Q06547 (GABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GA-binding protein subunit beta-1
Short name=GABP subunit beta-1
Short name=GABPB-1

Alternative name(s):
GABP subunit beta-2
Short name=GABPB-2
Nuclear respiratory factor 2
Transcription factor E4TF1-47
Transcription factor E4TF1-53

Gene names

Name:	GABPB1
Synonyms:	E4TF1B, GABPB, GABPB2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor capable of interacting with purine rich repeats (GA repeats). Necessary for the expression of the Adenovirus E4 gene. Ref.9 Ref.10
Subunit structure	Heterotetramer of two alpha and two beta subunits. Interacts with HCFC1, causing repression of transcriptional activity. Ref.10
Subcellular location	Nucleus.
Sequence similarities	Contains 5 ANK repeats.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Repeat
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 9857059. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay PubMed 9857059. Source: MGI
Molecular_function	protein heterodimerization activity Inferred from direct assay PubMed 9857059. Source: MGI sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc transcription regulatory region DNA binding Inferred from direct assay PubMed 9857059. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCFC1	P51610	6	EBI-618189,EBI-396176
MAGEB18	Q96M61	3	EBI-618165,EBI-741835

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q06547-1)

Also known as: GABPB-1; Beta-1;

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: Q06547-2)

Also known as: Beta-2;

The sequence of this isoform differs from the canonical sequence as follows:
     195-206: Missing.

Isoform 3 (identifier: Q06547-3)

Also known as: GABPB-2; Gamma-1;

The sequence of this isoform differs from the canonical sequence as follows:
     346-395: EREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRLQTNKEAV → VRSLLPGVLCRSHPK

Isoform 4 (identifier: Q06547-4)

Also known as: Gamma-2;

The sequence of this isoform differs from the canonical sequence as follows:
     195-206: Missing.
     346-395: EREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRLQTNKEAV → VRSLLPGVLCRSHPK

