P19419 (ELK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ETS domain-containing protein Elk-1

Gene names

Name:

ELK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.14 Ref.15 Ref.16 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome 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 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred by curator PubMed 14970218. Source: UniProtKB
Molecular_function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 14970218. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

ETS domain-containing protein Elk-1

PRO_0000204095

Regions

DNA binding

5 – 86

82

ETS

Region

349 – 399

51

Sufficient for interaction with MAD2L2

Amino acid modifications

Modified residue

324

1

Phosphoserine; by MAPK1 Ref.9 Ref.20

Modified residue

336

1

Phosphothreonine; by MAPK1 Ref.9

Modified residue

353

1

Phosphothreonine; by MAPK1 Ref.13

Modified residue

363

1

Phosphothreonine; by MAPK1 Ref.13

Modified residue

368

1

Phosphothreonine; by MAPK1 Ref.13

Modified residue

383

1

Phosphoserine; by MAPK1 and MAPK8 Ref.9 Ref.13 Ref.18

Modified residue

389

1

Phosphoserine; by MAPK1 Ref.9 Ref.13

Modified residue

417

1

Phosphothreonine; by MAPK1 Ref.13

Modified residue

422

1

Phosphoserine; by MAPK1 Ref.9 Ref.20

Cross-link

230

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15

Cross-link

249

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14 Ref.15

Cross-link

254

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15

Natural variations

Alternative sequence

91 – 95

5

VAGCS → SHCAP in isoform 2.

VSP_001466

Alternative sequence

96 – 428

333

Missing in isoform 2.

VSP_001467

Natural variant

144

1

G → S.
Corresponds to variant rs1997639 [ dbSNP | Ensembl ].

VAR_017108

Natural variant

183

1

S → N. Ref.1
Corresponds to variant rs1059579 [ dbSNP | Ensembl ].

VAR_017109

Experimental info

Mutagenesis

230

1

K → R: 9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation. Ref.14 Ref.15

Mutagenesis

249

1

K → R: 9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation. Ref.14 Ref.15

Mutagenesis

254

1

K → R: Reduction in sumoylation. Ref.15

Mutagenesis

324

1

S → A: No effect on ternary complex formation but loss of transcriptional activity positive regulation by MAD2L2. Ref.9

Mutagenesis

336

1

T → A: No effect on ternary complex formation. Ref.9

Mutagenesis

353

1

T → A: No effect on ternary complex formation. Ref.9

Mutagenesis

363

1

T → A: No effect on ternary complex formation. Ref.9

Mutagenesis

368

1

T → A: No effect on ternary complex formation. Ref.9

Mutagenesis

383

1

S → A: 17% reduction in ternary complex formation. Ref.9 Ref.18

Mutagenesis

389

1

S → A: 34% reduction in ternary complex formation. Ref.9

Mutagenesis

417

1

T → A: No effect on ternary complex formation. Ref.9

Mutagenesis

422

1

S → A: Slight reduction in ternary complex formation. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

428

Helix Strand Turn

Details...

Helix

7 – 17

11

Beta strand

19 – 23

5

Beta strand

25 – 28

4

Turn

29 – 32

4

Beta strand

33 – 35

3

Helix

39 – 48

10

Turn

49 – 51

3

Helix

57 – 67

11

Turn

68 – 71

4

Beta strand

72 – 75

4

Beta strand

82 – 87

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 68F71F8ADB9D38CA	FASTA	428	44,888
	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
	Isoform 2 (ELKV) [UniParc]. Checksum: 8347760EEE65634F	FASTA	95	11,217
	10 20 30 40 50 60 MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK NKTNMNYDKL 70 80 90 SRALRYYYDK NIIRKVSGQK FVYKFVSYPE SHCAP

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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.

IPI

IPI00220075.
IPI00301527.

PIR

TVHUEK. A41354.

RefSeq

NP_001107595.1. NM_001114123.2.
NP_001244097.1. NM_001257168.1.
NP_005220.2. NM_005229.4.

UniGene

Hs.181128.
Hs.715039.
Hs.740673.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DUX	X-ray	2.10	C/F	1-94	[»]

ProteinModelPortal

P19419.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36057N.

IntAct

P19419. 6 interactions.

MINT

MINT-3380115.

STRING

9606.ENSP00000247161.

PTM databases

PhosphoSite

P19419.

Polymorphism databases

DMDM

12643407.

Proteomic databases

PaxDb

P19419.

PRIDE

P19419.

Protocols and materials databases

DNASU

2002.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000247161; ENSP00000247161; ENSG00000126767.
ENST00000343894; ENSP00000345585; ENSG00000126767.
ENST00000376983; ENSP00000366182; ENSG00000126767.

GeneID

2002.

KEGG

hsa:2002.

UCSC

uc004dik.4. human.

Organism-specific databases

CTD

2002.

GeneCards

GC0XM047494.

H-InvDB

HIX0016766.

HGNC

HGNC:3321. ELK1.

HPA

CAB003808.

MIM

311040. gene.

neXtProt

NX_P19419.

PharmGKB

PA27749.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG269367.

HOVERGEN

HBG004344.

KO

K04375.

OMA

TPPAMDP.

OrthoDB

EOG41RPVX.

PhylomeDB

P19419.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
bcr_5pathway. BCR signaling pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
pdgfrapathway. PDGFR-alpha signaling pathway.
tcrraspathway. Ras signaling in the CD4+ TCR pathway.
s1p_s1p2_pathway. S1P2 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

SignaLink

P19419.

Gene expression databases

ArrayExpress

P19419.

Bgee

P19419.

CleanEx

HS_ELK1.

Genevestigator

P19419.

GermOnline

ENSG00000126767. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR000418. Ets_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00178. Ets. 1 hit.
[Graphical view]

PRINTS

PR00454. ETSDOMAIN.

SMART

SM00413. ETS. 1 hit.
[Graphical view]

PROSITE

PS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4453.

ChiTaRS

ELK1. human.

EvolutionaryTrace

P19419.

GenomeRNAi

2002.

NextBio

8101.

SOURCE

Search...

Entry information

Entry name

ELK1_HUMAN

Accession

Primary (citable) accession number: P19419
Secondary accession number(s): B2R7H4 , O75606, O95058, Q969X8, Q9UJM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 24, 2001
Last modified:	May 29, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.