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P28159 (SUH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Suppressor of hairless protein
Alternative name(s):
J kappa-recombination signal-binding protein
RBP-J kappa
Gene names
Name:Su(H)
Synonyms:dRBP-JK
ORF Names:CG3497
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Binds directly the 5'-GTGRGAR-3' DNA consensus sequence, which is present in the regulatory region of several genes. Required for neurogenesis in imaginal disks. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some Notch protein, it acts as a transcriptional activator that activates transcription of Notch target genes. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Required for transcription of Sim. Also functions independently of Notch pathway, in the development of the bristle sensory organ precursor cell. Ref.9 Ref.12 Ref.13

Subunit structure

Interacts with activated cleaved Notch. Interacts with Hairless, this interaction preventing its DNA-binding activity. Ref.10

Subcellular location

Nucleus. Cytoplasm. Note: In imaginal disk, at the onset of differentiation of socket cell, it is also present in the cytoplasm. Ref.11

Sequence similarities

Belongs to the Su(H) family.

Contains 1 IPT/TIG domain.

Caution

Despite some similarity with the "phage" integrase family, Ref.10 showed that it has no recombinase activity.

Sequence caution

The sequence AAA06211.1 differs from that shown. Reason: Frameshift at position 6.

The sequence CAA41282.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNotch signaling pathway
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB phosphorylation

Inferred from mutant phenotype PubMed 23861806. Source: FlyBase

Notch signaling pathway

Inferred from mutant phenotype Ref.12. Source: UniProtKB

asymmetric cell division

Traceable author statement PubMed 15018932. Source: FlyBase

cell fate determination

Traceable author statement PubMed 15018932. Source: FlyBase

crystal cell differentiation

Inferred from mutant phenotype PubMed 12445385. Source: FlyBase

hemopoiesis

Traceable author statement PubMed 14602069. Source: FlyBase

imaginal disc-derived wing vein morphogenesis

Inferred from mutant phenotype PubMed 16287856. Source: FlyBase

lateral inhibition

Traceable author statement PubMed 11932008. Source: FlyBase

long-term memory

Inferred from mutant phenotype PubMed 19863271. Source: FlyBase

negative regulation of compound eye cone cell fate specification

Traceable author statement PubMed 12419199. Source: FlyBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 19232522. Source: FlyBase

negative regulation of transcription, DNA-templated

Traceable author statement PubMed 12419199. Source: FlyBase

positive regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15809036. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 10603347PubMed 10929403. Source: FlyBase

positive regulation of transcription, DNA-templated

Traceable author statement PubMed 12419199. Source: FlyBase

sensory organ precursor cell fate determination

Inferred from mutant phenotype Ref.12. Source: UniProtKB

wing disc dorsal/ventral pattern formation

Inferred from genetic interaction PubMed 16307735. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: FlyBase

nucleus

Inferred from direct assay Ref.11. Source: FlyBase

polytene chromosome

Inferred from direct assay PubMed 17925233. Source: FlyBase

protein complex

Inferred from physical interaction PubMed 17535912. Source: FlyBase

transcriptional repressor complex

Inferred from genetic interaction PubMed 16763555. Source: FlyBase

   Molecular_functionDNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from direct assay PubMed 7590238. Source: FlyBase

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 19232522. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 21102556PubMed 21765394PubMed 7954795PubMed 8749394. Source: IntAct

sequence-specific DNA binding

Inferred from direct assay PubMed 16763555. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

insvQ9VQD53EBI-92180,EBI-192407
NP072074EBI-92180,EBI-103438
Notch1Q017053EBI-92180,EBI-1392707From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Suppressor of hairless protein
PRO_0000208572

Regions

Domain429 – 51991IPT/TIG
DNA binding132 – 1398 By similarity
DNA binding266 – 27510 By similarity
DNA binding339 – 37133 By similarity
Compositional bias35 – 428Gln-rich
Compositional bias58 – 8831Gln-rich
Compositional bias541 – 55818Asn-rich
Compositional bias569 – 5768Gln-rich

Natural variations

Natural variant80 – 823Missing in strain: LAMTO 3, LAMTO 4, LAMTO 12, LAMTO 18, LAMTO 19, LAMTO 21, LAMTO 31, LAMTO 35, LAMTO 101 and LAMTO 111.
Natural variant81 – 822Missing in strain: LAMTO 13, LAMTO 37 and LAMTO 134.
Natural variant821Missing in strain: LAMTO 124.