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 395	395	GA-binding protein subunit beta-1		PRO_0000066993
Regions
	Repeat	5 – 34	30	ANK 1
	Repeat	37 – 66	30	ANK 2
	Repeat	70 – 99	30	ANK 3
	Repeat	103 – 132	30	ANK 4
	Repeat	136 – 166	31	ANK 5
	Region	258 – 327	70	Transcription activation and HCFC1 interaction
Natural variations
	Alternative sequence	195 – 206	12	Missing in isoform 2 and isoform 4.		VSP_000275
	Alternative sequence	346 – 395	50	EREAL…NKEAV → VRSLLPGVLCRSHPK in isoform 3 and isoform 4.		VSP_009337
	Natural variant	31	1	P → A in a colorectal cancer sample; somatic mutation. Ref.12		VAR_035613
Experimental info
	Mutagenesis	262 – 263	2	QQ → AA: Minor reduction in transcriptional activation; when associated with A-295 or A-305 and A-306.
	Mutagenesis	264 – 265	2	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.
	Mutagenesis	270 – 271	2	QQ → AA: Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-305 and A-306.
	Mutagenesis	273 – 275	3	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. Ref.9
	Mutagenesis	295	1	Q → A: No effect on transcriptional activation. Minor reduction in activity; when associated with A-270 and A-271. Ref.9
	Mutagenesis	297 – 299	3	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. Ref.9 Ref.10
	Mutagenesis	305 – 306	2	QQ → AA: Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-270 and A-271.
	Mutagenesis	307 – 310	4	VLTV → ALTA: Moderately reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-273 and A-275. Ref.9 Ref.10
	Sequence conflict	76	1	H → L AA sequence Ref.7
	Sequence conflict	246	1	Missing in BAA02573. Ref.1
	Sequence conflict	274	1	T → A in AAH36080. Ref.6
	Sequence conflict	341	1	S → C AA sequence Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GABPB-1) (Beta-1) [UniParc]. Last modified September 19, 2002. Version 2. Checksum: 723D63962FB29BD9	FASTA	395	42,483
	10 20 30 40 50 60 MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA 70 80 90 100 110 120 GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV 130 140 150 160 170 180 ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT 190 200 210 220 230 240 PQFIIGPGGV VNLTGLVSSE NSSKATDETG VSAVQFGNSS TSVLATLAAL AEASAPLSNS 250 260 270 280 290 300 SETPVVATEE VVTAESVDGA IQQVVSSGGQ QVITIVTDGI QLGNLHSIPT SGIGQPIIVT 310 320 330 340 350 360 MPDGQQVLTV PATDIAEETV ISEEPPAKRQ CIEIIENRVE SAEIEEREAL QKQLDEANRE 370 380 390 AQKYRQQLLK KEQEAEAYRQ KLEAMTRLQT NKEAV
	Isoform 2 (Beta-2) [UniParc]. Checksum: 07E7081A60016288	FASTA	383	41,321
	10 20 30 40 50 60 MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA 70 80 90 100 110 120 GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV 130 140 150 160 170 180 ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT 190 200 210 220 230 240 PQFIIGPGGV VNLTDETGVS AVQFGNSSTS VLATLAALAE ASAPLSNSSE TPVVATEEVV 250 260 270 280 290 300 TAESVDGAIQ QVVSSGGQQV ITIVTDGIQL GNLHSIPTSG IGQPIIVTMP DGQQVLTVPA 310 320 330 340 350 360 TDIAEETVIS EEPPAKRQCI EIIENRVESA EIEEREALQK QLDEANREAQ KYRQQLLKKE 370 380 QEAEAYRQKL EAMTRLQTNK EAV
	Isoform 3 (GABPB-2) (Gamma-1) [UniParc]. Checksum: 39917E58EF91120F	FASTA	360	38,111
	10 20 30 40 50 60 MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA 70 80 90 100 110 120 GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV 130 140 150 160 170 180 ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT 190 200 210 220 230 240 PQFIIGPGGV VNLTGLVSSE NSSKATDETG VSAVQFGNSS TSVLATLAAL AEASAPLSNS 250 260 270 280 290 300 SETPVVATEE VVTAESVDGA IQQVVSSGGQ QVITIVTDGI QLGNLHSIPT SGIGQPIIVT 310 320 330 340 350 360 MPDGQQVLTV PATDIAEETV ISEEPPAKRQ CIEIIENRVE SAEIEVRSLL PGVLCRSHPK
	Isoform 4 (Gamma-2) [UniParc]. Checksum: 9657186214E046D5	FASTA	348	36,950
	10 20 30 40 50 60 MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA 70 80 90 100 110 120 GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV 130 140 150 160 170 180 ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT 190 200 210 220 230 240 PQFIIGPGGV VNLTDETGVS AVQFGNSSTS VLATLAALAE ASAPLSNSSE TPVVATEEVV 250 260 270 280 290 300 TAESVDGAIQ QVVSSGGQQV ITIVTDGIQL GNLHSIPTSG IGQPIIVTMP DGQQVLTVPA 310 320 330 340 TDIAEETVIS EEPPAKRQCI EIIENRVESA EIEVRSLLPG VLCRSHPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of transcription factor E4TF1 subunits with Ets and notch motifs." Watanabe H., Sawada J., Yano K., Yamaguchi K., Goto M., Handa H. Mol. Cell. Biol. 13:1385-1391(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Four structurally distinct, non-DNA-binding subunits of human nuclear respiratory factor 2 share a conserved transcriptional activation domain." Gugneja S., Virbasius J.V., Scarpulla R.C. Mol. Cell. Biol. 15:102-111(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). Tissue: Testis.
