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Q5TA89 (HES5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor HES-5
Alternative name(s):
Class B basic helix-loop-helix protein 38
Short name=bHLHb38
Hairy and enhancer of split 5
Gene names
Name:HES5
Synonyms:BHLHB38
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Transcriptional repressor of genes that require a bHLH protein for their transcription. Plays an important role as neurogenesis negative regulator By similarity.

Subunit structure

Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in fetal heart and brain tumors. Ref.4

Domain

Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG) By similarity.

The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins By similarity.

Sequence similarities

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

Contains 1 Orange domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionDevelopmental protein
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from mutant phenotype PubMed 19682396PubMed 19855400. Source: UniProtKB

S-shaped body morphogenesis

Inferred from electronic annotation. Source: Ensembl

astrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

auditory receptor cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

auditory receptor cell fate determination

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from sequence or structural similarity. Source: UniProtKB

camera-type eye development

Inferred from sequence or structural similarity. Source: UniProtKB

cartilage development

Inferred from direct assay PubMed 17093926. Source: UniProtKB

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cell maturation

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system myelination

Inferred from sequence or structural similarity. Source: UniProtKB

comma-shaped body morphogenesis

Inferred from electronic annotation. Source: Ensembl

forebrain radial glial cell differentiation

Inferred from electronic annotation. Source: Ensembl

glial cell fate commitment

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric nephron tubule morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of astrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of forebrain neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of inner ear receptor cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of oligodendrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of pro-B cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of stem cell differentiation

Inferred from mutant phenotype PubMed 19682396. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

neural tube development

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal stem cell maintenance

Inferred from expression pattern PubMed 19682396. Source: UniProtKB

oligodendrocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of BMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of JAK-STAT cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Notch signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 17849174. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from genetic interaction PubMed 19855400. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of myelination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

smoothened signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

specification of loop of Henle identity

Inferred from electronic annotation. Source: Ensembl

telencephalon development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Non-traceable author statement PubMed 17611704. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 166166Transcription factor HES-5
PRO_0000269175

Regions

Domain16 – 7257bHLH
Domain88 – 11932Orange
Motif163 – 1664WRPW motif
Compositional bias14 – 3118Arg/Lys-rich (basic)
Compositional bias122 – 14221Pro-rich
Compositional bias147 – 1537Poly-Ala

Sequences

Sequence LengthMass (Da)Tools
Q5TA89 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 6B0ECF2482EBE43B

FASTA16618,226
        10         20         30         40         50         60 
MAPSTVAVEL LSPKEKNRLR KPVVEKMRRD RINSSIEQLK LLLEQEFARH QPNSKLEKAD 

        70         80         90        100        110        120 
ILEMAVSYLK HSKAFVAAAG PKSLHQDYSE GYSWCLQEAV QFLTLHAASD TQMKLLYHFQ 

       130        140        150        160 
RPPAAPAAPA KEPKAPGAAP PPALSAKATA AAAAAHQPAC GLWRPW 

« Hide

References

« Hide 'large scale' references
[1]Wistow G.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
[3]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].
[4]"Identification and characterization of human HES2, HES3, and HES5 genes in silico."
Katoh M., Katoh M.
Int. J. Oncol. 25:529-534(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ272660 mRNA. Translation: ABB83829.1.
AL139246 Genomic DNA. Translation: CAX30820.1.
CH471183 Genomic DNA. Translation: EAW56096.1.
CCDSCCDS41233.1.
RefSeqNP_001010926.1. NM_001010926.3.
UniGeneHs.57971.

3D structure databases

ProteinModelPortalQ5TA89.
SMRQ5TA89. Positions 12-71.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid132759. 3 interactions.
STRING9606.ENSP00000367714.

PTM databases

PhosphoSiteQ5TA89.

Polymorphism databases

DMDM74745795.

Proteomic databases

PaxDbQ5TA89.
PRIDEQ5TA89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378453; ENSP00000367714; ENSG00000197921.
GeneID388585.
KEGGhsa:388585.
UCSCuc001ajn.3. human.

Organism-specific databases

CTD388585.
GeneCardsGC01M002450.
HGNCHGNC:19764. HES5.
MIM607348. gene.
neXtProtNX_Q5TA89.
PharmGKBPA134967985.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83691.
HOGENOMHOG000236346.
HOVERGENHBG005960.
InParanoidQ5TA89.
KOK06055.
OMAHSANTDT.
OrthoDBEOG7GN2PQ.
PhylomeDBQ5TA89.
TreeFamTF351373.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

BgeeQ5TA89.
CleanExHS_HES5.
GenevestigatorQ5TA89.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR003650. Orange.
[Graphical view]
PfamPF07527. Hairy_orange. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS51054. ORANGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHES5.
GenomeRNAi388585.
NextBio102194.
PROQ5TA89.
SOURCESearch...

Entry information

Entry nameHES5_HUMAN
AccessionPrimary (citable) accession number: Q5TA89
Secondary accession number(s): B9DI85
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 81 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

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