Reviewed, UniProtKB/Swiss-Prot Q9VPQ6 (USH_DROME)

Names and origin

Protein names

Recommended name:
    Zinc finger protein ush
Alternative name(s):
    Protein U-shaped

Gene names

Name:	ush
ORF Names:	CG2762

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 haematopoisis, 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. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10
Subunit structure	Interacts with pnr, although weak this interaction is essential. Interacts with the isoform SrpNC of srp. Interacts with CtBP corepressor. Ref.5 Ref.9
Subcellular location	Nucleus. Ref.1
Tissue specificity	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. Ref.1 Ref.7 Ref.8
Domain	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. Ref.6
Sequence similarities	Belongs to the FOG (Friend of GATA) family. Contains 4 C2H2-type zinc fingers. Contains 5 C2HC-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	amnioserosa maintenance Inferred from mutant phenotype. Source: FlyBase compound eye development Ref.8 Inferred from mutant phenotype. Source: FlyBase dorsal closure, leading edge cell fate determination Non-traceable author statement. Source: FlyBase ectoderm development Traceable author statement. Source: FlyBase germ-band shortening Inferred from mutant phenotype. Source: FlyBase head involution Non-traceable author statement. Source: FlyBase heart development Ref.8 Inferred from mutant phenotype. Source: FlyBase hemopoiesis Traceable author statement. Source: FlyBase lymph gland development Inferred from mutant phenotype. Source: FlyBase negative regulation of cell fate specification Traceable author statement. Source: FlyBase negative regulation of crystal cell differentiation Traceable author statement. Source: FlyBase pigment metabolic process Traceable author statement. Source: FlyBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW terminal region determination Inferred from genetic interaction. Source: FlyBase torso signaling pathway Inferred from genetic interaction. Source: FlyBase transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transcription factor binding Ref.1 Inferred from mutant phenotype. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1191

1191

Zinc finger protein ush

PRO_0000221047

Regions

Zinc finger

208 – 231

24

C2HC-type 1

Zinc finger

279 – 301

23

C2H2-type 1

Zinc finger

341 – 362

22

C2HC-type 2

Zinc finger

726 – 749

24

C2HC-type 3

Zinc finger

797 – 820

24

C2HC-type 4

Zinc finger

882 – 907

26

C2H2-type 2

Zinc finger

910 – 932

23

C2H2-type 3

Zinc finger

983 – 1006

24

C2H2-type 4

Zinc finger

1119 – 1142

24

C2HC-type 5

Amino acid modifications

Modified residue

116

1

Phosphoserine Ref.11

Modified residue

118

1

Phosphoserine Ref.11

Modified residue

1013

1

Phosphoserine Ref.11

Modified residue

1015

1

Phosphoserine Ref.11

Modified residue

1017

1

Phosphoserine Ref.11

Modified residue

1156

1

Phosphoserine Ref.11

Experimental info

Mutagenesis

231

1

C → A: Abolishes interaction with GATA-type zinc fingers. Ref.12

Mutagenesis

1142

1

C → H: Transforms the C2HC-type zinc finger into a C2H2-type, leading to abolish interaction with pnr.

Sequence conflict

524

1

P → H in CAA72991. Ref.1

Sequence conflict

532

1

A → S in CAA72991. Ref.1

Sequence conflict

1045

1

P → A in CAA72991. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

1191

Helix Strand Turn

Details...

