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Protein

Suppressor of hairless protein

Gene

Su(H)

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (PubMed:21262215, PubMed:1617729, PubMed:8674407, PubMed:10673509). Binds directly the 5'-GTGRGAR-3' DNA consensus sequence, which is present in the regulatory region of several genes (PubMed:10673509). Acts as a transcriptional repressor when it is not associated with Notch proteins (PubMed:10673509). When associated with some Notch protein, it acts as a transcriptional activator that activates transcription of Notch target genes (PubMed:10673509). Required for transcription of Sim (PubMed:10673509). Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence (PubMed:1744127, PubMed:1617730, PubMed:1617729). Required for neurogenesis in imaginal disks (PubMed:1617730, PubMed:7813798). In the larval brain, might play a role as a transducer of Notch signaling during type II neuroblast development (PubMed:21262215). Also functions independently of the Notch pathway, in the development of the bristle sensory organ precursor cell (PubMed:12642500).8 Publications

Caution

Despite some similarity with the "phage" integrase family, PubMed:7958912 showed that it has no recombinase activity.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi132 – 139By similarity8
DNA bindingi266 – 275By similarity10
DNA bindingi339 – 371By similarityAdd BLAST33

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: FlyBase
  • RNA polymerase II proximal promoter sequence-specific DNA binding Source: InterPro
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II sequence-specific DNA binding transcription factor binding Source: FlyBase
  • sequence-specific DNA binding Source: FlyBase
  • transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: FlyBase

GO - Biological processi

  • asymmetric cell division Source: FlyBase
  • cell fate determination Source: FlyBase
  • crystal cell differentiation Source: FlyBase
  • hemopoiesis Source: FlyBase
  • imaginal disc-derived wing vein morphogenesis Source: FlyBase
  • long-term memory Source: FlyBase
  • negative regulation of compound eye cone cell fate specification Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • negative regulation of transcription by RNA polymerase II Source: FlyBase
  • Notch signaling pathway Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • positive regulation of transcription by RNA polymerase II Source: FlyBase
  • sensory organ precursor cell fate determination Source: UniProtKB
  • wing disc dorsal/ventral pattern formation Source: FlyBase

Keywordsi

Molecular functionActivator, Developmental protein, DNA-binding, Repressor
Biological processNotch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiP28159

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of hairless protein
Alternative name(s):
J kappa-recombination signal-binding protein
RBP-J kappa
Gene namesi
Name:Su(H)
Synonyms:dRBP-JK
ORF Names:CG3497
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004837 Su(H)

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Lethal during the first day of pupal development (PubMed:1617730). At the larval stage, results in a "neurogenic" phenotype in imaginal disks, in which too many cells adopt the sensory organ precursor cell fate (PubMed:1617730). RNAi-mediated knockdown in type II neuroblasts, results in smaller cells (PubMed:1617730).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi315Y → F: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002085721 – 594Suppressor of hairless proteinAdd BLAST594

Proteomic databases

PaxDbiP28159
PRIDEiP28159

Expressioni

Developmental stagei

Expressed in early syncytial embryo (PubMed:1617730, PubMed:1617729). During cellularization, transient accumulation in a striped pattern (PubMed:1617730, PubMed:1617729). From late stage 11 onward, expressed gradually in a small number of segmentally reiterated cells of the peripheral nervous system (PNS) (PubMed:1617730, PubMed:1617729). This expression is specific to the external sensory organs (PubMed:1617730). In the thoracic and abdominal segments, expressed in the trichogen and tormogen cells, two outer accessory cells present in all larval external sensory organs (PubMed:1617730). During the late third larval instar, expressed in many larval and imaginal tissues (PubMed:1617730). Broadly distributed in the disks, but most abundant in the posterior region of the wing pouch (PubMed:1617730). In the leg disk, predominant in a zone largely overlapping the posterior region (PubMed:1617730). In the eye-antenna disk, low level in both the retinal field posterior to the morphogenetic furrow and the central antenna region, while higher levels appears on the margins of the disk and in the vicinity of the morphogenetic furrow (PubMed:1617730). In pupae, expressed in many tissues at this stage, including developing muscle and epidermis (PubMed:1617730). In both microchaetes and macrochaetes of 24 hr pupae, expressed on the notum and the head (PubMed:1617730). Expressed in the tormogen cell and in specific bristle cells (PubMed:1617730).2 Publications

Gene expression databases

BgeeiFBgn0004837
ExpressionAtlasiP28159 differential
GenevisibleiP28159 DM

Interactioni

Subunit structurei

Interacts with activated cleaved Notch. Interacts with Hairless, this interaction preventing its DNA-binding activity. Interacts with insv (via BEN domain).2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi60899, 63 interactors
DIPiDIP-177N
IntActiP28159, 24 interactors
MINTiP28159
STRINGi7227.FBpp0080261

Structurei

Secondary structure

1594
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi107 – 116Combined sources10
Beta strandi120 – 131Combined sources12
Beta strandi146 – 151Combined sources6
Helixi153 – 163Combined sources11
Helixi167 – 171Combined sources5
Beta strandi172 – 178Combined sources7
Beta strandi187 – 189Combined sources3
Beta strandi195 – 198Combined sources4
Beta strandi211 – 213Combined sources3
Beta strandi216 – 221Combined sources6
Beta strandi226 – 231Combined sources6
Beta strandi235 – 238Combined sources4
Helixi248 – 250Combined sources3
Beta strandi259 – 266Combined sources8
Beta strandi274 – 280Combined sources7
Beta strandi283 – 289Combined sources7
Beta strandi294 – 299Combined sources6
Beta strandi321 – 326Combined sources6
Turni327 – 329Combined sources3
Beta strandi336 – 342Combined sources7
Beta strandi345 – 347Combined sources3
Beta strandi359 – 364Combined sources6
Beta strandi367 – 375Combined sources9
Beta strandi378 – 383Combined sources6
Beta strandi388 – 395Combined sources8
Helixi398 – 400Combined sources3
Beta strandi402 – 416Combined sources15
Beta strandi430 – 437Combined sources8
Beta strandi439 – 442Combined sources4
Beta strandi444 – 450Combined sources7
Beta strandi456 – 460Combined sources5
Beta strandi467 – 471Combined sources5
Beta strandi474 – 477Combined sources4
Helixi483 – 488Combined sources6
Turni489 – 491Combined sources3
Beta strandi492 – 494Combined sources3
Beta strandi498 – 504Combined sources7
Beta strandi507 – 520Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5E24X-ray2.14E/F99-522[»]
ProteinModelPortaliP28159
SMRiP28159
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini429 – 519IPT/TIGAdd BLAST91

