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Protein

Protein suppressor of variegation 3-7

Gene

Su(var)3-7

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

Functioni

Dose-limiting factor in position-effect variegation, the inactivation in some cells of a gene translocated next to heterochromatin. It could play a role in chromosome condensation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri217 – 23620C2H2-type 1Add
BLAST
Zinc fingeri319 – 34325C2H2-type 2Add
BLAST
Zinc fingeri425 – 44622C2H2-type 3Add
BLAST
Zinc fingeri487 – 51226C2H2-type 4Add
BLAST
Zinc fingeri605 – 62925C2H2-type 5Add
BLAST
Zinc fingeri737 – 76125C2H2-type 6Add
BLAST
Zinc fingeri829 – 85224C2H2-type 7Add
BLAST

GO - Molecular functioni

  1. chromatin binding Source: FlyBase
  2. DNA binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dosage compensation by hyperactivation of X chromosome Source: FlyBase
  2. positive regulation of chromatin silencing at centromere Source: FlyBase
  3. positive regulation of heterochromatin assembly Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein suppressor of variegation 3-7
Gene namesi
Name:Su(var)3-7
Synonyms:Suvar(3)7
ORF Names:CG8599
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003598. Su(var)3-7.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. chromosome, centromeric region Source: FlyBase
  2. heterochromatin Source: FlyBase
  3. nucleus Source: FlyBase
  4. pericentric heterochromatin Source: FlyBase
  5. polytene chromosome chromocenter Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12501250Protein suppressor of variegation 3-7PRO_0000047060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei175 – 1751Phosphoserine1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei871 – 8711Phosphoserine1 Publication
Modified residuei873 – 8731Phosphoserine1 Publication
Modified residuei975 – 9751Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20193.
PRIDEiP20193.

Expressioni

Gene expression databases

BgeeiP20193.

Interactioni

Subunit structurei

Interacts with Su(var)39 through the BESS domain.1 Publication

Protein-protein interaction databases

BioGridi66711. 9 interactions.
IntActiP20193. 4 interactions.
MINTiMINT-1023300.
STRINGi7227.FBpp0082204.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini987 – 102640BESSPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 706Poly-Asp
Compositional biasi167 – 1737Poly-Asp
Compositional biasi670 – 6734Poly-Glu
Compositional biasi861 – 8699Poly-Ala
Compositional biasi1089 – 10924Poly-Asn
Compositional biasi1194 – 11974Poly-Asn

Sequence similaritiesi

Contains 1 BESS domain.PROSITE-ProRule annotation
Contains 7 C2H2-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri217 – 23620C2H2-type 1Add
BLAST
Zinc fingeri319 – 34325C2H2-type 2Add
BLAST
Zinc fingeri425 – 44622C2H2-type 3Add
BLAST
Zinc fingeri487 – 51226C2H2-type 4Add
BLAST
Zinc fingeri605 – 62925C2H2-type 5Add
BLAST
Zinc fingeri737 – 76125C2H2-type 6Add
BLAST
Zinc fingeri829 – 85224C2H2-type 7Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG288977.
InParanoidiP20193.
OMAiDMICSSF.
OrthoDBiEOG7GQXTW.
PhylomeDBiP20193.

Family and domain databases

InterProiIPR004210. BESS_motif.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF02944. BESS. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS51031. BESS. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20193-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDRDSSMQAK NLDAQCNPDL KMASANSETL ASATHELKIM DVEGGALVDP
60 70 80 90 100
DHIEEVETSM VIVVDDDDGD VAMVVEEDKH PMRDDPCIED IMDDEHAPLV
110 120 130 140 150
AELQSALNNP DDKQASEDPL LEDQEREPDA MSTKTEPSSD AESSHSYHDP
160 170 180 190 200
MGLLERIEIH DPGDSQDDDD EDDESSNGGG VDGGMRRKMP RAQRWLLWMK
210 220 230 240 250
RWPWILHEDS DGTLAFCLYC NISINVNNRS RHIQQHNVSL SHQERECNYL
260 270 280 290 300
AFKKSEEETR GAISDNEIKH EFGTKSYVAA MKQKRISETE AFNNFNWLRW
310 320 330 340 350
LRWHPWLERS MPTGTIGTCR ICSVRMNVEF VYLRKRHETT KGHMEALRNL
360 370 380 390 400
DSDKRSRKRK RSKSNSVTNS GGDEAEREKE SEPEVGPEDA QDTPVVMMNG
410 420 430 440 450
DVDSGDDPGK WCALIPDTNP QQCRCTLCNC TMAITSFLRH CKTRAHCHML
460 470 480 490 500
STPAEKGSSD IRGIWAVFAD MHPWLIADPE DPSIGYCSVC RKRFMYGNSE
510 520 530 540 550
IKRKNHEKSE KHTLALASAK AGIEVGSADG RGGDNMDEEE AAASDQAQSS
560 570 580 590 600
QTDDSEDNDD DNWSEIQKLG KGFAHKSSSE PRKATVRAGV RFYPWLCYSK
610 620 630 640 650
DRKTQICKFC RVRFHNEAAK ARHELSARHV KLVKQFKMRQ AKLHQGTNTQ
660 670 680 690 700
TKHNAQDDEE SQEQDEEYGE EEEDAEEDSQ SNFDLGTVQA RKTARADNKL
710 720 730 740 750
FVKPIPATMK GKVMVWKGRF PWLSYKKNEQ RGNYAWCKLC EVSLYLPSSK
760 770 780 790 800
WASKHQRTSR HIRLRIDRKR NGGNPLKTSN KNSGEISTVV ATASALASAE
810 820 830 840 850
ARQKAAMAEL QAKYDWLDPD ANDENHCHCR VCDSRLPIKV FYLRQHDASR
860 870 880 890 900
KHVENKERQR ANAAAAANAP SVSPTSTVDA ERQESGMDKE SENDMSVRSD
910 920 930 940 950
GSTAEPLAKR SRRSMEVRRI IRALRDSMGK RQEERSQMDM ARDMICSSFD
960 970 980 990 1000
IVTRLRTLER ESVAHNESMA QAPPSVTVSP IKPPEPRHVM DLFFDSISPT
1010 1020 1030 1040 1050
MKSLPPDLAA EGKSKIMQLV CSLELRAMQR NATTPTPATV SASSKWPSST
1060 1070 1080 1090 1100
TVTPVKTPPA PISAPLASVD ADLHSSVVTT PHEYNNGQNN NNDKETVPKE
1110 1120 1130 1140 1150
PVTGASSAQV TINGSAKDLP ENIRRILTSN QTQVTNRLET DSVRCVPLDK
1160 1170 1180 1190 1200
LTTQSRTNVN GRLSQGGTSE APSTPQADLS NGNTLAMIRQ IRVNNNNSSK
1210 1220 1230 1240 1250
ITVTNTPQMQ QPQQAQASIT SSTPIMRGGP SSNGCQITTF RTMVNHNRRP
Length:1,250
Mass (Da):139,990
Last modified:July 19, 2004 - v4
Checksum:i90D0338C894D074C
GO

