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Database: UniProt
Entry: Q00422
LinkDB: Q00422
Original site: Q00422 
ID   GABPA_MOUSE             Reviewed;         454 AA.
AC   Q00422; Q7TT22;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   07-OCT-2020, entry version 187.
DE   RecName: Full=GA-binding protein alpha chain;
DE            Short=GABP subunit alpha;
GN   Name=Gabpa; Synonyms=E4tf1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1876836; DOI=10.1126/science.1876836;
RA   Lamarco K., Thompson C.C., Byers B.P., Walton E.M., McKnight S.L.;
RT   "Identification of Ets- and notch-related subunits in GA binding protein.";
RL   Science 253:789-792(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 320-320.
RX   PubMed=9461436; DOI=10.1126/science.279.5353.1037;
RA   Batchelor A.H., Piper D.E., de la Brousse F.C., McKnight S.L.,
RA   Wolberger C.;
RT   "The structure of GABPalpha/beta: an ETS domain-ankyrin repeat heterodimer
RT   bound to DNA.";
RL   Science 279:1037-1041(1998).
CC   -!- FUNCTION: Transcription factor capable of interacting with purine rich
CC       repeats (GA repeats).
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
DR   EMBL; M74515; AAA53030.1; -; mRNA.
DR   EMBL; AK139916; BAE24181.1; -; mRNA.
DR   EMBL; AK145446; BAE26442.1; -; mRNA.
DR   EMBL; AK145838; BAE26687.1; -; mRNA.
DR   EMBL; AK148087; BAE28337.1; -; mRNA.
DR   EMBL; AK150455; BAE29575.1; -; mRNA.
DR   EMBL; CH466521; EDK98317.1; -; Genomic_DNA.
DR   EMBL; BC052448; AAH52448.1; -; mRNA.
DR   CCDS; CCDS28284.1; -.
DR   PIR; A40858; A40858.
DR   RefSeq; NP_032091.2; NM_008065.2.
DR   RefSeq; XP_006522970.1; XM_006522907.2.
DR   PDB; 1AWC; X-ray; 2.15 A; A=320-429.
DR   PDB; 1SXD; NMR; -; A=168-254.
DR   PDB; 2JUO; NMR; -; A=35-121.
DR   PDBsum; 1AWC; -.
DR   PDBsum; 1SXD; -.
DR   PDBsum; 2JUO; -.
DR   BMRB; Q00422; -.
DR   SMR; Q00422; -.
DR   BioGRID; 199795; 1.
DR   DIP; DIP-156N; -.
DR   IntAct; Q00422; 1.
DR   MINT; Q00422; -.
DR   STRING; 10090.ENSMUSP00000009120; -.
DR   iPTMnet; Q00422; -.
DR   PhosphoSitePlus; Q00422; -.
DR   EPD; Q00422; -.
DR   MaxQB; Q00422; -.
DR   PaxDb; Q00422; -.
DR   PeptideAtlas; Q00422; -.
DR   PRIDE; Q00422; -.
DR   Antibodypedia; 919; 397 antibodies.
DR   Ensembl; ENSMUST00000009120; ENSMUSP00000009120; ENSMUSG00000008976.
DR   Ensembl; ENSMUST00000114184; ENSMUSP00000109822; ENSMUSG00000008976.
DR   GeneID; 14390; -.
DR   KEGG; mmu:14390; -.
DR   UCSC; uc007ztj.1; mouse.
DR   CTD; 2551; -.
DR   MGI; MGI:95610; Gabpa.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000155799; -.
DR   HOGENOM; CLU_037064_0_0_1; -.
DR   InParanoid; Q00422; -.
DR   KO; K09441; -.
DR   OMA; QELEPHK; -.
DR   OrthoDB; 526256at2759; -.
DR   TreeFam; TF350537; -.
DR   Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   BioGRID-ORCS; 14390; 8 hits in 20 CRISPR screens.
DR   ChiTaRS; Gabpa; mouse.
DR   EvolutionaryTrace; Q00422; -.
DR   PRO; PR:Q00422; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q00422; protein.
DR   Bgee; ENSMUSG00000008976; Expressed in forelimb bud and 336 other tissues.
DR   Genevisible; Q00422; MM.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:1903351; P:cellular response to dopamine; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
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   3D-structure; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..454
FT                   /note="GA-binding protein alpha chain"
FT                   /id="PRO_0000204128"
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:0000250|UniProtKB:Q06546"
FT   CONFLICT        188
FT                   /note="H -> R (in Ref. 1; AAA53030)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..47
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   HELIX           48..50
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   HELIX           51..54
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   HELIX           56..59
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   STRAND          67..70
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   TURN            81..83
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   STRAND          90..99
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   STRAND          107..115
FT                   /evidence="ECO:0000244|PDB:2JUO"
FT   HELIX           168..177
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   TURN            178..180
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           186..188
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           191..204
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           213..215
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           219..224
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           227..233
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           238..249
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   TURN            250..252
FT                   /evidence="ECO:0000244|PDB:1SXD"
FT   HELIX           322..330
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   TURN            333..338
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   STRAND          339..341
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   STRAND          343..349
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   HELIX           353..364
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   HELIX           371..379
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   HELIX           380..383
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   STRAND          384..389
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   STRAND          396..399
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   HELIX           403..406
FT                   /evidence="ECO:0000244|PDB:1AWC"
FT   HELIX           411..428
FT                   /evidence="ECO:0000244|PDB:1AWC"
SQ   SEQUENCE   454 AA;  51344 MW;  2CBC40B895563685 CRC64;
     MTKREAEELI EIEIDGTEKA ECTEESIVEQ TYTPAECVSQ AIDINEPIGN LKKLLEPRLQ
     CSLDAHEICL QDIQLDPDRS LFDQGVKTDG TVQLSVQVIS YQGMEPKLNI LEIVKTAETV
     EVVIDPDAHH AEAEAHLVEE AQVITLDGTK HITTISDETS EQVTRWAAAL EGYRKEQERL
     GIPYDPIHWS TDQVLHWVVW VMKEFSMTDI DLTTLNISGR ELCSLNQEDF FQRVPRGEIL
     WSHLELLRKY VLASQEQQMN EIVTIDQPVQ IIPASVPPAT PTTIKVINSS AKAAKVQRSP
     RISGEDRSSP GNRTGNNGQI QLWQFLLELL TDKDARDCIS WVGDEGEFKL NQPELVAQKW
     GQRKNKPTMN YEKLSRALRY YYDGDMICKV QGKRFVYKFV CDLKTLIGYS AAELNRLVIE
     CEQKKLARMQ LHGIAQPVTA VALAATSLQA DKEI
//
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