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GA-binding protein subunit beta-1 (GABP subunit beta-1) (GABPB-1) (GABP subunit beta-2) (GABPB-2) (Nuclear respiratory factor 2) (Transcription factor E4TF1-47) (Transcription factor E4TF1-53)

 GABP1_HUMAN             Reviewed;         395 AA.
Q06547; A8IE52; Q06545; Q12940; Q12941; Q12942; Q8IYD0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
25-OCT-2017, entry version 182.
RecName: Full=GA-binding protein subunit beta-1;
Short=GABP subunit beta-1;
Short=GABPB-1;
AltName: Full=GABP subunit beta-2;
Short=GABPB-2;
AltName: Full=Nuclear respiratory factor 2;
AltName: Full=Transcription factor E4TF1-47;
AltName: Full=Transcription factor E4TF1-53;
Name=GABPB1; Synonyms=E4TF1B, GABPB, GABPB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8441384; DOI=10.1128/MCB.13.3.1385;
Watanabe H., Sawada J., Yano K., Yamaguchi K., Goto M., Handa H.;
"cDNA cloning of transcription factor E4TF1 subunits with Ets and
notch motifs.";
Mol. Cell. Biol. 13:1385-1391(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Testis;
PubMed=7799916; DOI=10.1128/MCB.15.1.102;
Gugneja S., Virbasius J.V., Scarpulla R.C.;
"Four structurally distinct, non-DNA-binding subunits of human nuclear
respiratory factor 2 share a conserved transcriptional activation
domain.";
Mol. Cell. Biol. 15:102-111(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hepatoma;
Yang S.J., Li K.N., Zhang Y.Q.;
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Prostate, Testis, and Uterus;
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).
[7]
PROTEIN SEQUENCE OF 74-81.
PubMed=7918435; DOI=10.1021/bi00206a017;
Cardot P., Pastier D., Lacorte J.-M., Mangeney M., Zannis V.I.,
Chambaz J.;
"Purification and characterization of nuclear factors binding to the
negative regulatory element D of human apolipoprotein A-II promoter: a
negative regulatory effect is reversed by GABP, an Ets-related
protein.";
Biochemistry 33:12139-12148(1994).
[8]
PROTEIN SEQUENCE OF 105-125 AND 339-385.
PubMed=8383622; DOI=10.1101/gad.7.3.380;
Virbasius J.V., Virbasius C.A., Scarpulla R.C.;
"Identity of GABP with NRF-2, a multisubunit activator of cytochrome
oxidase expression, reveals a cellular role for an ETS domain
activator of viral promoters.";
Genes Dev. 7:380-392(1993).
[9]
FUNCTION, AND MUTAGENESIS OF 262-GLN-GLN-263; 264-VAL-VAL-265;
270-GLN-GLN-271; 273-ILE--ILE-275; GLN-295; 297-ILE--VAL-299;
305-GLN-GLN-306 AND 307-VAL--VAL-310.
PubMed=8816484; DOI=10.1128/MCB.16.10.5708;
Gugneja S., Virbasius C.M., Scarpulla R.C.;
"Nuclear respiratory factors 1 and 2 utilize similar glutamine-
containing clusters of hydrophobic residues to activate
transcription.";
Mol. Cell. Biol. 16:5708-5716(1996).
[10]
FUNCTION, INTERACTION WITH HCFC1, AND MUTAGENESIS OF 264-VAL-VAL-265;
273-ILE--ILE-275; 297-ILE--VAL-299 AND 307-VAL--VAL-310.
PubMed=10675337; DOI=10.1093/emboj/19.4.683;
Vogel J.L., Kristie T.M.;
"The novel coactivator C1 (HCF) coordinates multiprotein enhancer
formation and mediates transcription activation by GABP.";
EMBO J. 19:683-690(2000).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
VARIANT [LARGE SCALE ANALYSIS] ALA-31.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Transcription factor capable of interacting with purine
rich repeats (GA repeats). Necessary for the expression of the
Adenovirus E4 gene. {ECO:0000269|PubMed:10675337,
ECO:0000269|PubMed:8816484}.
-!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
Interacts with HCFC1, causing repression of transcriptional
activity. {ECO:0000269|PubMed:10675337}.
