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Protein

Protein expanded

Gene

ex

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

Functioni

Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to regulate the Hippo signaling pathway. Involved in the control of cell proliferation in imaginal disks. May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains (PubMed:20159598). Required for apical localization of Schip1 (PubMed:26954546).2 Publications

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • cell cycle arrest Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • compound eye photoreceptor cell differentiation Source: FlyBase
  • decapentaplegic signaling pathway Source: FlyBase
  • endocytic recycling Source: FlyBase
  • hippo signaling Source: FlyBase
  • imaginal disc development Source: FlyBase
  • negative regulation of cell proliferation Source: FlyBase
  • negative regulation of hippo signaling Source: FlyBase
  • negative regulation of imaginal disc growth Source: FlyBase
  • negative regulation of organ growth Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of phosphorylation Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of cell differentiation Source: FlyBase
  • regulation of cell proliferation Source: FlyBase
  • regulation of exit from mitosis Source: FlyBase
  • regulation of growth Source: FlyBase
  • regulation of hippo signaling Source: UniProtKB
  • regulation of organ growth Source: FlyBase
  • regulation of signal transduction Source: FlyBase
  • signal transduction Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein expanded
Gene namesi
Name:ex
ORF Names:CG4114
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004583. ex.

Subcellular locationi

  • Apical cell membrane 1 Publication

  • Note: Apical surface of disk cells.

GO - Cellular componenti

  • apical plasma membrane Source: FlyBase
  • cytoskeleton Source: InterPro
  • Kibra-Ex-Mer complex Source: UniProtKB
  • zonula adherens Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Hyperplasia of the imaginal disk resulting in wing overgrowth (PubMed:8269855). This overgrowth is limited to specific regions along the 2 wing axes (PubMed:8269855). Defects also in eyes, head, thorax and limbs where duplication and bulging often occur (PubMed:8269855). RNAi-mediated knockdown reduces the amount of Schip1 in the apical region of the cell.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14271427Protein expandedPRO_0000219443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1181 – 11811Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ07436.

PTM databases

iPTMnetiQ07436.

Expressioni

Gene expression databases

BgeeiQ07436.
ExpressionAtlasiQ07436. differential.
GenevisibleiQ07436. DM.

Interactioni

Subunit structurei

Forms a complex with Kibra and Mer (PubMed:20159598). Interacts (via RXPPXY motif) with Kibra (via domain WW 1) (PubMed:20159598). Interacts with Mer and Hpo (via SARAH domain) (PubMed:20159598). Interacts with Schip1; the interaction results in recruitment of Schip1 to the apical cell membrane (PubMed:26954546).2 Publications

Protein-protein interaction databases

BioGridi59474. 9 interactions.
DIPiDIP-59337N.
STRINGi7227.FBpp0077719.

Structurei

3D structure databases

ProteinModelPortaliQ07436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 399374FERMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi842 – 8476RXPPXY motif
Motifi1008 – 102013SH3-bindingSequence analysisAdd
BLAST
Motifi1149 – 11579SH3-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi409 – 4124Poly-Glu
Compositional biasi782 – 7887Poly-Pro
Compositional biasi952 – 9554Poly-His
Compositional biasi1002 – 10054Poly-Pro
Compositional biasi1011 – 10177Poly-Pro
Compositional biasi1081 – 10844Poly-Pro
Compositional biasi1149 – 11546Poly-Pro
Compositional biasi1158 – 116811Poly-AlaAdd
BLAST
Compositional biasi1170 – 11745Poly-Ser
Compositional biasi1199 – 12057Poly-Pro
Compositional biasi1416 – 14227Poly-Gln

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG4371. Eukaryota.
ENOG410XSKD. LUCA.
GeneTreeiENSGT00840000129875.
InParanoidiQ07436.
KOiK16683.
OMAiSDCDYVT.
OrthoDBiEOG7GTT31.
PhylomeDBiQ07436.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR018980. FERM_PH-like_C.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07436-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAFCTVSAP LEVCASSAEQ LSPGSRFLAL RLLGQQQPKT LYFLVDAKSR
60 70 80 90 100
VREVYTQTCL HFATQGMLDT ELFGLAVLID GEYMFADPES KLSKYGPKSW
110 120 130 140 150
RSSHTHGLDA NGRPLLELHF RVQFYIESPF MLKDETSRHN YYLQLRHNIL
160 170 180 190 200
QRDLPREQAE QALVFLAGLA LQADLGDAPP GTSNSKDDSG EETSASPSNG
210 220 230 240 250
GRGLSATTTL PKISKRANER MLRLSTYVAS TSKRETIPLP PSLPPNGADY
260 270 280 290 300
YRIEDYLPSG LHTPWARSAM RACHREHLGM ATAEAELLYI QQACSLHETI
310 320 330 340 350
NAHTYRMRLA KSEQGSGSAW FVVYAKGIKI LGGESTNSSS NPETTTFLWP
360 370 380 390 400
NITKLSFERK KFEIRSGESR ITLYAASDEK NKLLLTLCKD THQWSMKLAA
410 420 430 440 450
RLKEVSKREE EEAAESQRLH ASYACSRSLL LPYKSKNEQR ISVISSTSSN
460 470 480 490 500
TTSGIVSDRV HSEDELEIMI NTPPAPLAAP STESLALAHL LDRPSVSRQT
510 520 530 540 550
SSVGQMSLKD LEEQLAALSV RPQDASSNGA TIVTNSSVQR NSMGTTANDS
560 570 580 590 600
STATDSPSSQ HNIGSQCSST CSTVVVTSPV NGAGASSSGA PIPVHSTSSS
610 620 630 640 650
LELGFSHTAQ NSALSETSPD DFLSTSAREE TESVSGASGV YTLAHGAPPT
660 670 680 690 700
ETSGVYTMHS SELTGQSSEI AESEKSSHYG MFQPQKLEET HVQHSDSVDG
710 720 730 740 750
KKKEDFRPRS DSNVSTGSSF RGDGSDPTDN KHSLLSAEEL TNLIVGRGTY
760 770 780 790 800
PSRKTVSSSL HSDCDYVTLP LGDQGEEEVD QPPAPPPPYS ARHEKTGLCG
810 820 830 840 850
PPIAKPIPKP IAVVAPKPDS PPCSPPVPPA PIPAPPPAIR RRDPPPYSIS
860 870 880 890 900
SKPRPTSLIS VSSSAHPAPS AAGSMSSLKS EEVTARFITT RPQISILKAH
910 920 930 940 950
TSLIPDGAKP SYAAPHHCSS VASSNGSVCS HQLSQQSLHN SNYAGGSQAS
960 970 980 990 1000
LHHHHVPSHH RHSGSAAIGI VPYGLHKSTA SLHHQQSCVL LPVIKPRQFL
1010 1020 1030 1040 1050
APPPPSLPRQ PPPPPPPNHP HLASHLYERE MARKQLELYQ QQLYSDVDYV
1060 1070 1080 1090 1100
IYPIQDPAVS QQEYLDAKQG SLLAAMAQAA PPPPHHPYLA MQVSPAIYRS
1110 1120 1130 1140 1150
TPYLPLTLST HSRYASTQNL SDTYVQLPGP GYSPLYSPSM ASLCSSYEPP
1160 1170 1180 1190 1200
PPPPLHPAAL AAAAAAGAGS SSSSMFARSR SDDNILNSLD LLPKGKRLPP
1210 1220 1230 1240 1250
PPPPPYVNRR LKKPPMPAPS EKPPPIPSKP IPSRMSPIPP RKPPTLNPHH
1260 1270 1280 1290 1300
ANSPLTKTSS GAQWAGERPR PDLGLGLGLN RGNNSILAQL QASMVAQSHA
1310 1320 1330 1340 1350
QAQAQALDIA LLREKSKHLD LPLISALCND RSLLKQTKVV INPKTGQEMP
1360 1370 1380 1390 1400
TSSAQPSGAT TNGVANSSAG AGTLSKARKG STVSHRHPQD KLPPLPVQQL
1410 1420
AEANNYVIDP AVMMKQQQQQ QQHNKTS
Length:1,427
Mass (Da):153,644
Last modified:June 21, 2005 - v3
Checksum:i3CC1AD0B4D900EB2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1612EQ → DE in AAB39774 (PubMed:8269855).Curated
Sequence conflicti194 – 1941S → L in AAB39774 (PubMed:8269855).Curated
Sequence conflicti347 – 3471F → S in AAB39774 (PubMed:8269855).Curated
Sequence conflicti563 – 5631I → T in AAB39774 (PubMed:8269855).Curated
Sequence conflicti671 – 6711A → D in AAB39774 (PubMed:8269855).Curated
Sequence conflicti693 – 6931Q → S in AAB39774 (PubMed:8269855).Curated
Sequence conflicti1293 – 12942SM → FN in AAB39774 (PubMed:8269855).Curated
Sequence conflicti1422 – 14221Q → QQQ in AAB39774 (PubMed:8269855).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14768 mRNA. Translation: AAB39774.1.
AE014134 Genomic DNA. Translation: AAF51495.1.
AY069068 mRNA. Translation: AAL39213.1.
PIRiT13720.
RefSeqiNP_001259823.1. NM_001272894.1.
NP_476840.2. NM_057492.4.
UniGeneiDm.247.