Experimental info

Mutagenesis3151Y → F: No effect. Ref.9
Sequence conflict116 – 1172ER → DG in AAA06211. Ref.1
Sequence conflict116 – 1172ER → DG in CAA41282. Ref.1
Sequence conflict4921V → A in AAA06211. Ref.1
Sequence conflict4921V → A in CAA41282. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28159 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 145144F336CD8F4C

FASTA59466,924
        10         20         30         40         50         60 
MKSYSQFNLN AAAPPAIAYE TTVVNPNGSP LDPHQQQQQQ SQDMPHFGLP GPQPPSSQQQ 

        70         80         90        100        110        120 
QQQLQVHHQQ QQQQQQQQQQ QQHQQQMQMS LLPGPYRPHI EEKKLTRDAM EKYMRERNDM 

       130        140        150        160        170        180 
VIVILHAKVA QKSYGNEKRF FCPPPCIYLF GSGWRRRYEE MLQQGEGEQG AQLCAFIGIG 

       190        200        210        220        230        240 
SSDQDMQQLD LNGKQYCAAK TLFISDSDKR KHFMLSVKMF YGNGHDIGVF NSKRIKVISK 

       250        260        270        280        290        300 
PSKKKQSLKN ADLCIASGTN VALFNRLRSQ TVSTRYLHVE NGHFHASSTQ WGAFTIHLLD 

       310        320        330        340        350        360 
DNESESEEFQ VRDGYIHYGA TVKLVCSVTG MALPRLIIRK VDKQMALLEA DDPVSQLHKC 

       370        380        390        400        410        420 
AFYMKDTDRM YLCLSQEKII QFQATPCPKE PNKEMINDGA CWTIISTDKA EYQFYEGMGP 

       430        440        450        460        470        480 
VASPVTPVPI VNSLNLNGGG DVAMLELSGD NFTPHLQVWF GDVEAETMYR CTETLLCVVP 

       490        500        510        520        530        540 
EISQFRGEWL WVRQPTQVPI SLVRNDGIIY ATGLTFTYTP EPGPRPHCNT QAEDVMRARQ 