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi35 – 42Gln-rich8
Compositional biasi58 – 88Gln-richAdd BLAST31
Compositional biasi541 – 558Asn-richAdd BLAST18
Compositional biasi569 – 576Gln-rich8

Sequence similaritiesi

Belongs to the Su(H) family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3743 Eukaryota
ENOG410XV7K LUCA
InParanoidiP28159
KOiK06053
OMAiDMPHFGL
OrthoDBiEOG091G057S
PhylomeDBiP28159

Family and domain databases

CDDicd01176 IPT_RBP-Jkappa, 1 hit
Gene3Di2.60.40.10, 1 hit
2.60.40.1450, 2 hits
InterProiView protein in InterPro
IPR015350 Beta-trefoil_DNA-bd_dom
IPR036358 BTD_sf
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR008967 p53-like_TF_DNA-bd
IPR015351 RBP-J/Cbf11/Cbf12_DNA-bd
IPR037095 RBP-J/Cbf11/Cbf12_DNA-bd_sf
IPR038007 RBP-Jkappa_IPT
PfamiView protein in Pfam
PF09270 BTD, 1 hit
PF09271 LAG1-DNAbind, 1 hit
SMARTiView protein in SMART
SM01268 BTD, 1 hit
SM01267 LAG1_DNAbind, 1 hit
SUPFAMiSSF110217 SSF110217, 1 hit
SSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit

Sequencei

Sequence statusi: Complete.

P28159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSYSQFNLN AAAPPAIAYE TTVVNPNGSP LDPHQQQQQQ SQDMPHFGLP
60 70 80 90 100
GPQPPSSQQQ QQQLQVHHQQ QQQQQQQQQQ QQHQQQMQMS LLPGPYRPHI
110 120 130 140 150
EEKKLTRDAM EKYMRERNDM VIVILHAKVA QKSYGNEKRF FCPPPCIYLF
160 170 180 190 200
GSGWRRRYEE MLQQGEGEQG AQLCAFIGIG SSDQDMQQLD LNGKQYCAAK
210 220 230 240 250
TLFISDSDKR KHFMLSVKMF YGNGHDIGVF NSKRIKVISK PSKKKQSLKN
260 270 280 290 300
ADLCIASGTN VALFNRLRSQ TVSTRYLHVE NGHFHASSTQ WGAFTIHLLD
310 320 330 340 350
DNESESEEFQ VRDGYIHYGA TVKLVCSVTG MALPRLIIRK VDKQMALLEA
360 370 380 390 400
DDPVSQLHKC AFYMKDTDRM YLCLSQEKII QFQATPCPKE PNKEMINDGA
410 420 430 440 450
CWTIISTDKA EYQFYEGMGP VASPVTPVPI VNSLNLNGGG DVAMLELSGD
460 470 480 490 500
NFTPHLQVWF GDVEAETMYR CTETLLCVVP EISQFRGEWL WVRQPTQVPI
510 520 530 540 550
SLVRNDGIIY ATGLTFTYTP EPGPRPHCNT QAEDVMRARQ NNNNNNITSI
560 570 580 590
SNNNNSNNAG SPAAGGGLQQ QQQQHQALPS ISEVQWNSHG SGLS
Length:594
Mass (Da):66,924
Last modified:July 1, 1993 - v1
Checksum:i145144F336CD8F4C
GO

Sequence cautioni

The sequence AAA06211 differs from that shown. Reason: Frameshift at position 6.Curated
The sequence CAA41282 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti116 – 117ER → DG in AAA06211 (PubMed:1744127).Curated2
Sequence conflicti116 – 117ER → DG in CAA41282 (PubMed:1744127).Curated2
Sequence conflicti492V → A in AAA06211 (PubMed:1744127).Curated1
Sequence conflicti492V → A in CAA41282 (PubMed:1744127).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti80 – 82Missing in strain: LAMTO 3, LAMTO 4, LAMTO 12, LAMTO 18, LAMTO 19, LAMTO 21, LAMTO 31, LAMTO 35, LAMTO 101 and LAMTO 111. 3
Natural varianti81 – 82Missing in strain: LAMTO 13, LAMTO 37 and LAMTO 134. 2
Natural varianti82Missing in strain: LAMTO 124. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA41585
A42770
RefSeqiNP_001285948.1, NM_001299019.1
NP_476868.1, NM_057520.4
UniGeneiDm.2288

Genome annotation databases

EnsemblMetazoaiFBtr0080700; FBpp0080261; FBgn0004837
FBtr0346621; FBpp0312201; FBgn0004837
GeneIDi34881
KEGGidme:Dmel_CG3497

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSUH_DROME
AccessioniPrimary (citable) accession number: P28159
Secondary accession number(s): Q3S1M8
, Q9TVK8, Q9TVY7, Q9TW34, Q9U8F9, Q9V446
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 25, 2018
This is version 179 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health