MAGA2_HUMAN
ID MAGA2_HUMAN Reviewed; 314 AA.
AC P43356; A8K328; Q32NC6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Melanoma-associated antigen 2;
DE AltName: Full=Cancer/testis antigen 1.2;
DE Short=CT1.2;
DE AltName: Full=MAGE-2 antigen;
GN Name=MAGEA2; Synonyms=MAGE2, MAGEA2A;
GN and
GN Name=MAGEA2B; Synonyms=MAGE2, MAGEA2;
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].
RX PubMed=8276455; DOI=10.1007/bf00188615;
RA De Smet C., Lurquin C., van der Bruggen P., De Plaen E., Brasseur F.,
RA Boon T.;
RT "Sequence and expression pattern of the human MAGE2 gene.";
RL Immunogenetics 39:121-129(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [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 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [7]
RP MUTAGENESIS.
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53 AND HDAC3.
RX PubMed=16847267; DOI=10.1073/pnas.0510834103;
RA Monte M., Simonatto M., Peche L.Y., Bublik D.R., Gobessi S., Pierotti M.A.,
RA Rodolfo M., Schneider C.;
RT "MAGE-A tumor antigens target p53 transactivation function through histone
RT deacetylase recruitment and confer resistance to chemotherapeutic agents.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11160-11165(2006).
RN [9]
RP FUNCTION.
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 [10]
RP FUNCTION, AND INTERACTION WITH TRIM28 AND UBE2H.
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
RX PubMed=22117195; DOI=10.1038/cdd.2011.173;
RA Peche L.Y., Scolz M., Ladelfa M.F., Monte M., Schneider C.;
RT "MageA2 restrains cellular senescence by targeting the function of
RT PMLIV/p53 axis at the PML-NBs.";
RL Cell Death Differ. 19:926-936(2012).
CC -!- FUNCTION: Reduces p53/TP53 transactivation function through recruitment
CC of HDAC3 to p53/TP53 transcription sites. Also represses p73/TP73
CC activity. Proposed to enhance ubiquitin ligase activity of RING-type
CC zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances
CC ubiquitin ligase activity of TRIM28 and stimulates p53/TP53
CC ubiquitination by TRIM28 potentially in presence of Ubl-conjugating
CC enzyme UBE2H. Proposed to act through recruitment and/or stabilization
CC of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May
CC play a role in embryonal development and tumor transformation or
CC aspects of tumor progression. In vitro promotes cell viability in
CC melanoma cell lines. Antigen recognized on a melanoma by autologous
CC cytolytic T-lymphocytes. Negatively regulates acetylation and
CC sumoylation of PML and represses PML-induced p53/TP53 acetylation and
CC activation. {ECO:0000269|PubMed:16847267, ECO:0000269|PubMed:17942928,
CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:22117195}.
CC -!- SUBUNIT: Interacts with TRIM28 and UBE2H. Interacts with HDAC3.
CC Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3,
CC isoform PML-4 and isoform PML-5). {ECO:0000269|PubMed:16847267,
CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:22117195}.
CC -!- INTERACTION:
CC P43356; Q08AH1: ACSM1; NbExp=3; IntAct=EBI-5650739, EBI-2818055;
CC P43356; O43865: AHCYL1; NbExp=3; IntAct=EBI-5650739, EBI-2371423;
CC P43356; Q5TZF3-1: ANKRD45; NbExp=3; IntAct=EBI-5650739, EBI-22011535;
CC P43356; Q9HBH7: BEX1; NbExp=3; IntAct=EBI-5650739, EBI-7162175;
CC P43356; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-5650739, EBI-745073;
CC P43356; P27797: CALR; NbExp=3; IntAct=EBI-5650739, EBI-1049597;
CC P43356; Q8N715: CCDC185; NbExp=3; IntAct=EBI-5650739, EBI-740814;
CC P43356; P12830: CDH1; NbExp=3; IntAct=EBI-5650739, EBI-727477;
CC P43356; Q15078: CDK5R1; NbExp=3; IntAct=EBI-5650739, EBI-746189;
CC P43356; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-5650739, EBI-11752486;
