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Protein

ETS domain-containing protein Elk-1

Gene

ELK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2. Induces target gene transcription upon JNK-signaling pathway stimulation (By similarity).By similarity2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi5 – 86ETSPROSITE-ProRule annotationAdd BLAST82

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126767-MONOMER.
ReactomeiR-HSA-198753. ERK/MAPK targets.
SignaLinkiP19419.
SIGNORiP19419.

Names & Taxonomyi

Protein namesi
Recommended name:
ETS domain-containing protein Elk-1
Gene namesi
Name:ELK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3321. ELK1.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: Ensembl
  • dendrite Source: Ensembl
  • mitochondrion Source: Ensembl
  • neuronal cell body Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi230K → R: 9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation. 2 Publications1
Mutagenesisi249K → R: 9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation. 2 Publications1
Mutagenesisi254K → R: Reduction in sumoylation. 1 Publication1
Mutagenesisi324S → A: No effect on ternary complex formation but loss of transcriptional activity positive regulation by MAD2L2. 1 Publication1
Mutagenesisi336T → A: No effect on ternary complex formation. 1 Publication1
Mutagenesisi353T → A: No effect on ternary complex formation. 1 Publication1
Mutagenesisi363T → A: No effect on ternary complex formation. 1 Publication1
Mutagenesisi368T → A: No effect on ternary complex formation. 1 Publication1
Mutagenesisi383S → A: 17% reduction in ternary complex formation. 2 Publications1
Mutagenesisi389S → A: 34% reduction in ternary complex formation. 1 Publication1
Mutagenesisi417T → A: No effect on ternary complex formation. 1 Publication1
Mutagenesisi422S → A: Slight reduction in ternary complex formation. 1 Publication1

Organism-specific databases

DisGeNETi2002.
OpenTargetsiENSG00000126767.
PharmGKBiPA27749.

Chemistry databases

ChEMBLiCHEMBL4453.

Polymorphism and mutation databases

BioMutaiELK1.
DMDMi12643407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002040951 – 428ETS domain-containing protein Elk-1Add BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei324Phosphoserine; by MAPK1Combined sources1 Publication1
Modified residuei336Phosphothreonine; by MAPK11 Publication1
Modified residuei353Phosphothreonine; by MAPK11 Publication1
Modified residuei363Phosphothreonine; by MAPK11 Publication1
Modified residuei368Phosphothreonine; by MAPK11 Publication1
Modified residuei383Phosphoserine; by MAPK1 and MAPK83 Publications1
Modified residuei389Phosphoserine; by MAPK12 Publications1
Modified residuei417Phosphothreonine; by MAPK11 Publication1
Modified residuei422Phosphoserine; by MAPK1Combined sources1 Publication1

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. Upon bFGF stimulus, phosphorylated by PAK1 (By similarity).By similarity5 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP19419.
MaxQBiP19419.
PaxDbiP19419.
PeptideAtlasiP19419.
PRIDEiP19419.

PTM databases

iPTMnetiP19419.
PhosphoSitePlusiP19419.

Expressioni

Tissue specificityi

Lung and testis.

Gene expression databases

BgeeiENSG00000126767.
CleanExiHS_ELK1.
ExpressionAtlasiP19419. baseline and differential.
GenevisibleiP19419. HS.

Organism-specific databases

HPAiCAB003808.
HPA036084.
HPA064381.

Interactioni

Subunit structurei

Interacts in its sumoylated form with PIAS2/PIASX which enhances its transcriptional activator activity (PubMed:15920481). Interacts with MAD2L2; the interaction is direct and promotes phosphorylation by the kinases MAPK8 and/or MAPK9 (PubMed:17296730). Interacts with POU1F1 (PubMed:26612202).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK3P273612EBI-726632,EBI-73995
SUMO1P631655EBI-726632,EBI-80140
UBE2IP632797EBI-726632,EBI-80168

