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Q06547 (GABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bai2Q8CGM13EBI-618165,EBI-8014984From a different organism.
HCFC1P516106EBI-618189,EBI-396176
MAGEB18Q96M613EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 395394GA-binding protein subunit beta-1
PRO_0000066993

Regions

Repeat5 – 3430ANK 1
Repeat37 – 6630ANK 2
Repeat70 – 9930ANK 3
Repeat103 – 13230ANK 4
Repeat136 – 16631ANK 5
Region258 – 32770Transcription activation and HCFC1 interaction

Amino acid modifications

Modified residue21N-acetylserine Ref.12

Natural variations

Alternative sequence195 – 20612Missing in isoform 2 and isoform 4.
VSP_000275
Alternative sequence346 – 39550EREAL…NKEAV → VRSLLPGVLCRSHPK in isoform 3 and isoform 4.
VSP_009337
Natural variant311P → A in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035613

Experimental info

Mutagenesis262 – 2632QQ → AA: Minor reduction in transcriptional activation; when associated with A-295 or A-305 and A-306.
Mutagenesis264 – 2652VV → 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.
Mutagenesis270 – 2712QQ → AA: Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-305 and A-306.
Mutagenesis273 – 2753ITI → 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
Mutagenesis2951Q → A: No effect on transcriptional activation. Minor reduction in activity; when associated with A-270 and A-271. Ref.9
Mutagenesis297 – 2993IIV → 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
Mutagenesis305 – 3062QQ → AA: Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-270 and A-271.
Mutagenesis307 – 3104VLTV → 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 conflict761H → L AA sequence Ref.7
Sequence conflict2461Missing in BAA02573. Ref.1
Sequence conflict2741T → A in AAH36080. Ref.6
Sequence conflict3411S → C AA sequence Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GABPB-1) (Beta-1) [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 723D63962FB29BD9

FASTA39542,483
        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 

« Hide

Isoform 2 (Beta-2) [UniParc].

Checksum: 07E7081A60016288
Show »

FASTA38341,321
Isoform 3 (GABPB-2) (Gamma-1) [UniParc].

Checksum: 39917E58EF91120F
Show »

FASTA36038,111
Isoform 4 (Gamma-2) [UniParc].

Checksum: 9657186214E046D5
Show »

FASTA34836,950

References

« Hide '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. expand/collapse author list , 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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"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. expand/collapse author list , 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.
CCDSCCDS10135.1. [Q06547-2]
CCDS10136.1. [Q06547-4]
CCDS32239.1. [Q06547-1]
CCDS45258.1. [Q06547-3]
PIRC48146.
I38741.
I38743.
I38744.
RefSeqNP_002032.2. NM_002041.4. [Q06547-3]
NP_005245.2. NM_005254.5. [Q06547-1]
NP_057738.1. NM_016654.4. [Q06547-2]
NP_057739.1. NM_016655.4. [Q06547-4]
NP_852092.1. NM_181427.3. [Q06547-4]
XP_005254330.1. XM_005254273.2. [Q06547-1]
XP_005254331.1. XM_005254274.2. [Q06547-1]
UniGeneHs.654350.

3D structure databases

ProteinModelPortalQ06547.
SMRQ06547. Positions 5-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108827. 14 interactions.
IntActQ06547. 15 interactions.
MINTMINT-1504045.
STRING9606.ENSP00000370259.

PTM databases

PhosphoSiteQ06547.

Polymorphism databases

DMDM23503070.

Proteomic databases

MaxQBQ06547.
PaxDbQ06547.
PRIDEQ06547.

Protocols and materials databases

DNASU2553.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220429; ENSP00000220429; ENSG00000104064. [Q06547-1]
ENST00000359031; ENSP00000351923; ENSG00000104064. [Q06547-4]
ENST00000380877; ENSP00000370259; ENSG00000104064. [Q06547-2]
ENST00000396464; ENSP00000379728; ENSG00000104064. [Q06547-4]
ENST00000429662; ENSP00000395771; ENSG00000104064. [Q06547-3]
GeneID2553.
KEGGhsa:2553.
UCSCuc001zya.3. human. [Q06547-2]
uc001zyb.3. human. [Q06547-1]
uc001zyc.3. human. [Q06547-4]
uc001zye.3. human. [Q06547-3]

Organism-specific databases

CTD2553.
GeneCardsGC15M050569.
HGNCHGNC:4074. GABPB1.
HPAHPA019653.
MIM600610. gene.
neXtProtNX_Q06547.
PharmGKBPA162389163.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG051686.
InParanoidQ06547.
KOK09454.
OMAVKRQCIE.
OrthoDBEOG7ZD1W2.
PhylomeDBQ06547.
TreeFamTF326036.

Enzyme and pathway databases

ReactomeREACT_200751. Organelle biogenesis and maintenance.

Gene expression databases

ArrayExpressQ06547.
BgeeQ06547.
CleanExHS_GABPB1.
HS_GABPB2.
GenevestigatorQ06547.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF00023. Ank. 3 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGABPB2.
GenomeRNAi2553.
NextBio10075.
PROQ06547.
SOURCESearch...

Entry information

Entry nameGABP1_HUMAN
AccessionPrimary (citable) accession number: Q06547
Secondary accession number(s): A8IE52 expand/collapse secondary AC list , Q06545, Q12940, Q12941, Q12942, Q8IYD0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 19, 2002
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM