxQBi P13020.
PaxDbi P13020.
PRIDEi P13020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028239 ; ENSMUSP00000028239 ; ENSMUSG00000026879 . [P13020-1 ]
GeneIDi 227753.
KEGGi mmu:227753.
UCSCi uc008jkc.2. mouse. [P13020-1 ]

Organism-specific databases

CTDi 2934.
MGIi MGI:95851. Gsn.

Phylogenomic databases

eggNOGi NOG304849.
GeneTreei ENSGT00760000119111.
HOGENOMi HOG000233630.
HOVERGENi HBG004183.
InParanoidi P13020.
KOi K05768.
OMAi RIEKFDL.
OrthoDBi EOG7288RJ.
PhylomeDBi P13020.
TreeFami TF313468.

Enzyme and pathway databases

Reactomei REACT_198563. Amyloids.
REACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

Miscellaneous databases

ChiTaRSi GSN. mouse.
EvolutionaryTracei P13020.
NextBioi 378824.
PROi P13020.
SOURCEi Search...

Gene expression databases

Bgeei P13020.
CleanExi MM_GSN.
ExpressionAtlasi P13020. baseline and differential.
Genevestigatori P13020.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of murine gelsolin and its regulation during differentiation of embryonal carcinoma cells."
    Dieffenbach C.W., Sengupta D.N., Krause D., Sawzak D., Silverman R.H.
    J. Biol. Chem. 264:13281-13288(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Head and Spleen.
  3. "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: Mammary gland.
  4. Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 50-70 (ISOFORM 2), PROTEIN SEQUENCE OF 74-97; 146-160; 167-186; 254-293; 301-336; 359-366; 372-388; 396-445; 456-479; 529-546; 552-562; 583-621; 625-646; 667-673; 712-736 AND 739-746 (ISOFORMS 1/2), CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2), ACETYLATION AT MET-1 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  5. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
    Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
    Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-73.
    Tissue: Fibroblast.
  6. "Regulation of actin dynamics by protein kinase R control of gelsolin enforces basal innate immune defense."
    Irving A.T., Wang D., Vasilevski O., Latchoumanin O., Kozer N., Clayton A.H., Szczepny A., Morimoto H., Xu D., Williams B.R., Sadler A.J.
    Immunity 36:795-806(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF2AK2.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiGELS_MOUSE
AccessioniPrimary (citable) accession number: P13020
Secondary accession number(s): Q3UPB1, Q8R590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 12, 2003
Last modified: October 29, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3