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P22415 (USF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Upstream stimulatory factor 1
Alternative name(s):
Class B basic helix-loop-helix protein 11
Short name=bHLHb11
Major late transcription factor 1
Gene names
Name:USF1
Synonyms:BHLHB11, USF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.

Subunit structure

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer (USF1/USF2). Interacts with varicella-zoster virus IE62 protein. Ref.10

Subcellular location

Nucleus.

Involvement in disease

Hyperlipidemia combined 1 (HYPLIP1) [MIM:602491]: A disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.12

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbon catabolite regulation of transcription

Traceable author statement PubMed 19303849. Source: BHF-UCL

cellular response to insulin stimulus

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

glucose homeostasis

Traceable author statement PubMed 15054483. Source: BHF-UCL

glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

late viral transcription

Inferred from direct assay Ref.1. Source: BHF-UCL

lipid homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of fibrinolysis

Inferred by curator PubMed 18234320. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18234320PubMed 8576131. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter by glucose

Inferred from mutant phenotype PubMed 7852331. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter by glucose

Inferred by curator PubMed 8576131. Source: BHF-UCL

response to UV

Inferred from sequence or structural similarity. Source: BHF-UCL

response to hypoxia

Inferred from mutant phenotype PubMed 12917334. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: BHF-UCL

   Cellular_componentnucleus

Inferred from direct assay PubMed 15358760PubMed 18234320Ref.1PubMed 8576131. Source: BHF-UCL

transcription factor complex

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

   Molecular_functionRNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.1. Source: BHF-UCL

bHLH transcription factor binding

Inferred from physical interaction PubMed 8576131. Source: BHF-UCL

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction PubMed 19303849. Source: BHF-UCL

histone deacetylase binding

Inferred from physical interaction PubMed 19303849. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 8576131. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction PubMed 8576131. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction PubMed 19303849. Source: BHF-UCL

sequence-specific DNA binding

Inferred from direct assay Ref.1PubMed 8576131. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KAT2BQ928315EBI-1054489,EBI-477430

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22415-1)

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: P22415-2)

Also known as: usf1-bd;

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Upstream stimulatory factor 1
PRO_0000127496

Regions

Domain199 – 25456bHLH
Region271 – 29222Leucine-zipper

Natural variations

Alternative sequence1 – 5959Missing in isoform 2.
VSP_047740

Secondary structure

......... 310
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1991. Version 1.
Checksum: BFDA91519B4B80AE

FASTA31033,538
        10         20         30         40         50         60 
MKGQQKTAET EEGTVQIQEG AVATGEDPTS VAIASIQSAA TFPDPNVKYV FRTENGGQVM 

        70         80         90        100        110        120 
YRVIQVSEGQ LDGQTEGTGA ISGYPATQSM TQAVIQGAFT SDDAVDTEGT AAETHYTYFP 

       130        140        150        160        170        180 
STAVGDGAGG TTSGSTAAVV TTQGSEALLG QATPPGTGQF FVMMSPQEVL QGGSQRSIAP 

       190        200        210        220        230        240 
RTHPYSPKSE APRTTRDEKR RAQHNEVERR RRDKINNWIV QLSKIIPDCS MESTKSGQSK 

       250        260        270        280        290        300 
GGILSKACDY IQELRQSNHR LSEELQGLDQ LQLDNDVLRQ QVEDLKNKNL LLRAQLRHHG 

       310 
LEVVIKNDSN 

« Hide

Isoform 2 (usf1-bd) [UniParc].

