ID MAGA3_HUMAN Reviewed; 314 AA. AC P43357; Q6FHI6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 186. DE RecName: Full=Melanoma-associated antigen 3 {ECO:0000305}; DE AltName: Full=Antigen MZ2-D; DE AltName: Full=Cancer/testis antigen 1.3; DE Short=CT1.3; DE AltName: Full=MAGE-3 antigen {ECO:0000303|PubMed:8113684}; GN Name=MAGEA3 {ECO:0000303|PubMed:29779948, ECO:0000312|HGNC:HGNC:6801}; GN Synonyms=MAGE3 {ECO:0000303|PubMed:8113684}; 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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF ASP-170 AND TYR-176. RC TISSUE=Blood; RX PubMed=8113684; DOI=10.1084/jem.179.3.921; RA Gaugler B., van den Eynde B., van der Bruggen P., Romero P., Gaforio J.J., RA De Plaen E., Lethe B.G., Brasseur F., Boon T.; RT "Human gene MAGE-3 codes for an antigen recognized on a melanoma by RT autologous cytolytic T lymphocytes."; RL J. Exp. Med. 179:921-930(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skin; RX PubMed=8037761; DOI=10.1006/bbrc.1994.1963; RA Ding M., Beck R.J., Keller C.J., Fenton R.G.; RT "Cloning and analysis of MAGE-1-related genes."; RL Biochem. Biophys. Res. Commun. 202:549-555(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10854409; DOI=10.1101/gr.10.6.758; RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., RA Greystrong J.S., Clarke D., Kimberley C., Goerdes M., Blechschmidt K., RA Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., RA Rhodes M., Denny P., Rosenthal A., Brown S.D.M.; RT "Comparative genome sequence analysis of the Bpa/Str region in mouse and RT man."; RL Genome Res. 10:758-775(2000). 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 MRNA]. RC TISSUE=Bone marrow, Lung, Prostate, 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 [8] RP FUNCTION, AND INTERACTION WITH TRIM28. RX PubMed=17942928; DOI=10.1158/0008-5472.can-07-1478; RA Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M., RA Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H., Ivanov A.V., RA Simpson A.J., Longley B.J.; RT "MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress RT p53-dependent apoptosis in MAGE-positive cell lines."; RL Cancer Res. 67:9954-9962(2007). RN [9] RP FUNCTION, AND INTERACTION WITH TRIM28. 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). RN [10] RP UBIQUITINATION. RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028; RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.; RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C- RT terminal degrons."; RL Cell 173:1622-1635(2018). RN [11] RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF GLU-314. RX PubMed=31267705; DOI=10.15252/embr.201847352; RA Ravichandran R., Kodali K., Peng J., Potts P.R.; RT "Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase and nutrient RT availability."; RL EMBO Rep. 20:e47352-e47352(2019). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 271-279 IN COMPLEX WITH HLA CLASS RP I HISTOCOMPATIBILITY COMPLEX. RA Orth P., Alings C., Saenger W., Ziegler A.; RT "Human class I histocompatibility antigen (HLA-A) complex with a nonameric RT peptide from melanoma-associated antigen 3 (residues 271-279)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Activator of ubiquitin ligase activity of RING-type zinc CC finger-containing E3 ubiquitin-protein ligases that acts as a repressor CC of autophagy (PubMed:20864041, PubMed:31267705). May enhance ubiquitin CC ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by CC TRIM28. Proposed to act through recruitment and/or stabilization of the CC Ubl-conjugating enzyme (E2) at the E3:substrate complex CC (PubMed:17942928, PubMed:20864041). May play a role in embryonal CC development and tumor transformation or aspects of tumor progression CC (PubMed:17942928, PubMed:20864041). In vitro promotes cell viability in CC melanoma cell lines (PubMed:17942928). Antigen recognized on a melanoma CC by autologous cytolytic T-lymphocytes (PubMed:8113684). CC {ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:20864041, CC ECO:0000269|PubMed:31267705, ECO:0000269|PubMed:8113684}. CC -!- SUBUNIT: Interacts with TRIM28. {ECO:0000269|PubMed:17942928, CC ECO:0000269|PubMed:20864041, ECO:0000269|Ref.12}. CC -!