Reviewed, UniProtKB/Swiss-Prot Q8INB9 (AKT1_DROME)

Names and origin

Protein names

Recommended name:
    RAC serine/threonine-protein kinase
      Short name=DRAC-PK
      Short name=Dakt1
      Short name=DAkt
    EC=2.7.11.1
Alternative name(s):
    Akt
    Protein kinase B
      Short name=PKB

Gene names

Name:	Akt1
ORF Names:	CG4006

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

General annotation (Comments)

Function	Serine/threonine kinase involved in various developmental processes. During early embryogenesis, acts as a survival protein. During mid-embryogenesis, phosphorylates and activates trh, a transcription factor required for tracheal cell fate determination. Also regulates tracheal cell migration. Later in development, acts downstream of PI3K and Pk61C/PDK1 in the insulin receptor transduction pathway which regulates cell growth and organ size, by phosphorylating and antagonizing FOXO transcription factor. Controls follicle cell size during oogenesis. May also stimulate cell growth by phosphorylating Gig/Tsc2 and inactivating the Tsc complex. Dephosphorylation of 'Ser-586' by Phlpp triggers apoptosis and suppression of tumor growth. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.2
Subcellular location	Cytoplasm › cytosol. Cell membrane. Note: Recruited to plasma membrane upon activation.
Tissue specificity	Ubiquitously expressed. Present in ovary, where it is concentrated at the basal side of follicle cells. Ref.2
Developmental stage	Expressed both maternally and zygotically. Strongly expressed in embryo and pupa. Weakly expressed in larva. Mildly expressed in adult. Ref.17 Ref.2
Domain	Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI3K) results in its targeting to the plasma membrane Probable.
Post-translational modification	Phosphorylated and activated by Pk61C/PDK1. Phosphorylated on Ser-586 by the rictor-Tor complex. Ref.8 Ref.10 Ref.18 Ref.19 Ref.20
Disruption phenotype	Death at the first instar larval stage. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 PH domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis Growth regulation
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative initiation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.6 Inferred from mutant phenotype. Source: FlyBase apoptosis Inferred from electronic annotation. Source: UniProtKB-KW chitin-based embryonic cuticle biosynthetic process Ref.9 Inferred from genetic interaction. Source: FlyBase epithelial cell migration, open tracheal system Ref.14 Inferred from mutant phenotype. Source: UniProtKB insulin receptor signaling pathway Ref.7 Ref.8 Inferred from direct assay. Source: UniProtKB intracellular signaling cascade Ref.8 Inferred from genetic interaction. Source: UniProtKB lipid storage Inferred from genetic interaction. Source: FlyBase positive regulation of cell growth Ref.7 Ref.8 Ref.12 Ref.17 Inferred from mutant phenotype. Source: UniProtKB positive regulation of multicellular organism growth Traceable author statement. Source: FlyBase positive regulation of organ growth Ref.7 Inferred from mutant phenotype. Source: UniProtKB protein amino acid phosphorylation Ref.12 Inferred from direct assay. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype. Source: FlyBase regulation of protein import into nucleus Traceable author statement. Source: FlyBase
Cellular component	cell surface Inferred from direct assay. Source: FlyBase cytosol Ref.12 Ref.13 Ref.15 Inferred from Experiment. Source: Reactome plasma membrane Ref.13 Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide binding Non-traceable author statement. Source: FlyBase protein binding Ref.18 Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Ref.6 Ref.12 Ref.15 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VPE1	1	EBI-162210,EBI-147129
	Q9VR24	1	EBI-162210,EBI-98854
Nle	Q9VPR4	1	EBI-162210,EBI-176424
PHDP	O76136	2	EBI-162210,EBI-466449

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform C (identifier: Q8INB9-1)

Also known as: PK85;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform A (identifier: Q8INB9-2)

