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Database: UniProt
Entry: Q06546
LinkDB: Q06546
Original site: Q06546 
ID   GABPA_HUMAN             Reviewed;         454 AA.
AC   Q06546; Q12939;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   07-OCT-2020, entry version 198.
DE   RecName: Full=GA-binding protein alpha chain;
DE            Short=GABP subunit alpha;
DE   AltName: Full=Nuclear respiratory factor 2 subunit alpha;
DE   AltName: Full=Transcription factor E4TF1-60;
GN   Name=GABPA; Synonyms=E4TF1A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8441384; DOI=10.1128/mcb.13.3.1385;
RA   Watanabe H., Sawada J., Yano K., Yamaguchi K., Goto M., Handa H.;
RT   "cDNA cloning of transcription factor E4TF1 subunits with Ets and notch
RT   motifs.";
RL   Mol. Cell. Biol. 13:1385-1391(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7799916; DOI=10.1128/mcb.15.1.102;
RA   Gugneja S., Virbasius J.V., Scarpulla R.C.;
RT   "Four structurally distinct, non-DNA-binding subunits of human nuclear
RT   respiratory factor 2 share a conserved transcriptional activation domain.";
RL   Mol. Cell. Biol. 15:102-111(1995).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Transcription factor capable of interacting with purine rich
CC       repeats (GA repeats). Necessary for the expression of the Adenovirus E4
CC       gene.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC   -!- INTERACTION:
CC       Q06546; Q06547: GABPB1; NbExp=3; IntAct=EBI-638925, EBI-618165;
CC       Q06546; Q8TAK5: GABPB2; NbExp=4; IntAct=EBI-638925, EBI-8468945;
CC       Q06546; P51610: HCFC1; NbExp=2; IntAct=EBI-638925, EBI-396176;
CC       Q06546; O75716: STK16; NbExp=3; IntAct=EBI-638925, EBI-749295;
CC       Q06546; Q5TFG8: ZC2HC1B; NbExp=3; IntAct=EBI-638925, EBI-12275374;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
DR   EMBL; D13318; BAA02575.1; -; mRNA.
DR   EMBL; U13044; AAA65706.1; -; mRNA.
DR   CCDS; CCDS13575.1; -.
DR   PIR; A48146; A48146.
DR   PIR; I38739; I38739.
DR   RefSeq; NP_001184226.1; NM_001197297.1.
DR   RefSeq; NP_002031.2; NM_002040.3.
DR   RefSeq; XP_005260995.1; XM_005260938.4.
DR   RefSeq; XP_011527822.1; XM_011529520.2.
DR   RefSeq; XP_011527823.1; XM_011529521.2.
DR   RefSeq; XP_016883802.1; XM_017028313.1.
DR   BMRB; Q06546; -.
DR   SMR; Q06546; -.
DR   BioGRID; 108826; 32.
DR   DIP; DIP-33980N; -.
DR   IntAct; Q06546; 12.
DR   MINT; Q06546; -.
DR   STRING; 9606.ENSP00000346886; -.
DR   GlyGen; Q06546; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q06546; -.
DR   PhosphoSitePlus; Q06546; -.
DR   BioMuta; GABPA; -.
DR   DMDM; 729553; -.
DR   EPD; Q06546; -.
DR   jPOST; Q06546; -.
DR   MassIVE; Q06546; -.
DR   MaxQB; Q06546; -.
DR   PaxDb; Q06546; -.
DR   PeptideAtlas; Q06546; -.
DR   PRIDE; Q06546; -.
DR   ProteomicsDB; 58457; -.
DR   Antibodypedia; 919; 397 antibodies.
DR   DNASU; 2551; -.
DR   Ensembl; ENST00000354828; ENSP00000346886; ENSG00000154727.
DR   Ensembl; ENST00000400075; ENSP00000382948; ENSG00000154727.
DR   GeneID; 2551; -.
DR   KEGG; hsa:2551; -.
DR   UCSC; uc002ylx.5; human.
DR   CTD; 2551; -.
DR   DisGeNET; 2551; -.
DR   EuPathDB; HostDB:ENSG00000154727.10; -.
DR   GeneCards; GABPA; -.
DR   HGNC; HGNC:4071; GABPA.
DR   HPA; ENSG00000154727; Low tissue specificity.
DR   MIM; 600609; gene.
DR   neXtProt; NX_Q06546; -.
DR   OpenTargets; ENSG00000154727; -.
DR   PharmGKB; PA28485; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000155799; -.
DR   HOGENOM; CLU_037064_0_0_1; -.
DR   InParanoid; Q06546; -.
DR   KO; K09441; -.
DR   OMA; QELEPHK; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; Q06546; -.
DR   TreeFam; TF350537; -.
DR   PathwayCommons; Q06546; -.
DR   Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   BioGRID-ORCS; 2551; 499 hits in 884 CRISPR screens.
DR   ChiTaRS; GABPA; human.
DR   GeneWiki; GABPA; -.
DR   GenomeRNAi; 2551; -.
DR   Pharos; Q06546; Tbio.
DR   PRO; PR:Q06546; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; Q06546; protein.
DR   Bgee; ENSG00000154727; Expressed in calcaneal tendon and 218 other tissues.
DR   ExpressionAtlas; Q06546; baseline and differential.
DR   Genevisible; Q06546; HS.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
DR   GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
DR   GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR024668; GABP_asu_N.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR016312; TF_GA-bd_asu.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF11620; GABP-alpha; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PIRSF; PIRSF001703; GABP_alpha; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..454
FT                   /note="GA-binding protein alpha chain"
FT                   /id="PRO_0000204127"
FT   DOMAIN          168..251
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        320..400
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VARIANT         291
FT                   /note="A -> V (in dbSNP:rs2829897)"
FT                   /id="VAR_020315"
FT   VARIANT         345
FT                   /note="E -> K (in dbSNP:rs2829900)"
FT                   /id="VAR_020316"
FT   CONFLICT        289..290
FT                   /note="SS -> RC (in Ref. 2; AAA65706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="A -> V (in Ref. 2; AAA65706)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  51295 MW;  1AF2ABBBC79191DD CRC64;
     MTKREAEELI EIEIDGTEKA ECTEESIVEQ TYAPAECVSQ AIDINEPIGN LKKLLEPRLQ
     CSLDAHEICL QDIQLDPERS LFDQGVKTDG TVQLSVQVIS YQGIEPKLNI LEIVKPADTV
     EVVIDPDAHH AESEAHLVEE AQVITLDGTK HITTISDETS EQVTRWAAAL EGYRKEQERL
     GIPYDPIQWS TDQVLHWVVW VMKEFSMTDI DLTTLNISGR ELCSLNQEDF FQRVPRGEIL
     WSHLELLRKY VLASQEQQMN EIVTIDQPVQ IIPASVQSAT PTTIKVINSS AKAAKVQRAP
     RISGEDRSSP GNRTGNNGQI QLWQFLLELL TDKDARDCIS WVGDEGEFKL NQPELVAQKW
     GQRKNKPTMN YEKLSRALRY YYDGDMICKV QGKRFVYKFV CDLKTLIGYS AAELNRLVTE
     CEQKKLAKMQ LHGIAQPVTA VALATASLQT EKDN
//
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