MAGD1_HUMAN
ID MAGD1_HUMAN Reviewed; 778 AA.
AC Q9Y5V3; Q5VSH6; Q8IZ84; Q8WY92; Q9H352; Q9HBT4; Q9UF36;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Melanoma-associated antigen D1;
DE AltName: Full=MAGE tumor antigen CCF;
DE AltName: Full=MAGE-D1 antigen;
DE AltName: Full=Neurotrophin receptor-interacting MAGE homolog;
GN Name=MAGED1; Synonyms=NRAGE; ORFNames=PP2250, PRO2292;
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).
RX PubMed=10985348; DOI=10.1016/s0896-6273(00)00036-2;
RA Salehi A.H., Roux P.P., Kubu C.J., Zeindler C., Bhakar A., Tannis L.-L.,
RA Verdi J.M., Barker P.A.;
RT "NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor
RT and facilitates nerve growth factor dependent apoptosis.";
RL Neuron 27:279-288(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15094062; DOI=10.1016/s0014-5793(04)00353-9;
RA Wen C.-J., Xue B., Qin W.-X., Yu M., Zhang M.-Y., Zhao D.-H., Gao X.,
RA Gu J.-R., Li C.-J.;
RT "hNRAGE, a human neurotrophin receptor interacting MAGE homologue,
RT regulates p53 transcriptional activity and inhibits cell proliferation.";
RL FEBS Lett. 564:171-176(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chen Y.;
RT "Identification and characterization of a new member of the MAGE gene
RT family.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-778 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=10409427; DOI=10.1006/geno.1999.5870;
RA Pold M., Zhou J., Chen G.L., Hall J.M., Vescio R.A., Berenson J.R.;
RT "Identification of a new, unorthodox member of the MAGE gene family.";
RL Genomics 59:161-167(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-778.
RC TISSUE=Testis;
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] OF 396-778.
RC TISSUE=Fetal liver;
RX PubMed=11280991;
RA Zhang C.G., Xing G.C., Wei H.D., Yu Y.T., He F.C.;
RT "A new melanoma antigen-encoding gene subfamily in human chromosome X.";
RL Yi Chuan Xue Bao 28:197-203(2001).
RN [9]
RP IDENTIFICATION OF THE TRANSLATIONAL INITIATION CODON.
RX PubMed=11087672; DOI=10.1006/geno.2000.6356;
RA Kubu C.J., Goldhawk D.G., Barker P.A., Verdi J.M.;
RT "Identification of the translational initiation codon in human MAGED1.";
RL Genomics 70:150-152(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH TRIM28 AND PJA1.
RX PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
RA Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
RT "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.";
RL Mol. Cell 39:963-974(2010).
CC -!- FUNCTION: Involved in the apoptotic response after nerve growth factor
CC (NGF) binding in neuronal cells. Inhibits cell cycle progression, and
CC facilitates NGFR-mediated apoptosis. May act as a regulator of the
CC function of DLX family members. May enhance ubiquitin ligase activity
CC of RING-type zinc finger-containing E3 ubiquitin-protein ligases.
CC Proposed to act through recruitment and/or stabilization of the Ubl-
CC conjugating enzyme (E2) at the E3:substrate complex. Plays a role in
CC the circadian rhythm regulation. May act as RORA co-regulator,
CC modulating the expression of core clock genes such as ARNTL/BMAL1 and
CC NFIL3, induced, or NR1D1, repressed. {ECO:0000269|PubMed:20864041}.
CC -!- SUBUNIT: Interacts with DLX5, DLX7 and MSX2 and forms homomultimers.
CC Interacts with UNC5A. Interacts with TRIM28 and PJA1. Interacts with
CC NGFR/p75NTR and RORA. {ECO:0000269|PubMed:20864041}.