GO - Molecular functioni

  • RNA polymerase II transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108317. 28 interactors.
DIPiDIP-36057N.
IntActiP19419. 10 interactors.
MINTiMINT-3380115.
STRINGi9606.ENSP00000247161.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 17Combined sources11
Beta strandi19 – 23Combined sources5
Beta strandi25 – 28Combined sources4
Turni29 – 32Combined sources4
Beta strandi33 – 35Combined sources3
Helixi39 – 48Combined sources10
Turni49 – 51Combined sources3
Helixi57 – 67Combined sources11
Turni68 – 71Combined sources4
Beta strandi72 – 75Combined sources4
Beta strandi82 – 87Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DUXX-ray2.10C/F1-94[»]
ProteinModelPortaliP19419.
SMRiP19419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19419.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni349 – 399Sufficient for interaction with MAD2L21 PublicationAdd BLAST51

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3806. Eukaryota.
ENOG410Z0ZF. LUCA.
GeneTreeiENSGT00760000118907.
HOVERGENiHBG004344.
InParanoidiP19419.
KOiK04375.
OMAiKSEEPNM.
OrthoDBiEOG091G0CL4.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_017108144G → S.Corresponds to variant rs1997639dbSNPEnsembl.1
Natural variantiVAR_017109183S → N.1 PublicationCorresponds to variant rs1059579dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00146691 – 95VAGCS → SHCAP in isoform 2. Curated5
Alternative sequenceiVSP_00146796 – 428Missing in isoform 2. CuratedAdd BLAST333

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]
XP_016884828.1. XM_017029339.1. [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.6. human. [P19419-1]

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.
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]
XP_016884828.1. XM_017029339.1. [P19419-1]
UniGeneiHs.181128.
Hs.715039.
Hs.740673.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DUXX-ray2.10C/F1-94[»]
ProteinModelPortaliP19419.
SMRiP19419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108317. 28 interactors.
DIPiDIP-36057N.
IntActiP19419. 10 interactors.
MINTiMINT-3380115.
STRINGi9606.ENSP00000247161.

Chemistry databases

ChEMBLiCHEMBL4453.

PTM databases

iPTMnetiP19419.
PhosphoSitePlusiP19419.

Polymorphism and mutation databases

BioMutaiELK1.
DMDMi12643407.

Proteomic databases

EPDiP19419.
MaxQBiP19419.
PaxDbiP19419.
PeptideAtlasiP19419.
PRIDEiP19419.

Protocols and materials databases

DNASUi2002.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247161; ENSP00000247161; ENSG00000126767. [P19419-1]
ENST00000343894; ENSP00000345585; ENSG00000126767. [P19419-2]
ENST00000376983; ENSP00000366182; ENSG00000126767. [P19419-1]
GeneIDi2002.
KEGGihsa:2002.
UCSCiuc004dik.6. human. [P19419-1]

Organism-specific databases

CTDi2002.
DisGeNETi2002.
GeneCardsiELK1.
H-InvDBHIX0016766.
HGNCiHGNC:3321. ELK1.
HPAiCAB003808.
HPA036084.
HPA064381.
MIMi311040. gene.
neXtProtiNX_P19419.
OpenTargetsiENSG00000126767.
PharmGKBiPA27749.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3806. Eukaryota.
ENOG410Z0ZF. LUCA.
GeneTreeiENSGT00760000118907.
HOVERGENiHBG004344.
InParanoidiP19419.
KOiK04375.
OMAiKSEEPNM.
OrthoDBiEOG091G0CL4.
PhylomeDBiP19419.
TreeFamiTF317732.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126767-MONOMER.
ReactomeiR-HSA-198753. ERK/MAPK targets.
SignaLinkiP19419.
SIGNORiP19419.

Miscellaneous databases

ChiTaRSiELK1. human.
EvolutionaryTraceiP19419.
GeneWikiiELK1.
GenomeRNAii2002.
PROiP19419.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126767.
CleanExiHS_ELK1.
ExpressionAtlasiP19419. baseline and differential.
GenevisibleiP19419. HS.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 189 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.