ID ENSA_HUMAN Reviewed; 121 AA. AC O43768; A8K1Z9; E9PB69; Q5T5H2; Q68D48; Q6FHW0; Q6IAM4; Q6NUL2; Q6VUC6; AC Q6VUC7; Q6VUC8; Q6VUC9; Q6VUD0; Q6VUD1; Q9NRZ0; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=Alpha-endosulfine; DE AltName: Full=ARPP-19e; GN Name=ENSA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP PHOSPHORYLATION. RC TISSUE=Brain; RX PubMed=9653196; DOI=10.1073/pnas.95.14.8387; RA Heron L., Virsolvy A., Peyrollier K., Gribble F.M., Le Cam A., RA Ashcroft F.M., Bataille D.; RT "Human alpha-endosulfine, a possible regulator of sulfonylurea-sensitive RT K(ATP) channel: molecular cloning, expression and biological properties."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8387-8391(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10480622; DOI=10.2337/diabetes.48.9.1873; RA Heron L., Virsolvy A., Apiou F., Le Cam A., Bataille D.; RT "Isolation, characterization, and chromosomal localization of the human RT ENSA gene that encodes alpha-endosulfine, a regulator of beta-cell K(ATP) RT channels."; RL Diabetes 48:1873-1876(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; RP 5; 7 AND 8), AND TISSUE SPECIFICITY. RX PubMed=14728987; DOI=10.1016/j.ymgme.2003.09.013; RA Thameem F., Farook V.S., Yang X., Lee Y.-H., Permana P.A., Bogardus C., RA Prochazka M.; RT "The transcribed endosulfine alpha gene is located within a type 2 RT diabetes-linked region on 1q: sequence and expression analysis in Pima RT Indians."; RL Mol. Genet. Metab. 81:16-21(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhang Q., Fu G., Wu J., Zhou J., Ye M., Shen Y., Kan L., He K., Gu B., RA Chen S., Mao M., Chen Z.; RT "Human alpha endosulfine gene."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RA Scott V.E.S., Roch J.-M., Davis-Taber R.A., Molinari E.J., Whiteaker K.L., RA Gopalakrishnan M., Idler K., Sullivan J.P.; RT "Cloning and molecular characterization of two isoforms of human RT endosulfine."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6 AND 9). RC TISSUE=Placenta, and Pulmonary artery; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Liver; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=B-cell, Lung, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP INTERACTION WITH SNCA. RX PubMed=17893145; DOI=10.1074/jbc.m705283200; RA Woods W.S., Boettcher J.M., Zhou D.H., Kloepper K.D., Hartman K.L., RA Ladror D.T., Qi Z., Rienstra C.M., George J.M.; RT "Conformation-specific binding of alpha-synuclein to novel protein partners RT detected by phage display and NMR spectroscopy."; RL J. Biol. Chem. 282:34555-34567(2007). RN [14] RP INTERACTION WITH SNCA, PHOSPHORYLATION AT SER-109, AND MUTAGENESIS OF RP SER-109. RX PubMed=18973346; DOI=10.1021/bi801450t; RA Boettcher J.M., Hartman K.L., Ladror D.T., Qi Z., Woods W.S., George J.M., RA Rienstra C.M.; RT "Membrane-induced folding of the cAMP-regulated phosphoprotein endosulfine- RT alpha."; RL Biochemistry 47:12357-12364(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2 AND SER-109, CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2 AND SER-109, CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-21 AND SER-43, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Protein phosphatase inhibitor that specifically inhibits CC protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at CC Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) CC and inhibits its activity, leading to inactivation of PP2A, an CC essential condition to keep cyclin-B1-CDK1 activity high during M phase CC (By similarity). Also acts as a stimulator of insulin secretion by CC interacting with sulfonylurea receptor (ABCC8), thereby preventing CC sulfonylurea from binding to its receptor and reducing K(ATP) channel CC currents. {ECO:0000250, ECO:0000269|PubMed:9653196}. CC -!