CC -!- INTERACTION:
CC Q9Y5V3; O00468-6: AGRN; NbExp=3; IntAct=EBI-716006, EBI-17740588;
CC Q9Y5V3; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-716006, EBI-9641546;
CC Q9Y5V3; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-716006, EBI-1057448;
CC Q9Y5V3; Q03989: ARID5A; NbExp=3; IntAct=EBI-716006, EBI-948603;
CC Q9Y5V3; O95817: BAG3; NbExp=6; IntAct=EBI-716006, EBI-747185;
CC Q9Y5V3; O95429: BAG4; NbExp=3; IntAct=EBI-716006, EBI-2949658;
CC Q9Y5V3; O14503: BHLHE40; NbExp=6; IntAct=EBI-716006, EBI-711810;
CC Q9Y5V3; Q6PIA0: BIRC8; NbExp=3; IntAct=EBI-716006, EBI-2129837;
CC Q9Y5V3; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-716006, EBI-946029;
CC Q9Y5V3; P35219: CA8; NbExp=9; IntAct=EBI-716006, EBI-718700;
CC Q9Y5V3; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-716006, EBI-1765641;
CC Q9Y5V3; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-716006, EBI-744556;
CC Q9Y5V3; O95400: CD2BP2; NbExp=3; IntAct=EBI-716006, EBI-768015;
CC Q9Y5V3; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-716006, EBI-396137;
CC Q9Y5V3; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-716006, EBI-12261896;
CC Q9Y5V3; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-716006, EBI-749051;
CC Q9Y5V3; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-716006, EBI-2555370;
CC Q9Y5V3; O75553: DAB1; NbExp=3; IntAct=EBI-716006, EBI-7875264;
CC Q9Y5V3; Q15038: DAZAP2; NbExp=4; IntAct=EBI-716006, EBI-724310;
CC Q9Y5V3; P26196: DDX6; NbExp=3; IntAct=EBI-716006, EBI-351257;
CC Q9Y5V3; Q9Y5R5: DMRT2; NbExp=3; IntAct=EBI-716006, EBI-18072054;
CC Q9Y5V3; O60573: EIF4E2; NbExp=3; IntAct=EBI-716006, EBI-398610;
CC Q9Y5V3; P19447: ERCC3; NbExp=3; IntAct=EBI-716006, EBI-1183307;
CC Q9Y5V3; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-716006, EBI-1384254;
CC Q9Y5V3; O60548: FOXD2; NbExp=3; IntAct=EBI-716006, EBI-17282008;
CC Q9Y5V3; O75593: FOXH1; NbExp=3; IntAct=EBI-716006, EBI-1759806;
CC Q9Y5V3; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-716006, EBI-12018822;
CC Q9Y5V3; Q9BWX5: GATA5; NbExp=3; IntAct=EBI-716006, EBI-12132270;
CC Q9Y5V3; P23415: GLRA1; NbExp=3; IntAct=EBI-716006, EBI-12020340;
CC Q9Y5V3; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-716006, EBI-748515;
CC Q9Y5V3; O95872: GPANK1; NbExp=3; IntAct=EBI-716006, EBI-751540;
CC Q9Y5V3; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-716006, EBI-10329202;
CC Q9Y5V3; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-716006, EBI-16429135;
CC Q9Y5V3; O14964: HGS; NbExp=6; IntAct=EBI-716006, EBI-740220;
CC Q9Y5V3; P31943: HNRNPH1; NbExp=3; IntAct=EBI-716006, EBI-351590;
CC Q9Y5V3; P31274: HOXC9; NbExp=3; IntAct=EBI-716006, EBI-1779423;
CC Q9Y5V3; O75031: HSF2BP; NbExp=3; IntAct=EBI-716006, EBI-7116203;
CC Q9Y5V3; P52292: KPNA2; NbExp=4; IntAct=EBI-716006, EBI-349938;
CC Q9Y5V3; O60684: KPNA6; NbExp=3; IntAct=EBI-716006, EBI-359923;
CC Q9Y5V3; Q3LI72: KRTAP19-5; NbExp=9; IntAct=EBI-716006, EBI-1048945;
CC Q9Y5V3; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-716006, EBI-12111050;
CC Q9Y5V3; Q92615: LARP4B; NbExp=3; IntAct=EBI-716006, EBI-1052558;
CC Q9Y5V3; Q96PV6: LENG8; NbExp=3; IntAct=EBI-716006, EBI-739546;
CC Q9Y5V3; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-716006, EBI-2341787;
CC Q9Y5V3; Q9Y5V3: MAGED1; NbExp=4; IntAct=EBI-716006, EBI-716006;
CC Q9Y5V3; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-716006, EBI-741424;
CC Q9Y5V3; Q99750: MDFI; NbExp=6; IntAct=EBI-716006, EBI-724076;
CC Q9Y5V3; P50222: MEOX2; NbExp=3; IntAct=EBI-716006, EBI-748397;
CC Q9Y5V3; Q13064: MKRN3; NbExp=3; IntAct=EBI-716006, EBI-2340269;
CC Q9Y5V3; Q96HR8: NAF1; NbExp=3; IntAct=EBI-716006, EBI-2515597;
