Q9VFG8 (KIBRA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kibra

Gene names

Name:	kibra
ORF Names:	CG33967

Organism

Drosophila melanogaster (Fruit fly)

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	1288 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Kibra acts synergistically along with Ex and Mer to regulate the Hippo signaling pathway. Ref.5 Ref.6 Ref.7
Subunit structure	Forms a complex with Mer and Ex. Interacts (via domain WW 1) with Ex (via RXPPXY motif). Interacts with Mer, Sav, Hpo and Wts. Ref.5 Ref.6 Ref.7
Subcellular location	Cytoplasm. Apical cell membrane. Note: Localizes at the apical cortex of epithelial cells and cytoplasmic, punctate. Ref.5 Ref.7
Tissue specificity	Expressed in ovarian posterior follicle cells and wing disks (at protein level). Ref.6
Disruption phenotype	Homozygous embryonic lethality, oogenesis defects, tissue overgrowth characterized by excessive cell proliferation and diminished apoptosis. Ref.5 Ref.6 Ref.7
Sequence similarities	Belongs to the WWC family. KIBRA subfamily. Contains 1 C2 domain. Contains 2 WW domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of hippo signaling cascade Inferred from mutant phenotype Ref.5Ref.6Ref.7. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from direct assay Ref.7. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1288	1288	Protein kibra		PRO_0000392971
Regions
	Domain	54 – 87	34	WW 1
	Domain	101 – 134	34	WW 2
	Domain	693 – 795	103	C2
	Coiled coil	201 – 229	29	Potential
	Coiled coil	335 – 463	129	Potential
	Coiled coil	1049 – 1076	28	Potential
	Compositional bias	5 – 49	45	Gln-rich
	Compositional bias	13 – 51	39	His-rich
	Compositional bias	190 – 196	7	Poly-Ser
	Compositional bias	533 – 536	4	Poly-Gln
	Compositional bias	832 – 841	10	Poly-Ala
	Compositional bias	899 – 904	6	Poly-Asp
	Compositional bias	905 – 908	4	Poly-Glu
	Compositional bias	1166 – 1176	11	Poly-Glu
	Compositional bias	1224 – 1271	48	Ala-rich
Amino acid modifications
	Modified residue	992	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	230	1	Y → C in AAX33444. Ref.3
	Sequence conflict	743	1	T → A in AAX33444. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9VFG8 [UniParc]. Last modified February 7, 2006. Version 2. Checksum: C450A07D640D6492	FASTA	1,288	144,350
	10 20 30 40 50 60 MPNLQQTASQ SQHHLHPHHL RPQQQQQQHH HHHQQQQQQQ HTHHQQQQQH HSDFPLPDGW 70 80 90 100 110 120 DIAKDFDGKT YYIDHINKKT TWLDPRDCYT KPQTFEDCVG DELPMGWEES YDPNIGPYYI 130 140 150 160 170 180 NHLAQSTQLE DPRQEWKTVQ EQMLSDYLSA AQDQLENKRE MFDVKQQRLL WAQEEYNHLK 190 200 210 220 230 240 LAASRSSLCS SSSSMSRHDP ELLRADLMLA RERVHQLKQE LTHITNDISY TERGMNTLYS 250 260 270 280 290 300 VGEKINAREN GCYDIAEVHA IREEMLKVHK SLVSGEKVRE ELMRSLVQIK NELGRQQISE 310 320 330 340 350 360 ENSDLASPFD RVCVASQTDL CGSSGENLNG GARFAEMAKT KWQYAEWRKH IKKLQQQLAD 370 380 390 400 410 420 HVERIEPGQL ESDKDRILLI QEKEKLLNDL NSISLKSRSE EEKRVIHQTR HKLEEDLKEA 430 440 450 460 470 480 YEANNTCVAN RLRFHEEKQL LLDKLQEALK STKLLEERLK SFSSESTFSI SSGSSLGSLS 490 500 510 520 530 540 TASSKSALSF TDIYIDPFAV DSPIDVVDLR RRSQRLFQQH QQQRLHPVHP VLQQQQSAEV 550 560 570 580 590 600 TLSPRSSLSM ETPPASPMKY NAGADQTPQA LKEEPTYANA LPAPPAYTAP PPVPISGVRA 610 620 630 640 650 660 RPYDLDSTVL DCMMLEAKLQ KLNMGTPLNL AVAPLSPISE