ID   MAGA4_HUMAN             Reviewed;         317 AA.
AC   P43358; Q14798;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   02-SEP-2026, entry version 195.
DE   RecName: Full=Melanoma-associated antigen 4;
DE   AltName: Full=Cancer/testis antigen 1.4;
DE            Short=CT1.4;
DE   AltName: Full=MAGE-4 antigen;
DE   AltName: Full=MAGE-41 antigen;
DE   AltName: Full=MAGE-X2 antigen;
GN   Name=MAGEA4; Synonyms=MAGE4;
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], AND VARIANT THR-173.
RC   TISSUE=Blood;
RX   PubMed=7927540; DOI=10.1007/bf01246677;
RA   De Plaen E., Arden K., Traversari C., Gaforio J.J., Szikora J.-P.,
RA   De Smet C., Brasseur F., van der Bruggen P., Lethe B.G., Lurquin C.,
RA   Brasseur R., Chomez P., de Backer O., Cavenee W., Boon T.;
RT   "Structure, chromosomal localization, and expression of 12 genes of the
RT   MAGE family.";
RL   Immunogenetics 40:360-369(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-173.
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 [MRNA], AND VARIANT THR-173.
RX   PubMed=7642112; DOI=10.1016/0378-1119(94)00680-q;
RA   Imai Y., Shichijo S., Yamada A., Katayama T., Yano H., Itoh K.;
RT   "Sequence analysis of the MAGE gene family encoding human tumor-rejection
RT   antigens.";
RL   Gene 160:287-290(1995).
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], AND VARIANT THR-173.
RC   TISSUE=Duodenum;
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   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   [7]
RP   FUNCTION.
RX   PubMed=22842486; DOI=10.3892/or.2012.1934;
RA   Bhan S., Chuang A., Negi S.S., Glazer C.A., Califano J.A.;
RT   "MAGEA4 induces growth in normal oral keratinocytes by inhibiting growth
RT   arrest and apoptosis.";
RL   Oncol. Rep. 28:1498-1502(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 230-239.
RX   PubMed=11502003; DOI=10.1006/jmbi.2001.4816;
RA   Hillig R.C., Coulie P.G., Stroobant V., Saenger W., Ziegler A.,
RA   Hulsmeyer M.;
RT   "High-resolution structure of HLA-A*0201 in complex with a tumour-specific
RT   antigenic peptide encoded by the MAGE-A4 gene.";
RL   J. Mol. Biol. 310:1167-1176(2001).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-153.
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).
RN   [10]
RP   VARIANT GLN-137.
RX   PubMed=23092983; DOI=10.1038/tp.2012.102;
RA   Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA   Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA   Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA   Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA   Brice A., Depienne C.;
RT   "Analysis of the chromosome X exome in patients with autism spectrum
RT   disorders identified novel candidate genes, including TMLHE.";
RL   Transl. Psychiatry 2:E179-E179(2012).
RN   [11]
RP   VARIANT GLU-230.
RX   PubMed=28229514; DOI=10.1002/humu.23200;
RA   Imagawa E., Higashimoto K., Sakai Y., Numakura C., Okamoto N.,
RA   Matsunaga S., Ryo A., Sato Y., Sanefuji M., Ihara K., Takada Y.,
RA   Nishimura G., Saitsu H., Mizuguchi T., Miyatake S., Nakashima M.,
RA   Miyake N., Soejima H., Matsumoto N.;
RT   "Mutations in genes encoding polycomb repressive complex 2 subunits cause
RT   Weaver syndrome.";
RL   Hum. Mutat. 38:637-648(2017).
CC   -!- FUNCTION: Regulates cell proliferation through the inhibition of cell
CC       cycle arrest at the G1 phase (PubMed:22842486). Also negatively
CC       regulates p53-mediated apoptosis (PubMed:22842486).
CC       {ECO:0000269|PubMed:22842486}.
