Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P19419 (ELK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ETS domain-containing protein Elk-1
Gene names
Name:ELK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.17 Ref.18

Subcellular location

Nucleus.

Tissue specificity

Lung and testis.

Post-translational modification

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.18

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

innate immune response

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14970218. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.18. Source: UniProtKB

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentnucleus

Inferred by curator PubMed 14970218. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.18. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 14970218. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SUMO1P631653EBI-726632,EBI-80140
UBE2IP632795EBI-726632,EBI-80168

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19419-1)

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.
Isoform 2 (identifier: P19419-2)

Also known as: ELKV;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428ETS domain-containing protein Elk-1
PRO_0000204095

Regions

DNA binding5 – 8682ETS
Region349 – 39951Sufficient for interaction with MAD2L2

Amino acid modifications

Modified residue3241Phosphoserine; by MAPK1 Ref.9 Ref.20
Modified residue3361Phosphothreonine; by MAPK1 Ref.9
Modified residue3531Phosphothreonine; by MAPK1 Ref.13
Modified residue3631Phosphothreonine; by MAPK1 Ref.13
Modified residue3681Phosphothreonine; by MAPK1 Ref.13
Modified residue3831Phosphoserine; by MAPK1 and MAPK8 Ref.9 Ref.13 Ref.18
Modified residue3891Phosphoserine; by MAPK1 Ref.9 Ref.13
Modified residue4171Phosphothreonine; by MAPK1 Ref.13
Modified residue4221Phosphoserine; by MAPK1 Ref.9 Ref.20
Cross-link230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15
Cross-link249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14 Ref.15
Cross-link254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15

Natural variations

Alternative sequence91 – 955VAGCS → SHCAP in isoform 2.
VSP_001466
Alternative sequence96 – 428333Missing in isoform 2.
VSP_001467
Natural variant1441G → S.
Corresponds to variant rs1997639 [ dbSNP | Ensembl ].
VAR_017108
Natural variant1831S → N. Ref.1
Corresponds to variant rs1059579 [ dbSNP | Ensembl ].
VAR_017109

Experimental info

Mutagenesis2301K → R: 9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation. Ref.14 Ref.15
Mutagenesis2491K → R: 9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation. Ref.14 Ref.15
Mutagenesis2541K → R: Reduction in sumoylation. Ref.15
Mutagenesis3241S → A: No effect on ternary complex formation but loss of transcriptional activity positive regulation by MAD2L2. Ref.9
Mutagenesis3361T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3531T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3631T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3681T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3831S → A: 17% reduction in ternary complex formation. Ref.9 Ref.18
Mutagenesis3891S → A: 34% reduction in ternary complex formation. Ref.9
Mutagenesis4171T → A: No effect on ternary complex formation. Ref.9
Mutagenesis4221S → A: Slight reduction in ternary complex formation. Ref.9

Secondary structure

.................. 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 68F71F8ADB9D38CA

FASTA42844,888
        10         20         30         40         50         60 
MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK NKTNMNYDKL 

        70         80         90        100        110        120 
SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP PQPEVSVTST MPNVAPAAIH 

       130        140        150        160        170        180 
AAPGDTVSGK PGTPKGAGMA GPGGLARSSR NEYMRSGLYS TFTIQSLQPQ PPPHPRPAVV 

       190        200        210        220        230        240 
LPSAAPAGAA APPSGSRSTS PSPLEACLEA EEAGLPLQVI LTPPEAPNLK SEELNVEPGL 

       250        260        270        280        290        300 
GRALPPEVKV EGPKEELEVA GERGFVPETT KAEPEVPPQE GVPARLPAVV MDTAGQAGGH 

       310        320        330        340        350        360 
AASSPEISQP QKGRKPRDLE LPLSPSLLGG PGPERTPGSG SGSGLQAPGP ALTPSLLPTH 

       370        380        390        400        410        420 
TLTPVLLTPS SLPPSIHFWS TLSPIAPRSP AKLSFQFPSS GSAQVHIPSI SVDGLSTPVV 


LSPGPQKP 

« Hide

Isoform 2 (ELKV) [UniParc].

Checksum: 8347760EEE65634F
Show »

FASTA9511,217

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"SUMOylation regulates nucleo-cytoplasmic shuttling of Elk-1."
Salinas S., Briancon-Marjollet A., Bossis G., Lopez M.-A., Piechaczyk M., Jariel-Encontre I., Debant A., Hipskind R.A.
J. Cell Biol. 165:767-773(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14283.1. [P19419-1]
CCDS59165.1. [P19419-2]
PIRTVHUEK. A41354.
RefSeqNP_001107595.1. NM_001114123.2. [P19419-1]
NP_001244097.1. NM_001257168.1. [P19419-2]
NP_005220.2. NM_005229.4. [P19419-1]
UniGeneHs.181128.
Hs.715039.
Hs.740673.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DUXX-ray2.10C/F1-94[»]
ProteinModelPortalP19419.
SMRP19419. Positions 5-90.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108317. 28 interactions.
DIPDIP-36057N.
IntActP19419. 8 interactions.
MINTMINT-3380115.
STRING9606.ENSP00000247161.

Chemistry

ChEMBLCHEMBL4453.

PTM databases

PhosphoSiteP19419.

Polymorphism databases

DMDM12643407.

Proteomic databases

MaxQBP19419.
PaxDbP19419.
PRIDEP19419.

Protocols and materials databases

DNASU2002.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247161; ENSP00000247161; ENSG00000126767. [P19419-1]
ENST00000343894; ENSP00000345585; ENSG00000126767. [P19419-2]
ENST00000376983; ENSP00000366182; ENSG00000126767. [P19419-1]
GeneID2002.
KEGGhsa:2002.
UCSCuc004dik.5. human. [P19419-1]
uc004dil.5. human. [P19419-2]

Organism-specific databases

CTD2002.
GeneCardsGC0XM047494.
H-InvDBHIX0016766.
HGNCHGNC:3321. ELK1.
HPACAB003808.
HPA036084.
MIM311040. gene.
neXtProtNX_P19419.
PharmGKBPA27749.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269367.
HOVERGENHBG004344.
KOK04375.
OMAPNPLEAC.
OrthoDBEOG7NPFTD.
PhylomeDBP19419.
TreeFamTF317732.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP19419.

Gene expression databases

ArrayExpressP19419.
BgeeP19419.
CleanExHS_ELK1.
GenevestigatorP19419.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR000418. Ets_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00178. Ets. 1 hit.
[Graphical view]
PRINTSPR00454. ETSDOMAIN.
SMARTSM00413. ETS. 1 hit.
[Graphical view]
PROSITEPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSELK1. human.
EvolutionaryTraceP19419.
GeneWikiELK1.
GenomeRNAi2002.
NextBio8101.
PROP19419.
SOURCESearch...

Entry information

Entry nameELK1_HUMAN
AccessionPrimary (citable) accession number: P19419
Secondary accession number(s): B2R7H4 expand/collapse secondary AC list , O75606, O95058, Q969X8, Q9UJM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM