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Protein

Activator of basal transcription 1

Gene

ABT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could be a novel TATA-binding protein (TBP) which can function as a basal transcription activator. Can act as a regulator of basal transcription for class II genes (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: GO_Central
  • transcription coactivator activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Activator of basal transcription 1
Short name:
hABT1
Alternative name(s):
Basal transcriptional activator
Gene namesi
Name:ABT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17369. ABT1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: GO_Central
  • nucleus Source: ProtInc
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38451.

Polymorphism and mutation databases

BioMutaiABT1.
DMDMi74753396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Activator of basal transcription 1PRO_0000233168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9ULW3.
MaxQBiQ9ULW3.
PaxDbiQ9ULW3.
PeptideAtlasiQ9ULW3.
PRIDEiQ9ULW3.

PTM databases

iPTMnetiQ9ULW3.
PhosphoSiteiQ9ULW3.

Expressioni

Gene expression databases

BgeeiQ9ULW3.
CleanExiHS_ABT1.
ExpressionAtlasiQ9ULW3. baseline and differential.
GenevisibleiQ9ULW3. HS.

Interactioni

Subunit structurei

Interacts with ESF1/ABTAP (By similarity). Interacts with IGHMBP2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC136Q96JN2-23EBI-2602396,EBI-10171416
CDCA7LQ96GN53EBI-2602396,EBI-5278764
CEP70Q8NHQ13EBI-2602396,EBI-739624
EMDP504023EBI-2602396,EBI-489887
FAM9BQ8IZU03EBI-2602396,EBI-10175124
LZTS2Q9BRK43EBI-2602396,EBI-741037
SYNE4Q8N2053EBI-2602396,EBI-7131783

Protein-protein interaction databases

BioGridi118909. 26 interactions.
IntActiQ9ULW3. 15 interactions.
MINTiMINT-3082379.
STRINGi9606.ENSP00000274849.

Structurei

3D structure databases

ProteinModelPortaliQ9ULW3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 14297RRMAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili161 – 19131Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi90 – 945Poly-Ala

Sequence similaritiesi

Belongs to the ESF2/ABP1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3152. Eukaryota.
ENOG4111JJV. LUCA.
GeneTreeiENSGT00390000002062.
HOGENOMiHOG000242500.
HOVERGENiHBG057308.
InParanoidiQ9ULW3.
KOiK14785.
OMAiHVPPRFR.
OrthoDBiEOG7Q2N67.
PhylomeDBiQ9ULW3.
TreeFamiTF314506.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9ULW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAEESEKAA TEQEPLEGTE QTLDAEEEQE ESEEAACGSK KRVVPGIVYL
60 70 80 90 100
GHIPPRFRPL HVRNLLSAYG EVGRVFFQAE DRFVRRKKKA AAAAGGKKRS
110 120 130 140 150
YTKDYTEGWV EFRDKRIAKR VAASLHNTPM GARRRSPFRY DLWNLKYLHR
160 170 180 190 200
FTWSHLSEHL AFERQVRRQR LRAEVAQAKR ETDFYLQSVE RGQRFLAADG
210 220 230 240 250
DPARPDGSWT FAQRPTEQEL RARKAARPGG RERARLATAQ DKARSNKGLL
260 270
ARIFGAPPPS ESMEGPSLVR DS
Length:272
Mass (Da):31,079
Last modified:May 1, 2000 - v1
Checksum:iFB9B44192C16BD8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027258 mRNA. Translation: BAA86886.1.
AL513548 Genomic DNA. Translation: CAC40824.1.
BC048812 mRNA. Translation: AAH48812.1.
BC066313 mRNA. Translation: AAH66313.1.
CCDSiCCDS4616.1.
RefSeqiNP_037507.1. NM_013375.3.
UniGeneiHs.254406.

Genome annotation databases

EnsembliENST00000274849; ENSP00000274849; ENSG00000146109.
GeneIDi29777.
KEGGihsa:29777.
UCSCiuc003nii.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027258 mRNA. Translation: BAA86886.1.
AL513548 Genomic DNA. Translation: CAC40824.1.
BC048812 mRNA. Translation: AAH48812.1.
BC066313 mRNA. Translation: AAH66313.1.
CCDSiCCDS4616.1.
RefSeqiNP_037507.1. NM_013375.3.
UniGeneiHs.254406.

3D structure databases

ProteinModelPortaliQ9ULW3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118909. 26 interactions.
IntActiQ9ULW3. 15 interactions.
MINTiMINT-3082379.
STRINGi9606.ENSP00000274849.

PTM databases

iPTMnetiQ9ULW3.
PhosphoSiteiQ9ULW3.

Polymorphism and mutation databases

BioMutaiABT1.
DMDMi74753396.

Proteomic databases

EPDiQ9ULW3.
MaxQBiQ9ULW3.
PaxDbiQ9ULW3.
PeptideAtlasiQ9ULW3.
PRIDEiQ9ULW3.

Protocols and materials databases

DNASUi29777.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274849; ENSP00000274849; ENSG00000146109.
GeneIDi29777.
KEGGihsa:29777.
UCSCiuc003nii.4. human.

Organism-specific databases

CTDi29777.
GeneCardsiABT1.
HGNCiHGNC:17369. ABT1.
neXtProtiNX_Q9ULW3.
PharmGKBiPA38451.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3152. Eukaryota.
ENOG4111JJV. LUCA.
GeneTreeiENSGT00390000002062.
HOGENOMiHOG000242500.
HOVERGENiHBG057308.
InParanoidiQ9ULW3.
KOiK14785.
OMAiHVPPRFR.
OrthoDBiEOG7Q2N67.
PhylomeDBiQ9ULW3.
TreeFamiTF314506.

Miscellaneous databases

ChiTaRSiABT1. human.
GenomeRNAii29777.
PROiQ9ULW3.

Gene expression databases

BgeeiQ9ULW3.
CleanExiHS_ABT1.
ExpressionAtlasiQ9ULW3. baseline and differential.
GenevisibleiQ9ULW3. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel TATA-binding protein-binding protein, ABT1, activates basal transcription and has a yeast homolog that is essential for growth."
    Oda T., Kayukawa K., Hagiwara H., Yudate H.T., Masuho Y., Murakami Y., Tamura T.-A., Muramatsu M.-A.
    Mol. Cell. Biol. 20:1407-1418(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Duodenum and Testis.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery."
    de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A., Mourelatos Z.
    Hum. Mol. Genet. 18:2115-2126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGHMBP2.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiABT1_HUMAN
AccessioniPrimary (citable) accession number: Q9ULW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.