-!- INTERACTION:
Q8CGM1:Adgrb2 (xeno); NbExp=3; IntAct=EBI-618165, EBI-8014984;
Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-618165, EBI-6658203;
Q06546:GABPA; NbExp=4; IntAct=EBI-618165, EBI-638925;
P51610:HCFC1; NbExp=6; IntAct=EBI-618189, EBI-396176;
P25800:LMO1; NbExp=4; IntAct=EBI-618165, EBI-8639312;
P61968:LMO4; NbExp=5; IntAct=EBI-618165, EBI-2798728;
Q96M61:MAGEB18; NbExp=3; IntAct=EBI-618165, EBI-741835;
Q7Z3K3:POGZ; NbExp=5; IntAct=EBI-618165, EBI-1389308;
P57052:RBM11; NbExp=3; IntAct=EBI-618165, EBI-741332;
Q9UHP6:RSPH14; NbExp=3; IntAct=EBI-618165, EBI-748350;
P09012:SNRPA; NbExp=3; IntAct=EBI-618165, EBI-607085;
P08579:SNRPB2; NbExp=3; IntAct=EBI-618165, EBI-1053651;
Q8NHU6:TDRD7; NbExp=4; IntAct=EBI-618165, EBI-624505;
Q12933:TRAF2; NbExp=6; IntAct=EBI-618165, EBI-355744;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=GABPB-1, Beta-1;
IsoId=Q06547-1; Sequence=Displayed;
Name=2; Synonyms=Beta-2;
IsoId=Q06547-2; Sequence=VSP_000275;
Name=3; Synonyms=GABPB-2, Gamma-1;
IsoId=Q06547-3; Sequence=VSP_009337;
Name=4; Synonyms=Gamma-2;
IsoId=Q06547-4; Sequence=VSP_000275, VSP_009337;
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EMBL; D13316; BAA02573.1; -; mRNA.
EMBL; D13317; BAA02574.1; -; mRNA.
EMBL; U13045; AAA65707.1; -; mRNA.
EMBL; U13046; AAA65708.1; -; mRNA.
EMBL; U13047; AAA65709.1; -; mRNA.
EMBL; U13048; AAA65710.1; -; mRNA.
EMBL; EU159454; ABV90874.1; -; mRNA.
EMBL; BT006652; AAP35298.1; -; mRNA.
EMBL; CH471082; EAW77395.1; -; Genomic_DNA.
EMBL; BC016910; AAH16910.1; -; mRNA.
EMBL; BC036080; AAH36080.1; -; mRNA.
EMBL; BC050702; AAH50702.1; -; mRNA.
CCDS; CCDS10135.1; -. [Q06547-2]
CCDS; CCDS10136.1; -. [Q06547-4]
CCDS; CCDS32239.1; -. [Q06547-1]
CCDS; CCDS45258.1; -. [Q06547-3]
PIR; C48146; C48146.
PIR; I38741; I38741.
PIR; I38743; I38743.
PIR; I38744; I38744.
RefSeq; NP_001307839.1; NM_001320910.1. [Q06547-1]
RefSeq; NP_002032.2; NM_002041.4. [Q06547-3]
RefSeq; NP_005245.2; NM_005254.5. [Q06547-1]
RefSeq; NP_057738.1; NM_016654.4. [Q06547-2]
RefSeq; NP_057739.1; NM_016655.4. [Q06547-4]
RefSeq; NP_852092.1; NM_181427.3. [Q06547-4]
RefSeq; XP_005254331.1; XM_005254274.3. [Q06547-1]
RefSeq; XP_016877542.1; XM_017022053.1. [Q06547-2]
UniGene; Hs.654350; -.
ProteinModelPortal; Q06547; -.
SMR; Q06547; -.
BioGrid; 108827; 28.
DIP; DIP-33979N; -.
IntAct; Q06547; 26.
MINT; MINT-1504045; -.
STRING; 9606.ENSP00000220429; -.
iPTMnet; Q06547; -.
PhosphoSitePlus; Q06547; -.
BioMuta; GABPB1; -.
DMDM; 23503070; -.
EPD; Q06547; -.
MaxQB; Q06547; -.
PaxDb; Q06547; -.
PeptideAtlas; Q06547; -.
PRIDE; Q06547; -.
DNASU; 2553; -.
Ensembl; ENST00000220429; ENSP00000220429; ENSG00000104064. [Q06547-1]
Ensembl; ENST00000359031; ENSP00000351923; ENSG00000104064. [Q06547-4]
Ensembl; ENST00000380877; ENSP00000370259; ENSG00000104064. [Q06547-2]
Ensembl; ENST00000396464; ENSP00000379728; ENSG00000104064. [Q06547-4]
Ensembl; ENST00000429662; ENSP00000395771; ENSG00000104064. [Q06547-3]
GeneID; 2553; -.
KEGG; hsa:2553; -.
UCSC; uc001zya.4; human. [Q06547-1]
CTD; 2553; -.
DisGeNET; 2553; -.
EuPathDB; HostDB:ENSG00000104064.16; -.
GeneCards; GABPB1; -.
GeneCards; GABPB1-IT1; -.
HGNC; HGNC:4074; GABPB1.
HPA; HPA019653; -.
HPA; HPA067444; -.
