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Protein

Zinc finger protein ush

Gene

ush

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription regulator that modulates expression mediated by transcription factors of the GATA family such as pnr and srp. Represses transcription of proneural achaete-scute complex (AS-C), which is usually activated by pnr. Involved in cardiogenesis, blood, and eye development. During hematopoiesis, it is required to restrict the number of crystal cells, probably via its interaction with the isoform SrpNC of srp. Negatively regulates expression of sr. Probably acts by interacting with the GATA-type zinc finger of proteins such as pnr and srp, possibly antagonizing the interaction between the GATA-type zinc finger and some cofactor.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri208 – 23124C2HC-type 1Add
BLAST
Zinc fingeri279 – 30123C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri341 – 36222C2HC-type 2Add
BLAST
Zinc fingeri726 – 74924C2HC-type 3Add
BLAST
Zinc fingeri797 – 82024C2HC-type 4Add
BLAST
Zinc fingeri882 – 90726C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri910 – 93223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri983 – 100624C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1119 – 114224C2HC-type 5Add
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II activating transcription factor binding Source: FlyBase
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • amnioserosa maintenance Source: FlyBase
  • chaeta development Source: FlyBase
  • compound eye development Source: FlyBase
  • dorsal closure Source: FlyBase
  • dorsal closure, leading edge cell fate determination Source: FlyBase
  • ectoderm development Source: FlyBase
  • germ-band shortening Source: FlyBase
  • head involution Source: FlyBase
  • heart development Source: FlyBase
  • hemopoiesis Source: FlyBase
  • larval lymph gland hemopoiesis Source: FlyBase
  • lymph gland development Source: FlyBase
  • negative regulation of cell fate specification Source: FlyBase
  • negative regulation of crystal cell differentiation Source: FlyBase
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: FlyBase
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • pigment metabolic process Source: FlyBase
  • regulation of antimicrobial peptide biosynthetic process Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • terminal region determination Source: FlyBase
  • torso signaling pathway Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein ush
Alternative name(s):
Protein U-shaped
Gene namesi
Name:ush
ORF Names:CG2762
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0003963. ush.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi231 – 2311C → A: Abolishes interaction with GATA-type zinc fingers. 1 Publication
Mutagenesisi1142 – 11421C → H: Transforms the C2HC-type zinc finger into a C2H2-type, leading to abolish interaction with pnr.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11911191Zinc finger protein ushPRO_0000221047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161Phosphoserine1 Publication
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei1013 – 10131Phosphoserine1 Publication
Modified residuei1015 – 10151Phosphoserine1 Publication
Modified residuei1017 – 10171Phosphoserine1 Publication
Modified residuei1156 – 11561Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VPQ6.
PRIDEiQ9VPQ6.

PTM databases

iPTMnetiQ9VPQ6.

Expressioni

Tissue specificityi

First expressed in stage 5 at high levels in the primordium of the amnioserosa. Also expressed in germ band extending embryos in cells of the developing anterior and posterior midgut and in hemocyte precursors present in the cephalic mesoderm. In embryonic stage 8, it is expressed in blood cell precursors. By stage 10, it is expressed in hemocyte precursors that have spread throughout the lateral and ventral head mesoderm. By stage 11, it is expressed in the dorsal ectoderm and in precursor cells of the hemocytes and fat body. As embryogenesis proceeds, it is also expressed in stage 13 plasmatocytes migrating throughout the head mesoderm and down the ventral midline. By late embryogenesis, expression strongly decreases but remains in the dorsal ectoderm during dorsal closure, in cells within, or associated with, the central nervous system, and in plasmatocytes circulating throughout the embryonic hemolymph. During larval development, it is expressed in primary and secondary lobes of lymph glands. Expressed in the dorsal part of the thoracic imaginal disk.3 Publications

Gene expression databases

BgeeiQ9VPQ6.
ExpressionAtlasiQ9VPQ6. differential.
GenevisibleiQ9VPQ6. DM.

Interactioni

Subunit structurei

Interacts with pnr, although weak this interaction is essential. Interacts with the isoform SrpNC of srp. Interacts with CtBP corepressor.2 Publications

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: FlyBase
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi59481. 6 interactions.
STRINGi7227.FBpp0302929.

Structurei

Secondary structure

1
1191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi202 – 2043Combined sources
Turni211 – 2133Combined sources
Helixi220 – 22910Combined sources
Beta strandi1113 – 11153Combined sources
Beta strandi1118 – 11214Combined sources
Turni1122 – 11243Combined sources
Helixi1131 – 114010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU9NMR-A1113-1146[»]
1FV5NMR-A202-235[»]
1JN7NMR-A1113-1146[»]
1Y0JNMR-B202-235[»]
2L6ZNMR-B202-235[»]
ProteinModelPortaliQ9VPQ6.
SMRiQ9VPQ6. Positions 202-235, 1111-1146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VPQ6.