Sequence cautioni

The sequence CAA36434.1 differs from that shown. Reason: Frameshift at positions 4 and 81. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 542IE → MQ in CAA36434. (PubMed:7708496)Curated
Sequence conflicti265 – 2651D → S in CAA36434. (PubMed:7708496)Curated
Sequence conflicti385 – 3851V → A in CAA36434. (PubMed:7708496)Curated
Sequence conflicti943 – 9431D → N in CAA36434. (PubMed:7708496)Curated
Sequence conflicti1148 – 11481L → V in CAA36434. (PubMed:7708496)Curated
Sequence conflicti1159 – 11591V → A in CAA36434. (PubMed:7708496)Curated
Sequence conflicti1193 – 11931V → A in CAA36434. (PubMed:7708496)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52187 mRNA. Translation: CAA36434.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF54918.2.
PIRiS09151.
RefSeqiNP_524342.3. NM_079618.4.
UniGeneiDm.6402.

Genome annotation databases

EnsemblMetazoaiFBtr0082736; FBpp0082204; FBgn0003598.
GeneIDi41627.
KEGGidme:Dmel_CG8599.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52187 mRNA. Translation: CAA36434.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF54918.2.
PIRiS09151.
RefSeqiNP_524342.3. NM_079618.4.
UniGeneiDm.6402.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66711. 9 interactions.
IntActiP20193. 4 interactions.
MINTiMINT-1023300.
STRINGi7227.FBpp0082204.

Proteomic databases

PaxDbiP20193.
PRIDEiP20193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082736; FBpp0082204; FBgn0003598.
GeneIDi41627.
KEGGidme:Dmel_CG8599.

Organism-specific databases

CTDi41627.
FlyBaseiFBgn0003598. Su(var)3-7.

Phylogenomic databases

eggNOGiNOG288977.
InParanoidiP20193.
OMAiDMICSSF.
OrthoDBiEOG7GQXTW.
PhylomeDBiP20193.

Miscellaneous databases

GenomeRNAii41627.
NextBioi824709.

Gene expression databases

BgeeiP20193.

Family and domain databases

InterProiIPR004210. BESS_motif.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF02944. BESS. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS51031. BESS. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The modifier of position-effect variegation Suvar(3)7 of Drosophila: there are two alternative transcripts and seven scattered zinc fingers, each preceded by a tryptophan box."
    Cleard F., Matsarskaia M., Spierer P.
    Nucleic Acids Res. 23:796-802(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Erratum
    Cleard F., Matsarskaia M., Spierer P.
    Nucleic Acids Res. 23:3804-3804(1995)
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "Dependence of position-effect variegation in Drosophila on dose of a gene encoding an unusual zinc-finger protein."
    Reuter G., Giarre M., Farah J., Gausz J., Spierer A., Spierer P.
    Nature 344:219-223(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 336-1250.
  6. "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing."
    Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S., Jenuwein T., Dorn R., Reuter G.
    EMBO J. 21:1121-1131(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SU(VAR)39.
  7. "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-165; SER-175; SER-176; SER-871; SER-873 AND SER-975, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiSUV37_DROME
AccessioniPrimary (citable) accession number: P20193
Secondary accession number(s): Q9VFX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 19, 2004
Last modified: January 7, 2015
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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

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 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.