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P28159

- SUH_DROME

UniProt

P28159 - SUH_DROME

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Protein

Suppressor of hairless protein

Gene

Su(H)

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- 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. 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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi132 – 1398By similarity
DNA bindingi266 – 27510By similarity
DNA bindingi339 – 37133By similarityAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: InterPro
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: FlyBase
  4. RNA polymerase II distal enhancer sequence-specific DNA binding Source: FlyBase
  5. sequence-specific DNA binding Source: FlyBase

GO - Biological processi

  1. asymmetric cell division Source: FlyBase
  2. cell fate determination Source: FlyBase
  3. crystal cell differentiation Source: FlyBase
  4. hemopoiesis Source: FlyBase
  5. I-kappaB phosphorylation Source: FlyBase
  6. imaginal disc-derived wing vein morphogenesis Source: FlyBase
  7. lateral inhibition Source: FlyBase
  8. long-term memory Source: FlyBase
  9. negative regulation of compound eye cone cell fate specification Source: FlyBase
  10. negative regulation of transcription, DNA-templated Source: FlyBase
  11. negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  12. Notch signaling pathway Source: UniProtKB
  13. positive regulation of G1/S transition of mitotic cell cycle Source: FlyBase
  14. positive regulation of transcription, DNA-templated Source: FlyBase
  15. positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  16. sensory organ precursor cell fate determination Source: UniProtKB
  17. wing disc dorsal/ventral pattern formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor

Keywords - Biological processi

Notch signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004837. Su(H).

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: In imaginal disk, at the onset of differentiation of socket cell, it is also present in the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleus Source: FlyBase
  3. polytene chromosome Source: FlyBase
  4. protein complex Source: FlyBase
  5. transcriptional repressor complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi315 – 3151Y → F: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Suppressor of hairless proteinPRO_0000208572Add
BLAST

Proteomic databases

PaxDbiP28159.
PRIDEiP28159.

Expressioni

Gene expression databases

BgeeiP28159.

Interactioni

Subunit structurei

Interacts with activated cleaved Notch. Interacts with Hairless, this interaction preventing its DNA-binding activity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
insvQ9VQD53EBI-92180,EBI-192407
NP072074EBI-92180,EBI-103438
Notch1Q017053EBI-92180,EBI-1392707From a different organism.

Protein-protein interaction databases

BioGridi60899. 39 interactions.
DIPiDIP-177N.
IntActiP28159. 11 interactions.
MINTiMINT-335544.

Structurei

3D structure databases

ProteinModelPortaliP28159.
SMRiP28159. Positions 103-522.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini429 – 51991IPT/TIGAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi35 – 428Gln-rich
Compositional biasi58 – 8831Gln-richAdd
BLAST
Compositional biasi541 – 55818Asn-richAdd
BLAST
Compositional biasi569 – 5768Gln-rich

Sequence similaritiesi

Belongs to the Su(H) family.Curated
Contains 1 IPT/TIG domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG295376.
GeneTreeiENSGT00390000005197.
InParanoidiP28159.
KOiK06053.
OMAiMGPVHAP.
OrthoDBiEOG7BP826.
PhylomeDBiP28159.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProiIPR015350. 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]
PfamiPF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
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 AAA06211.1 differs from that shown. Reason: Frameshift at position 6.
The sequence CAA41282.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1172ER → DG in AAA06211. (PubMed:1744127)Curated
Sequence conflicti116 – 1172ER → DG in CAA41282. (PubMed:1744127)Curated
Sequence conflicti492 – 4921V → A in AAA06211. (PubMed:1744127)Curated
Sequence conflicti492 – 4921V → A in CAA41282. (PubMed:1744127)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 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 varianti81 – 822Missing in strain: LAMTO 13, LAMTO 37 and LAMTO 134.
Natural varianti82 – 821Missing in strain: LAMTO 124.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_476868.1. NM_057520.4.
UniGeneiDm.2288.

Genome annotation databases

EnsemblMetazoaiFBtr0080700; FBpp0080261; FBgn0004837.
GeneIDi34881.
KEGGidme:Dmel_CG3497.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A41585.
A42770.
RefSeqi NP_476868.1. NM_057520.4.
UniGenei Dm.2288.

3D structure databases

ProteinModelPortali P28159.
SMRi P28159. Positions 103-522.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60899. 39 interactions.
DIPi DIP-177N.
IntActi P28159. 11 interactions.
MINTi MINT-335544.

Proteomic databases

PaxDbi P28159.
PRIDEi P28159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080700 ; FBpp0080261 ; FBgn0004837 .
GeneIDi 34881.
KEGGi dme:Dmel_CG3497.

Organism-specific databases

CTDi 34881.
FlyBasei FBgn0004837. Su(H).

Phylogenomic databases

eggNOGi NOG295376.
GeneTreei ENSGT00390000005197.
InParanoidi P28159.
KOi K06053.
OMAi MGPVHAP.
OrthoDBi EOG7BP826.
PhylomeDBi P28159.

Enzyme and pathway databases

SignaLinki P28159.

Miscellaneous databases

GenomeRNAii 34881.
NextBioi 790672.
PROi P28159.

Gene expression databases

Bgeei P28159.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProi IPR015350. 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 ]
Pfami PF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view ]
SUPFAMi SSF110217. SSF110217. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. 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.

Entry informationi

Entry nameiSUH_DROME
AccessioniPrimary (citable) accession number: P28159
Secondary accession number(s): Q3S1M8
, Q9TVK8, Q9TVY7, Q9TW34, Q9U8F9, Q9V446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3