Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Brain tumor protein

Gene

brat

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

Functioni

Plays a central role in translation repression of hb mRNA by being recruited by nos and pum to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR. Probably recruited by other proteins to repress translation of other mRNAs in other tissues. Involved in the regulation of ribosomal RNA synthesis and cell growth. Participates in abdominal segmentation and imaginal disk development. Involved in brain tumor suppression, by acting as a growth suppressor in the larval brain.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri174 – 22249B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri323 – 36644B box-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • translation regulator activity Source: FlyBase
  • translation repressor activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • asymmetric cell division Source: FlyBase
  • asymmetric neuroblast division resulting in ganglion mother cell formation Source: FlyBase
  • axon guidance Source: FlyBase
  • brain development Source: FlyBase
  • ganglion mother cell fate determination Source: FlyBase
  • negative regulation of cell proliferation Source: FlyBase
  • negative regulation of neuroblast proliferation Source: FlyBase
  • negative regulation of translation Source: GOC
  • neuroblast fate determination Source: FlyBase
  • neuroblast proliferation Source: FlyBase
  • neurogenesis Source: FlyBase
  • neuron differentiation Source: FlyBase
  • oogenesis Source: FlyBase
  • phagocytosis Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of neurogenesis Source: FlyBase
  • regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • regulation of synaptic vesicle endocytosis Source: FlyBase
  • regulation of translation Source: FlyBase
  • rRNA transcription Source: UniProtKB
  • segmentation Source: FlyBase
  • ventral cord development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Brain tumor protein
Gene namesi
Name:brat
ORF Names:CG10719
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0010300. brat.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • neuronal cell body Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi802 – 8021H → L in bratfs3; induces production of tumor-like neoplasms in the larval brain. Disrupts interaction with nos and pum.
Mutagenesisi829 – 8291Y → A: Disrupts recruitment by pum. 1 Publication
Mutagenesisi847 – 8471R → A: Disrupts recruitment by pum. 1 Publication
Mutagenesisi859 – 8591Y → A: Does not affect recruitment by pum. 1 Publication
Mutagenesisi860 – 8601G → D in bratts1; induces production of tumor-like neoplasms in the larval brain. Disrupts interaction with nos and pum.
Mutagenesisi875 – 8751R → A: Disrupts recruitment by pum. 1 Publication
Mutagenesisi970 – 9701E → A: Does not affect recruitment by pum. 1 Publication
Mutagenesisi1012 – 10121D → A: Does not affect recruitment by pum. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10371037Brain tumor proteinPRO_0000220368Add
BLAST

Proteomic databases

PaxDbiQ8MQJ9.
PRIDEiQ8MQJ9.

Expressioni

Tissue specificityi

Expressed during embryogenesis, mainly in nervous tissues. Expressed in the embryonic central and peripheral nervous systems including the embryonic brain. In third instar larva it is expressed in the larval central nervous system including the brain and the ventral ganglion, in two glands (the ring gland and the salivary gland, and in parts of the foregut) the gastric caeca and the proventriculus.1 Publication

Gene expression databases

BgeeiQ8MQJ9.
ExpressionAtlasiQ8MQJ9. differential.
GenevisibleiQ8MQJ9. DM.

Interactioni

Subunit structurei

Interacts with nos and pum. Acts via the formation of a quaternary complex composed of pum, nos, brat and the 3'-UTR mRNA of hb. Not recruited by nos and pum to cyclin B 3'-UTR mRNA.1 Publication

Protein-protein interaction databases

BioGridi61181. 3 interactions.
DIPiDIP-37857N.
IntActiQ8MQJ9. 3 interactions.
MINTiMINT-1602052.
STRINGi7227.FBpp0293081.

