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Protein

ETS domain-containing protein Elk-1

Gene

ELK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000126767.17
HGNCiHGNC:3321 ELK1
MIMi311040 gene
neXtProtiNX_P19419

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Show more details

GO - Molecular functioni

  • RNA polymerase II transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108317, 28 interactors
CORUMiP19419
DIPiDIP-36057N
ELMiP19419
IntActiP19419, 10 interactors
MINTiP19419
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[»]
5VVTX-ray2.80B/D378-385[»]
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

Phylogenomic databases

eggNOGiKOG3806 Eukaryota
ENOG410Z0ZF LUCA
GeneTreeiENSGT00760000118907
HOVERGENiHBG004344
InParanoidiP19419
KOiK04375
OMAiRRATHRF
OrthoDBiEOG091G0CL4
PhylomeDBiP19419
TreeFamiTF317732

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR000418 Ets_dom
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00178 Ets, 1 hit
PRINTSiPR00454 ETSDOMAIN
SMARTiView protein in SMART
SM00413 ETS, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00345 ETS_DOMAIN_1, 1 hit
PS00346 ETS_DOMAIN_2, 1 hit
PS50061 ETS_DOMAIN_3, 1 hit

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 dbSNP:rs1997639Ensembl.1
Natural variantiVAR_017109183S → N1 PublicationCorresponds to variant dbSNP:rs1059579Ensembl.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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiELK1_HUMAN
AccessioniPrimary (citable) accession number: P19419
Secondary accession number(s): B2R7H4
, O75606, O95058, Q969X8, Q9UJM4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 24, 2001
Last modified: March 28, 2018
This is version 200 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health