Also known as: PK66;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: Major form.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 611	611	RAC serine/threonine-protein kinase		PRO_0000045784
Regions
	Domain	106 – 211	106	PH
	Domain	266 – 523	258	Protein kinase
	Domain	524 – 597	74	AGC-kinase C-terminal
	Nucleotide binding	272 – 280	9	ATP By similarity
Sites
	Active site	389	1	Proton acceptor By similarity
	Binding site	295	1	ATP Probable
Amino acid modifications
	Modified residue	30	1	Phosphoserine Ref.20
	Modified residue	586	1	Phosphoserine Ref.8 Ref.18 Ref.19
Natural variations
	Alternative sequence	1 – 81	81	Missing in isoform A.		VSP_018833
Experimental info
	Mutagenesis	180	1	G → S: Fails to be recruited at the membrane upon activation. Ref.13
	Mutagenesis	260	1	K → A: Abolishes enzymatic activity.
	Mutagenesis	295	1	K → M: Abolishes enzymatic activity. Ref.7
	Mutagenesis	408	1	F → I: Abolishes enzymatic activity. Ref.6 Ref.13
	Sequence conflict	73	1	A → T in CAA58499. Ref.2
	Sequence conflict	200 – 201	2	QQ → HE in CAA81204. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform C (PK85) [UniParc]. Last modified December 7, 2004. Version 3. Checksum: C139380152580934	FASTA	611	68,485
	10 20 30 40 50 60 MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN SSPTSGSAEK 70 80 90 100 110 120 FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA LTEQTQVVKE GWLMKRGEHI 130 140 150 160 170 180 KNWRQRYFVL HSDGRLMGYR SKPADSASTP SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG 190 200 210 220 230 240 LQWTTVIERT FAVESELERQ QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED 250 260 270 280 290 300 ELSEQFSVQG TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE 310 320 330 340 350 360 VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE LFWHLSHERI 370 380 390 400 410 420 FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD GHIKVADFGL CKEDITYGRT 430 440 450 460 470 480 TKTFCGTPEY LAPEVLDDND YGQAVDWWGT GVVMYEMICG RLPFYNRDHD VLFTLILVEE 490 500 510 520 530 540 VKFPRNITDE AKNLLAGLLA KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF 550 560 570 580 590 600 KPQVTSDTDT RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH 610 ISTSTSLASM Q
	Isoform A (PK66). Checksum: F7508582C7F4A288	FASTA	530	59,911
	10 20 30 40 50 60 MSINTTFDLS SPSVTSGHAL TEQTQVVKEG WLMKRGEHIK NWRQRYFVLH SDGRLMGYRS 70 80 90 100 110 120 KPADSASTPS DFLLNNFTVR GCQIMTVDRP KPFTFIIRGL QWTTVIERTF AVESELERQQ 130 140 150 160 170 180 WTEAIRNVSS RLIDVGEVAM TPSEQTDMTD VDMATIAEDE LSEQFSVQGT TCNSSGVKKV 190 200 210 220 230 240 TLENFEFLKV LGKGTFGKVI LCREKATAKL YAIKILKKEV IIQKDEVAHT LTESRVLKST 250 260 270 280 290 300 NHPFLISLKY SFQTNDRLCF VMQYVNGGEL FWHLSHERIF TEDRTRFYGA EIISALGYLH 310 320 330 340 350 360 SQGIIYRDLK LENLLLDKDG HIKVADFGLC KEDITYGRTT KTFCGTPEYL APEVLDDNDY 370 380 390 400 410 420 GQAVDWWGTG VVMYEMICGR LPFYNRDHDV LFTLILVEEV KFPRNITDEA KNLLAGLLAK 430 440 450 460 470 480 DPKKRLGGGK DDVKEIQAHP FFASINWTDL VLKKIPPPFK PQVTSDTDTR YFDKEFTGES 490 500 510 520 530 VELTPPDPTG PLGSIAEEPL FPQFSYQGDM ASTLGTSSHI STSTSLASMQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The SH2-like Akt homology (AH) domain of c-akt is present in multiple copies in the genome of vertebrate and invertebrate eucaryotes. Cloning and characterisation of the Drosophila melanogaster c-akt homolog Dakt1." Franke T.F., Tartof K.D., Tsichlis P.N. Oncogene 9:141-148(1994) [PubMed: 8302573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]	"Developmental regulation of expression and activity of multiple forms of the Drosophila RAC protein kinase." Andjelkovic M., Jones P.F., Grossniklaus U., Cron P., Schier A.F., Dick M., Bilbe G., Hemmings B.A. J. Biol. Chem. 270:4066-4075(1995) [PubMed: 7876156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION (ISOFORMS A AND C), ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"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, ALTERNATIVE INITIATION.
[5]	"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] (ISOFORM A). Strain: Berkeley. Tissue: Embryo.
[6]	"Genetic analysis of protein kinase B (AKT) in Drosophila." Staveley B.E., Ruel L., Jin J., Stambolic V., Mastronardi F.G., Heitzler P., Woodgett J.R., Manoukian A.S. Curr. Biol. 8:599-602(1998) [PubMed: 9601646] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-408, DISRUPTION PHENOTYPE.
[7]	"Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB." Verdu J., Buratovich M.A., Wilder E.L., Birnbaum M.J. Nat. Cell Biol. 1:500-506(1999) [PubMed: 10587646] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-295.
