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P41969

- ELK1_MOUSE

UniProt

P41969 - ELK1_MOUSE

Protein

ETS domain-containing protein Elk-1

Gene

Elk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Stimulates transcription. Binds to purine-rich DNA sequences. Can form a ternary complex with the serum response factor and the ETS and SRF motifs of the fos serum response element.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi5 – 8682ETSPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. sequence-specific DNA binding Source: InterPro
    2. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
    3. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: RefGenome
    2. positive regulation of transcription, DNA-templated Source: MGI
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: MGI
    5. regulation of transcription from RNA polymerase II promoter Source: RefGenome
    6. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_215063. ERK/MAPK targets.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ETS domain-containing protein Elk-1
    Gene namesi
    Name:Elk1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:101833. Elk1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: RefGenome

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429ETS domain-containing protein Elk-1PRO_0000204096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki231 – 231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki250 – 250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki255 – 255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei325 – 3251Phosphoserine; by MAPK1By similarity
    Modified residuei337 – 3371Phosphothreonine; by MAPK1By similarity
    Modified residuei354 – 3541Phosphothreonine; by MAPK1By similarity
    Modified residuei364 – 3641Phosphothreonine; by MAPK1By similarity
    Modified residuei369 – 3691Phosphothreonine; by MAPK1By similarity
    Modified residuei384 – 3841Phosphoserine; by MAPK1 and MAPK8By similarity
    Modified residuei390 – 3901Phosphoserine; by MAPK1By similarity
    Modified residuei418 – 4181Phosphothreonine; by MAPK1By similarity
    Modified residuei423 – 4231Phosphoserine; by MAPK1By similarity

    Post-translational modificationi

    Sumoylation represses transcriptional activator activity as it results in recruitment of HDAC2 to target gene promoters which leads to decreased histone acetylation and reduced transactivator activity. It also regulates nuclear retention By similarity.By similarity
    On mitogenic stimulation, phosphorylated on C-terminal serine and threonine residues by MAPK1 but also MAPK8 and/or MAPK9. Phosphorylation leads to loss of sumoylation and restores transcriptional activator activity. Phosphorylated and activated by CaMK4, MAPK11, MAPK12 and MAPK14 By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP41969.

    PTM databases

    PhosphoSiteiP41969.

    Expressioni

    Tissue specificityi

    Predominantly expressed in the brain, and to a lesser extent in the heart, liver and muscle.

    Gene expression databases

    ArrayExpressiP41969.
    BgeeiP41969.
    CleanExiMM_ELK1.
    GenevestigatoriP41969.

    Interactioni

    Subunit structurei

    Interacts in its sumoylated form with PIAS2 which enhances its transcriptional activator activity. Interacts with MAD2L2; the interaction is direct and promotes phosphorylation by the kinases MAPK8 and/or MAPK9 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199429. 2 interactions.
    STRINGi10090.ENSMUSP00000009550.