Structurei

Secondary structure

1
1037
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi762 – 7643Combined sources
Beta strandi766 – 7705Combined sources
Beta strandi773 – 7764Combined sources
Beta strandi779 – 7813Combined sources
Beta strandi783 – 7886Combined sources
Beta strandi794 – 7985Combined sources
Helixi799 – 8013Combined sources
Beta strandi803 – 8075Combined sources
Beta strandi813 – 8175Combined sources
Beta strandi820 – 8234Combined sources
Beta strandi827 – 8359Combined sources
Turni837 – 8393Combined sources
Beta strandi842 – 8465Combined sources
Helixi848 – 8503Combined sources
Beta strandi852 – 8565Combined sources
Beta strandi862 – 8665Combined sources
Turni868 – 8703Combined sources
Beta strandi874 – 8796Combined sources
Beta strandi885 – 8895Combined sources
Turni890 – 8934Combined sources
Beta strandi894 – 8985Combined sources
Beta strandi904 – 9096Combined sources
Turni911 – 9133Combined sources
Beta strandi915 – 9228Combined sources
Beta strandi924 – 9329Combined sources
Helixi933 – 9353Combined sources
Beta strandi937 – 9426Combined sources
Beta strandi947 – 9526Combined sources
Turni954 – 9563Combined sources
Beta strandi959 – 9657Combined sources
Beta strandi971 – 9755Combined sources
Beta strandi977 – 9793Combined sources
Beta strandi981 – 9855Combined sources
Beta strandi991 – 9999Combined sources
Beta strandi1004 – 10107Combined sources
Turni1011 – 10133Combined sources
Beta strandi1014 – 10196Combined sources
Turni1020 – 10223Combined sources
Beta strandi1023 – 10286Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7FX-ray1.95A/B756-1037[»]
4ZLRX-ray2.30A/B756-1037[»]
5EX7X-ray2.60A758-1037[»]
ProteinModelPortaliQ8MQJ9.
SMRiQ8MQJ9. Positions 756-1037.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8MQJ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati767 – 81044NHL 1Add
BLAST
Repeati814 – 85946NHL 2Add
BLAST
Repeati860 – 90142NHL 3Add
BLAST
Repeati902 – 94443NHL 4Add
BLAST
Repeati945 – 98844NHL 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 175173Ser-richAdd
BLAST
Compositional biasi259 – 32567Gln-richAdd
BLAST
Compositional biasi579 – 60022His-richAdd
BLAST

Domaini

The NHL repeats form six-bladed beta-propeller that mediate the interaction with the pumilio repeats of pum, and are essential for translational effector function.1 Publication

Sequence similaritiesi

Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 5 NHL repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri174 – 22249B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri323 – 36644B box-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG410XQJ4. LUCA.
GeneTreeiENSGT00550000074377.
InParanoidiQ8MQJ9.
OrthoDBiEOG7NGQ9V.
PhylomeDBiQ8MQJ9.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
[Graphical view]
PfamiPF01436. NHL. 4 hits.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 2 hits.
[Graphical view]
PROSITEiPS51125. NHL. 5 hits.
PS50119. ZF_BBOX. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8MQJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSPTPSLD SMRGGANSIE SYEHAGYLSD SPLTLSGSSP PASDSAICSD
60 70 80 90 100
EYTGGSSVKS RSEVTVINGH HPISASVSSS SSASSSSCSS SSSSSSSSSS
110 120 130 140 150
SSSSTSGLSG CGSTSSSVIS ANNVASSNGP GVIGSNLQSS NNGGNSGISS
160 170 180 190 200
LVVGAGKGSN SSSNSSSSNT SANGSPPRCT ACKSKCSDAV AKCFECQSYL
210 220 230 240 250
CANCVTAHEF MHCFNGHNVC LIKGFEASTT GTPLSVGSPS NNPASNEFKY
260 270 280 290 300
ASSLTMMLQQ QQQLDSQQQQ QQQQLLPAQP MSQLSKIVLA AAAQANSQEQ
310 320 330 340 350
QREDSIYGSL HPQQQQQQQQ QQQRQLFCPR HKQELLKFSC RTCCILVCKE
360 370 380 390 400
CIVLEHSTGL HELENVQSPG MTTSTGSTAN ESALQTLLAD MRGKIGEIVG
410 420 430 440 450
IAGNSDQNLT KVKLQYQKAH NELNETHQFF ASMLDERKTE LLKELETLYT
460 470 480 490 500
AKVNSNNSWQ QRSRDLIDKG LATCEAVERS PAPPSSLLTE ALLLRKSLEQ
510 520 530 540 550
QLQTGIQEMQ LPFEIEFMSN YQSIQAGVRN TFGYIRANSS DGGPTGMSLT
560 570 580 590 600
SNGHGKQPPI ARPTQSASNS SASSAGSGHH GHHQQSHHHG HHNHHQTAHH
610 620 630 640 650
QQLQAQSSLH GLGLGLSGAS LLDSSSSAGG AVGAFSNGGL LLGGRDRNAL
660 670 680 690 700
AVEQHFGELM PKRGGGGYTG SNGSATSAVA HYNPYEKWSN GGSDNLFSSV
710 720 730 740 750
TSGVSGSSAV ADAFASLSAV GGSVVSGAGA GGSTVSSESL LDLTNKLLSA
760 770 780 790 800
TIYPPKSQIK RQKMIYHCKF GEFGVMEGQF TEPSGVAVNA QNDIIVADTN
810 820 830 840 850
NHRIQIFDKE GRFKFQFGEC GKRDSQLLYP NRVAVVRNSG DIIVTERSPT
860 870 880 890 900
HQIQIYNQYG QFVRKFGATI LQHPRGVTVD NKGRIIVVEC KVMRVIIFDQ
910 920 930 940 950
NGNVLHKFGC SKHLEFPNGV VVNDKQEIFI SDNRAHCVKV FNYEGQYLRQ
960 970 980 990 1000
IGGEGITNYP IGVGINSNGE ILIADNHNNF NLTIFTQDGQ LISALESKVK
1010 1020 1030
HAQCFDVALM DDGSVVLASK DYRLYIYRYV QLAPVGM
Length:1,037
Mass (Da):110,366
Last modified:February 2, 2004 - v2
Checksum:i6B829CD924139DDF
GO

Sequence cautioni

The sequence AAM76183.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti591 – 5911H → Y in ABA86472 (PubMed:16120803).Curated
Sequence conflicti643 – 6431G → S in AAF13928 (PubMed:10949924).Curated
Sequence conflicti643 – 6431G → S in AAF13929 (PubMed:10949924).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119332 mRNA. Translation: AAF03086.1.
AF195870 Genomic DNA. Translation: AAF13926.1.
AF195871 Genomic DNA. Translation: AAF13927.1.
AF195872 Genomic DNA. Translation: AAF13928.1.
AF195873 Genomic DNA. Translation: AAF13929.1.
AB022432 mRNA. Translation: BAA82071.1.
AE014134 Genomic DNA. Translation: AAN11027.1.
AE014134 Genomic DNA. Translation: AAS64719.1.
AY122207 mRNA. Translation: AAM52719.1.
AY129441 mRNA. Translation: AAM76183.1. Different initiation.
DQ138866 Genomic DNA. Translation: ABA86472.1.
RefSeqiNP_001286083.1. NM_001299154.1.
NP_476945.1. NM_057597.4.
NP_599129.1. NM_134302.2.
NP_995726.1. NM_206004.2.
UniGeneiDm.6426.

