Unreviewed, UniProtKB/TrEMBL Q9VAK1 (Q9VAK1_DROME)

Names and origin

Protein names

Submitted name:
    Alphabet, isoform A EMBL AAF56905.1
Submitted name:
    Alphabet, isoform C EMBL AAN14177.1
    Alphabet, isoform D EMBL AAN14178.1

Gene names

Name:	alph FlyBase FBgn0086361
ORF Names:	CG1906 FlyBase FBgn0039672, Dmel_CG1906 EMBL AAF56905.1

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

General annotation (Comments)

Sequence similarities

Belongs to the PP2C family. RuleBase RU003465V0

Ontologies

Keywords
Ligand	Magnesium RuleBase RU003465V0 Metal-binding RuleBase RU003465V0
Molecular function	Hydrolase Protein phosphatase RuleBase RU003465V0
Gene Ontology (GO)
Biological process	imaginal disc-derived wing morphogenesis Inferred from mutant phenotype. Source: FlyBase mitotic cell cycle Inferred from mutant phenotype. Source: FlyBase negative regulation of MAP kinase activity Inferred from mutant phenotype. Source: FlyBase negative regulation of Ras protein signal transduction Inferred from mutant phenotype. Source: FlyBase positive regulation of R7 cell differentiation Inferred from genetic interaction. Source: FlyBase protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	protein serine/threonine phosphatase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9VAK1-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6ED4A4354159F274	FASTA	368	40,955
	10 20 30 40 50 60 MGGFLDKPKT AKHNDEGEGN KLLFGVSSMQ GWRSEMEDAY YARAGLGDAL PDWSFFAVFD 70 80 90 100 110 120 GHAGCKVSEH CAKHLLESII STEEFIGGDH VKGIRTGFLR IDEVMRELPE FTRESEKCGG 130 140 150 160 170 180 TTAVCAFVGL TQVYIANCGD SRAVLCRQGV PVFATQDHKP ILPEEKERIY NAGGSVMIKR 190 200 210 220 230 240 VNGTLAVSRA LGDYDFKNVK EKGQCEQLVS PEPEIFCQSR QDSDEFLVLA CDGIWDVMSN 250 260 270 280 290 300 EDVCSFIHSR MRVTSNLVSI ANQVVDTCLH KGSRDNMSII IIAFPGAPKP TEEAIEAEHR 310 320 330 340 350 360 LEKQIEKITR DEIESSKITD YVDLLKCLQN RDDIEGLPPG GGLQSKYHVI ERTFKQEFPD RPCESPTH

References

[1]	"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: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"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], MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF56905.1. AE014297 Genomic DNA. Translation: AAN14177.1. AE014297 Genomic DNA. Translation: AAN14178.1.
RefSeq	NP_733295.1. NP_733296.1. NP_733297.1.
UniGene	Dm.7085
3D structure databases
HSSP	HSSP built from PDB template 1A6Q based on UniProtKB P35813.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VAK1. 12 interactions.
Proteomic databases
PRIDE	Q9VAK1.
Genome annotation databases
Ensembl	FBgn0086361. Drosophila melanogaster. [Contig view]
GeneID	43481.
Organism-specific databases
FlyBase	FBgn0086361. alph.
Gene expression databases
ArrayExpress	Q9VAK1.
Family and domain databases
InterPro	IPR015655. PP2C. IPR001932. PP2C-related. IPR012911. PP2C_C. IPR000222. PP2C_Mn2_Asp60_BS. IPR014045. PP2C_N. [Graphical view]
Gene3D	G3DSA:3.60.40.10. PP2C-related. 1 hit. G3DSA:1.10.10.430. PP2C_C. 1 hit.
PANTHER	PTHR13832. PP2C. 1 hit.
Pfam	PF00481. PP2C. 1 hit. PF07830. PP2C_C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	834154.

Entry information

Entry name

Q9VAK1_DROME

Accession

Primary (citable) accession number: Q9VAK1

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)