KPSLLDLPQE MLSRSSSTSN 670 680 690 700 710 720 TRSVSAAVSN ESVAGDSGVF EASRAHLPRK ELAQVQIGLK YLKQEGVLVV SLERANNLLA 730 740 750 760 770 780 LWTASADNSQ VYLRAALLPN SLTSIRTKAL GDFQKPVFND TFAVPITLDK LLTKSLQVTV 790 800 810 820 830 840 VTMTGQKEEI IGTVQISMAE FNPEDSTLKW YNVLSSKFIP SFESLDIPST SAAAAAAAVA 850 860 870 880 890 900 ASNAPNPGNN REESSDESTI TSSQTSTLTR NQAPCMELQE QMAAELLGLG PLNEPECSDD 910 920 930 940 950 960 DDDDEEEELD DKQLVSDVGL MNSSSMLHAY LQNMKQEFAD KETNTDRAYL PEKSRGQSQL 970 980 990 1000 1010 1020 MDDRPVKRSQ TFTPSEAFSK NRYNCRLNRS DSDSAMHCGV APHTFQRGAA ERRSLRFHSK 1030 1040 1050 1060 1070 1080 APKSVTKLHH THIPRTSLDL ELDLQAQHSK LYFLNDQIAK LQNLKEVLQK ACENKDPLVA 1090 1100 1110 1120 1130 1140 AWAIENEEFQ RLVARADPAK CPEERQLQKL LMKTAKEIHK LRKTKVPKGC PDLVSFKEKI 1150 1160 1170 1180 1190 1200 TFFTRKGLSV PELPSEFTLP EANPIEEEEE EEDENEFYNS AETAIAINTA LVASSNRNKN 1210 1220 1230 1240 1250 1260 LSEHPHRATS GAVPKIPAPV VTPAATPAAT PAATPAATSA ATPAATPVVS PAAQPDAKPA 1270 1280 DAPIPVASND AEQQRFDYVV DRNYGVEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"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-992, MASS SPECTROMETRY. Tissue: Embryo.
[5]	"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: 20159598] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH HPO; SAV; MER AND EX.
[6]	"Kibra Is a regulator of the Salvador/Warts/Hippo signaling network." Genevet A., Wehr M.C., Brain R., Thompson B.J., Tapon N. Dev. Cell 18:300-308(2010) [PubMed: 20159599] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH MER; EX AND WTS.
[7]	"The WW domain protein Kibra acts upstream of Hippo in Drosophila." Baumgartner R., Poernbacher I., Buser N., Hafen E., Stocker H. Dev. Cell 18:309-316(2010) [PubMed: 20159600] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH MER.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF55090.2. BT021296 mRNA. Translation: AAX33444.1.
RefSeq	NP_001034055.1. NM_001038966.1.
UniGene	Dm.16870.
3D structure databases
ProteinModelPortal	Q9VFG8.
SMR	Q9VFG8. Positions 52-135, 692-815.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VFG8. 1 interaction.
MINT	MINT-283318.
STRING	Q9VFG8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0100008; FBpp0099467; FBgn0262127.
GeneID	41783.
KEGG	dme:Dmel_CG33967.
UCSC	CG33967-RA. d. melanogaster.
Organism-specific databases
CTD	41783.
FlyBase	FBgn0262127. kibra.
Phylogenomic databases
GeneTree	EMGT00050000010318.
InParanoid	Q9VFG8.
OMA	DSDSAMH.
OrthoDB	EOG408KPW.
PhylomeDB	Q9VFG8.
Gene expression databases
ArrayExpress	Q9VFG8.
Bgee	Q9VFG8.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR001202. WW_Rsp5_WWP. [Graphical view]
Gene3D	G3DSA:2.20.70.10. G3DSA:2.20.70.10. 2 hits.
Pfam	PF00397. WW. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. SM00456. WW. 2 hits. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51045. WW_Rsp5_WWP. 2 hits.
PROSITE	PS50004. C2. False negative. PS01159. WW_DOMAIN_1. 1 hit. PS50020. WW_DOMAIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	825550.

Entry information

Entry name

KIBRA_DROME

Accession

Primary (citable) accession number: Q9VFG8
Secondary accession number(s): Q5BIC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	February 7, 2006
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project