CC Q9Y5V3; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-716006, EBI-17490746;
CC Q9Y5V3; O43189: PHF1; NbExp=3; IntAct=EBI-716006, EBI-530034;
CC Q9Y5V3; P78337: PITX1; NbExp=4; IntAct=EBI-716006, EBI-748265;
CC Q9Y5V3; Q8NG27: PJA1; NbExp=7; IntAct=EBI-716006, EBI-714606;
CC Q9Y5V3; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-716006, EBI-10171633;
CC Q9Y5V3; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-716006, EBI-11956563;
CC Q9Y5V3; O43741: PRKAB2; NbExp=4; IntAct=EBI-716006, EBI-1053424;
CC Q9Y5V3; O75360: PROP1; NbExp=3; IntAct=EBI-716006, EBI-9027467;
CC Q9Y5V3; P86480: PRR20D; NbExp=3; IntAct=EBI-716006, EBI-12754095;
CC Q9Y5V3; P0CG20: PRR35; NbExp=3; IntAct=EBI-716006, EBI-11986293;
CC Q9Y5V3; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-716006, EBI-744023;
CC Q9Y5V3; O43251: RBFOX2; NbExp=3; IntAct=EBI-716006, EBI-746056;
CC Q9Y5V3; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-716006, EBI-11963050;
CC Q9Y5V3; Q86U06: RBM23; NbExp=3; IntAct=EBI-716006, EBI-780319;
CC Q9Y5V3; Q93062: RBPMS; NbExp=3; IntAct=EBI-716006, EBI-740322;
CC Q9Y5V3; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-716006, EBI-11987469;
CC Q9Y5V3; Q9BQY4: RHOXF2; NbExp=6; IntAct=EBI-716006, EBI-372094;
CC Q9Y5V3; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-716006, EBI-16428950;
CC Q9Y5V3; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-716006, EBI-6257312;
CC Q9Y5V3; Q8WU79: SMAP2; NbExp=6; IntAct=EBI-716006, EBI-2822515;
CC Q9Y5V3; Q16637: SMN2; NbExp=3; IntAct=EBI-716006, EBI-395421;
CC Q9Y5V3; P09234: SNRPC; NbExp=3; IntAct=EBI-716006, EBI-766589;
CC Q9Y5V3; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-716006, EBI-10246938;
CC Q9Y5V3; P56693: SOX10; NbExp=3; IntAct=EBI-716006, EBI-1167533;
CC Q9Y5V3; P35711-4: SOX5; NbExp=3; IntAct=EBI-716006, EBI-11954419;
CC Q9Y5V3; O95947: TBX6; NbExp=3; IntAct=EBI-716006, EBI-2824328;
CC Q9Y5V3; Q92734: TFG; NbExp=8; IntAct=EBI-716006, EBI-357061;
CC Q9Y5V3; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-716006, EBI-11064654;
CC Q9Y5V3; O43711: TLX3; NbExp=3; IntAct=EBI-716006, EBI-3939165;
CC Q9Y5V3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-716006, EBI-10241197;
CC Q9Y5V3; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-716006, EBI-6447954;
CC Q9Y5V3; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-716006, EBI-9090990;
CC Q9Y5V3; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-716006, EBI-8636434;
CC Q9Y5V3; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-716006, EBI-947187;
CC Q9Y5V3; O95231: VENTX; NbExp=3; IntAct=EBI-716006, EBI-10191303;
CC Q9Y5V3; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-716006, EBI-1051237;
CC Q9Y5V3; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-716006, EBI-8656416;
CC Q9Y5V3; Q15915: ZIC1; NbExp=3; IntAct=EBI-716006, EBI-11963196;
CC Q9Y5V3; Q96MN9: ZNF488; NbExp=3; IntAct=EBI-716006, EBI-948288;
CC Q9Y5V3; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-716006, EBI-16429014;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Expression shifts from the cytoplasm to the plasma
CC membrane upon stimulation with NGF. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5V3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5V3-2; Sequence=VSP_009286;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow stromal cells from both
CC multiple myeloma patients and healthy donors. Seems to be ubiquitously
CC expressed.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31421.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG35551.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF217963; AAG09704.1; -; mRNA.
DR EMBL; AF258554; AAG23757.1; -; mRNA.
DR EMBL; AF300328; AAQ14483.1; -; mRNA.