[3]	Yang S.J., Li K.N., Zhang Y.Q. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Hepatoma.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1; 2 AND 3). Tissue: Prostate, Testis and Uterus.
[7]	"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." Cardot P., Pastier D., Lacorte J.-M., Mangeney M., Zannis V.I., Chambaz J. Biochemistry 33:12139-12148(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 74-81.
[8]	"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." Virbasius J.V., Virbasius C.A., Scarpulla R.C. Genes Dev. 7:380-392(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 105-125 AND 339-385.
[9]	"Nuclear respiratory factors 1 and 2 utilize similar glutamine-containing clusters of hydrophobic residues to activate transcription." Gugneja S., Virbasius C.M., Scarpulla R.C. Mol. Cell. Biol. 16:5708-5716(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, 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.
[10]	"The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation and mediates transcription activation by GABP." Vogel J.L., Kristie T.M. EMBO J. 19:683-690(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HCFC1, MUTAGENESIS OF 264-VAL-VAL-265; 273-ILE--ILE-275; 297-ILE--VAL-299 AND 307-VAL--VAL-310.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-31.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13316 mRNA. Translation: BAA02573.1. D13317 mRNA. Translation: BAA02574.1. U13045 mRNA. Translation: AAA65707.1. U13046 mRNA. Translation: AAA65708.1. U13047 mRNA. Translation: AAA65709.1. U13048 mRNA. Translation: AAA65710.1. EU159454 mRNA. Translation: ABV90874.1. BT006652 mRNA. Translation: AAP35298.1. CH471082 Genomic DNA. Translation: EAW77395.1. BC016910 mRNA. Translation: AAH16910.1. BC036080 mRNA. Translation: AAH36080.1. BC050702 mRNA. Translation: AAH50702.1.
IPI	IPI00010301. IPI00031516. IPI00218611. IPI00219016.
PIR	C48146. I38741. I38743. I38744.
RefSeq	NP_002032.2. NM_002041.4. NP_005245.2. NM_005254.5. NP_057738.1. NM_016654.4. NP_057739.1. NM_016655.4. NP_852092.1. NM_181427.3.
UniGene	Hs.654350.
3D structure databases
ProteinModelPortal	Q06547.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06547. 10 interactions.
MINT	MINT-1504045.
STRING	9606.ENSP00000370259.
PTM databases
PhosphoSite	Q06547.
Polymorphism databases
DMDM	23503070.
Proteomic databases
PaxDb	Q06547.
PRIDE	Q06547.
Protocols and materials databases
DNASU	2553.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000220429; ENSP00000220429; ENSG00000104064. ENST00000359031; ENSP00000351923; ENSG00000104064. ENST00000380877; ENSP00000370259; ENSG00000104064. ENST00000396464; ENSP00000379728; ENSG00000104064. ENST00000429662; ENSP00000395771; ENSG00000104064.
GeneID	2553.
KEGG	hsa:2553.
UCSC	uc001zya.3. human. uc001zyb.3. human. uc001zyc.3. human. uc001zye.3. human.
Organism-specific databases
CTD	2553.
GeneCards	GC15M050569.
HGNC	HGNC:4074. GABPB1.
HPA	HPA019653.
MIM	600610. gene.
neXtProt	NX_Q06547.
PharmGKB	PA162389163.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0666.
HOVERGEN	HBG051686.
InParanoid	Q06547.
KO	K09454.
OMA	VKRQCIE.
OrthoDB	EOG4MCX0P.
Gene expression databases
ArrayExpress	Q06547.
Bgee	Q06547.
CleanEx	HS_GABPB1. HS_GABPB2.
Genevestigator	Q06547.
GermOnline	ENSG00000104064. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 2 hits.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. [Graphical view]
Pfam	PF00023. Ank. 3 hits. [Graphical view]
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 4 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	2553.
NextBio	10075.
SOURCE	Search...

Entry information

Entry name

GABP1_HUMAN

Accession

Primary (citable) accession number: Q06547
Secondary accession number(s): A8IE52 , Q06545, Q12940, Q12941, Q12942, Q8IYD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	September 19, 2002
Last modified:	May 1, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.