Beta strand

202 – 204

3

Turn

211 – 213

3

Helix

220 – 229

10

Turn

1122 – 1124

3

Helix

1131 – 1140

10

Sequences

	Sequence		Length	Mass (Da)
	Q9VPQ6-1 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: 77A9D990767FE6ED	FASTA	1,191	124,533
	10 20 30 40 50 60 MLSSNTRGDC SDTAEEMTVD SRDSKDLSAQ DIGEQKQQQM EDQLEDQLND SRDPQNNNNN 70 80 90 100 110 120 IDDDADEDAE FEEPEKANPQ QDQDLGETEM EQEHDLQQED LQQELPANSP STPPRSPSSP 130 140 150 160 170 180 QLIPKLEQPA TPPSEPEASP CPSPSPCPTP KYPKVRLNAL LASDPALKPD AKELTLPDSR 190 200 210 220 230 240 LLAPPPLVKP DTQAQPEVAE PLLKPARFMC LPCGIAFSSP STLEAHQAYY CSHRIKDTDE 250 260 270 280 290 300 AGSDKSGAGG SGATAGDAAG LTGGSTEPPA KMARTGKQYG CTQCSYSADK KVSLNRHMRM 310 320 330 340 350 360 HQTSPAAPTL AGLPSLLQNG IAPPGVTPNP MEDSSSQQTD RYCSHCDIRF NNIKTYRAHK 370 380 390 400 410 420 QHYCSSRRPE GQLTPKPDAS PGAGSGPGSA GGSIGVSAQA ATPGKLSPQA RNKTPTPAMV 430 440 450 460 470 480 AVAAAAAAAA ASLQATPHSH PPFLALPTHP IIIVPCSLIR AASFIPGPLP TPNSGIVNPE 490 500 510 520 530 540 TTCFTVDNGT IKPLATALVG ATLEPERPSA PSSAAEATEA KSSPPEPKRK EAGLTRESAP 550 560 570 580 590 600 LDLSLRRSPI TLNSLSLRQR QLRNALLDVE EVLLAGVGTG KENVETPRGG GSVTPEQIVC 610 620 630 640 650 660 APSLPSSPSM SPSPKRRAIS PRSSGAGSAS SMSPPGLNVA VPHLLDMRSM LPADFGLSES 670 680 690 700 710 720 LLAKTNPELA LKLAAAAAAA AVAGSSGAAA FPPASLPAQT SSGNPGSGGS AGGAQQPQIY 730 740 750 760 770 780 VKKGVSKCME CNIVFCKYEN YLAHKQHYCS ARSQEGASEV DVKSAVSPSI AGAGGLGAGA 790 800 810 820 830 840 AEAASSVETT PVAYQQLICA ACGIKYTSLD NLRAHQNYYC PKGGAVAAPA ATPTDPGQLG 850 860 870 880 890 900 MPKEKCGKCK TLHEIGLPCP PPVANPLAAP TVNPQPATNS LNKCPVCGVV SPTAALAKKH 910 920 930 940 950 960 MEMHGTVKAY RCSICQYKGN TLRGMRTHIR THFDKKTSDV NEELYMTCIF EEDASALSQE 970 980 990 1000 1010 1020 LVTPTGASTT TGHDSMDHPS QMFNCDYCNY VSTYKGNVLR HMKLMHPHVA INSPSISPDT 1030 1040 1050 1060 1070 1080 RDQDVTSNPT TNQHSNSDVS NGEAPSFHIK SEPLDPPPTV NLVHENNNSP IATPHIKAEP 1090 1100 1110 1120 1130 1140 IEVGADAAPG GLVPPMTSPL GNSSSVAAAA AAAAEVMKKY CSTCDISFNY VKTYLAHKQF 1150 1160 1170 1180 1190 YCKNKPIRPE ASDSPSPNHL GGGVAVGLGI GGLVGGHGQQ KNKENLQEAA I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9367989] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 9367990] [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: 10329627] [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: 10861002] [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: 11404479] [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: 12374748] [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: 12782269] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-1013; SER-1015; SER-1017 AND SER-1156, 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: 11080638] [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: 12110675] [Abstract] Cited for: STRUCTURE BY NMR OF 1113-1146 MUTANT CYS-1142.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y12322 mRNA. Translation: CAA72991.1.
AE014134 Genomic DNA. Translation: AAF51488.2.
BT015278 mRNA. Translation: AAT94507.1.

PIR

T13850.

RefSeq

NP_476780.1.

UniGene

Dm.4716

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FU9	NMR	-	A	1113-1146	[»]
1FV5	NMR	-	A	202-235	[»]
1JN7	NMR	-	A	1113-1146	[»]
1Y0J	NMR	-	B	202-235	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9VPQ6. 2 interactions.

Proteomic databases

PRIDE

Q9VPQ6.

Genome annotation databases

Ensembl

FBgn0003963. Drosophila melanogaster. [Contig view]

GeneID

33225.

KEGG

dme:Dmel_CG2762.

NMPDR

fig|7227.3.peg.108.

Organism-specific databases

FlyBase

FBgn0003963. ush.

Phylogenomic databases

HOGENOM

Q9VPQ6.

OMA

Q9VPQ6. HKQHYCS.

Enzyme and pathway databases

BioCyc

DMEL-XXX-02:DMEL-XXX-02-006719-MON.

Gene expression databases

ArrayExpress

Q9VPQ6.

GermOnline

CG2762. Drosophila melanogaster.

Family and domain databases

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]

Pfam

PF00096. zf-C2H2. 4 hits.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 8 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. False negative.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

782532.

Entry information

Entry name

USH_DROME

Accession

Primary (citable) accession number: Q9VPQ6
Secondary accession number(s): O18414, Q6AWH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project