[8]	"The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila." Scanga S.E., Ruel L., Binari R.C., Snow B., Stambolic V., Bouchard D., Peters M., Calvieri B., Mak T.W., Woodgett J.R., Manoukian A.S. Oncogene 19:3971-3977(2000) [PubMed: 10962553] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-586.
[9]	"Regulation of Drosophila tracheal system development by protein kinase B." Jin J., Anthopoulos N., Wetsch B., Binari R.C., Isaac D.D., Andrew D.J., Woodgett J.R., Manoukian A.S. Dev. Cell 1:817-827(2001) [PubMed: 11740943] [Abstract] Cited for: FUNCTION.
[10]	"Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and growth via the phosphoinositide 3-kinase-dependent signaling pathway." Cho K.S., Lee J.H., Kim S., Kim D., Koh H., Lee J., Kim C., Kim J., Chung J. Proc. Natl. Acad. Sci. U.S.A. 98:6144-6149(2001) [PubMed: 11344272] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"PDK1 regulates growth through Akt and S6K in Drosophila." Rintelen F., Stocker H., Thomas G., Hafen E. Proc. Natl. Acad. Sci. U.S.A. 98:15020-15025(2001) [PubMed: 11752451] [Abstract] Cited for: FUNCTION.
[12]	"Akt regulates growth by directly phosphorylating Tsc2." Potter C.J., Pedraza L.G., Xu T. Nat. Cell Biol. 4:658-665(2002) [PubMed: 12172554] [Abstract] Cited for: FUNCTION.
[13]	"Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB." Stocker H., Andjelkovic M., Oldham S., Laffargue M., Wymann M.P., Hemmings B.A., Hafen E. Science 295:2088-2091(2002) [PubMed: 11872800] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-180 AND PHE-408.
[14]	"Coordinated functions of Akt/PKB and ETS1 in tubule formation." Lavenburg K.R., Ivey J., Hsu T., Muise-Helmericks R.C. FASEB J. 17:2278-2280(2003) [PubMed: 14525946] [Abstract] Cited for: FUNCTION.
[15]	"Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway." Puig O., Marr M.T., Ruhf M.L., Tjian R. Genes Dev. 17:2006-2020(2003) [PubMed: 12893776] [Abstract] Cited for: FUNCTION.
[16]	"Tsc2 is not a critical target of Akt during normal Drosophila development." Dong J., Pan D. Genes Dev. 18:2479-2484(2004) [PubMed: 15466161] [Abstract] Cited for: FUNCTION.
[17]	"dAkt kinase controls follicle cell size during Drosophila oogenesis." Cavaliere V., Donati A., Hsouna A., Hsu T., Gargiulo G. Dev. Dyn. 232:845-854(2005) [PubMed: 15712201] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[18]	"PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth." Gao T., Furnari F., Newton A.C. Mol. Cell 18:13-24(2005) [PubMed: 15808505] [Abstract] Cited for: DEPHOSPHORYLATION AT SER-586.
[19]	"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex." Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Science 307:1098-1101(2005) [PubMed: 15718470] [Abstract] Cited for: PHOSPHORYLATION AT SER-586.
[20]	"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-30, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z26242 mRNA. Translation: CAA81204.1. X83510 Genomic DNA. Translation: CAA58499.2. X83510 Genomic DNA. Translation: CAA58500.1. AE014297 Genomic DNA. Translation: AAF55275.1. AE014297 Genomic DNA. Translation: AAN13699.3. AY069856 mRNA. Translation: AAL40001.1.
PIR	A55888.
RefSeq	NP_732113.3. NP_732114.1.
UniGene	Dm.1219
3D structure databases
HSSP	HSSP built from PDB template 1A06 based on UniProtKB Q63450.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8INB9. 42 interactions.
Proteomic databases
PRIDE	Q8INB9.
Genome annotation databases
Ensembl	FBgn0010379. Drosophila melanogaster. [Contig view]
GeneID	41957.
KEGG	dme:Dmel_CG4006.
Organism-specific databases
FlyBase	FBgn0010379. Akt1.
Phylogenomic databases
OMA	Q8INB9. SHERIFT.
Enzyme and pathway databases
BRENDA	2.7.11.1. 48.
Reactome	REACT_6313. Insulin receptor mediated signaling.
Gene expression databases
ArrayExpress	Q8INB9.
GermOnline	CG4006. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011993. PH_type. IPR017892. Pkinase_C. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. IPR015744. Serine/threonine_Kinase_Rac. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR22985:SF69. Akt. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	826461.

Entry information

Entry name

AKT1_DROME

Accession

Primary (citable) accession number: Q8INB9
Secondary accession number(s): Q0KI65 , Q24293, Q24469, Q24470, Q7JN11, Q8T9A5, Q9VEY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	December 7, 2004
Last modified:	June 16, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project