- INTERACTION: CC P43357; O00154-4: ACOT7; NbExp=3; IntAct=EBI-5651459, EBI-12007918; CC P43357; Q8IXM2: BACC1; NbExp=5; IntAct=EBI-5651459, EBI-4280811; CC P43357; Q9BQE9: BCL7B; NbExp=3; IntAct=EBI-5651459, EBI-2560588; CC P43357; Q9BW66: CINP; NbExp=3; IntAct=EBI-5651459, EBI-739784; CC P43357; O00471: EXOC5; NbExp=3; IntAct=EBI-5651459, EBI-949824; CC P43357; P42858: HTT; NbExp=6; IntAct=EBI-5651459, EBI-466029; CC P43357; A0A0C4DGT3: IQSEC1; NbExp=3; IntAct=EBI-5651459, EBI-12064916; CC P43357; Q86VH2: KIF27; NbExp=3; IntAct=EBI-5651459, EBI-7950718; CC P43357; Q9Y333: LSM2; NbExp=3; IntAct=EBI-5651459, EBI-347416; CC P43357; P49585: PCYT1A; NbExp=3; IntAct=EBI-5651459, EBI-2563309; CC P43357; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-5651459, EBI-6257312; CC P43357; P06702: S100A9; NbExp=3; IntAct=EBI-5651459, EBI-1055001; CC P43357; Q96FJ0: STAMBPL1; NbExp=6; IntAct=EBI-5651459, EBI-745021; CC P43357; Q13263: TRIM28; NbExp=3; IntAct=EBI-5651459, EBI-78139; CC -!- TISSUE SPECIFICITY: Expressed in many tumors of several types, such as CC melanoma, head and neck squamous cell carcinoma, lung carcinoma and CC breast carcinoma, but not in normal tissues except for testes and CC placenta. Never expressed in kidney tumors, Leukemias and lymphomas. CC {ECO:0000269|PubMed:8113684}. CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes CC the diglutamate (Glu-Glu) at the C-terminus, leading to its CC degradation. {ECO:0000269|PubMed:29779948, CC ECO:0000269|PubMed:31267705}. CC -!- CAUTION: In vitro experiments measuring cell viability in melanoma cell CC lines used siRNA specific for MAGEA3 and MAGEA6. CC {ECO:0000269|PubMed:17942928}. 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; U03735; AAA17446.1; -; Genomic_DNA. DR EMBL; U82671; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR541767; CAG46566.1; -; mRNA. DR EMBL; CR541774; CAG46573.1; -; mRNA. DR EMBL; AK292384; BAF85073.1; -; mRNA. DR EMBL; BC000340; AAH00340.1; -; mRNA. DR EMBL; BC005963; AAH05963.1; -; mRNA. DR EMBL; BC011744; AAH11744.1; -; mRNA. DR EMBL; BC016803; AAH16803.1; -; mRNA. DR EMBL; BC017389; AAH17389.1; -; mRNA. DR CCDS; CCDS76045.1; -. DR PIR; JC2361; JC2361. DR RefSeq; NP_005353.1; NM_005362.4. DR RefSeq; XP_005274733.1; XM_005274676.4. DR RefSeq; XP_006724881.1; XM_006724818.3. DR RefSeq; XP_011529462.1; XM_011531160.4. DR RefSeq; XP_011529463.1; XM_011531161.2. DR RefSeq; XP_054189312.1; XM_054333337.1. DR RefSeq; XP_054189313.1; XM_054333338.1. DR RefSeq; XP_054189314.1; XM_054333339.1. DR RefSeq; XP_054189315.1; XM_054333340.1. DR PDB; 1QEW; X-ray; 2.20 A; C=271-279. DR PDB; 4V0P; X-ray; 2.07 A; A=104-314. DR PDB; 5BRZ; X-ray; 2.62 A; C=168-176. DR PDB; 8T9A; EM; 3.17 A; C=104-314. DR PDB; 9BD2; X-ray; 2.24 A; A/B/C=104-310. DR PDB; 9YTF; EM; 2.60 A; C=168-176. DR AlphaFoldDB; P43357; -. DR EMDB; EMD-41105; -. DR EMDB; EMD-73460; -. DR SMR; P43357; -. DR BioGRID; 110276; 142. DR CORUM; P43357; -. DR DIP; DIP-44886N; -. DR FunCoup; P43357; 24. DR IntAct; P43357; 44. DR STRING; 9606.ENSP00000473093; -. DR ChEMBL; CHEMBL4662941; -. DR DrugBank; DB14816; Biropepimut-S. DR iPTMnet; P43357; -. DR PhosphoSitePlus; P43357; -. DR BioMuta; MAGEA3; -. DR DMDM; 1170857; -. DR jPOST; P43357; -. DR MassIVE; P43357; -. DR PaxDb; 9606-ENSP00000473093; -. DR PeptideAtlas; P43357; -. DR ProteomicsDB; 55619; -. DR Pumba; P43357; -. DR Antibodypedia; 30766; 512 antibodies from 34 providers. DR DNASU; 4102; -. DR Ensembl; ENST00000370278.4; ENSP00000359301.3; ENSG00000221867.10. DR Ensembl; ENST00000598245.2; ENSP00000473093.1; ENSG00000221867.10. DR Ensembl; ENST00000709974.1; ENSP00000517961.1; ENSG00000292186.1. DR Ensembl; ENST00000709975.1; ENSP00000517962.1; ENSG00000292186.1. DR Ensembl; ENST00000933889.1; ENSP00000603948.1; ENSG00000221867.10. DR GeneID; 4102; -. DR KEGG; hsa:4102; -. DR MANE-Select; ENST00000370278.4; ENSP00000359301.3; NM_005362.4; NP_005353.1. DR UCSC; uc033faf.1; human. DR AGR; HGNC:6801; -. DR ClinPGx; PA30547; -. DR CTD; 4102; -. DR DisGeNET; 4102; -. DR GeneCards; MAGEA3; -. DR HGNC; HGNC:6801; MAGEA3. DR HPA; ENSG00000221867; Tissue enriched (testis). DR MIM; 300174; gene. DR