MIM; 600610; gene.
neXtProt; NX_Q06547; -.
OpenTargets; ENSG00000104064; -.
PharmGKB; PA162389163; -.
eggNOG; ENOG410IE1V; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00900000140840; -.
HOVERGEN; HBG051686; -.
InParanoid; Q06547; -.
KO; K09454; -.
OMA; HAQSKFC; -.
OrthoDB; EOG091G0AIM; -.
PhylomeDB; Q06547; -.
TreeFam; TF326036; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
SIGNOR; Q06547; -.
ChiTaRS; GABPB1; human.
GeneWiki; GABPB2; -.
GenomeRNAi; 2553; -.
PRO; PR:Q06547; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000104064; -.
CleanEx; HS_GABPB1; -.
CleanEx; HS_GABPB2; -.
ExpressionAtlas; Q06547; baseline and differential.
Genevisible; Q06547; HS.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF12796; Ank_2; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 4.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Complete proteome;
Direct protein sequencing; Nucleus; Polymorphism; Reference proteome;
Repeat; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 395 GA-binding protein subunit beta-1.
/FTId=PRO_0000066993.
REPEAT 5 34 ANK 1.
REPEAT 37 66 ANK 2.
REPEAT 70 99 ANK 3.
REPEAT 103 132 ANK 4.
REPEAT 136 166 ANK 5.
REGION 258 327 Transcription activation and HCFC1
interaction.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 195 206 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7799916,
ECO:0000303|PubMed:8441384}.
/FTId=VSP_000275.
VAR_SEQ 346 395 EREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMT
RLQTNKEAV -> VRSLLPGVLCRSHPK (in isoform
3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7799916,
ECO:0000303|Ref.4}.
/FTId=VSP_009337.
VARIANT 31 31 P -> A (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035613.
MUTAGEN 262 263 QQ->AA: Minor reduction in
transcriptional activation; when
associated with A-295 or A-305 and A-306.
{ECO:0000269|PubMed:8816484}.
MUTAGEN 264 265 VV->AA: Minor effect upon interaction
with HCFC1 and transcriptional
activation. Loss of activity; when
associated with A-297; A-298 and A-299,
or with A-307 and A-310.
{ECO:0000269|PubMed:10675337,
ECO:0000269|PubMed:8816484}.
MUTAGEN 270 271 QQ->AA: Minor reduction in
transcriptional activation. Moderate
reduction in activity; when associated
with A-305 and A-306.
{ECO:0000269|PubMed:8816484}.
MUTAGEN 273 275 ITI->ATA: Strongly reduces interaction
with HCFC1 and transcriptional
activation. Loss of activity; when
associated with A-297; A-298 and A-299,
or with A-307 and A-310.
{ECO:0000269|PubMed:10675337,
ECO:0000269|PubMed:8816484}.
MUTAGEN 295 295 Q->A: No effect on transcriptional
activation. Minor reduction in activity;
when associated with A-270 and A-271.
{ECO:0000269|PubMed:8816484}.
MUTAGEN 297 299 IIV->AAA: Strongly reduces interaction
with HCFC1 and transcriptional
activation. Loss of activity; when
associated with A-264 and A-265, or A-273
and A-275. {ECO:0000269|PubMed:10675337,
ECO:0000269|PubMed:8816484}.
MUTAGEN 305 306 QQ->AA: Minor reduction in
transcriptional activation. Moderate
reduction in activity; when associated
with A-270 and A-271.
{ECO:0000269|PubMed:8816484}.
MUTAGEN 307 310 VLTV->ALTA: Moderately reduces
interaction with HCFC1 and
transcriptional activation. Loss of
activity; when associated with A-273 and
A-275. {ECO:0000269|PubMed:10675337,
ECO:0000269|PubMed:8816484}.
CONFLICT 76 76 H -> L (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 246 246 Missing (in Ref. 1; BAA02573).
{ECO:0000305}.
CONFLICT 274 274 T -> A (in Ref. 6; AAH36080).
{ECO:0000305}.
CONFLICT 341 341 S -> C (in Ref. 8; AA sequence).
{ECO:0000305}.
SEQUENCE 395 AA; 42483 MW; 723D63962FB29BD9 CRC64;
MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA
GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV
ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT
PQFIIGPGGV VNLTGLVSSE NSSKATDETG VSAVQFGNSS TSVLATLAAL AEASAPLSNS
SETPVVATEE VVTAESVDGA IQQVVSSGGQ QVITIVTDGI QLGNLHSIPT SGIGQPIIVT
MPDGQQVLTV PATDIAEETV ISEEPPAKRQ CIEIIENRVE SAEIEEREAL QKQLDEANRE
AQKYRQQLLK KEQEAEAYRQ KLEAMTRLQT NKEAV


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
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GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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