DR EMBL; AL929410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014070; AAH14070.1; -; mRNA.
DR EMBL; BC032473; AAH32473.1; -; mRNA.
DR EMBL; AF124440; AAD31421.1; ALT_INIT; mRNA.
DR EMBL; AL133628; CAB63752.1; -; mRNA.
DR EMBL; AF132205; AAG35551.1; ALT_INIT; mRNA.
DR CCDS; CCDS14337.1; -. [Q9Y5V3-1]
DR CCDS; CCDS35279.1; -. [Q9Y5V3-2]
DR PIR; T43464; T43464.
DR RefSeq; NP_001005332.1; NM_001005332.1. [Q9Y5V3-1]
DR RefSeq; NP_001005333.1; NM_001005333.1. [Q9Y5V3-2]
DR RefSeq; NP_008917.3; NM_006986.3. [Q9Y5V3-1]
DR RefSeq; XP_011529137.1; XM_011530835.2. [Q9Y5V3-1]
DR RefSeq; XP_016885467.1; XM_017029978.1. [Q9Y5V3-1]
DR RefSeq; XP_016885468.1; XM_017029979.1. [Q9Y5V3-1]
DR RefSeq; XP_016885469.1; XM_017029980.1. [Q9Y5V3-1]
DR AlphaFoldDB; Q9Y5V3; -.
DR SMR; Q9Y5V3; -.
DR BioGRID; 114879; 279.
DR IntAct; Q9Y5V3; 174.
DR MINT; Q9Y5V3; -.
DR STRING; 9606.ENSP00000364847; -.
DR iPTMnet; Q9Y5V3; -.
DR PhosphoSitePlus; Q9Y5V3; -.
DR BioMuta; MAGED1; -.
DR DMDM; 62906893; -.
DR EPD; Q9Y5V3; -.
DR jPOST; Q9Y5V3; -.
DR MassIVE; Q9Y5V3; -.
DR MaxQB; Q9Y5V3; -.
DR PaxDb; Q9Y5V3; -.
DR PeptideAtlas; Q9Y5V3; -.
DR PRIDE; Q9Y5V3; -.
DR ProteomicsDB; 86514; -. [Q9Y5V3-1]
DR ProteomicsDB; 86515; -. [Q9Y5V3-2]
DR Antibodypedia; 4194; 361 antibodies from 36 providers.
DR DNASU; 9500; -.
DR Ensembl; ENST00000326587.12; ENSP00000325333.8; ENSG00000179222.18. [Q9Y5V3-1]
DR Ensembl; ENST00000375695.2; ENSP00000364847.2; ENSG00000179222.18. [Q9Y5V3-2]
DR Ensembl; ENST00000375722.5; ENSP00000364874.1; ENSG00000179222.18. [Q9Y5V3-1]
DR Ensembl; ENST00000375772.7; ENSP00000364927.3; ENSG00000179222.18. [Q9Y5V3-1]
DR GeneID; 9500; -.
DR KEGG; hsa:9500; -.
DR MANE-Select; ENST00000326587.12; ENSP00000325333.8; NM_006986.4; NP_008917.3.
DR UCSC; uc004dpm.5; human. [Q9Y5V3-1]
DR CTD; 9500; -.
DR DisGeNET; 9500; -.
DR GeneCards; MAGED1; -.
DR HGNC; HGNC:6813; MAGED1.
DR HPA; ENSG00000179222; Low tissue specificity.
DR MIM; 300224; gene.
DR neXtProt; NX_Q9Y5V3; -.
DR OpenTargets; ENSG00000179222; -.
DR PharmGKB; PA30559; -.
DR VEuPathDB; HostDB:ENSG00000179222; -.
DR eggNOG; KOG4562; Eukaryota.
DR GeneTree; ENSGT00940000162070; -.
DR HOGENOM; CLU_394113_0_0_1; -.
DR InParanoid; Q9Y5V3; -.
DR OMA; AVCHPLP; -.
DR OrthoDB; 1195799at2759; -.
DR PhylomeDB; Q9Y5V3; -.
DR TreeFam; TF352132; -.
DR PathwayCommons; Q9Y5V3; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR SignaLink; Q9Y5V3; -.
DR SIGNOR; Q9Y5V3; -.
DR BioGRID-ORCS; 9500; 7 hits in 701 CRISPR screens.
DR ChiTaRS; MAGED1; human.
DR GeneWiki; MAGED1; -.
