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P19419

- ELK1_HUMAN

UniProt

P19419 - ELK1_HUMAN

Protein

ETS domain-containing protein Elk-1

Gene

ELK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      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. protein binding Source: UniProtKB
    2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: RefGenome
    2. innate immune response Source: Reactome
    3. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    5. neurotrophin TRK receptor signaling pathway Source: Reactome
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. stress-activated MAPK cascade Source: Reactome
    9. toll-like receptor 10 signaling pathway Source: Reactome
    10. toll-like receptor 2 signaling pathway Source: Reactome
    11. toll-like receptor 3 signaling pathway Source: Reactome
    12. toll-like receptor 4 signaling pathway Source: Reactome
    13. toll-like receptor 5 signaling pathway Source: Reactome
    14. toll-like receptor 9 signaling pathway Source: Reactome
    15. toll-like receptor signaling pathway Source: Reactome
    16. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    17. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    18. transcription from RNA polymerase II promoter Source: GOC
    19. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_12599. ERK/MAPK targets.
    SignaLinkiP19419.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ETS domain-containing protein Elk-1
    Gene namesi
    Name:ELK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3321. ELK1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi230 – 2301K → R: 9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation. 2 Publications
    Mutagenesisi249 – 2491K → R: 9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation. 2 Publications
    Mutagenesisi254 – 2541K → R: Reduction in sumoylation. 1 Publication
    Mutagenesisi324 – 3241S → A: No effect on ternary complex formation but loss of transcriptional activity positive regulation by MAD2L2. 1 Publication
    Mutagenesisi336 – 3361T → A: No effect on ternary complex formation. 1 Publication
    Mutagenesisi353 – 3531T → A: No effect on ternary complex formation. 1 Publication
    Mutagenesisi363 – 3631T → A: No effect on ternary complex formation. 1 Publication
    Mutagenesisi368 – 3681T → A: No effect on ternary complex formation. 1 Publication
    Mutagenesisi383 – 3831S → A: 17% reduction in ternary complex formation. 2 Publications
    Mutagenesisi389 – 3891S → A: 34% reduction in ternary complex formation. 1 Publication
    Mutagenesisi417 – 4171T → A: No effect on ternary complex formation. 1 Publication
    Mutagenesisi422 – 4221S → A: Slight reduction in ternary complex formation. 1 Publication

    Organism-specific databases

    PharmGKBiPA27749.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428ETS domain-containing protein Elk-1PRO_0000204095Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki249 – 249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei324 – 3241Phosphoserine; by MAPK12 Publications
    Modified residuei336 – 3361Phosphothreonine; by MAPK11 Publication
    Modified residuei353 – 3531Phosphothreonine; by MAPK11 Publication
    Modified residuei363 – 3631Phosphothreonine; by MAPK11 Publication
    Modified residuei368 – 3681Phosphothreonine; by MAPK11 Publication
    Modified residuei383 – 3831Phosphoserine; by MAPK1 and MAPK83 Publications
    Modified residuei389 – 3891Phosphoserine; by MAPK12 Publications
    Modified residuei417 – 4171Phosphothreonine; by MAPK11 Publication
    Modified residuei422 – 4221Phosphoserine; by MAPK12 Publications

    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.
    On mitogenic stimulation, phosphorylated on C-terminal serine and threonine residues by MAPK1. Ser-383 and Ser-389 are the preferred sites for MAPK1. In vitro, phosphorylation by MAPK1 potentiates ternary complex formation with the serum responses factors, SRE and SRF. Also phosphorylated on Ser-383 by MAPK8 and/or MAKP9. Phosphorylation leads to loss of sumoylation and restores transcriptional activator activity. Phosphorylated and activated by CAMK4, MAPK11, MAPK12 and MAPK14.6 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP19419.
    PaxDbiP19419.
    PRIDEiP19419.

    PTM databases

    PhosphoSiteiP19419.

    Expressioni

    Tissue specificityi

    Lung and testis.