- SUBUNIT: Interacts (when phosphorylated at Ser-67) with PPP2R2D (By CC similarity). Interacts with ABCC8. Interacts with SNCA; interaction is CC disrupted when phosphorylated at Ser-109. {ECO:0000250, CC ECO:0000269|PubMed:17893145, ECO:0000269|PubMed:18973346}. CC -!- INTERACTION: CC O43768; Q96AP0: ACD; NbExp=2; IntAct=EBI-714511, EBI-717666; CC O43768-8; P22607: FGFR3; NbExp=3; IntAct=EBI-25853109, EBI-348399; CC O43768-8; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-25853109, EBI-741480; CC O43768-8; Q9Y649; NbExp=3; IntAct=EBI-25853109, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=Alpha; CC IsoId=O43768-1; Sequence=Displayed; CC Name=2; Synonyms=Beta; CC IsoId=O43768-2; Sequence=VSP_001443; CC Name=3; CC IsoId=O43768-3; Sequence=VSP_037065; CC Name=4; CC IsoId=O43768-4; Sequence=VSP_037066, VSP_001443; CC Name=5; CC IsoId=O43768-5; Sequence=VSP_037063, VSP_037064; CC Name=6; CC IsoId=O43768-6; Sequence=VSP_037063, VSP_037064, VSP_001443; CC Name=7; CC IsoId=O43768-7; Sequence=VSP_037063, VSP_037064, VSP_037065; CC Name=8; CC IsoId=O43768-8; Sequence=VSP_037067; CC Name=9; CC IsoId=O43768-9; Sequence=VSP_037065, VSP_001443; CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in skeletal CC muscle and brain and lower levels in the pancreas. CC {ECO:0000269|PubMed:14728987, ECO:0000269|PubMed:9653196}. CC -!- PTM: Phosphorylation at Ser-67 by GWL during mitosis is essential for CC interaction with PPP2R2D (PR55-delta) and subsequent inactivation of CC PP2A (By similarity). Phosphorylated by PKA. {ECO:0000250, CC ECO:0000269|PubMed:18973346, ECO:0000269|PubMed:9653196}. CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X99906; CAA68180.1; -; mRNA. DR EMBL; AJ010966; CAB65125.1; -; Genomic_DNA. DR EMBL; AY326403; AAQ73827.1; -; Genomic_DNA. DR EMBL; AY326400; AAQ73827.1; JOINED; Genomic_DNA. DR EMBL; AY326401; AAQ73827.1; JOINED; Genomic_DNA. DR EMBL; AY326402; AAQ73827.1; JOINED; Genomic_DNA. DR EMBL; AY326403; AAQ73828.1; -; Genomic_DNA. DR EMBL; AY326400; AAQ73828.1; JOINED; Genomic_DNA. DR EMBL; AY326401; AAQ73828.1; JOINED; Genomic_DNA. DR EMBL; AY326402; AAQ73828.1; JOINED; Genomic_DNA. DR EMBL; AY326402; AAQ73829.1; -; Genomic_DNA. DR EMBL; AY326400; AAQ73829.1; JOINED; Genomic_DNA. DR EMBL; AY326401; AAQ73829.1; JOINED; Genomic_DNA. DR EMBL; AY326401; AAQ73830.1; -; Genomic_DNA. DR EMBL; AY326400; AAQ73830.1; JOINED; Genomic_DNA. DR EMBL; AY326403; AAQ73831.1; -; Genomic_DNA. DR EMBL; AY326400; AAQ73831.1; JOINED; Genomic_DNA. DR EMBL; AY326401; AAQ73831.1; JOINED; Genomic_DNA. DR EMBL; AY326402; AAQ73831.1; JOINED; Genomic_DNA. DR EMBL; AY326403; AAQ73832.1; -; Genomic_DNA. DR EMBL; AY326400; AAQ73832.1; JOINED; Genomic_DNA. DR EMBL; AY326401; AAQ73832.1; JOINED; Genomic_DNA. DR EMBL; AY326402; AAQ73832.1; JOINED; Genomic_DNA. DR EMBL; AF067170; AAD32454.1; -; mRNA. DR EMBL; AF157509; AAF80340.1; -; mRNA. DR EMBL; AF157510; AAF80341.1; -; mRNA. DR EMBL; AK001981; BAG50998.1; -; mRNA. DR EMBL; AK290064; BAF82753.1; -; mRNA. DR EMBL; DA888224; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR749580; CAH18372.1; -; mRNA. DR EMBL; CR457130; CAG33411.1; -; mRNA. DR EMBL; CR536578; CAG38815.1; -; mRNA. DR EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53528.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53529.