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Protein

TATA box-binding protein-like protein 1

Gene

TBPL1

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

Functioni

Part of a specialized transcription system that mediates the transcription of most ribosomal proteins through the 5'-TCT-3' motif which is a core promoter element at these genes. Seems to also mediate the transcription of NF1. Does not bind the TATA box.4 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
TATA box-binding protein-like protein 1
Short name:
TBP-like protein 1
Alternative name(s):
21 kDa TBP-like protein
Second TBP of unique DNA protein
Short name:
STUD
TATA box-binding protein-related factor 2
Short name:
TBP-related factor 2
TBP-like factor
TBP-related protein
Gene namesi
Name:TBPL1
Synonyms:TLF, TLP, TLP21, TRF2, TRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11589. TBPL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36353.

Polymorphism and mutation databases

BioMutaiTBPL1.
DMDMi61248509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 186186TATA box-binding protein-like protein 1PRO_0000153992Add
BLAST

Proteomic databases

MaxQBiP62380.
PaxDbiP62380.
PRIDEiP62380.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in the testis and ovary.2 Publications

Gene expression databases

BgeeiP62380.
CleanExiHS_TBPL1.
ExpressionAtlasiP62380. baseline and differential.
GenevisibleiP62380. HS.

Interactioni

Subunit structurei

Binds TFIIA and TFIIB.

Binary interactionsi

WithEntry#Exp.IntActNotes
TNNT1P138053EBI-716225,EBI-726527

Protein-protein interaction databases

BioGridi114896. 22 interactions.
IntActiP62380. 11 interactions.
STRINGi9606.ENSP00000237264.

Structurei

3D structure databases

ProteinModelPortaliP62380.
SMRiP62380. Positions 13-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TBP family.Curated

Phylogenomic databases

eggNOGiCOG2101.
GeneTreeiENSGT00410000025389.
HOGENOMiHOG000105162.
HOVERGENiHBG044997.
InParanoidiP62380.
KOiK03120.
OMAiEGTNVIY.
OrthoDBiEOG7M3J1J.
PhylomeDBiP62380.
TreeFamiTF300102.

Family and domain databases

Gene3Di3.30.310.10. 2 hits.
InterProiIPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
[Graphical view]
PANTHERiPTHR10126. PTHR10126. 1 hit.
PfamiPF00352. TBP. 2 hits.
[Graphical view]
PRINTSiPR00686. TIFACTORIID.

Sequencei

Sequence statusi: Complete.

P62380-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDADSDVALD ILITNVVCVF RTRCHLNLRK IALEGANVIY KRDVGKVLMK
60 70 80 90 100
LRKPRITATI WSSGKIICTG ATSEEEAKFG ARRLARSLQK LGFQVIFTDF
110 120 130 140 150
KVVNVLAVCN MPFEIRLPEF TKNNRPHASY EPELHPAVCY RIKSLRATLQ
160 170 180
IFSTGSITVT GPNVKAVATA VEQIYPFVFE SRKEIL
Length:186
Mass (Da):20,887
Last modified:July 5, 2004 - v1
Checksum:i2CDD9F5E7BDDE63F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441V → A in AAH00381 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020881 mRNA. Translation: BAA75218.1.
AF136570 mRNA. Translation: AAD28785.1.
AF130312 mRNA. Translation: AAD24800.1.
AK292320 mRNA. Translation: BAF85009.1.
AK313645 mRNA. Translation: BAG36402.1.
AL035699 Genomic DNA. Translation: CAB43704.1.
CH471051 Genomic DNA. Translation: EAW47995.1.
CH471051 Genomic DNA. Translation: EAW47996.1.
BC000381 mRNA. Translation: AAH00381.1.
BC017559 mRNA. Translation: AAH17559.1.
CCDSiCCDS5168.1.
PIRiJG0162.
RefSeqiNP_001240605.1. NM_001253676.1.
NP_004856.1. NM_004865.3.
UniGeneiHs.486507.