    Gene expression databases

    ArrayExpressiP19419.
    BgeeiP19419.
    CleanExiHS_ELK1.
    GenevestigatoriP19419.

    Organism-specific databases

    HPAiCAB003808.
    HPA036084.

    Interactioni

    Subunit structurei

    Interacts in its sumoylated form with PIAS2/PIASX which enhances its transcriptional activator activity. Interacts with MAD2L2; the interaction is direct and promotes phosphorylation by the kinases MAPK8 and/or MAPK9.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK3P273612EBI-726632,EBI-73995
    SUMO1P631653EBI-726632,EBI-80140
    UBE2IP632795EBI-726632,EBI-80168

    Protein-protein interaction databases

    BioGridi108317. 28 interactions.
    DIPiDIP-36057N.
    IntActiP19419. 8 interactions.
    MINTiMINT-3380115.
    STRINGi9606.ENSP00000247161.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1711
    Beta strandi19 – 235
    Beta strandi25 – 284
    Turni29 – 324
    Beta strandi33 – 353
    Helixi39 – 4810
    Turni49 – 513
    Helixi57 – 6711
    Turni68 – 714
    Beta strandi72 – 754
    Beta strandi82 – 876

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DUXX-ray2.10C/F1-94[»]
    ProteinModelPortaliP19419.
    SMRiP19419. Positions 5-90.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19419.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni349 – 39951Sufficient for interaction with MAD2L2Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG269367.
    HOVERGENiHBG004344.
    KOiK04375.
    OMAiPNPLEAC.
    OrthoDBiEOG7NPFTD.
    PhylomeDBiP19419.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19419-1) [UniParc]FASTAAdd to Basket

    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

    MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK    50
    NKTNMNYDKL SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP 100
    PQPEVSVTST MPNVAPAAIH AAPGDTVSGK PGTPKGAGMA GPGGLARSSR 150
    NEYMRSGLYS TFTIQSLQPQ PPPHPRPAVV LPSAAPAGAA APPSGSRSTS 200
    PSPLEACLEA EEAGLPLQVI LTPPEAPNLK SEELNVEPGL GRALPPEVKV 250
    EGPKEELEVA GERGFVPETT KAEPEVPPQE GVPARLPAVV MDTAGQAGGH 300
    AASSPEISQP QKGRKPRDLE LPLSPSLLGG PGPERTPGSG SGSGLQAPGP 350
    ALTPSLLPTH TLTPVLLTPS SLPPSIHFWS TLSPIAPRSP AKLSFQFPSS 400
    GSAQVHIPSI SVDGLSTPVV LSPGPQKP 428
    Length:428
    Mass (Da):44,888
    Last modified:January 24, 2001 - v2
    Checksum:i68F71F8ADB9D38CA
    GO
    Isoform 2 (identifier: P19419-2) [UniParc]FASTAAdd to Basket

    Also known as: ELKV

    The sequence of this isoform differs from the canonical sequence as follows:
         91-95: VAGCS → SHCAP
         96-428: Missing.

    Show »
    Length:95
    Mass (Da):11,217
    Checksum:i8347760EEE65634F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441G → S.
    Corresponds to variant rs1997639 [ dbSNP | Ensembl ].
    VAR_017108
    Natural varianti183 – 1831S → N.1 Publication
    Corresponds to variant rs1059579 [ dbSNP | Ensembl ].
    VAR_017109