DR GenomeRNAi; 9500; -.
DR Pharos; Q9Y5V3; Tbio.
DR PRO; PR:Q9Y5V3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y5V3; protein.
DR Bgee; ENSG00000179222; Expressed in ventricular zone and 200 other tissues.
DR Genevisible; Q9Y5V3; HS.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS: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; IPR030083; MAGED1.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR PANTHER; PTHR11736:SF28; PTHR11736:SF28; 1.
DR Pfam; PF01454; MAGE; 1.
DR SMART; SM01373; MAGE; 1.
DR PROSITE; PS50838; MAGE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cell membrane; Cytoplasm;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Tumor antigen; Ubl conjugation pathway.
FT CHAIN 1..778
FT /note="Melanoma-associated antigen D1"
FT /id="PRO_0000156723"
FT REPEAT 296..301
FT /note="1"
FT REPEAT 302..307
FT /note="2"
FT REPEAT 308..313
FT /note="3"
FT REPEAT 332..337
FT /note="4"
FT REPEAT 338..343
FT /note="5"
FT REPEAT 344..349
FT /note="6"
FT REPEAT 350..355
FT /note="7"
FT REPEAT 356..361
FT /note="8"
FT REPEAT 362..367
FT /note="9"
FT REPEAT 368..373
FT /note="10"
FT REPEAT 374..379
FT /note="11"
FT REPEAT 380..385
FT /note="12"
FT REPEAT 386..391
FT /note="13"
FT REPEAT 392..397
FT /note="14"
FT REPEAT 398..403
FT /note="15"
FT REPEAT 404..409
FT /note="16"
FT REPEAT 410..415
FT /note="17"
FT REPEAT 416..421
FT /note="18"
FT REPEAT 422..427
FT /note="19"
FT REPEAT 428..432
FT /note="20; approximate"
FT REPEAT 433..438
FT /note="21"
FT REPEAT 439..444
FT /note="22"
FT DOMAIN 471..669
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..444
FT /note="22 X 6 AA tandem repeats of W-[PQ]-X-P-X-X"
FT REGION 376..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT VAR_SEQ 15
FT /note="Q -> QNPDACRAVCHPLPQPPASTLPLSAFPTLCDPPYSQLRDPPAVLSCY
FT CTPLGASPAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009286"
FT VARIANT 238
FT /note="L -> M (in dbSNP:rs12689461)"
FT /id="VAR_060070"
FT CONFLICT 119
FT /note="P -> S (in Ref. 1; AAG09704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 86161 MW; D818690052D166CE CRC64;
MAQKMDCGAG LLGFQAEASV EDSALLMQTL MEAIQISEAP PTNQATAAAS PQSSQPPTAN
EMADIQVSAA AARPKSAFKV QNATTKGPNG VYDFSQAHNA KDVPNTQPKA AFKSQNATPK
GPNAAYDFSQ AATTGELAAN KSEMAFKAQN ATTKVGPNAT YNFSQSLNAN DLANSRPKTP
FKAWNDTTKA PTADTQTQNV NQAKMATSQA DIETDPGISE PDGATAQTSA DGSQAQNLES
RTIIRGKRTR KINNLNVEEN SSGDQRRAPL AAGTWRSAPV PVTTQNPPGA PPNVLWQTPL
AWQNPSGWQN QTARQTPPAR QSPPARQTPP AWQNPVAWQN PVIWPNPVIW QNPVIWPNPI
VWPGPVVWPN PLAWQNPPGW QTPPGWQTPP GWQGPPDWQG PPDWPLPPDW PLPPDWPLPT
DWPLPPDWIP ADWPIPPDWQ NLRPSPNLRP SPNSRASQNP GAAQPRDVAL LQERANKLVK
YLMLKDYTKV PIKRSEMLRD IIREYTDVYP EIIERACFVL EKKFGIQLKE IDKEEHLYIL
ISTPESLAGI LGTTKDTPKL GLLLVILGVI FMNGNRASEA VLWEALRKMG LRPGVRHPLL
GDLRKLLTYE FVKQKYLDYR RVPNSNPPEY EFLWGLRSYH ETSKMKVLRF IAEVQKRDPR
DWTAQFMEAA DEALDALDAA AAEAEARAEA RTRMGIGDEA VSGPWSWDDI EFELLTWDEE
GDFGDPWSRI PFTFWARYHQ NARSRFPQTF AGPIIGPGGT ASANFAANFG AIGFFWVE