CC P43356; Q9Y3A0: COQ4; NbExp=3; IntAct=EBI-5650739, EBI-12284865;
CC P43356; P15954: COX7C; NbExp=3; IntAct=EBI-5650739, EBI-2606678;
CC P43356; P36957: DLST; NbExp=3; IntAct=EBI-5650739, EBI-351007;
CC P43356; Q9NP97: DYNLRB1; NbExp=3; IntAct=EBI-5650739, EBI-372128;
CC P43356; O15379: HDAC3; NbExp=4; IntAct=EBI-5650739, EBI-607682;
CC P43356; O95983-2: MBD3; NbExp=3; IntAct=EBI-5650739, EBI-11978579;
CC P43356; P19404: NDUFV2; NbExp=3; IntAct=EBI-5650739, EBI-713665;
CC P43356; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-5650739, EBI-1055945;
CC P43356; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-5650739, EBI-741158;
CC P43356; Q7Z4N8: P4HA3; NbExp=4; IntAct=EBI-5650739, EBI-10181968;
CC P43356; P15735: PHKG2; NbExp=3; IntAct=EBI-5650739, EBI-1383819;
CC P43356; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-5650739, EBI-10320765;
CC P43356; P62191: PSMC1; NbExp=3; IntAct=EBI-5650739, EBI-357598;
CC P43356; Q99719: SEPTIN5; NbExp=4; IntAct=EBI-5650739, EBI-373345;
CC P43356; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-5650739, EBI-358489;
CC P43356; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-5650739, EBI-2509913;
CC P43356; P04637: TP53; NbExp=7; IntAct=EBI-5650739, EBI-366083;
CC P43356; Q13263: TRIM28; NbExp=6; IntAct=EBI-5650739, EBI-78139;
CC P43356; P62256: UBE2H; NbExp=2; IntAct=EBI-5650739, EBI-2129909;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body.
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.
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DR EMBL; L18920; AAA17729.1; -; Genomic_DNA.
DR EMBL; AK290443; BAF83132.1; -; mRNA.
DR EMBL; U82671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471169; EAW99429.1; -; Genomic_DNA.
DR EMBL; BC108720; AAI08721.1; -; mRNA.
DR EMBL; BC112158; AAI12159.1; -; mRNA.
DR EMBL; BC112160; AAI12161.1; -; mRNA.
DR CCDS; CCDS76046.1; -.
DR CCDS; CCDS76049.1; -.
DR PIR; I68889; I68889.
DR RefSeq; NP_001269430.1; NM_001282501.1.
DR RefSeq; NP_001269431.1; NM_001282502.1.
DR RefSeq; NP_001269433.1; NM_001282504.1.
DR RefSeq; NP_001269434.1; NM_001282505.1.
DR RefSeq; NP_001308329.1; NM_001321400.1.
DR RefSeq; NP_001308330.1; NM_001321401.1.
DR RefSeq; NP_001308331.1; NM_001321402.1.
DR RefSeq; NP_001308332.1; NM_001321403.1.
DR RefSeq; NP_001308333.1; NM_001321404.1.
DR RefSeq; NP_005352.1; NM_005361.3.
DR RefSeq; NP_705692.1; NM_153488.4.
DR RefSeq; NP_786884.1; NM_175742.2.
DR RefSeq; NP_786885.1; NM_175743.2.
DR RefSeq; XP_016884895.1; XM_017029406.1.
DR RefSeq; XP_016885008.1; XM_017029519.1.
DR AlphaFoldDB; P43356; -.
DR SMR; P43356; -.
DR BioGRID; 110275; 34.
DR BioGRID; 129334; 27.
DR DIP; DIP-61231N; -.
DR IntAct; P43356; 31.
DR STRING; 9606.ENSP00000333487; -.
DR GlyConnect; 1497; 7 N-Linked glycans (1 site).
DR GlyGen; P43356; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; P43356; -.
DR PhosphoSitePlus; P43356; -.
DR BioMuta; MAGEA2B; -.
DR DMDM; 1170856; -.
DR jPOST; P43356; -.
DR MassIVE; P43356; -.
DR MaxQB; P43356; -.
DR PaxDb; P43356; -.
DR PeptideAtlas; P43356; -.
DR PRIDE; P43356; -.
DR ProteomicsDB; 55618; -.
DR Antibodypedia; 30741; 56 antibodies from 18 providers.
DR Antibodypedia; 73570; 100 antibodies from 13 providers.
DR DNASU; 4101; -.
DR Ensembl; ENST00000331220.6; ENSP00000333487.2; ENSG00000183305.14.
DR Ensembl; ENST00000370293.6; ENSP00000359316.2; ENSG00000183305.14.
DR Ensembl; ENST00000595583.5; ENSP00000470872.1; ENSG00000268606.6.
DR Ensembl; ENST00000598543.5; ENSP00000469919.1; ENSG00000268606.6.
DR Ensembl; ENST00000611557.4; ENSP00000480738.1; ENSG00000268606.6.
DR Ensembl; ENST00000611674.4; ENSP00000480491.1; ENSG00000268606.6.