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei91 – 955VAGCS → SHCAP in isoform 2. CuratedVSP_001466
    Alternative sequencei96 – 428333Missing in isoform 2. CuratedVSP_001467Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25269 mRNA. Translation: AAA52384.1.
    AF080616 Genomic DNA. Translation: AAC82466.1.
    AF000672 mRNA. Translation: AAD00862.1.
    AB016193 mRNA. Translation: BAA36616.1.
    AB016194 Genomic DNA. Translation: BAA36617.1.
    AK312984 mRNA. Translation: BAG35821.1.
    AL009172 Genomic DNA. Translation: CAA15659.1.
    CH471164 Genomic DNA. Translation: EAW59321.1.
    BC056150 mRNA. Translation: AAH56150.1.
    CCDSiCCDS14283.1. [P19419-1]
    CCDS59165.1. [P19419-2]
    PIRiA41354. TVHUEK.
    RefSeqiNP_001107595.1. NM_001114123.2. [P19419-1]
    NP_001244097.1. NM_001257168.1. [P19419-2]
    NP_005220.2. NM_005229.4. [P19419-1]
    UniGeneiHs.181128.
    Hs.715039.
    Hs.740673.

    Genome annotation databases

    EnsembliENST00000247161; ENSP00000247161; ENSG00000126767. [P19419-1]
    ENST00000343894; ENSP00000345585; ENSG00000126767. [P19419-2]
    ENST00000376983; ENSP00000366182; ENSG00000126767. [P19419-1]
    GeneIDi2002.
    KEGGihsa:2002.
    UCSCiuc004dik.5. human. [P19419-1]
    uc004dil.5. human. [P19419-2]

    Polymorphism databases

    DMDMi12643407.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25269 mRNA. Translation: AAA52384.1 .
    AF080616 Genomic DNA. Translation: AAC82466.1 .
    AF000672 mRNA. Translation: AAD00862.1 .
    AB016193 mRNA. Translation: BAA36616.1 .
    AB016194 Genomic DNA. Translation: BAA36617.1 .
    AK312984 mRNA. Translation: BAG35821.1 .
    AL009172 Genomic DNA. Translation: CAA15659.1 .
    CH471164 Genomic DNA. Translation: EAW59321.1 .
    BC056150 mRNA. Translation: AAH56150.1 .
    CCDSi CCDS14283.1. [P19419-1 ]
    CCDS59165.1. [P19419-2 ]
    PIRi A41354. TVHUEK.
    RefSeqi NP_001107595.1. NM_001114123.2. [P19419-1 ]
    NP_001244097.1. NM_001257168.1. [P19419-2 ]
    NP_005220.2. NM_005229.4. [P19419-1 ]
    UniGenei Hs.181128.
    Hs.715039.
    Hs.740673.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DUX X-ray 2.10 C/F 1-94 [» ]
    ProteinModelPortali P19419.
    SMRi P19419. Positions 5-90.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108317. 28 interactions.
    DIPi DIP-36057N.
    IntActi P19419. 8 interactions.
    MINTi MINT-3380115.
    STRINGi 9606.ENSP00000247161.

    Chemistry

    ChEMBLi CHEMBL4453.

    PTM databases

    PhosphoSitei P19419.

    Polymorphism databases

    DMDMi 12643407.

    Proteomic databases

    MaxQBi P19419.
    PaxDbi P19419.
    PRIDEi P19419.

    Protocols and materials databases

    DNASUi 2002.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247161 ; ENSP00000247161 ; ENSG00000126767 . [P19419-1 ]
    ENST00000343894 ; ENSP00000345585 ; ENSG00000126767 . [P19419-2 ]
    ENST00000376983 ; ENSP00000366182 ; ENSG00000126767 . [P19419-1 ]
    GeneIDi 2002.
    KEGGi hsa:2002.
    UCSCi uc004dik.5. human. [P19419-1 ]
    uc004dil.5. human. [P19419-2 ]

    Organism-specific databases

    CTDi 2002.
    GeneCardsi GC0XM047494.
    H-InvDB HIX0016766.
    HGNCi HGNC:3321. ELK1.
    HPAi CAB003808.
    HPA036084.
    MIMi 311040. gene.
    neXtProti NX_P19419.
    PharmGKBi PA27749.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269367.
    HOVERGENi HBG004344.
    KOi K04375.
    OMAi PNPLEAC.
    OrthoDBi EOG7NPFTD.
    PhylomeDBi P19419.
    TreeFami TF317732.

