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ETS domain-containing protein Elk-4 (Serum response factor accessory protein 1) (SAP-1) (SRF accessory protein 1)

 ELK4_HUMAN              Reviewed;         431 AA.
P28324; P28323; Q6GSJ2;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 3.
18-JUL-2018, entry version 174.
RecName: Full=ETS domain-containing protein Elk-4;
AltName: Full=Serum response factor accessory protein 1;
Short=SAP-1;
Short=SRF accessory protein 1;
Name=ELK4; Synonyms=SAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=1339307; DOI=10.1016/0092-8674(92)90194-H;
Dalton S., Treisman R.;
"Characterization of SAP-1, a protein recruited by serum response
factor to the c-fos serum response element.";
Cell 68:597-612(1992).
[2]
SEQUENCE REVISION.
PubMed=8293474;
Dalton S., Treisman R.;
"Characterization of SAP-1, a protein recruited by serum response
factor to the c-fos serum response element.";
Cell 76:411-411(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[7]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[8]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-93.
PubMed=9734357; DOI=10.1016/S1097-2765(00)80130-6;
Mo Y., Vaessen B., Johnston K., Marmorstein R.;
"Structures of SAP-1 bound to DNA targets from the E74 and c-fos
promoters: insights into DNA sequence discrimination by Ets
proteins.";
Mol. Cell 2:201-212(1998).
[9]
FUNCTION, AND INTERACTION WITH SIRT7.
PubMed=22722849; DOI=10.1038/nature11043;
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.;
"SIRT7 links H3K18 deacetylation to maintenance of oncogenic
transformation.";
Nature 487:114-118(2012).
-!- 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. {ECO:0000269|PubMed:22722849}.
-!- SUBUNIT: Interacts with SIRT7. {ECO:0000269|PubMed:22722849}.
-!- INTERACTION:
Q9NRC8:SIRT7; NbExp=3; IntAct=EBI-11277718, EBI-716046;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=SAP-1A;
IsoId=P28324-1; Sequence=Displayed;
Name=2; Synonyms=SAP-1B;
IsoId=P28324-2; Sequence=VSP_001468;
-!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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EMBL; M85165; AAA03631.1; -; mRNA.
EMBL; M85164; AAA03632.1; -; mRNA.
EMBL; CH471067; EAW91570.1; -; Genomic_DNA.
EMBL; BC063676; AAH63676.1; -; mRNA.
CCDS; CCDS1456.1; -. [P28324-1]
CCDS; CCDS1457.1; -. [P28324-2]
PIR; A42093; A42093.
PIR; A53012; A53012.
PIR; B42093; B42093.
RefSeq; NP_001964.2; NM_001973.3. [P28324-1]
RefSeq; NP_068567.1; NM_021795.2. [P28324-2]
RefSeq; XP_005245007.1; XM_005244950.4. [P28324-1]
RefSeq; XP_005245008.1; XM_005244951.4. [P28324-1]
UniGene; Hs.497520; -.
UniGene; Hs.602654; -.
PDB; 1BC7; X-ray; 2.01 A; C=1-93.
PDB; 1BC8; X-ray; 1.93 A; C=1-93.
PDB; 1HBX; X-ray; 3.15 A; G/H=2-156.
PDB; 1K6O; X-ray; 3.19 A; A=1-93.
PDBsum; 1BC7; -.
PDBsum; 1BC8; -.
PDBsum; 1HBX; -.
PDBsum; 1K6O; -.
ProteinModelPortal; P28324; -.
SMR; P28324; -.
BioGrid; 108320; 12.
CORUM; P28324; -.
DIP; DIP-59907N; -.
IntAct; P28324; 3.
STRING; 9606.ENSP00000350681; -.
iPTMnet; P28324; -.
PhosphoSitePlus; P28324; -.
BioMuta; ELK4; -.
DMDM; 12585557; -.
MaxQB; P28324; -.
PaxDb; P28324; -.
PeptideAtlas; P28324; -.
PRIDE; P28324; -.
ProteomicsDB; 54462; -.
ProteomicsDB; 54463; -. [P28324-2]
DNASU; 2005; -.
Ensembl; ENST00000289703; ENSP00000289703; ENSG00000158711. [P28324-2]
Ensembl; ENST00000357992; ENSP00000350681; ENSG00000158711. [P28324-1]
Ensembl; ENST00000616704; ENSP00000483628; ENSG00000158711. [P28324-1]
GeneID; 2005; -.