OpenTargets; ENSG00000221867; -. DR VEuPathDB; HostDB:ENSG00000221867; -. DR eggNOG; KOG4562; Eukaryota. DR GeneTree; ENSGT00940000164672; -. DR HOGENOM; CLU_039582_1_2_1; -. DR InParanoid; P43357; -. DR OrthoDB; 9536323at2759; -. DR PAN-GO; P43357; 3 GO annotations based on evolutionary models. DR PhylomeDB; P43357; -. DR PathwayCommons; P43357; -. DR SignaLink; P43357; -. DR SIGNOR; P43357; -. DR Agora; ENSG00000221867; -. DR BioGRID-ORCS; 4102; 6 hits in 680 CRISPR screens. DR ChiTaRS; MAGEA3; human. DR EvolutionaryTrace; P43357; -. DR GeneWiki; MAGEA3; -. DR GenomeRNAi; 4102; -. DR Pharos; P43357; Tbio. DR PRO; PR:P43357; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P43357; protein. DR Bgee; ENSG00000221867; Expressed in primordial germ cell in gonad and 33 other cell types or tissues. DR ExpressionAtlas; P43357; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0089720; F:caspase binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central. DR GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB. DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0010955; P:negative regulation of protein processing; IDA:ParkinsonsUK-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR FunFam; 1.10.10.1200:FF:000002; MAGE family member A11; 1. DR FunFam; 1.10.10.1210:FF:000001; melanoma-associated antigen D1; 1. 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; IPR021072; MAGE_N. DR InterPro; IPR041898; MAGE_WH1. DR InterPro; IPR041899; MAGE_WH2. DR InterPro; IPR002190; MHD_dom. DR PANTHER; PTHR11736:SF60; MELANOMA-ASSOCIATED ANTIGEN 3-RELATED; 1. DR PANTHER; PTHR11736; MELANOMA-ASSOCIATED ANTIGEN MAGE ANTIGEN; 1. DR Pfam; PF01454; MAGE; 1. DR Pfam; PF12440; MAGE_N; 1. DR SMART; SM01373; MAGE; 1. DR SMART; SM01392; MAGE_N; 1. DR PROSITE; PS50838; MAGE; 1. DR PDBsum; 1QEW; -. DR PDBsum; 4V0P; -. DR PDBsum; 5BRZ; -. DR PDBsum; 8T9A; -. DR PDBsum; 9BD2; -. DR PDBsum; 9YTF; -. PE 1: Evidence at protein level; KW 3D-structure; Proteomics identification; Reference proteome; Tumor antigen; KW Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..314 FT /note="Melanoma-associated antigen 3" FT /id="PRO_0000156703" FT DOMAIN 109..308 FT /note="MAGE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127" FT REGION 1..99 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..44 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 65..87 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 170 FT /note="D->A: Abolishes HLA-A1 binding." FT /evidence="ECO:0000269|PubMed:8113684" FT MUTAGEN 176 FT /note="Y->A: Abolishes HLA-A1 binding." FT /evidence="ECO:0000269|PubMed:8113684" FT MUTAGEN 314 FT /note="E->EDNYNEPKANQ: Abolished recognition by the FT DCX(DCAF12) complex and ubiquitination." FT /evidence="ECO:0000269|PubMed:31267705" FT HELIX 104..126 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 132..138 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 141..146 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 147..162 FT /evidence="ECO:0007829|PDB:4V0P" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:4V0P" FT TURN 171..174 FT /evidence="ECO:0007829|PDB:4V0P" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 199..212 FT /evidence="ECO:0007829|PDB:4V0P" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:9BD2" FT HELIX 218..225 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 242..252 FT /evidence="ECO:0007829|PDB:4V0P" FT STRAND 255..260 FT /evidence="ECO:0007829|PDB:4V0P" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 275..280 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 283..292 FT /evidence="ECO:0007829|PDB:4V0P" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 301..303 FT /evidence="ECO:0007829|PDB:4V0P" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:4V0P" SQ SEQUENCE 314 AA; 34747 MW; 3F5EB13D1C9946A1 CRC64; MPLEQRSQHC KPEEGLEARG EALGLVGAQA PATEEQEAAS SSSTLVEVTL GEVPAAESPD PPQSPQGASS LPTTMNYPLW SQSYEDSSNQ EEEGPSTFPD LESEFQAALS RKVAELVHFL LLKYRAREPV TKAEMLGSVV GNWQYFFPVI FSKASSSLQL VFGIELMEVD PIGHLYIFAT CLGLSYDGLL GDNQIMPKAG LLIIVLAIIA REGDCAPEEK IWEELSVLEV FEGREDSILG DPKKLLTQHF VQENYLEYRQ VPGSDPACYE FLWGPRALVE TSYVKVLHHM VKISGGPHIS YPPLHEWVLR EGEE //