ID MAGD2_HUMAN Reviewed; 606 AA. AC Q9UNF1; A6NMX0; O76058; Q5BJF3; Q8NAL6; Q9H218; Q9P0U9; Q9UM52; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Melanoma-associated antigen D2; DE AltName: Full=11B6; DE AltName: Full=Breast cancer-associated gene 1 protein; DE Short=BCG-1; DE AltName: Full=Hepatocellular carcinoma-associated protein JCL-1; DE AltName: Full=MAGE-D2 antigen; GN Name=MAGED2; Synonyms=BCG1; 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), AND VARIANT ARG-266. RC TISSUE=Fetal lung, Mammary cancer, and Mammary gland; RX PubMed=10752678; DOI=10.1023/a:1006315919985; RA Kurt R.A., Urba W.J., Schoof D.D.; RT "Isolation of genes overexpressed in freshly isolated breast cancer RT specimens."; RL Breast Cancer Res. Treat. 59:41-48(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11856887; DOI=10.1159/000048822; RA Langnaese K., Kloos D.U., Wehnert M., Seidel B., Wieacker P.; RT "Expression pattern and further characterization of human MAGED2 and RT identification of rodent orthologues."; RL Cytogenet. Cell Genet. 94:233-240(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Jin C.L., Wang D.Y., Wan D.F., Gu J.R.; RT "Hepatocellular carcinoma associated gene JCL-1."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RA Dong X.-Y., Chen W.-F.; RT "Identification of genes which are differentially expressed in RT hepatocellular carcinoma by SSH method."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Skeletal muscle; 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 [9] RP PROTEIN SEQUENCE OF 2-13; 77-100; 182-203; 220-227; 262-274; 312-323; RP 386-397 AND 431-446, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE OF 346-424. RC TISSUE=Prostatic carcinoma; RA Stubbs A.P., Abel P.D., Lalani E.-N., Stamp G.W.H.; RT "Isolation of genes which are differentially expressed in prostate cancer RT cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE OF 369-503. RC TISSUE=Testis; RX PubMed=10463614; RA Lucas S., Brasseur F., Boon T.; RT "A new MAGE gene with ubiquitous expression does not code for known MAGE RT antigens recognized by T cells."; RL Cancer Res. 59:4100-4103(1999). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY RP MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-191 AND SER-194, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-190; SER-191; RP SER-194; SER-197; SER-247 AND SER-265, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-5; THR-72; SER-191; SER-244; SER-247 AND SER-265, CLEAVAGE RP OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 [21] 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 [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-247, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-264 AND SER-265, 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 [26] RP FUNCTION, INTERACTION WITH GNAS AND DNAJB1, TISSUE SPECIFICITY, INVOLVEMENT RP IN BARTS5, VARIANTS BARTS5 CYS-446 AND 488-GLU--ALA-491 DEL, AND RP CHARACTERIZATION OF VARIANT BARTS5 CYS-446. RX PubMed=27120771; DOI=10.1056/nejmoa1507629; RA Laghmani K., Beck B.B., Yang S.S., Seaayfan E., Wenzel A., Reusch B., RA Vitzthum H., Priem D., Demaretz S., Bergmann K., Duin L.K., Goebel H., RA Mache C., Thiele H., Bartram M.P., Dombret C., Altmueller J., Nuernberg P., RA Benzing T., Levtchenko E., Seyberth H.W., Klaus G., Yigit G., Lin S.H., RA Timmer A., de Koning T.J., Scherjon S.A., Schlingmann K.P., Bertrand M.J., RA Rinschen M.M., de Backer O., Konrad M., Koemhoff M.; RT "Polyhydramnios, transient antenatal Bartter's syndrome, and MAGED2 RT mutations."; RL N. Engl. J. Med. 374:1853-1863(2016). RN [27] RP VARIANT [LARGE SCALE ANALYSIS] GLN-458. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Regulates the expression, localization to the plasma membrane CC and function of the sodium chloride cotransporters SLC12A1 and SLC12A3, CC two key components of salt reabsorption in the distal renal tubule. CC {ECO:0000269|PubMed:27120771}. CC -!- SUBUNIT: Interacts with GNAS. May interact with DNAJB1. CC {ECO:0000269|PubMed:27120771}. CC -!- INTERACTION: CC Q9UNF1; P52333: JAK3; NbExp=4; IntAct=EBI-725832, EBI-518246; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UNF1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UNF1-2; Sequence=VSP_008030; CC -!- TISSUE SPECIFICITY: Widely expressed. In the developing and adult CC kidney, expressed in the thick ascending limb of the loop of Henle and CC the distal convoluted tubules outside the loop. CC {ECO:0000269|PubMed:11856887, ECO:0000269|PubMed:27120771}. CC -!- DISEASE: Bartter syndrome 5, antenatal, transient (BARTS5) CC [MIM:300971]: An X-linked recessive form of Bartter syndrome, a CC disorder characterized by impaired salt reabsorption in the thick CC ascending loop of Henle with pronounced salt wasting, hypokalemic CC metabolic alkalosis, and varying degrees of hypercalciuria. BARTS5 is CC an antenatal form beginning in utero with marked fetal polyuria that CC leads to polyhydramnios and premature delivery. It is characterized by CC severe but transient symptoms that can resolve with age. CC {ECO:0000269|PubMed:27120771}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AF128527; AAD33392.1; -; mRNA. DR EMBL; AF128528; AAD33393.1; -; mRNA. DR EMBL; AF126181; AAD28598.1; -; mRNA. DR EMBL; AJ293618; CAC19410.1; -; mRNA. DR EMBL; U92544; AAD00728.1; -; mRNA. DR EMBL; AF320070; AAG35066.2; -; mRNA. DR EMBL; AK092463; BAC03896.1; -; mRNA. DR EMBL; Z98046; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471154; EAW93189.1; -; Genomic_DNA. DR EMBL; BC000304; AAH00304.1; -; mRNA. DR EMBL; BC091503; AAH91503.1; -; mRNA. DR EMBL; AF148815; AAF73137.1; -; mRNA. DR EMBL; AF320907; AAG38603.1; -; mRNA. DR CCDS; CCDS14362.1; -. [Q9UNF1-1] DR RefSeq; NP_055414.2; NM_014599.5. [Q9UNF1-1] DR RefSeq; NP_803182.1; NM_177433.2. [Q9UNF1-1] DR RefSeq; NP_957516.1; NM_201222.2. [Q9UNF1-1] DR AlphaFoldDB; Q9UNF1; -. DR SMR; Q9UNF1; -. DR BioGRID; 116121; 234. DR DIP; DIP-50722N; -. DR IntAct; Q9UNF1; 70. DR MINT; Q9UNF1; -. DR STRING; 9606.ENSP00000364193; -. DR GlyGen; Q9UNF1; 9 sites, 2 O-linked glycans (9 sites). DR iPTMnet; Q9UNF1; -. DR MetOSite; Q9UNF1; -. DR PhosphoSitePlus; Q9UNF1; -. DR SwissPalm; Q9UNF1; -. DR BioMuta; MAGED2; -. DR DMDM; 17380153; -. DR EPD; Q9UNF1; -. DR jPOST; Q9UNF1; -. DR MassIVE; Q9UNF1; -. DR MaxQB; Q9UNF1; -. DR PaxDb; 9606-ENSP00000364209; -. DR PeptideAtlas; Q9UNF1; -. DR ProteomicsDB; 85286; -. [Q9UNF1-1] DR ProteomicsDB; 85287; -. [Q9UNF1-2] DR Pumba; Q9UNF1; -. DR Antibodypedia; 26825; 246 antibodies from 29 providers. DR DNASU; 10916; -. DR Ensembl; ENST00000218439.8; ENSP00000218439.4; ENSG00000102316.17. [Q9UNF1-1] DR Ensembl; ENST00000375053.6; ENSP00000364193.2; ENSG00000102316.17. [Q9UNF1-1] DR Ensembl; ENST00000375058.5; ENSP00000364198.1; ENSG00000102316.17. [Q9UNF1-1] DR Ensembl; ENST00000375068.6; ENSP00000364209.1; ENSG00000102316.17. [Q9UNF1-1] DR Ensembl; ENST00000396224.1; ENSP00000379526.1; ENSG00000102316.17. [Q9UNF1-1] DR GeneID; 10916; -. DR KEGG; hsa:10916; -. DR MANE-Select; ENST00000375068.6; ENSP00000364209.1; NM_177433.3; NP_803182.1. DR UCSC; uc004dtk.3; human. [Q9UNF1-1] DR AGR; HGNC:16353; -. DR CTD; 10916; -. DR DisGeNET; 10916; -. DR GeneCards; MAGED2; -. DR HGNC; HGNC:16353; MAGED2. DR HPA; ENSG00000102316; Low tissue specificity. DR MalaCards; MAGED2; -. DR MIM; 300470; gene. DR MIM; 300971; phenotype. DR neXtProt; NX_Q9UNF1; -. DR OpenTargets; ENSG00000102316; -. DR Orphanet; 570371; Bartter syndrome type 5. DR PharmGKB; PA30560; -. DR VEuPathDB; HostDB:ENSG00000102316; -. DR