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P28324 (ELK4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ETS domain-containing protein Elk-4
Alternative name(s):
Serum response factor accessory protein 1
Short name=SAP-1
Short name=SRF accessory protein 1
Gene names
Name:ELK4
Synonyms:SAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in both transcriptional activation and repression. Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 at promoters, followed by deacetylation of histone H3 at 'Lys-18' (H3K18Ac) and subsequent transcription repression. Forms a ternary complex with the serum response factor (SRF). Requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5'side of SRF, but does not bind DNA autonomously. Ref.7

Subunit structure

Interacts with SIRT7. Ref.7

Subcellular location

Nucleus.

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
   LigandDNA-binding
   Molecular functionActivator
Repressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

histone H3 deacetylation

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.7. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

chromatin binding

Inferred from direct assay Ref.7. Source: UniProtKB

core promoter binding

Traceable author statement Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. 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

Non-traceable author statement PubMed 7851904. Source: ProtInc

transcription cofactor activity

Traceable author statement PubMed 7851904. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28324-1)

Also known as: SAP-1A;

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: P28324-2)

Also known as: SAP-1B;

The sequence of this isoform differs from the canonical sequence as follows:
     361-431: TPIILTPSPL...GPFSPDLQKT → VACSLFMVSP...VLERLCVTVM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431ETS domain-containing protein Elk-4
PRO_0000204099

Regions

DNA binding5 – 8581ETS

Natural variations

Alternative sequence361 – 43171TPIIL…DLQKT → VACSLFMVSPLLSFICPFKQ IQNLYTQVCFLLLRFVLERL CVTVM in isoform 2.
VSP_001468

Experimental info

Sequence conflict3261E → G in AAA03631. Ref.1

Secondary structure

......................... 431
Helix Strand Turn

Details...

Sequences

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

Last modified January 24, 2001. Version 3.
Checksum: 80EE3E69995C7A7D

FASTA43146,900
        10         20         30         40         50         60 
MDSAITLWQF LLQLLQKPQN KHMICWTSND GQFKLLQAEE VARLWGIRKN KPNMNYDKLS 

        70         80         90        100        110        120 
RALRYYYVKN IIKKVNGQKF VYKFVSYPEI LNMDPMTVGR IEGDCESLNF SEVSSSSKDV 

       130        140        150        160        170        180 
ENGGKDKPPQ PGAKTSSRND YIHSGLYSSF TLNSLNSSNV KLFKLIKTEN PAEKLAEKKS 

       190        200        210        220        230        240 
PQEPTPSVIK FVTTPSKKPP VEPVAATISI GPSISPSSEE TIQALETLVS PKLPSLEAPT 

       250        260        270        280        290        300 
SASNVMTAFA TTPPISSIPP LQEPPRTPSP PLSSHPDIDT DIDSVASQPM ELPENLSLEP 

       310        320        330        340        350        360 
KDQDSVLLEK DKVNNSSRSK KPKGLELAPT LVITSSDPSP LGILSPSLPT ASLTPAFFSQ 

       370        380        390        400        410        420 
TPIILTPSPL LSSIHFWSTL SPVAPLSPAR LQGANTLFQF PSVLNSHGPF TLSGLDGPST 

       430 
PGPFSPDLQK T 

« Hide

Isoform 2 (SAP-1B) [UniParc].

Checksum: 13DC31EA9C6D5B89
Show »

FASTA40544,674

References

« Hide 'large scale' references
[1]"Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element."
Dalton S., Treisman R.
Cell 68:597-612(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[2]"Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element."
Dalton S., Treisman R.
Cell 76:411-411(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]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].
[4]"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 2).
Tissue: Lymph.
[5]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[6]"Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: insights into DNA sequence discrimination by Ets proteins."
Mo Y., Vaessen B., Johnston K., Marmorstein R.
Mol. Cell 2:201-212(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-93.
[7]"SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation."
Barber M.F., Michishita-Kioi E., Xi Y., Tasselli L., Kioi M., Moqtaderi Z., Tennen R.I., Paredes S., Young N.L., Chen K., Struhl K., Garcia B.A., Gozani O., Li W., Chua K.F.
Nature 487:114-118(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIRT7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85165 mRNA. Translation: AAA03631.1.
M85164 mRNA. Translation: AAA03632.1.
CH471067 Genomic DNA. Translation: EAW91570.1.
BC063676 mRNA. Translation: AAH63676.1.
CCDSCCDS1456.1. [P28324-1]
CCDS1457.1. [P28324-2]
PIRA42093.
A53012.
B42093.
RefSeqNP_001964.2. NM_001973.3. [P28324-1]
NP_068567.1. NM_021795.2. [P28324-2]
XP_005245007.1. XM_005244950.2. [P28324-1]
XP_005245008.1. XM_005244951.2. [P28324-1]
UniGeneHs.497520.
Hs.602654.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BC7X-ray2.01C1-93[»]
1BC8X-ray1.93C1-93[»]
1HBXX-ray3.15G/H2-156[»]
1K6OX-ray3.19A1-93[»]
ProteinModelPortalP28324.
SMRP28324. Positions 1-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108320. 5 interactions.
DIPDIP-59907N.
STRING9606.ENSP00000350681.

PTM databases

PhosphoSiteP28324.

Polymorphism databases

DMDM12585557.

Proteomic databases

PaxDbP28324.
PRIDEP28324.

Protocols and materials databases

DNASU2005.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289703; ENSP00000289703; ENSG00000158711. [P28324-2]
ENST00000357992; ENSP00000350681; ENSG00000158711. [P28324-1]
GeneID2005.
KEGGhsa:2005.
UCSCuc001hcy.2. human. [P28324-1]
uc001hcz.3. human. [P28324-2]

Organism-specific databases

CTD2005.
GeneCardsGC01M205577.
HGNCHGNC:3326. ELK4.
HPAHPA028863.
MIM600246. gene.
neXtProtNX_P28324.
PharmGKBPA27753.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317055.
HOVERGENHBG004344.
InParanoidP28324.
KOK04376.
OMAICWTSNN.
OrthoDBEOG7NPFTD.
PhylomeDBP28324.
TreeFamTF317732.

Enzyme and pathway databases

SignaLinkP28324.

Gene expression databases

ArrayExpressP28324.
BgeeP28324.
CleanExHS_ELK4.
GenevestigatorP28324.

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

EvolutionaryTraceP28324.
GeneWikiELK4.
GenomeRNAi2005.
NextBio8113.
PROP28324.
SOURCESearch...

Entry information

Entry nameELK4_HUMAN
AccessionPrimary (citable) accession number: P28324
Secondary accession number(s): P28323, Q6GSJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 141 of the entry and version 3 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM