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P20290 (BTF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Transcription factor BTF3
Alternative name(s):
Nascent polypeptide-associated complex subunit beta
Short name=NAC-beta
RNA polymerase B transcription factor 3
Gene names
Name:BTF3
Synonyms:NACB
ORF Names:OK/SW-cl.8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription. Ref.9

Subunit structure

Part of the nascent polypeptide-associated complex (NAC), which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC associates with ribosomes through the BTF3/NACB subunit. Both subunits can contact nascent polypeptide chains. Ref.12

Subcellular location

Cytoplasm. Nucleus. Note: The heterodimer with NACA is cytoplasmic. Ref.9

Sequence similarities

Belongs to the NAC-beta family.

Contains 1 NAC-A/B (NAC-alpha/beta) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033725EBI-1054703,EBI-78473

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20290-1)

Also known as: BTF3a;

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: P20290-2)

Also known as: BTF3b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Transcription factor BTF3
PRO_0000213548

Regions

Domain82 – 14766NAC-A/B
Compositional bias185 – 1884Poly-Asp

Amino acid modifications

Modified residue301Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 4444Missing in isoform 2.
VSP_013587

Experimental info

Sequence conflict411Q → E in AAA58398. Ref.2
Sequence conflict68 – 10538Missing in AAA58398. Ref.2
Sequence conflict192 – 1965DLVEN → GG Ref.2
Sequence conflict1981D → Q Ref.2

Secondary structure

................ 206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BTF3a) [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 9653AC480EAF64C6

FASTA20622,168
        10         20         30         40         50         60 
MRRTGAPAQA DSRGRGRARG GCPGGEATLS QPPPRGGTRG QEPQMKETIM NQEKLAKLQA 

        70         80         90        100        110        120 
QVRIGGKGTA RRKKKVVHRT ATADDKKLQF SLKKLGVNNI SGIEEVNMFT NQGTVIHFNN 

       130        140        150        160        170        180 
PKVQASLAAN TFTITGHAET KQLTEMLPSI LNQLGADSLT SLRRLAEALP KQSVDGKAPL 

       190        200 
ATGEDDDDEV PDLVENFDEA SKNEAN 

« Hide

Isoform 2 (BTF3b) [UniParc].

Checksum: 5062DE8858CEE979
Show »

FASTA16217,699

References

« Hide 'large scale' references
[1]"Sequencing and expression of complementary DNA for the general transcription factor BTF3."
Zheng X.M., Black D., Chambon P., Egly J.-M.
Nature 344:556-559(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Genomic structure of the putative BTF3 transcription factor."
Kanno M., Chalut C., Egly J.-M.
Gene 117:219-228(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leukocyte.
[3]"cDNA expression and human 2D-gel data bases: towards integrating protein and DNA information."
Leffers H., Honore B., Madsen A., Nielsen M.S., Anderson A.H., Celis J.E.
Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon adenocarcinoma.
[5]"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 2).
[6]"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. expand/collapse author list , 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] (ISOFORM 2).
[7]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].
[8]"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] (ISOFORM 2).
Tissue: Skin.
[9]"The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions."
Beatrix B., Sakai H., Wiedmann M.
J. Biol. Chem. 275:37838-37845(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NACA, ASSOCIATION WITH RIBOSOMES, SUBCELLULAR LOCATION.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[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]"Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit."
Wang L., Zhang W., Wang L., Zhang X.C., Li X., Rao Z.
Protein Cell 1:406-416(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 97-154, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53280 mRNA. Translation: CAA37375.1.
X53281 mRNA. Translation: CAA37376.1.
M90357, M90352 Genomic DNA. Translation: AAA58398.1.
X74070 mRNA. Translation: CAA52200.1.
AB062126 mRNA. Translation: BAB93458.1.
BT007120 mRNA. Translation: AAP35784.1.
AK291125 mRNA. Translation: BAF83814.1.
CH471084 Genomic DNA. Translation: EAW95727.1.
BC008062 mRNA. Translation: AAH08062.1.
CCDSCCDS34185.1. [P20290-1]
CCDS4019.1. [P20290-2]
PIRJC1235.
RefSeqNP_001032726.1. NM_001037637.1. [P20290-1]
NP_001198.2. NM_001207.4. [P20290-2]
UniGeneHs.591768.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LKXX-ray2.50A97-162[»]
3MCBX-ray1.90B97-154[»]
ProteinModelPortalP20290.
SMRP20290. Positions 97-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107154. 17 interactions.
IntActP20290. 6 interactions.
MINTMINT-5002480.
STRING9606.ENSP00000369965.

PTM databases

PhosphoSiteP20290.

Polymorphism databases

DMDM115143.

Proteomic databases

MaxQBP20290.
PaxDbP20290.
PRIDEP20290.

Protocols and materials databases

DNASU689.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335895; ENSP00000338516; ENSG00000145741. [P20290-2]
ENST00000380591; ENSP00000369965; ENSG00000145741. [P20290-1]
GeneID689.
KEGGhsa:689.
UCSCuc003kcq.1. human. [P20290-1]

Organism-specific databases

CTD689.
GeneCardsGC05P072794.
HGNCHGNC:1125. BTF3.
HPACAB013007.
HPA056420.
MIM602542. gene.
neXtProtNX_P20290.
PharmGKBPA25445.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283773.
HOGENOMHOG000261245.
HOVERGENHBG004906.
InParanoidP20290.
KOK01527.
OMADGKAPIA.
OrthoDBEOG7CVPXQ.
PhylomeDBP20290.
TreeFamTF317546.

Gene expression databases

ArrayExpressP20290.
BgeeP20290.
CleanExHS_BTF3.
GenevestigatorP20290.

Family and domain databases

InterProIPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PfamPF01849. NAC. 1 hit.
[Graphical view]
PROSITEPS51151. NAC_AB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBTF3. human.
EvolutionaryTraceP20290.
GeneWikiBTF3.
GenomeRNAi689.
NextBio2836.
PROP20290.
SOURCESearch...

Entry information

Entry nameBTF3_HUMAN
AccessionPrimary (citable) accession number: P20290
Secondary accession number(s): A8K510, Q13893, Q76M56
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 128 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM