ENSA_HUMAN
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 03-AUG-2022, entry version 169.
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}.
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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 BioGRID; 108343; 62.
DR IntAct; O43768; 35.
DR MINT; O43768; -.
DR GlyGen; O43768; 1 site, 1 O-linked glycan (1 site).
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 PRIDE; 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 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; 241 antibodies from 27 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 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; 1494565at2759; -.
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; 68 hits in 1043 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 204 other tissues.
DR ExpressionAtlas; O43768; baseline and differential.
DR Genevisible; O43768; HS.
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; PTHR10358; 1.
DR Pfam; PF04667; Endosulfine; 1.
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