Genome annotation databases

EnsemblMetazoaiFBtr0078059; FBpp0077719; FBgn0004583.
FBtr0329832; FBpp0302878; FBgn0004583.
GeneIDi33218.
KEGGidme:Dmel_CG4114.
UCSCiCG4114-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14768 mRNA. Translation: AAB39774.1.
AE014134 Genomic DNA. Translation: AAF51495.1.
AY069068 mRNA. Translation: AAL39213.1.
PIRiT13720.
RefSeqiNP_001259823.1. NM_001272894.1.
NP_476840.2. NM_057492.4.
UniGeneiDm.247.

3D structure databases

ProteinModelPortaliQ07436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59474. 9 interactions.
DIPiDIP-59337N.
STRINGi7227.FBpp0077719.

PTM databases

iPTMnetiQ07436.

Proteomic databases

PaxDbiQ07436.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078059; FBpp0077719; FBgn0004583.
FBtr0329832; FBpp0302878; FBgn0004583.
GeneIDi33218.
KEGGidme:Dmel_CG4114.
UCSCiCG4114-RA. d. melanogaster.

Organism-specific databases

CTDi110023.
FlyBaseiFBgn0004583. ex.

Phylogenomic databases

eggNOGiKOG4371. Eukaryota.
ENOG410XSKD. LUCA.
GeneTreeiENSGT00840000129875.
InParanoidiQ07436.
KOiK16683.
OMAiSDCDYVT.
OrthoDBiEOG7GTT31.
PhylomeDBiQ07436.

Miscellaneous databases

ChiTaRSiex. fly.
GenomeRNAii33218.
PROiQ07436.

Gene expression databases

BgeeiQ07436.
ExpressionAtlasiQ07436. differential.
GenevisibleiQ07436. DM.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR018980. FERM_PH-like_C.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expanded: a gene involved in the control of cell proliferation in imaginal discs."
    Boedigheimer M., Laughon A.
    Development 118:1291-1301(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
    Tissue: Imaginal disk.
  2. Boedigheimer M.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  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: Head.
  6. "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-1181, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. "Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded."
    Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.
    Dev. Cell 18:288-299(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIBRA; MER AND HPO.
  8. "Drosophila Schip1 links Expanded and Tao-1 to regulate hippo signaling."
    Chung H.L., Augustine G.J., Choi K.W.
    Dev. Cell 36:511-524(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SCHIP1, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiEXPA_DROME
AccessioniPrimary (citable) accession number: Q07436
Secondary accession number(s): Q9VPQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2005
Last modified: July 6, 2016
This is version 123 of the entry and version 3 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

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.