Genome annotation databases

EnsemblMetazoaiFBtr0081158; FBpp0080702; FBgn0010300.
FBtr0081159; FBpp0080703; FBgn0010300.
FBtr0081160; FBpp0089239; FBgn0010300.
FBtr0344846; FBpp0311161; FBgn0010300.
GeneIDi35197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119332 mRNA. Translation: AAF03086.1.
AF195870 Genomic DNA. Translation: AAF13926.1.
AF195871 Genomic DNA. Translation: AAF13927.1.
AF195872 Genomic DNA. Translation: AAF13928.1.
AF195873 Genomic DNA. Translation: AAF13929.1.
AB022432 mRNA. Translation: BAA82071.1.
AE014134 Genomic DNA. Translation: AAN11027.1.
AE014134 Genomic DNA. Translation: AAS64719.1.
AY122207 mRNA. Translation: AAM52719.1.
AY129441 mRNA. Translation: AAM76183.1. Different initiation.
DQ138866 Genomic DNA. Translation: ABA86472.1.
RefSeqiNP_001286083.1. NM_001299154.1.
NP_476945.1. NM_057597.4.
NP_599129.1. NM_134302.2.
NP_995726.1. NM_206004.2.
UniGeneiDm.6426.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7FX-ray1.95A/B756-1037[»]
4ZLRX-ray2.30A/B756-1037[»]
5EX7X-ray2.60A758-1037[»]
ProteinModelPortaliQ8MQJ9.
SMRiQ8MQJ9. Positions 756-1037.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61181. 3 interactions.
DIPiDIP-37857N.
IntActiQ8MQJ9. 3 interactions.
MINTiMINT-1602052.
STRINGi7227.FBpp0293081.

Proteomic databases

PaxDbiQ8MQJ9.
PRIDEiQ8MQJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081158; FBpp0080702; FBgn0010300.
FBtr0081159; FBpp0080703; FBgn0010300.
FBtr0081160; FBpp0089239; FBgn0010300.
FBtr0344846; FBpp0311161; FBgn0010300.
GeneIDi35197.

Organism-specific databases

CTDi35197.
FlyBaseiFBgn0010300. brat.

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG410XQJ4. LUCA.
GeneTreeiENSGT00550000074377.
InParanoidiQ8MQJ9.
OrthoDBiEOG7NGQ9V.
PhylomeDBiQ8MQJ9.

Miscellaneous databases

ChiTaRSibrat. fly.
EvolutionaryTraceiQ8MQJ9.
GenomeRNAii35197.
NextBioi792330.
PROiQ8MQJ9.

Gene expression databases

BgeeiQ8MQJ9.
ExpressionAtlasiQ8MQJ9. differential.
GenevisibleiQ8MQJ9. DM.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
[Graphical view]
PfamiPF01436. NHL. 4 hits.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 2 hits.
[Graphical view]
PROSITEiPS51125. NHL. 5 hits.
PS50119. ZF_BBOX. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the beta-propeller domain of the Drosophila brain tumor (brat) protein induce neoplasm in the larval brain."
    Arama E., Dickman D., Kimchie Z., Shearn A., Lev Z.
    Oncogene 19:3706-3716(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, MUTANTS BRATTS1 AND BRATFS3.
  2. "Putative Drosophila transcription factor."
    Lukacsovich T.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo, Larva and Pupae.
  6. "Intragenic Hill-Robertson interference influences selection intensity on synonymous mutations in Drosophila."
    Comeron J.M., Guthrie T.B.
    Mol. Biol. Evol. 22:2519-2530(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-1031.
    Strain: Ral1.
  7. "Drosophila Brain tumor is a translational repressor."
    Sonoda J., Wharton R.P.
    Genes Dev. 15:762-773(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH BRAT AND NOS.
  8. "The Drosophila melanogaster gene brain tumor negatively regulates cell growth and ribosomal RNA synthesis."
    Frank D.J., Edgar B.A., Roth M.B.
    Development 129:399-407(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Model of the brain tumor-Pumilio translation repressor complex."
    Edwards T.A., Wilkinson B.D., Wharton R.P., Aggarwal A.K.
    Genes Dev. 17:2508-2513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 757-1037, MUTAGENESIS OF TYR-829; ARG-847; TYR-859; ARG-875; GLU-970 AND ASP-1012.

Entry informationi

Entry nameiBRAT_DROME
AccessioniPrimary (citable) accession number: Q8MQJ9
Secondary accession number(s): A4V0U9
, Q0E8P2, Q2XXZ6, Q8MR02, Q9U633, Q9U634, Q9U635, Q9U636, Q9Y1W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: May 11, 2016
This is version 124 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.