P60840 (ENSA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-endosulfine

Alternative name(s):
ARPP-19e

Gene names

Name:

Ensa

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents By similarity.
Subunit structure	Interacts (when phosphorylated at Ser-67) with PPP2R2D. Interacts with ABCC8. Interacts with SNCA; interaction is disrupted when phosphorylated at Ser-109 By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Present in striatum (at protein level). Ref.5
Post-translational modification	Phosphorylation at Ser-67 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A. Phosphorylated by PKA By similarity. Ref.5
Sequence similarities	Belongs to the endosulfine family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Protein phosphatase inhibitor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from sequence or structural similarity. Source: UniProtKB response to glucose stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatase inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB protein phosphatase 2A binding Inferred from sequence or structural similarity. Source: UniProtKB protein phosphatase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW protein phosphatase type 2A regulator activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P60840-1)

Also known as: Alpha;

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 2 (identifier: P60840-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     118-121: Missing.

Isoform 3 (identifier: P60840-3)

The sequence of this isoform differs from the canonical sequence as follows:
     62-72: QKYFDSGDYNM → VWDTLILWHLG
     73-121: Missing.

Note: May be due to an intron retention.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 121	120	Alpha-endosulfine		PRO_0000146759
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	67	1	Phosphoserine; by GWL Probable
	Modified residue	108	1	Phosphoserine; by PKA By similarity
	Modified residue	109	1	Phosphoserine Ref.5 Ref.7
Natural variations
	Alternative sequence	62 – 72	11	QKYFDSGDYNM → VWDTLILWHLG in isoform 3.		VSP_037068
	Alternative sequence	73 – 121	49	Missing in isoform 3.		VSP_037069
	Alternative sequence	118 – 121	4	Missing in isoform 2.		VSP_001444
Experimental info
	Sequence conflict	24	1	K → E in BAB27552. Ref.2
	Sequence conflict	24	1	K → E in BAB31584. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified April 13, 2004. Version 1. Checksum: A84632C9085FFC5A	FASTA	121	13,335
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 110 120 GQKYFDSGDY NMAKAKMKNK QLPSAGADKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E
	Isoform 2 (Beta) [UniParc] [UniParc]. Checksum: B85FFC5A907676C6	FASTA	117	12,922
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 110 GQKYFDSGDY NMAKAKMKNK QLPSAGADKN LVTGDHIPTP QDLPQRKSSL VTSKLAG
	Isoform 3 [UniParc] [UniParc]. Checksum: 6B020743FC2590B9	FASTA	72	8,183
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 GVWDTLILWH LG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human alpha-endosulfine, a possible regulator of sulfonylurea-sensitive K(ATP) channel: molecular cloning, expression and biological properties." Heron L., Virsolvy A., Peyrollier K., Gribble F.M., Le Cam A., Ashcroft F.M., Bataille D. Proc. Natl. Acad. Sci. U.S.A. 95:8387-8391(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Bone marrow, Embryo and Testis.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Strain: FVB/N. Tissue: Colon and Testis.
[5]	"ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins." Dulubova I., Horiuchi A., Snyder G.L., Girault J.-A., Czernik A.J., Shao L., Ramabhadran R., Greengard P., Nairn A.C. J. Neurochem. 77:229-238(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-109.
[6]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ005985 mRNA. Translation: CAA06799.1. AK006149 mRNA. Translation: BAB24433.1. AK011334 mRNA. Translation: BAB27552.1. AK149726 mRNA. Translation: BAE29049.1. AK161290 mRNA. Translation: BAE36298.1. AK019170 mRNA. Translation: BAB31584.1. CH466620 Genomic DNA. Translation: EDL38827.1. BC058802 mRNA. Translation: AAH58802.1. BC059724 mRNA. Translation: AAH59724.1.
IPI	IPI00230470. IPI00409045. IPI00461342.
RefSeq	NP_001021383.1. NM_001026212.1. NP_062507.1. NM_019561.2.
UniGene	Mm.241365.
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P60840.
Proteomic databases
PaxDb	P60840.
PRIDE	P60840.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000037983; ENSMUSP00000045937; ENSMUSG00000038619. ENSMUST00000058230; ENSMUSP00000051799; ENSMUSG00000038619.
GeneID	56205.
KEGG	mmu:56205.
UCSC	uc008qki.1. mouse. uc008qkj.1. mouse. uc008qkk.1. mouse.
Organism-specific databases
CTD	2029.
MGI	MGI:1891189. Ensa.
Phylogenomic databases
eggNOG	NOG312450.
GeneTree	ENSGT00390000010139.
HOGENOM	HOG000232115.
HOVERGEN	HBG000297.
InParanoid	Q5D069.
OMA	QEDENPA.
OrthoDB	EOG4KSPM7.
Gene expression databases
Bgee	P60840.
CleanEx	MM_ENSA.
Genevestigator	P60840.
GermOnline	ENSMUSG00000038619. Mus musculus.
Family and domain databases
InterPro	IPR006760. Endosulphine. [Graphical view]
Pfam	PF04667. Endosulfine. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ENSA. mouse.
NextBio	312033.
SOURCE	Search...

Entry information

Entry name

ENSA_MOUSE

Accession

Primary (citable) accession number: P60840
Secondary accession number(s): Q5D069 , Q6PBG4, Q9CQZ9, Q9Z0G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program