MAGD2_HUMAN
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 03-AUG-2022, entry version 183.
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.
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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; 195.
DR DIP; DIP-50722N; -.
DR IntAct; Q9UNF1; 65.
DR MINT; Q9UNF1; -.
DR STRING; 9606.ENSP00000364209; -.
DR GlyGen; Q9UNF1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UNF1; -.
DR MetOSite; Q9UNF1; -.
DR PhosphoSitePlus; Q9UNF1; -.
DR BioMuta; MAGED2; -.
DR DMDM; 17380153; -.
DR EPD; Q9UNF1; -.
DR jPOST; Q9UNF1; -.
DR MassIVE; Q9UNF1; -.
DR MaxQB; Q9UNF1; -.
DR PaxDb; Q9UNF1; -.
DR PeptideAtlas; Q9UNF1; -.
DR PRIDE; Q9UNF1; -.
DR ProteomicsDB; 85286; -. [Q9UNF1-1]
DR ProteomicsDB; 85287; -. [Q9UNF1-2]
DR Antibodypedia; 26825; 224 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 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 PhylomeDB; Q9UNF1; -.
DR TreeFam; TF352132; -.
DR PathwayCommons; Q9UNF1; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q9UNF1; -.
DR BioGRID-ORCS; 10916; 7 hits in 706 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 202 other tissues.
DR ExpressionAtlas; Q9UNF1; baseline and differential.
DR Genevisible; Q9UNF1; HS.
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; -; 1.
DR Gene3D; 1.10.10.1210; -; 1.
DR InterPro; IPR037445; MAGE.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR028810; MAGED2.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR PANTHER; PTHR11736:SF11; PTHR11736:SF11; 1.
DR Pfam; PF01454; MAGE; 1.
DR SMART; SM01373; MAGE; 1.
DR PROSITE; PS50838; MAGE; 1.
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