    Structurei

    3D structure databases

    ProteinModelPortaliP41969.
    SMRiP41969. Positions 5-90.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni350 – 40051Sufficient for interaction with MAD2L2By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ETS family.Curated
    Contains 1 ETS DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG269367.
    GeneTreeiENSGT00750000117271.
    HOGENOMiHOG000237332.
    HOVERGENiHBG004344.
    InParanoidiQ3V1M9.
    KOiK04375.
    OMAiPNPLEAC.
    OrthoDBiEOG7NPFTD.
    TreeFamiTF317732.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR000418. Ets_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00178. Ets. 1 hit.
    [Graphical view]
    PRINTSiPR00454. ETSDOMAIN.
    SMARTiSM00413. ETS. 1 hit.
    [Graphical view]
    PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
    PS00346. ETS_DOMAIN_2. 1 hit.
    PS50061. ETS_DOMAIN_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P41969-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK    50
    NKTNMNYDKL SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP 100
    PQPEVSVTSA IAMAPATVHA GPGDTATGKP GTPKGAGMTG QGGLARSSRN 150
    EYMRSGLYST FTIQSLQPQP QPPIPPRPAS VLPNTTPAGV PAPASGSRST 200
    SPNPLEACLE AEEAGLPLQV ILTPPEAPNQ KSEELSLDPS FGHPQPPEVK 250
    VEGPKEELEA ARAGGFSSEA VKAEPEVSAS EGLLARLPAI LTENTAQVCG 300
    LSTSTTEITQ PQKGRKPRDL ELPLSPSLLG GQGPERTPGS GTSSGLQAPG 350
    PALTPSLLPT HTLTPVLLTP SSLPPSIHFW STLSPIAPRS PAKLSFQFPS 400
    SGSAQVHIPS ISVDGLSTPV VLSPGPQKP 429
    Length:429
    Mass (Da):45,271
    Last modified:July 27, 2011 - v3
    Checksum:i2E1C5B80790C6DA7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331P → T in CAA85391. (PubMed:7958835)Curated
    Sequence conflicti249 – 2491V → A in CAA60715. (PubMed:8863747)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87257 mRNA. Translation: CAA60715.1.
    AK132354 mRNA. Translation: BAE21121.1.
    AL671853 Genomic DNA. Translation: CAM19337.1.
    CH466625 Genomic DNA. Translation: EDL00733.1.
    Z36939 mRNA. Translation: CAA85391.1.
    CCDSiCCDS30048.1.
    PIRiJC4965.
    RefSeqiNP_031948.4. NM_007922.5.
    UniGeneiMm.405823.
    Mm.490895.

    Genome annotation databases

    EnsembliENSMUST00000009550; ENSMUSP00000009550; ENSMUSG00000009406.
    GeneIDi13712.
    KEGGimmu:13712.
    UCSCiuc009suc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87257 mRNA. Translation: CAA60715.1 .
    AK132354 mRNA. Translation: BAE21121.1 .
    AL671853 Genomic DNA. Translation: CAM19337.1 .
    CH466625 Genomic DNA. Translation: EDL00733.1 .
    Z36939 mRNA. Translation: CAA85391.1 .
    CCDSi CCDS30048.1.
    PIRi JC4965.
    RefSeqi NP_031948.4. NM_007922.5.
    UniGenei Mm.405823.
    Mm.490895.

    3D structure databases

    ProteinModelPortali P41969.
    SMRi P41969. Positions 5-90.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199429. 2 interactions.
    STRINGi 10090.ENSMUSP00000009550.

    PTM databases

    PhosphoSitei P41969.

    Proteomic databases

    PRIDEi P41969.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000009550 ; ENSMUSP00000009550 ; ENSMUSG00000009406 .
    GeneIDi 13712.
    KEGGi mmu:13712.
    UCSCi uc009suc.2. mouse.

    Organism-specific databases

    CTDi 2002.
    MGIi MGI:101833. Elk1.

    Phylogenomic databases

    eggNOGi NOG269367.
    GeneTreei ENSGT00750000117271.
    HOGENOMi HOG000237332.
    HOVERGENi HBG004344.
    InParanoidi Q3V1M9.
    KOi K04375.
    OMAi PNPLEAC.
    OrthoDBi EOG7NPFTD.
    TreeFami TF317732.

    Enzyme and pathway databases

    Reactomei REACT_215063. ERK/MAPK targets.

    Miscellaneous databases

    NextBioi 284482.
    PROi P41969.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41969.
    Bgeei P41969.
    CleanExi MM_ELK1.
    Genevestigatori P41969.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR000418. Ets_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00178. Ets. 1 hit.
    [Graphical view ]
    PRINTSi PR00454. ETSDOMAIN.
    SMARTi SM00413. ETS. 1 hit.
    [Graphical view ]
    PROSITEi PS00345. ETS_DOMAIN_1. 1 hit.
    PS00346. ETS_DOMAIN_2. 1 hit.
    PS50061. ETS_DOMAIN_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Embryo.
    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].
      Strain: C57BL/6J.
      Tissue: Head.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Net, a new ets transcription factor that is activated by Ras."
      Giovane A., Pintzas A., Maira S.-M., Sobieszczuk P., Wasylyk B.
      Genes Dev. 8:1502-1513(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-224.
      Tissue: Embryo.

    Entry informationi

    Entry nameiELK1_MOUSE
    AccessioniPrimary (citable) accession number: P41969
    Secondary accession number(s): Q3V1M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 121 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3