Checksum: AA50D545E179EFCB
Show »

FASTA25127,372

References

« Hide 'large scale' references
[1]"The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer."
Gregor P.D., Sawadogo M., Roeder R.G.
Genes Dev. 4:1730-1740(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-25.
[2]"Human USF1 genomic sequence."
Fukamizu A.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning and characterization of a novel splicing isoform of USF1."
Saito T., Oishi T., Yanai K., Shimamoto Y., Fukamizu A.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[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. 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 1).
Tissue: Testis.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal kidney.
[6]SeattleSNPs variation discovery resource
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 1).
Tissue: Kidney.
[10]"Transcription factor USF, expressed during the entire phase of Varicella-zoster virus infection, interacts physically with the major viral transactivator IE62 and plays a significant role in virus replication."
Rahaus M., Desloges N., Yang M., Ruyechan W.T., Wolff M.H.
J. Gen. Virol. 84:2957-2967(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN.
[11]"Structure and function of the b/HLH/Z domain of USF."
Ferre-D'Amare A.R., Pognonec P., Roeder R.G., Burley S.K.
EMBO J. 13:180-189(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 197-260.
[12]"Familial combined hyperlipidemia is associated with upstream transcription factor 1 (USF1)."
Pajukanta P., Lilja H.E., Sinsheimer J.S., Cantor R.M., Lusis A.J., Gentile M., Duan X.J., Soro-Paavonen A., Naukkarinen J., Saarela J., Laakso M., Ehnholm C., Taskinen M.-R., Peltonen L.
Nat. Genet. 36:371-376(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HYPLIP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55666 mRNA. Translation: CAA39201.1.
AB017568 Genomic DNA. Translation: BAA76541.1.
AB098540 mRNA. Translation: BAC78384.1.
AK314876 mRNA. Translation: BAG37391.1.
AL832119 mRNA. No translation available.
AY593992 Genomic DNA. Translation: AAS89301.1.
AL591806 Genomic DNA. Translation: CAI15372.1.
CH471121 Genomic DNA. Translation: EAW52675.1.
BC035505 mRNA. Translation: AAH35505.1.
PIRS13525.
RefSeqNP_001263302.1. NM_001276373.1.
NP_009053.1. NM_007122.4.
NP_996888.1. NM_207005.2.
UniGeneHs.414880.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AN4X-ray2.90A/B197-260[»]
ProteinModelPortalP22415.
SMRP22415. Positions 197-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113237. 41 interactions.
DIPDIP-654N.
IntActP22415. 13 interactions.
STRING9606.ENSP00000356999.

PTM databases

PhosphoSiteP22415.

Polymorphism databases

DMDM137170.

Proteomic databases

PaxDbP22415.
PRIDEP22415.

Protocols and materials databases

DNASU7391.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368020; ENSP00000356999; ENSG00000158773. [P22415-1]
ENST00000368021; ENSP00000357000; ENSG00000158773. [P22415-1]
ENST00000435396; ENSP00000390109; ENSG00000158773. [P22415-2]
GeneID7391.
KEGGhsa:7391.
UCSCuc001fxi.4. human. [P22415-1]

Organism-specific databases

CTD7391.
GeneCardsGC01M161009.
HGNCHGNC:12593. USF1.
HPACAB001480.
HPA036233.
HPA036535.
MIM144250. phenotype.
191523. gene.
602491. phenotype.
neXtProtNX_P22415.
PharmGKBPA37223.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272240.
HOGENOMHOG000294174.
HOVERGENHBG004346.
InParanoidP22415.
KOK09106.
OMAATETHYT.
OrthoDBEOG7GXPBW.
PhylomeDBP22415.
TreeFamTF323338.

Enzyme and pathway databases

SignaLinkP22415.

Gene expression databases

ArrayExpressP22415.
BgeeP22415.
CleanExHS_USF1.
GenevestigatorP22415.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSF1. human.
EvolutionaryTraceP22415.
GeneWikiUSF1.
GenomeRNAi7391.
NextBio28938.
PROP22415.
SOURCESearch...

Entry information

Entry nameUSF1_HUMAN
AccessionPrimary (citable) accession number: P22415
Secondary accession number(s): B2RBZ4, Q5SY46, Q7Z5Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 142 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 1

Human chromosome 1: entries, gene names and cross-references to MIM