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P19419

- ELK1_HUMAN

UniProt

P19419 - ELK1_HUMAN

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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

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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  3. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP19419.
CleanExiHS_ELK1.
ExpressionAtlasiP19419. baseline and differential.
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
SUMO1P631655EBI-726632,EBI-80140
UBE2IP632797EBI-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 – 1711Combined sources
Beta strandi19 – 235Combined sources
Beta strandi25 – 284Combined sources
Turni29 – 324Combined sources
Beta strandi33 – 353Combined sources
Helixi39 – 4810Combined sources
Turni49 – 513Combined sources
Helixi57 – 6711Combined sources
Turni68 – 714Combined sources
Beta strandi72 – 754Combined sources
Beta strandi82 – 876Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118996.
HOVERGENiHBG004344.
InParanoidiP19419.
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

        10         20         30         40         50
MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK
60 70 80 90 100
NKTNMNYDKL SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP
110 120 130 140 150
PQPEVSVTST MPNVAPAAIH AAPGDTVSGK PGTPKGAGMA GPGGLARSSR
160 170 180 190 200
NEYMRSGLYS TFTIQSLQPQ PPPHPRPAVV LPSAAPAGAA APPSGSRSTS
210 220 230 240 250
PSPLEACLEA EEAGLPLQVI LTPPEAPNLK SEELNVEPGL GRALPPEVKV
260 270 280 290 300
EGPKEELEVA GERGFVPETT KAEPEVPPQE GVPARLPAVV MDTAGQAGGH
310 320 330 340 350
AASSPEISQP QKGRKPRDLE LPLSPSLLGG PGPERTPGSG SGSGLQAPGP
360 370 380 390 400
ALTPSLLPTH TLTPVLLTPS SLPPSIHFWS TLSPIAPRSP AKLSFQFPSS
410 420
GSAQVHIPSI SVDGLSTPVV LSPGPQKP
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000619324; ENSP00000483056; 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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ]
ENST00000619324 ; ENSP00000483056 ; 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.
GeneTreei ENSGT00760000118996.
HOVERGENi HBG004344.
InParanoidi P19419.
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

Bgeei P19419.
CleanExi HS_ELK1.
ExpressionAtlasi P19419. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 169 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

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