CC   -!- INTERACTION:
CC       P43358; A2BDD9: AMOT; NbExp=5; IntAct=EBI-743122, EBI-17286414;
CC       P43358; Q4VCS5: AMOT; NbExp=4; IntAct=EBI-743122, EBI-2511319;
CC       P43358; P10176: COX8A; NbExp=3; IntAct=EBI-743122, EBI-3904738;
CC       P43358; Q8N4P3-2: HDDC3; NbExp=3; IntAct=EBI-743122, EBI-12037393;
CC       P43358; Q5SW96: LDLRAP1; NbExp=3; IntAct=EBI-743122, EBI-747813;
CC       P43358; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-743122, EBI-79165;
CC       P43358; Q9NUX5: POT1; NbExp=2; IntAct=EBI-743122, EBI-752420;
CC       P43358; O75832: PSMD10; NbExp=5; IntAct=EBI-743122, EBI-752185;
CC       P43358; Q08623: PUDP; NbExp=3; IntAct=EBI-743122, EBI-12807240;
CC       P43358; Q9NS91: RAD18; NbExp=7; IntAct=EBI-743122, EBI-2339393;
CC       P43358; Q8WW24: TEKT4; NbExp=7; IntAct=EBI-743122, EBI-750487;
CC       P43358; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-743122, EBI-749955;
CC       P43358; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-743122, EBI-11525489;
CC       P43358; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-743122, EBI-723389;
CC       P43358; Q9UJ04: TSPYL4; NbExp=9; IntAct=EBI-743122, EBI-308511;
CC       P43358; Q99757: TXN2; NbExp=3; IntAct=EBI-743122, EBI-2932492;
CC       P43358; Q9BZV1: UBXN6; NbExp=4; IntAct=EBI-743122, EBI-1993899;
CC       P43358; P14927: UQCRB; NbExp=8; IntAct=EBI-743122, EBI-743128;
CC       P43358; Q2YD98: UVSSA; NbExp=3; IntAct=EBI-743122, EBI-11153331;
CC       P43358; Q13105: ZBTB17; NbExp=5; IntAct=EBI-743122, EBI-372156;
CC       P43358; Q9H609: ZNF576; NbExp=5; IntAct=EBI-743122, EBI-3921014;
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.
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DR   EMBL; U10687; AAA68871.1; -; Genomic_DNA.
DR   EMBL; U10688; AAA68872.1; -; Genomic_DNA.
DR   EMBL; U10340; AAA19007.1; -; mRNA.
DR   EMBL; D32075; BAA06841.1; -; mRNA.
DR   EMBL; D32077; BAA06843.1; -; mRNA.
DR   EMBL; AF274855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017723; AAH17723.1; -; mRNA.
DR   CCDS; CCDS14702.1; -.
DR   PIR; I38661; I38661.
DR   RefSeq; NP_001011548.1; NM_001011548.1.
DR   RefSeq; NP_001011549.1; NM_001011549.1.
DR   RefSeq; NP_001011550.1; NM_001011550.1.
DR   RefSeq; NP_001373125.1; NM_001386196.1.
DR   RefSeq; NP_001373126.1; NM_001386197.1.
DR   RefSeq; NP_001373127.1; NM_001386198.1.
DR   RefSeq; NP_001373128.1; NM_001386199.1.
DR   RefSeq; NP_001373129.1; NM_001386200.1.
DR   RefSeq; NP_001373131.1; NM_001386202.1.
DR   RefSeq; NP_001373132.1; NM_001386203.1.
DR   RefSeq; NP_002353.3; NM_002362.4.
DR   RefSeq; XP_054183033.1; XM_054327058.1.
DR   PDB; 1I4F; X-ray; 1.40 A; C=230-239.
DR   PDB; 2WA0; X-ray; 2.30 A; A=99-317.
DR   PDB; 6TRN; X-ray; 1.35 A; C=230-239.
DR   PDB; 6TRO; X-ray; 3.00 A; C=230-239.
DR   PDB; 7UOA; X-ray; 3.50 A; A=101-317.
DR   PDB; 8ES8; EM; 2.65 A; P=230-239.
DR   PDB; 8ES9; EM; 3.25 A; P=230-239.
DR   PDB; 8FJA; EM; 3.00 A; C=230-239.
DR   PDB; 9BD3; X-ray; 2.58 A; A/C=101-317.
DR   AlphaFoldDB; P43358; -.
DR   EMDB; EMD-28571; -.
DR   EMDB; EMD-28572; -.