    Enzyme and pathway databases

    Reactomei REACT_12599. ERK/MAPK targets.
    SignaLinki P19419.

    Miscellaneous databases

    ChiTaRSi ELK1. human.
    EvolutionaryTracei P19419.
    GeneWikii ELK1.
    GenomeRNAii 2002.
    NextBioi 8101.
    PROi P19419.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19419.
    Bgeei P19419.
    CleanExi HS_ELK1.
    Genevestigatori P19419.

    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. "elk, tissue-specific ets-related genes on chromosomes X and 14 near translocation breakpoints."
      Rao V.N., Huebner K., Isobe M., Ar-Rushdi A., Croce C.M., Reddy E.S.P.
      Science 244:66-70(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-183.
    2. "The human elk-1 gene family: the functional gene and two processed pseudogenes embedded in the IgH locus."
      Harindranath N., Mills F.C., Mitchell M.P., Meindl A., Max E.E.
      Gene 221:215-224(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "Novel family members HuER71, ELFR, and ELKv among ETS-related genes coexpressed with EWS-FLI1 in Ewing tumor cell lines."
      Aryee D.N.T., Kovar H.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    4. "Structural organization of the human ELK1 gene and its processed pseudogene ELK2 genes."
      Yamauchi T., Toko M., Suga M., Hatakeyama T., Isobe M.
      DNA Res. 6:21-27(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
      Tissue: Hippocampus.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Urinary bladder.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Uterus.
    9. "ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation."
      Gille H., Kortenjann M., Thomae O., Moomaw C., Slaughter C., Cobb M.H., Shaw P.E.
      EMBO J. 14:951-962(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 318-331; 336-364 AND 380-408, PHOSPHORYLATION AT SER-324; THR-336; SER-383; SER-389 AND SER-422, MUTAGENESIS OF SER-324; THR-336; THR-353; THR-363; THR-368; SER-383; SER-389; THR-417 AND SER-422.
    10. "Elk-1 protein domains required for direct and SRF-assisted DNA-binding."
      Janknecht R., Nordheim A.
      Nucleic Acids Res. 20:3317-3324(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    11. "Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade."
      Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.
      Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMK4.
    12. "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6."
      Enslen H., Raingeaud J., Davis R.J.
      J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPK11; MAPK12 AND MAPK14.
    13. "ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry."
      Cruzalegui F.H., Cano E., Treisman R.
      Oncogene 18:7948-7957(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-353; THR-363; THR-368; SER-383; SER-389 AND THR-417.
    14. "Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity."
      Yang S.-H., Jaffray E., Hay R.T., Sharrocks A.D.
      Mol. Cell 12:63-74(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-249, MUTAGENESIS OF LYS-230 AND LYS-249.
    15. Cited for: SUMOYLATION AT LYS-230; LYS-249 AND LYS-254, MUTAGENESIS OF LYS-230; LYS-249 AND LYS-254.
    16. "SUMO promotes HDAC-mediated transcriptional repression."
      Yang S.-H., Sharrocks A.D.
      Mol. Cell 13:611-617(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    17. "PIASx acts as an Elk-1 coactivator by facilitating derepression."
      Yang S.-H., Sharrocks A.D.
      EMBO J. 24:2161-2171(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIAS2.
    18. "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1."
      Zhang L., Yang S.H., Sharrocks A.D.
      Mol. Cell. Biol. 27:2861-2869(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAD2L2, PHOSPHORYLATION AT SER-383, MUTAGENESIS OF SER-383.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Structure of the elk-1-DNA complex reveals how DNA-distal residues affect ETS domain recognition of DNA."
      Mo Y., Vaessen B., Johnston K., Marmorstein R.
      Nat. Struct. Biol. 7:292-297(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-94.

    Entry informationi

    Entry nameiELK1_HUMAN
    AccessioniPrimary (citable) accession number: P19419
    Secondary accession number(s): B2R7H4
    , O75606, O95058, Q969X8, Q9UJM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 167 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3