eggNOG; KOG4562; Eukaryota. DR GeneTree; ENSGT00940000161795; -. DR InParanoid; Q9UNF1; -. DR OMA; IDKSDHL; -. DR OrthoDB; 3128316at2759; -. DR PhylomeDB; Q9UNF1; -. DR TreeFam; TF352132; -. DR PathwayCommons; Q9UNF1; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR SignaLink; Q9UNF1; -. DR BioGRID-ORCS; 10916; 10 hits in 785 CRISPR screens. DR ChiTaRS; MAGED2; human. DR GeneWiki; MAGED2; -. DR GenomeRNAi; 10916; -. DR Pharos; Q9UNF1; Tbio. DR PRO; PR:Q9UNF1; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9UNF1; Protein. DR Bgee; ENSG00000102316; Expressed in adenohypophysis and 204 other cell types or tissues. DR ExpressionAtlas; Q9UNF1; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0007565; P:female pregnancy; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0070294; P:renal sodium ion absorption; IMP:UniProtKB. DR Gene3D; 1.10.10.1200; MAGE homology domain, winged helix WH1 motif; 1. DR Gene3D; 1.10.10.1210; MAGE homology domain, winged helix WH2 motif; 1. DR InterPro; IPR037445; MAGE. DR InterPro; IPR041898; MAGE_WH1. DR InterPro; IPR041899; MAGE_WH2. DR InterPro; IPR002190; MHD_dom. DR PANTHER; PTHR11736:SF11; MELANOMA-ASSOCIATED ANTIGEN D2; 1. DR PANTHER; PTHR11736; MELANOMA-ASSOCIATED ANTIGEN MAGE ANTIGEN; 1. DR Pfam; PF01454; MAGE; 1. DR SMART; SM01373; MAGE; 1. DR PROSITE; PS50838; MAGE; 1. DR Genevisible; Q9UNF1; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Bartter syndrome; KW Direct protein sequencing; Disease variant; Phosphoprotein; KW Reference proteome; Tumor antigen. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..606 FT /note="Melanoma-associated antigen D2" FT /id="PRO_0000156727" FT DOMAIN 279..478 FT /note="MAGE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127" FT REGION 1..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 248..275 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 534..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..41 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..121 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 542..563 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 72 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648" FT MOD_RES 197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT VAR_SEQ 45..62 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_008030" FT VARIANT 187 FT /note="E -> D (in dbSNP:rs12014977)" FT /id="VAR_053508" FT VARIANT 266 FT /note="Q -> R (in dbSNP:rs1021000890)" FT /evidence="ECO:0000269|PubMed:10752678" FT /id="VAR_011639" FT VARIANT 446 FT /note="R -> C (in BARTS5; loss of interaction with GNAS; FT dbSNP:rs878854407)" FT /evidence="ECO:0000269|PubMed:27120771" FT /id="VAR_076836" FT VARIANT 458 FT /note="K -> Q (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036584" FT VARIANT 488..491 FT /note="Missing (in BARTS5)" FT /evidence="ECO:0000269|PubMed:27120771" FT /id="VAR_076837" FT CONFLICT 73 FT /note="P -> S (in Ref. 3; AAD00728)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="S -> C (in Ref. 5; BAC03896)" FT /evidence="ECO:0000305" SQ SEQUENCE 606 AA; 64954 MW; 352FD5BAF5088652 CRC64; MSDTSESGAG LTRFQAEASE KDSSSMMQTL LTVTQNVEVP ETPKASKALE VSEDVKVSKA SGVSKATEVS KTPEAREAPA TQASSTTQLT DTQVLAAENK SLAADTKKQN ADPQAVTMPA TETKKVSHVA DTKVNTKAQE TEAAPSQAPA DEPEPESAAA QSQENQDTRP KVKAKKARKV KHLDGEEDGS SDQSQASGTT GGRRVSKALM ASMARRASRG PIAFWARRAS RTRLAAWARR ALLSLRSPKA RRGKARRRAA KLQSSQEPEA PPPRDVALLQ GRANDLVKYL LAKDQTKIPI KRSDMLKDII KEYTDVYPEI IERAGYSLEK VFGIQLKEID KNDHLYILLS TLEPTDAGIL GTTKDSPKLG LLMVLLSIIF MNGNRSSEAV IWEVLRKLGL RPGIHHSLFG DVKKLITDEF VKQKYLDYAR VPNSNPPEYE FFWGLRSYYE TSKMKVLKFA CKVQKKDPKE WAAQYREAME ADLKAAAEAA AEAKARAEIR ARMGIGLGSE NAAGPCNWDE ADIGPWAKAR IQAGAEAKAK AQESGSASTG ASTSTNNSAS ASASTSGGFS AGASLTATLT FGLFAGLGGA GASTSGSSGA CGFSYK //