KEGG; hsa:2005; -.
UCSC; uc001hcy.3; human. [P28324-1]
CTD; 2005; -.
DisGeNET; 2005; -.
EuPathDB; HostDB:ENSG00000158711.13; -.
GeneCards; ELK4; -.
HGNC; HGNC:3326; ELK4.
HPA; HPA028863; -.
MIM; 600246; gene.
neXtProt; NX_P28324; -.
OpenTargets; ENSG00000158711; -.
PharmGKB; PA27753; -.
eggNOG; KOG3806; Eukaryota.
eggNOG; ENOG410Z0ZF; LUCA.
GeneTree; ENSGT00760000118907; -.
HOVERGEN; HBG004344; -.
InParanoid; P28324; -.
KO; K04376; -.
OMA; ICWTSNN; -.
OrthoDB; EOG091G0COO; -.
PhylomeDB; P28324; -.
TreeFam; TF317732; -.
SignaLink; P28324; -.
SIGNOR; P28324; -.
ChiTaRS; ELK4; human.
EvolutionaryTrace; P28324; -.
GeneWiki; ELK4; -.
GenomeRNAi; 2005; -.
PRO; PR:P28324; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158711; -.
CleanEx; HS_ELK4; -.
ExpressionAtlas; P28324; baseline and differential.
Genevisible; P28324; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; TAS:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003700; F:DNA binding transcription factor activity; NAS:ProtInc.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003712; F:transcription coregulator activity; TAS:ProtInc.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IC:NTNU_SB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0070932; P:histone H3 deacetylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00178; Ets; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00345; ETS_DOMAIN_1; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 431 ETS domain-containing protein Elk-4.
/FTId=PRO_0000204099.
DNA_BIND 5 85 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 361 431 TPIILTPSPLLSSIHFWSTLSPVAPLSPARLQGANTLFQFP
SVLNSHGPFTLSGLDGPSTPGPFSPDLQKT -> VACSLFM
VSPLLSFICPFKQIQNLYTQVCFLLLRFVLERLCVTVM
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_001468.
CONFLICT 326 326 E -> G (in Ref. 1; AAA03631).
{ECO:0000305}.
HELIX 7 14 {ECO:0000244|PDB:1BC8}.
HELIX 18 20 {ECO:0000244|PDB:1BC8}.
TURN 21 23 {ECO:0000244|PDB:1BC8}.
STRAND 24 26 {ECO:0000244|PDB:1BC8}.
STRAND 28 34 {ECO:0000244|PDB:1BC8}.
HELIX 38 49 {ECO:0000244|PDB:1BC8}.
HELIX 56 69 {ECO:0000244|PDB:1BC8}.
STRAND 71 74 {ECO:0000244|PDB:1BC8}.
STRAND 76 78 {ECO:0000244|PDB:1K6O}.
STRAND 81 84 {ECO:0000244|PDB:1BC8}.
TURN 85 88 {ECO:0000244|PDB:1BC8}.
HELIX 89 91 {ECO:0000244|PDB:1BC8}.
HELIX 138 143 {ECO:0000244|PDB:1HBX}.
STRAND 144 152 {ECO:0000244|PDB:1HBX}.
HELIX 153 155 {ECO:0000244|PDB:1HBX}.
SEQUENCE 431 AA; 46900 MW; 80EE3E69995C7A7D CRC64;
MDSAITLWQF LLQLLQKPQN KHMICWTSND GQFKLLQAEE VARLWGIRKN KPNMNYDKLS
RALRYYYVKN IIKKVNGQKF VYKFVSYPEI LNMDPMTVGR IEGDCESLNF SEVSSSSKDV
ENGGKDKPPQ PGAKTSSRND YIHSGLYSSF TLNSLNSSNV KLFKLIKTEN PAEKLAEKKS
PQEPTPSVIK FVTTPSKKPP VEPVAATISI GPSISPSSEE TIQALETLVS PKLPSLEAPT
SASNVMTAFA TTPPISSIPP LQEPPRTPSP PLSSHPDIDT DIDSVASQPM ELPENLSLEP
KDQDSVLLEK DKVNNSSRSK KPKGLELAPT LVITSSDPSP LGILSPSLPT ASLTPAFFSQ
TPIILTPSPL LSSIHFWSTL SPVAPLSPAR LQGANTLFQF PSVLNSHGPF TLSGLDGPST
PGPFSPDLQK T


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