P12982 (PP12_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase alpha-2 isoform
EC=3.1.3.16

Gene names

Name:	Pp1-87B
ORF Names:	CG5650

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is essential for the regulation of mitotic chromosomal segregation as well as regulation of chromatin condensation during interphase. Ref.2 Ref.6
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from mutant phenotype PubMed 8382739. Source: FlyBase axon guidance Inferred from mutant phenotype PubMed 16280124. Source: FlyBase chromosome condensation Inferred from mutant phenotype Ref.2. Source: FlyBase mitotic metaphase plate congression Inferred from mutant phenotype PubMed 17306545. Source: FlyBase mitotic spindle elongation Inferred from mutant phenotype PubMed 17412918. Source: FlyBase olfactory learning Inferred from mutant phenotype PubMed 8382739. Source: FlyBase oogenesis Inferred from mutant phenotype PubMed 8224813. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype PubMed 16336044. Source: FlyBase protein dephosphorylation Inferred from mutant phenotype PubMed 8224813. Source: FlyBase spindle assembly Inferred from mutant phenotype PubMed 17306545. Source: FlyBase visual learning Inferred from mutant phenotype PubMed 8382739. Source: FlyBase
Cellular_component	polytene chromosome Inferred from direct assay PubMed 12524522. Source: FlyBase protein phosphatase type 1 complex Inferred from sequence or structural similarity Ref.1. Source: FlyBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin phosphatase activity Inferred from direct assay PubMed 15269282. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ppi20	Q0E9G3	3	EBI-152633,EBI-150380

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Serine/threonine-protein phosphatase alpha-2 isoform		PRO_0000058792
Sites
	Active site	123	1	Proton donor By similarity
	Metal binding	62	1	Iron By similarity
	Metal binding	64	1	Iron By similarity
	Metal binding	90	1	Iron By similarity
	Metal binding	90	1	Manganese By similarity
	Metal binding	122	1	Manganese By similarity
	Metal binding	171	1	Manganese By similarity
	Metal binding	246	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12982 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 68FE054996C9A062	FASTA	302	34,542
	10 20 30 40 50 60 MGDVMNIDSI ISRLLEVRGA RPGKNVQLSE GEIRGLCLKS REIFLSQPIL LELEAPLKIC 70 80 90 100 110 120 GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE TICLLLAYKI KYSENFFLLR 130 140 150 160 170 180 GNHECASINR IYGFYDECKR RYSIKLWKTF TDCFNCLPVA AIVDEKIFCC HGGLSPDLTS 190 200 210 220 230 240 MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TMGWGENDRG VSFTFGAEVV AKFLQKHEFD 250 260 270 280 290 300 LICRAHQVVE DGYEFFAKRM LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic subunit of protein phosphatase 1 alpha. High conservation between mammalian and insect sequences." Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W. Eur. J. Biochem. 183:603-610(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Head.
[2]	"Protein phosphorylation is involved in the regulation of chromatin condensation during interphase." Dombradi V., Cohen P.T.W. FEBS Lett. 312:21-26(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: Canton-S.
[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]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Protein phosphatase 1 activity in Drosophila mutants with abnormalities in mitosis and chromosome condensation." Dombradi V., Axton J.M., Barker H.M., Cohen P.T.W. FEBS Lett. 275:39-43(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15583 mRNA. Translation: CAA33609.1. S47852 Genomic DNA. Translation: AAB23957.1. AE014297 Genomic DNA. Translation: AAF54810.1. AY061063 mRNA. Translation: AAL28611.1.
PIR	PAFF1A. S12960.
RefSeq	NP_524937.1. NM_080198.3.
UniGene	Dm.1623.
3D structure databases
ProteinModelPortal	P12982.
SMR	P12982. Positions 5-297.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-18465N.
IntAct	P12982. 41 interactions.
MINT	MINT-741838.
Proteomic databases
PaxDb	P12982.
PRIDE	P12982.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082595; FBpp0082067; FBgn0004103.
GeneID	49260.
KEGG	dme:Dmel_CG5650.
Organism-specific databases
CTD	49260.
FlyBase	FBgn0004103. Pp1-87B.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
InParanoid	P12982.
KO	K06269.
OMA	APNYCNE.
OrthoDB	EOG4SF7NF.
PhylomeDB	P12982.
Gene expression databases
Bgee	P12982.
GermOnline	CG5650. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Pp1-87B. drosophila.
GenomeRNAi	49260.
NextBio	839723.

Entry information

Entry name

PP12_DROME

Accession

Primary (citable) accession number: P12982
Secondary accession number(s): Q4PIY5, Q9VG75

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project