DR Ensembl; ENST00000620710.4; ENSP00000484290.1; ENSG00000268606.6.
DR Ensembl; ENST00000623438.3; ENSP00000485391.1; ENSG00000268606.6.
DR Ensembl; ENST00000623806.3; ENSP00000485541.1; ENSG00000268606.6.
DR Ensembl; ENST00000682532.1; ENSP00000507594.1; ENSG00000183305.14.
DR Ensembl; ENST00000684311.1; ENSP00000507899.1; ENSG00000268606.6.
DR GeneID; 266740; -.
DR GeneID; 4101; -.
DR KEGG; hsa:266740; -.
DR KEGG; hsa:4101; -.
DR MANE-Select; ENST00000682532.1; ENSP00000507594.1; NM_001386132.1; NP_001373061.1.
DR MANE-Select; ENST00000684311.1; ENSP00000507899.1; NM_001386130.2; NP_001373059.1.
DR UCSC; uc004fgg.3; human.
DR CTD; 266740; -.
DR CTD; 4101; -.
DR DisGeNET; 266740; -.
DR DisGeNET; 4101; -.
DR GeneCards; MAGEA2; -.
DR GeneCards; MAGEA2B; -.
DR HGNC; HGNC:6800; MAGEA2.
DR HGNC; HGNC:19340; MAGEA2B.
DR HPA; ENSG00000183305; Tissue enriched (testis).
DR HPA; ENSG00000268606; Tissue enriched (testis).
DR MIM; 300173; gene.
DR MIM; 300549; gene.
DR neXtProt; NX_P43356; -.
DR OpenTargets; ENSG00000183305; -.
DR PharmGKB; PA30546; -.
DR VEuPathDB; HostDB:ENSG00000183305; -.
DR VEuPathDB; HostDB:ENSG00000268606; -.
DR eggNOG; KOG4562; Eukaryota.
DR GeneTree; ENSGT00940000164673; -.
DR HOGENOM; CLU_039582_1_1_1; -.
DR InParanoid; P43356; -.
DR OrthoDB; 1195799at2759; -.
DR PhylomeDB; P43356; -.
DR TreeFam; TF328505; -.
DR PathwayCommons; P43356; -.
DR SignaLink; P43356; -.
DR BioGRID-ORCS; 266740; 14 hits in 603 CRISPR screens.
DR BioGRID-ORCS; 4101; 63 hits in 586 CRISPR screens.
DR ChiTaRS; MAGEA2B; human.
DR GeneWiki; MAGEA2; -.
DR Pharos; P43356; Tbio.
DR PRO; PR:P43356; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P43356; protein.
DR Bgee; ENSG00000183305; Expressed in testis and 50 other tissues.
DR ExpressionAtlas; P43356; baseline and differential.
DR Genevisible; P43356; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IDA:UniProtKB.
DR GO; GO:1901984; P:negative regulation of protein acetylation; IDA:UniProtKB.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0072331; P:signal transduction by p53 class mediator; IDA:UniProtKB.
DR Gene3D; 1.10.10.1200; -; 1.
DR Gene3D; 1.10.10.1210; -; 1.
DR InterPro; IPR037445; MAGE.
DR InterPro; IPR021072; MAGE_N.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR030103; MAGEA2.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR PANTHER; PTHR11736:SF74; PTHR11736:SF74; 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.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor antigen; Ubl conjugation pathway.
FT CHAIN 1..314
FT /note="Melanoma-associated antigen 2"
FT /id="PRO_0000156702"
FT DOMAIN 109..308
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43355"
FT MUTAGEN 170
FT /note="V->D: Improves ability to bind to HLA-A1."
FT /evidence="ECO:0000269|PubMed:8113684"
SQ SEQUENCE 314 AA; 35055 MW; 844F16335A2BECE7 CRC64;
MPLEQRSQHC KPEEGLEARG EALGLVGAQA PATEEQQTAS SSSTLVEVTL GEVPAADSPS
PPHSPQGASS FSTTINYTLW RQSDEGSSNQ EEEGPRMFPD LESEFQAAIS RKMVELVHFL
LLKYRAREPV TKAEMLESVL RNCQDFFPVI FSKASEYLQL VFGIEVVEVV PISHLYILVT
CLGLSYDGLL GDNQVMPKTG LLIIVLAIIA IEGDCAPEEK IWEELSMLEV FEGREDSVFA
HPRKLLMQDL VQENYLEYRQ VPGSDPACYE FLWGPRALIE TSYVKVLHHT LKIGGEPHIS
YPPLHERALR EGEE