Genome annotation databases

EnsembliENST00000237264; ENSP00000237264; ENSG00000028839.
ENST00000613034; ENSP00000478795; ENSG00000028839.
GeneIDi9519.
KEGGihsa:9519.
UCSCiuc003qel.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020881 mRNA. Translation: BAA75218.1.
AF136570 mRNA. Translation: AAD28785.1.
AF130312 mRNA. Translation: AAD24800.1.
AK292320 mRNA. Translation: BAF85009.1.
AK313645 mRNA. Translation: BAG36402.1.
AL035699 Genomic DNA. Translation: CAB43704.1.
CH471051 Genomic DNA. Translation: EAW47995.1.
CH471051 Genomic DNA. Translation: EAW47996.1.
BC000381 mRNA. Translation: AAH00381.1.
BC017559 mRNA. Translation: AAH17559.1.
CCDSiCCDS5168.1.
PIRiJG0162.
RefSeqiNP_001240605.1. NM_001253676.1.
NP_004856.1. NM_004865.3.
UniGeneiHs.486507.

3D structure databases

ProteinModelPortaliP62380.
SMRiP62380. Positions 13-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114896. 22 interactions.
IntActiP62380. 11 interactions.
STRINGi9606.ENSP00000237264.

Polymorphism and mutation databases

BioMutaiTBPL1.
DMDMi61248509.

Proteomic databases

MaxQBiP62380.
PaxDbiP62380.
PRIDEiP62380.

Protocols and materials databases

DNASUi9519.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237264; ENSP00000237264; ENSG00000028839.
ENST00000613034; ENSP00000478795; ENSG00000028839.
GeneIDi9519.
KEGGihsa:9519.
UCSCiuc003qel.3. human.

Organism-specific databases

CTDi9519.
GeneCardsiGC06P134273.
HGNCiHGNC:11589. TBPL1.
MIMi605521. gene.
neXtProtiNX_P62380.
PharmGKBiPA36353.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2101.
GeneTreeiENSGT00410000025389.
HOGENOMiHOG000105162.
HOVERGENiHBG044997.
InParanoidiP62380.
KOiK03120.
OMAiEGTNVIY.
OrthoDBiEOG7M3J1J.
PhylomeDBiP62380.
TreeFamiTF300102.

Miscellaneous databases

ChiTaRSiTBPL1. human.
GeneWikiiTBPL1.
GenomeRNAii9519.
NextBioi35674.
PROiP62380.
SOURCEiSearch...

Gene expression databases

BgeeiP62380.
CleanExiHS_TBPL1.
ExpressionAtlasiP62380. baseline and differential.
GenevisibleiP62380. HS.

Family and domain databases

Gene3Di3.30.310.10. 2 hits.
InterProiIPR012295. Beta2_adaptin/TBP_C_dom.
IPR000814. TBP.
[Graphical view]
PANTHERiPTHR10126. PTHR10126. 1 hit.
PfamiPF00352. TBP. 2 hits.
[Graphical view]
PRINTSiPR00686. TIFACTORIID.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of cDNA, chromosome mapping, and expression of the human TBP-like protein."
    Ohbayashi T., Kishimoto T., Makino Y., Shimada M., Nakadi T., Aoki T., Kawata T., Niwa S., Tamura T.-A.
    Biochem. Biophys. Res. Commun. 255:137-142(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Retina.
  2. "TATA box-binding protein (TBP)-related factor 2 (TRF2), a third member of the TBP family."
    Rabenstein M.D., Zhou S., Lis J.T., Tjian R.
    Proc. Natl. Acad. Sci. U.S.A. 96:4791-4796(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TFIIA AND TFIIB.
  3. "TATA-binding protein (TBP)-like factor (TLF) is a functional regulator of transcription: reciprocal regulation of the neurofibromatosis type 1 and c-fos genes by TLF/TRF2 and TBP."
    Chong J.A., Moran M.M., Teichmann M., Kaczmarek J.S., Roeder R., Clapham D.E.
    Mol. Cell. Biol. 25:2632-2643(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis and Uterus.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung and Uterus.
  8. Cited for: TISSUE SPECIFICITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "TRF2, but not TBP, mediates the transcription of ribosomal protein genes."
    Wang Y.L., Duttke S.H., Chen K., Johnston J., Kassavetis G.A., Zeitlinger J., Kadonaga J.T.
    Genes Dev. 28:1550-1555(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTBPL1_HUMAN
AccessioniPrimary (citable) accession number: P62380
Secondary accession number(s): A8K8F5
, O95753, Q9BWD5, Q9Z2Z0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 108 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.