Family & Domainsi

Domaini

The CCHC-type zinc fingers 1, 5 and 9 directly bind to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC-type zinc finger is essential for the interaction with GATA-type zinc fingers.1 Publication

Sequence similaritiesi

Belongs to the FOG (Friend of GATA) family.Curated
Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 5 C2HC-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri208 – 23124C2HC-type 1Add
BLAST
Zinc fingeri279 – 30123C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri341 – 36222C2HC-type 2Add
BLAST
Zinc fingeri726 – 74924C2HC-type 3Add
BLAST
Zinc fingeri797 – 82024C2HC-type 4Add
BLAST
Zinc fingeri882 – 90726C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri910 – 93223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri983 – 100624C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1119 – 114224C2HC-type 5Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
InParanoidiQ9VPQ6.
OrthoDBiEOG70W3F7.
PhylomeDBiQ9VPQ6.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 8 hits.
[Graphical view]
PROSITEiPS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VPQ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSNTRGDC SDTAEEMTVD SRDSKDLSAQ DIGEQKQQQM EDQLEDQLND
60 70 80 90 100
SRDPQNNNNN IDDDADEDAE FEEPEKANPQ QDQDLGETEM EQEHDLQQED
110 120 130 140 150
LQQELPANSP STPPRSPSSP QLIPKLEQPA TPPSEPEASP CPSPSPCPTP
160 170 180 190 200
KYPKVRLNAL LASDPALKPD AKELTLPDSR LLAPPPLVKP DTQAQPEVAE
210 220 230 240 250
PLLKPARFMC LPCGIAFSSP STLEAHQAYY CSHRIKDTDE AGSDKSGAGG
260 270 280 290 300
SGATAGDAAG LTGGSTEPPA KMARTGKQYG CTQCSYSADK KVSLNRHMRM
310 320 330 340 350
HQTSPAAPTL AGLPSLLQNG IAPPGVTPNP MEDSSSQQTD RYCSHCDIRF
360 370 380 390 400
NNIKTYRAHK QHYCSSRRPE GQLTPKPDAS PGAGSGPGSA GGSIGVSAQA
410 420 430 440 450
ATPGKLSPQA RNKTPTPAMV AVAAAAAAAA ASLQATPHSH PPFLALPTHP
460 470 480 490 500
IIIVPCSLIR AASFIPGPLP TPNSGIVNPE TTCFTVDNGT IKPLATALVG
510 520 530 540 550
ATLEPERPSA PSSAAEATEA KSSPPEPKRK EAGLTRESAP LDLSLRRSPI
560 570 580 590 600
TLNSLSLRQR QLRNALLDVE EVLLAGVGTG KENVETPRGG GSVTPEQIVC
610 620 630 640 650
APSLPSSPSM SPSPKRRAIS PRSSGAGSAS SMSPPGLNVA VPHLLDMRSM
660 670 680 690 700
LPADFGLSES LLAKTNPELA LKLAAAAAAA AVAGSSGAAA FPPASLPAQT
710 720 730 740 750
SSGNPGSGGS AGGAQQPQIY VKKGVSKCME CNIVFCKYEN YLAHKQHYCS
760 770 780 790 800
ARSQEGASEV DVKSAVSPSI AGAGGLGAGA AEAASSVETT PVAYQQLICA
810 820 830 840 850
ACGIKYTSLD NLRAHQNYYC PKGGAVAAPA ATPTDPGQLG MPKEKCGKCK
860 870 880 890 900
TLHEIGLPCP PPVANPLAAP TVNPQPATNS LNKCPVCGVV SPTAALAKKH
910 920 930 940 950
MEMHGTVKAY RCSICQYKGN TLRGMRTHIR THFDKKTSDV NEELYMTCIF
960 970 980 990 1000
EEDASALSQE LVTPTGASTT TGHDSMDHPS QMFNCDYCNY VSTYKGNVLR
1010 1020 1030 1040 1050
HMKLMHPHVA INSPSISPDT RDQDVTSNPT TNQHSNSDVS NGEAPSFHIK
1060 1070 1080 1090 1100
SEPLDPPPTV NLVHENNNSP IATPHIKAEP IEVGADAAPG GLVPPMTSPL
1110 1120 1130 1140 1150
GNSSSVAAAA AAAAEVMKKY CSTCDISFNY VKTYLAHKQF YCKNKPIRPE
1160 1170 1180 1190
ASDSPSPNHL GGGVAVGLGI GGLVGGHGQQ KNKENLQEAA I
Length:1,191
Mass (Da):124,533
Last modified:October 1, 2002 - v2
Checksum:i77A9D990767FE6ED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti524 – 5241P → H in CAA72991 (PubMed:9367989).Curated
Sequence conflicti532 – 5321A → S in CAA72991 (PubMed:9367989).Curated
Sequence conflicti1045 – 10451P → A in CAA72991 (PubMed:9367989).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12322 mRNA. Translation: CAA72991.1.
AE014134 Genomic DNA. Translation: AAF51488.2.
BT015278 mRNA. Translation: AAT94507.1.
PIRiT13850.
RefSeqiNP_476780.1. NM_057432.3.
UniGeneiDm.4716.

