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P13020

- GELS_MOUSE

UniProt

P13020 - GELS_MOUSE

Protein

Gelsolin

Gene

Gsn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (12 Feb 2003)
      Previous versions | rss
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    Functioni

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

    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
    2. protein binding Source: MGI

    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

    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. cytosol Source: UniProtKB
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: Ensembl
    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

    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

    ArrayExpressiP13020.
    BgeeiP13020.
    CleanExiMM_GSN.
    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.
    GeneTreeiENSGT00620000087675.
    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

    MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM    50
    VVEHPEFLKA GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ 100
    LRNGNLQYDL HYWLGNECSQ DESGAAAIFT VQLDDYLNGR AVQHREVQGF 150
    ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN EVVVQRLFQV KGRRVVRATE 200
    VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ VSKGIRDNER 250
    SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK 300
    VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM 350
    EERKAALKTA SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT 400
    DGPGLGYLSS HIANVERVPF DAATLHTSTA MAAQHGMDDD GTGQKQIWRI 450
    EGSNKVPVDP ATYGQFYGGD SYIILYNYRH GGRQGQIIYN WQGAQSTQDE 500
    VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK PMIIYKGGTS 550
    RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA 600
    YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW EALGGKTAYR 650
    TSPRLKDKKM DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD 700
    TWDQVFVWVG KDSQEEEKTE ALTSAKRYIE TDPANRDRRT PITVVRQGFE 750
    PPSFVGWFLG WDDNYWSVDP LDRALAELAA 780
    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 ENSGT00620000087675.
    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

    ArrayExpressi P13020.
    Bgeei P13020.
    CleanExi MM_GSN.
    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

    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 1, 2014
    This is version 149 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