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 14-DEC-2022, entry version 204. 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 BMAL1 and NFIL3, CC 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}; 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; 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; 286. DR IntAct; Q9Y5V3; 175. 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 ProteomicsDB; 86514; -. [Q9Y5V3-1] DR ProteomicsDB; 86515; -. [Q9Y5V3-2] DR Antibodypedia; 4194; 361 antibodies from 35 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 AGR; HGNC:6813; -. 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 DNA-templated transcription; 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:SF28; MELANOMA-ASSOCIATED ANTIGEN D1; 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. 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 //