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53530.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53532.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53533.1; -; Genomic_DNA. DR EMBL; BC000436; AAH00436.1; -; mRNA. DR EMBL; BC004461; AAH04461.1; -; mRNA. DR EMBL; BC068544; AAH68544.1; -; mRNA. DR EMBL; BC069208; AAH69208.1; -; mRNA. DR CCDS; CCDS958.1; -. [O43768-1] DR CCDS; CCDS959.1; -. [O43768-3] DR CCDS; CCDS960.1; -. [O43768-7] DR CCDS; CCDS961.1; -. [O43768-5] DR CCDS; CCDS962.1; -. [O43768-9] DR CCDS; CCDS963.1; -. [O43768-2] DR CCDS; CCDS964.1; -. [O43768-6] DR CCDS; CCDS965.1; -. [O43768-8] DR RefSeq; NP_004427.1; NM_004436.2. [O43768-1] DR RefSeq; NP_996925.1; NM_207042.1. [O43768-3] DR RefSeq; NP_996926.1; NM_207043.1. [O43768-9] DR RefSeq; NP_996927.1; NM_207044.1. [O43768-2] DR RefSeq; NP_996928.1; NM_207045.1. [O43768-7] DR RefSeq; NP_996929.1; NM_207046.1. [O43768-5] DR RefSeq; NP_996930.1; NM_207047.1. [O43768-6] DR RefSeq; NP_997051.1; NM_207168.1. [O43768-8] DR AlphaFoldDB; O43768; -. DR BMRB; O43768; -. DR SMR; O43768; -. DR BioGRID; 108343; 69. DR IntAct; O43768; 36. DR MINT; O43768; -. DR STRING; 9606.ENSP00000341743; -. DR GlyGen; O43768; 3 sites, 2 O-linked glycans (3 sites). DR iPTMnet; O43768; -. DR MetOSite; O43768; -. DR PhosphoSitePlus; O43768; -. DR BioMuta; ENSA; -. DR EPD; O43768; -. DR jPOST; O43768; -. DR MassIVE; O43768; -. DR MaxQB; O43768; -. DR PeptideAtlas; O43768; -. DR ProteomicsDB; 19158; -. DR ProteomicsDB; 49158; -. [O43768-1] DR ProteomicsDB; 49159; -. [O43768-2] DR ProteomicsDB; 49160; -. [O43768-3] DR ProteomicsDB; 49161; -. [O43768-4] DR ProteomicsDB; 49162; -. [O43768-5] DR ProteomicsDB; 49163; -. [O43768-6] DR ProteomicsDB; 49164; -. [O43768-7] DR ProteomicsDB; 49165; -. [O43768-8] DR Pumba; O43768; -. DR TopDownProteomics; O43768-1; -. [O43768-1] DR TopDownProteomics; O43768-2; -. [O43768-2] DR TopDownProteomics; O43768-3; -. [O43768-3] DR TopDownProteomics; O43768-5; -. [O43768-5] DR Antibodypedia; 34035; 275 antibodies from 28 providers. DR DNASU; 2029; -. DR Ensembl; ENST00000271690.12; ENSP00000271690.7; ENSG00000143420.19. [O43768-2] DR Ensembl; ENST00000339643.9; ENSP00000341743.5; ENSG00000143420.19. [O43768-3] DR Ensembl; ENST00000361532.9; ENSP00000354835.5; ENSG00000143420.19. [O43768-5] DR Ensembl; ENST00000361631.9; ENSP00000355239.5; ENSG00000143420.19. [O43768-7] DR Ensembl; ENST00000362052.7; ENSP00000355220.7; ENSG00000143420.19. [O43768-8] DR Ensembl; ENST00000369014.10; ENSP00000358010.6; ENSG00000143420.19. [O43768-1] DR Ensembl; ENST00000503241.1; ENSP00000424242.1; ENSG00000143420.19. [O43768-9] DR Ensembl; ENST00000503345.1; ENSP00000421458.1; ENSG00000143420.19. [O43768-8] DR Ensembl; ENST00000509582.5; ENSP00000426110.1; ENSG00000143420.19. [O43768-8] DR Ensembl; ENST00000513281.5; ENSP00000422343.1; ENSG00000143420.19. [O43768-6] DR GeneID; 2029; -. DR KEGG; hsa:2029; -. DR MANE-Select; ENST00000369014.10; ENSP00000358010.6; NM_004436.4; NP_004427.1. DR UCSC; uc001evb.4; human. [O43768-1] DR AGR; HGNC:3360; -. DR CTD; 2029; -. DR DisGeNET; 2029; -. DR GeneCards; ENSA; -. DR HGNC; HGNC:3360; ENSA. DR HPA; ENSG00000143420; Low tissue specificity. DR MIM; 603061; gene. DR neXtProt; NX_O43768; -. DR OpenTargets; ENSG00000143420; -. DR PharmGKB; PA27796; -. DR VEuPathDB; HostDB:ENSG00000143420; -. DR GeneTree; ENSGT00940000155413; -. DR HOGENOM; CLU_125025_1_0_1; -. DR InParanoid; O43768; -. DR OrthoDB; 3495120at2759; -. DR PhylomeDB; O43768; -. DR