Genome annotation databases

EnsemblMetazoaiFBtr0078063; FBpp0077723; FBgn0003963.
GeneIDi33225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12322 mRNA. Translation: CAA72991.1.
AE014134 Genomic DNA. Translation: AAF51488.2.
BT015278 mRNA. Translation: AAT94507.1.
PIRiT13850.
RefSeqiNP_476780.1. NM_057432.3.
UniGeneiDm.4716.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU9NMR-A1113-1146[»]
1FV5NMR-A202-235[»]
1JN7NMR-A1113-1146[»]
1Y0JNMR-B202-235[»]
2L6ZNMR-B202-235[»]
ProteinModelPortaliQ9VPQ6.
SMRiQ9VPQ6. Positions 202-235, 1111-1146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59481. 6 interactions.
STRINGi7227.FBpp0302929.

PTM databases

iPTMnetiQ9VPQ6.

Proteomic databases

PaxDbiQ9VPQ6.
PRIDEiQ9VPQ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078063; FBpp0077723; FBgn0003963.
GeneIDi33225.

Organism-specific databases

CTDi33225.
FlyBaseiFBgn0003963. ush.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
InParanoidiQ9VPQ6.
OrthoDBiEOG70W3F7.
PhylomeDBiQ9VPQ6.

Miscellaneous databases

ChiTaRSiush. fly.
EvolutionaryTraceiQ9VPQ6.
GenomeRNAii33225.
NextBioi782532.
PROiQ9VPQ6.

Gene expression databases

BgeeiQ9VPQ6.
ExpressionAtlasiQ9VPQ6. differential.
GenevisibleiQ9VPQ6. DM.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 8 hits.
[Graphical view]
PROSITEiPS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "U-shaped encodes a zinc finger protein that regulates the proneural genes achaete and scute during the formation of bristles in Drosophila."
    Cubadda Y., Heitzler P., Ray R.P., Bourouis M., Ramain P., Gelbart W., Simpson P., Haenlin M.
    Genes Dev. 11:3083-3095(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Transcriptional activity of pannier is regulated negatively by heterodimerization of the GATA DNA-binding domain with a cofactor encoded by the u-shaped gene of Drosophila."
    Haenlin M., Cubadda Y., Blondeau F., Heitzler P., Lutz Y., Simpson P., Ramain P.
    Genes Dev. 11:3096-3108(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PNR.
  6. "Transcriptional cofactors of the FOG family interact with GATA proteins by means of multiple zinc fingers."
    Fox A.H., Liew C., Holmes M., Kowalski K., Mackay J., Crossley M.
    EMBO J. 18:2812-2822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  7. "The multitype zinc-finger protein U-shaped functions in heart cell specification in the Drosophila embryo."
    Fossett N., Zhang Q., Gajewski K., Choi C.Y., Kim Y., Schulz R.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:7348-7353(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "The Friend of GATA proteins U-shaped, FOG-1, and FOG-2 function as negative regulators of blood, heart, and eye development in Drosophila."
    Fossett N., Tevosian S.G., Gajewski K., Zhang Q., Orkin S.H., Schulz R.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:7342-7347(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "Two isoforms of Serpent containing either one or two GATA zinc fingers have different roles in Drosophila haematopoiesis."
    Waltzer L., Bataille L., Peyrefitte S., Haenlin M.
    EMBO J. 21:5477-5486(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRP AND CTBP.
  10. "Prepattern genes and signaling molecules regulate stripe expression to specify Drosophila flight muscle attachment sites."
    Ghazi A., Paul L., VijayRaghavan K.
    Mech. Dev. 120:519-528(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-1013; SER-1015; SER-1017 AND SER-1156, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  12. "Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions."
    Liew C.K., Kowalski K., Fox A.H., Newton A., Sharpe B.K., Crossley M., Mackay J.P.
    Structure 8:1157-1166(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 202-235 AND 1113-1146, ZINC-BINDING, MUTAGENESIS OF CYS-231.
  13. "Characterization of the conserved interaction between GATA and FOG family proteins."
    Kowalski K., Liew C.K., Matthews J.M., Gell D.A., Crossley M., Mackay J.P.
    J. Biol. Chem. 277:35720-35729(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1113-1146 MUTANT CYS-1142.

Entry informationi

Entry nameiUSH_DROME
AccessioniPrimary (citable) accession number: Q9VPQ6
Secondary accession number(s): O18414, Q6AWH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.