DR   EMDB; EMD-29220; -.
DR   SMR; P43358; -.
DR   BioGRID; 110277; 60.
DR   FunCoup; P43358; 1.
DR   IntAct; P43358; 49.
DR   MINT; P43358; -.
DR   NDEx; MUSIC2-C5177-MAGEA4; Osteosarcoma (U2OS) cell map - C5177 (84 proteins).
DR   STRING; 9606.ENSP00000353379; -.
DR   BindingDB; P43358; -.
DR   ChEMBL; CHEMBL4296022; -.
DR   GlyGen; P43358; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P43358; -.
DR   PhosphoSitePlus; P43358; -.
DR   BioMuta; MAGEA4; -.
DR   DMDM; 322510046; -.
DR   jPOST; P43358; -.
DR   MassIVE; P43358; -.
DR   PaxDb; 9606-ENSP00000353379; -.
DR   PeptideAtlas; P43358; -.
DR   ProteomicsDB; 55620; -.
DR   Pumba; P43358; -.
DR   ABCD; P43358; 130 sequenced antibodies.
DR   Antibodypedia; 17051; 401 antibodies from 34 providers.
DR   CPTC; P43358; 3 antibodies.
DR   DNASU; 4103; -.
DR   Ensembl; ENST00000276344.6; ENSP00000276344.2; ENSG00000147381.13.
DR   Ensembl; ENST00000360243.6; ENSP00000353379.2; ENSG00000147381.13.
DR   Ensembl; ENST00000370335.5; ENSP00000359360.1; ENSG00000147381.13.
DR   Ensembl; ENST00000370340.7; ENSP00000359365.3; ENSG00000147381.13.
DR   Ensembl; ENST00000393920.6; ENSP00000377497.1; ENSG00000147381.13.
DR   Ensembl; ENST00000393921.6; ENSP00000377498.1; ENSG00000147381.13.
DR   Ensembl; ENST00000430273.6; ENSP00000394149.2; ENSG00000147381.13.
DR   Ensembl; ENST00000457310.6; ENSP00000402186.2; ENSG00000147381.13.
DR   Ensembl; ENST00000682265.1; ENSP00000506838.1; ENSG00000147381.13.
DR   Ensembl; ENST00000684668.1; ENSP00000507023.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911914.1; ENSP00000581973.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911915.1; ENSP00000581974.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911916.1; ENSP00000581975.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911917.1; ENSP00000581976.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911918.1; ENSP00000581977.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911919.1; ENSP00000581978.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911920.1; ENSP00000581979.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911921.1; ENSP00000581980.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911922.1; ENSP00000581981.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911923.1; ENSP00000581982.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911924.1; ENSP00000581983.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911925.1; ENSP00000581984.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911926.1; ENSP00000581985.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911927.1; ENSP00000581986.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911928.1; ENSP00000581987.1; ENSG00000147381.13.
DR   Ensembl; ENST00000911929.1; ENSP00000581988.1; ENSG00000147381.13.
DR   GeneID; 4103; -.
DR   KEGG; hsa:4103; -.
DR   MANE-Select; ENST00000276344.6; ENSP00000276344.2; NM_001011548.1; NP_001011548.1.
DR   UCSC; uc004ffa.3; human.
DR   AGR; HGNC:6802; -.
DR   CIViC; 4103; 1 evidence item across 3 molecular profiles.
DR   ClinPGx; PA30548; -.
DR   CTD; 4103; -.
DR   DisGeNET; 4103; -.
DR   GeneCards; MAGEA4; -.
DR   HGNC; HGNC:6802; MAGEA4.
DR   HPA; ENSG00000147381; Tissue enriched (testis).
DR   MIM; 300175; gene.
DR   OpenTargets; ENSG00000147381; -.
DR   VEuPathDB; HostDB:ENSG00000147381; -.
DR   eggNOG; KOG4562; Eukaryota.
DR   GeneTree; ENSGT00940000166837; -.
DR   HOGENOM; CLU_039582_1_2_1; -.
DR   InParanoid; P43358; -.
DR   OMA; VNFTCWR; -.
DR   OrthoDB; 9665809at2759; -.
DR   PAN-GO; P43358; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P43358; -.
DR   PathwayCommons; P43358; -.
DR   SignaLink; P43358; -.
DR   Agora; ENSG00000147381; -.
DR   BioGRID-ORCS; 4103; 10 hits in 761 CRISPR screens.
DR   CD-CODE; DEE660B4; Stress granule.
DR   ChiTaRS; MAGEA4; human.
DR   EvolutionaryTrace; P43358; -.
DR   GeneWiki; MAGEA4; -.
DR   GenomeRNAi; 4103; -.
DR   Pharos; P43358; Tbio.
DR   PRO; PR:P43358; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P43358; protein.
DR   Bgee; ENSG00000147381; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 54 other cell types or tissues.
DR   ExpressionAtlas; P43358; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
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:SF48; MELANOMA-ASSOCIATED ANTIGEN 4; 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; 1I4F; -.
DR   PDBsum; 2WA0; -.
DR   PDBsum; 6TRN; -.
DR   PDBsum; 6TRO; -.
DR   PDBsum; 7UOA; -.
DR   PDBsum; 8ES8; -.
DR   PDBsum; 8ES9; -.
DR   PDBsum; 8FJA; -.
DR   PDBsum; 9BD3; -.
PE   1: Evidence at protein level;
KW   3D-structure; Proteomics identification; Reference proteome; Tumor antigen.
FT   CHAIN           1..317
FT                   /note="Melanoma-associated antigen 4"
FT                   /id="PRO_0000156704"
FT   DOMAIN          110..309
FT                   /note="MAGE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..14
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         137
FT                   /note="L -> Q (in dbSNP:rs1224431639)"
FT                   /evidence="ECO:0000269|PubMed:23092983"
FT                   /id="VAR_076262"
FT   VARIANT         153
FT                   /note="G -> D (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036582"
FT   VARIANT         173
FT                   /note="A -> T (in dbSNP:rs1047251)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:7642112, ECO:0000269|PubMed:7927540,
FT                   ECO:0000269|PubMed:8037761"
FT                   /id="VAR_004284"
FT   VARIANT         230
FT                   /note="G -> E (in dbSNP:rs773875619)"
FT                   /evidence="ECO:0000269|PubMed:28229514"
FT                   /id="VAR_078319"
FT   CONFLICT        3
FT                   /note="S -> L (in Ref. 3; BAA06841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="P -> L (in Ref. 3; BAA06841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="E -> K (in Ref. 3; BAA06841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="G -> D (in Ref. 3; BAA06841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95..96
FT                   /note="GP -> EA (in Ref. 3; BAA06841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="E -> Q (in Ref. 2; AAA19007)"
FT                   /evidence="ECO:0000305"
FT   HELIX           102..126
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:7UOA"
FT   HELIX           133..139
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:7UOA"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           148..158
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           159..163
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   TURN            172..175
FT                   /evidence="ECO:0007829|PDB:9BD3"
FT   STRAND          176..181
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           200..213
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:7UOA"
FT   HELIX           219..228
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   TURN            238..240
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           246..250
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           276..281
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           284..295
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           297..300
FT                   /evidence="ECO:0007829|PDB:7UOA"
FT   HELIX           301..304
FT                   /evidence="ECO:0007829|PDB:2WA0"
FT   HELIX           305..309
FT                   /evidence="ECO:0007829|PDB:2WA0"
SQ   SEQUENCE   317 AA;  34899 MW;  C6AA2EE306963E7D CRC64;
     MSSEQKSQHC KPEEGVEAQE EALGLVGAQA PTTEEQEAAV SSSSPLVPGT LEEVPAAESA
     GPPQSPQGAS ALPTTISFTC WRQPNEGSSS QEEEGPSTSP DAESLFREAL SNKVDELAHF
     LLRKYRAKEL VTKAEMLERV IKNYKRCFPV IFGKASESLK MIFGIDVKEV DPASNTYTLV
     TCLGLSYDGL LGNNQIFPKT GLLIIVLGTI AMEGDSASEE EIWEELGVMG VYDGREHTVY
     GEPRKLLTQD WVQENYLEYR QVPGSNPARY EFLWGPRALA ETSYVKVLEH VVRVNARVRI
     AYPSLREAAL LEEEEGV
//