TreeFam; TF314718; -. DR PathwayCommons; O43768; -. DR Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression. DR SignaLink; O43768; -. DR SIGNOR; O43768; -. DR BioGRID-ORCS; 2029; 86 hits in 1119 CRISPR screens. DR ChiTaRS; ENSA; human. DR GeneWiki; ENSA_(gene); -. DR GenomeRNAi; 2029; -. DR Pharos; O43768; Tbio. DR PRO; PR:O43768; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O43768; Protein. DR Bgee; ENSG00000143420; Expressed in cervix squamous epithelium and 206 other cell types or tissues. DR ExpressionAtlas; O43768; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0008200; F:ion channel inhibitor activity; TAS:ProtInc. DR GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB. DR GO; GO:0019870; F:potassium channel inhibitor activity; IDA:MGI. DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB. DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central. DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IBA:GO_Central. DR GO; GO:0050796; P:regulation of insulin secretion; IDA:MGI. DR GO; GO:0007584; P:response to nutrient; TAS:ProtInc. DR InterPro; IPR006760; Endosulphine. DR PANTHER; PTHR10358:SF21; ALPHA-ENDOSULFINE; 1. DR PANTHER; PTHR10358; ENDOSULFINE; 1. DR Pfam; PF04667; Endosulfine; 1. DR Genevisible; O43768; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm; KW Mitosis; Phosphoprotein; Protein phosphatase inhibitor; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT CHAIN 2..121 FT /note="Alpha-endosulfine" FT /id="PRO_0000146758" FT REGION 1..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 79..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..40 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 102..121 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 21 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 43 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 67 FT /note="Phosphoserine; by GWL" FT /evidence="ECO:0000250" FT MOD_RES 109 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:18973346, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT VAR_SEQ 1..4 FT /note="Missing (in isoform 5, isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037063" FT VAR_SEQ 5..19 FT /note="QEEENPAEETGEEKQ -> MAGGLGCDVCYWFVE (in isoform 5, FT isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037064" FT VAR_SEQ 61 FT /note="G -> GDYKSLHWSVLLCADEM (in isoform 3, isoform 7 and FT isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037065" FT VAR_SEQ 61 FT /note="G -> GVWGIASYPLSLGLKEVLRMKSVE (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_037066" FT VAR_SEQ 62..121 FT /note="QKYFDSGDYNMAKAKMKNKQLPSAGPDKNLVTGDHIPTPQDLPQRKSSLVTS FT KLAGGQVE -> VWGIVSYPLSLELKEVLRMKSVEVLLDPFLEVLLLNRSRGEFEI FT (in isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_037067" FT VAR_SEQ 118..121 FT /note="Missing (in isoform 2, isoform 4, isoform 6 and FT isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|Ref.5, ECO:0000303|Ref.8" FT /id="VSP_001443" FT MUTAGEN 109 FT /note="S->E: Mimicks a phosphorylated state and impairs FT interaction with SNCA." FT /evidence="ECO:0000269|PubMed:18973346" FT CONFLICT 5 FT /note="Q -> R (in Ref. 8; CAG38815)" FT /evidence="ECO:0000305" FT CONFLICT 21 FT /note="T -> M (in Ref. 6; BAF82753)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="Q -> L (in Ref. 11; AAH68544)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="K -> Q (in Ref. 8; CAG33411)" FT /evidence="ECO:0000305" SQ SEQUENCE 121 AA; 13389 MW; 7C76315AA17E7542 CRC64; MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E //