       550        560        570        580        590 
NNNNNNITSI SNNNNSNNAG SPAAGGGLQQ QQQQHQALPS ISEVQWNSHG SGLS 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila RBP-J kappa gene encodes the binding protein for the immunoglobulin J kappa recombination signal sequence."
Furukawa T., Kawaichi M., Matsunami N., Ryo H., Nishida Y., Honjo T.
J. Biol. Chem. 266:23334-23340(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Embryo.
[2]"Suppressor of Hairless, the Drosophila homolog of the mouse recombination signal-binding protein gene, controls sensory organ cell fates."
Schweisguth F., Posakony J.W.
Cell 69:1199-1212(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Imaginal disk.
[3]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[7]"Selective sweep at the Drosophila melanogaster Suppressor of Hairless locus and its association with the In(2L)t inversion polymorphism."
Depaulis F., Brazier L., Veuille M.
Genetics 152:1017-1024(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-128.
Strain: LAMTO 101, LAMTO 106, LAMTO 111, LAMTO 12, LAMTO 120, LAMTO 124, LAMTO 13, LAMTO 134, LAMTO 19, LAMTO 21, LAMTO 27, LAMTO 28, LAMTO 3, LAMTO 31, LAMTO 33, LAMTO 35, LAMTO 37, LAMTO 4, LAMTO 5 and LAMTP 18.
[8]"The Drosophila homolog of the immunoglobulin recombination signal-binding protein regulates peripheral nervous system development."
Furukawa T., Maruyama S., Kawaichi M., Honjo T.
Cell 69:1191-1197(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"The sequence similarity of the Drosophila suppressor of hairless protein to the integrase domain has no functional significance in vivo."
Schweisguth F., Nero P., Posakony J.W.
Dev. Biol. 166:812-814(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-315.
[10]"Inhibition of the DNA-binding activity of Drosophila suppressor of hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein-protein interaction with Drosophila hairless."
Brou C., Logeat F., Lecourtois M., Vandekerckhove J., Kourilsky P., Schweisguth F., Israel A.
Genes Dev. 8:2491-2503(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAIRLESS.
[11]"Subcellular localization of Suppressor of Hairless in Drosophila sense organ cells during Notch signalling."
Gho M., Lecourtois M., Geraud G., Posakony J.W., Schweisguth F.
Development 122:1673-1682(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Repression by suppressor of hairless and activation by Notch are required to define a single row of single-minded expressing cells in the Drosophila embryo."
Morel V., Schweisguth F.
Genes Dev. 14:377-388(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING.
[13]"A Notch-independent function of Suppressor of Hairless during the development of the bristle sensory organ precursor cell of Drosophila."
Koelzer S., Klein T.
Development 130:1973-1988(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S69213 Genomic DNA. Translation: AAA06211.1. Frameshift.
X58393 mRNA. Translation: CAA41282.1. Different initiation.
M94383 mRNA. Translation: AAA28919.1.
AE014134 Genomic DNA. Translation: AAF53434.1.
AY069091 mRNA. Translation: AAL39236.1.
AF088255 Genomic DNA. Translation: AAD39698.1.
AF088256 Genomic DNA. Translation: AAD39699.1.
AF088257 Genomic DNA. Translation: AAD39700.1.
AF088258 Genomic DNA. Translation: AAD39701.1.
AF088259 Genomic DNA. Translation: AAD39702.1.
AF088260 Genomic DNA. Translation: AAD39703.1.
AF088261 Genomic DNA. Translation: AAD39704.1.
AF088262 Genomic DNA. Translation: AAD39705.1.
AF088263 Genomic DNA. Translation: AAD39706.1.
AF088264 Genomic DNA. Translation: AAD39707.1.
AF088265 Genomic DNA. Translation: AAD39708.1.
AF088266 Genomic DNA. Translation: AAD39709.1.
AF088267 Genomic DNA. Translation: AAD39710.1.
AF088268 Genomic DNA. Translation: AAD39711.1.
AF088269 Genomic DNA. Translation: AAD39712.1.
AF088270 Genomic DNA. Translation: AAD39713.1.
AF088271 Genomic DNA. Translation: AAD39714.1.
AF088272 Genomic DNA. Translation: AAD39715.1.
AF088273 Genomic DNA. Translation: AAD39716.1.
AF088274 Genomic DNA. Translation: AAD39717.1.
PIRA41585.
A42770.
RefSeqNP_476868.1. NM_057520.3.
UniGeneDm.2288.

3D structure databases

ProteinModelPortalP28159.
SMRP28159. Positions 103-522.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60899. 39 interactions.
DIPDIP-177N.
IntActP28159. 11 interactions.
MINTMINT-335544.

Proteomic databases

PaxDbP28159.
PRIDEP28159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080700; FBpp0080261; FBgn0004837.
GeneID34881.
KEGGdme:Dmel_CG3497.

Organism-specific databases

CTD34881.
FlyBaseFBgn0004837. Su(H).

Phylogenomic databases

eggNOGNOG295376.
GeneTreeENSGT00390000005197.
InParanoidP28159.
KOK06053.
OMAMGPVHAP.
OrthoDBEOG7BP826.
PhylomeDBP28159.

Enzyme and pathway databases

SignaLinkP28159.

Gene expression databases

BgeeP28159.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProIPR015350. Beta-trefoil_DNA-bd_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR015351. LAG1_DNA-bd.
IPR008967. p53-like_TF_DNA-bd.
[Graphical view]
PfamPF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
SUPFAMSSF110217. SSF110217. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi34881.
NextBio790672.
PROP28159.

Entry information

Entry nameSUH_DROME
AccessionPrimary (citable) accession number: P28159
Secondary accession number(s): Q3S1M8 expand/collapse secondary AC list , Q9TVK8, Q9TVY7, Q9TW34, Q9U8F9, Q9V446
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase