MAGF1_HUMAN
ID MAGF1_HUMAN Reviewed; 307 AA.
AC Q9HAY2; Q9H215;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Melanoma-associated antigen F1 {ECO:0000305};
DE Short=MAGE-F1 {ECO:0000303|PubMed:11313144, ECO:0000303|PubMed:29225034};
DE AltName: Full=MAGE-F1 antigen;
GN Name=MAGEF1 {ECO:0000312|HGNC:HGNC:29639};
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], AND TISSUE SPECIFICITY.
RX PubMed=11313144; DOI=10.1016/s0378-1119(01)00406-1;
RA Stone B., Schummer M., Paley P.J., Crawford M., Ford M., Urban N.,
RA Nelson B.H.;
RT "MAGE-F1, a novel ubiquitously expressed member of the MAGE superfamily.";
RL Gene 267:173-182(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-283.
RC TISSUE=Kidney;
RX PubMed=11454705;
RA Chomez P., De Backer O., Bertrand M., De Plaen E., Boon T., Lucas S.;
RT "An overview of the MAGE gene family with the identification of all human
RT members of the family.";
RL Cancer Res. 61:5544-5551(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH LNX1; TRIM27 AND NSMCE1.
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 [6]
RP FUNCTION, INTERACTION WITH NSMCE1, AND MUTAGENESIS OF 87-LYS-LYS-88.
RX PubMed=29225034; DOI=10.1016/j.molcel.2017.11.010;
RA Weon J.L., Yang S.W., Potts P.R.;
RT "Cytosolic Iron-Sulfur Assembly Is Evolutionarily Tuned by a Cancer-
RT Amplified Ubiquitin Ligase.";
RL Mol. Cell 69:113-125(2018).
CC -!- FUNCTION: Enhances ubiquitin ligase activity of RING-type zinc finger-
CC containing E3 ubiquitin ligases. Proposed to act through recruitment
CC and/or stabilization of the E2 ubiquitin-conjugating enzyme at the
CC E3:substrate complex. MAGEF1-NSMCE1 ubiquitin ligase complex promotes
CC proteasomal degradation of MMS19, a key component of the cytosolic
CC iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19
CC impairs the activity of several DNA repair and metabolism enzymes such
CC as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters
CC as cofactors. May negatively regulate genome integrity by inhibiting
CC homologous recombination-mediated double-strand break DNA repair
CC (PubMed:29225034). {ECO:0000269|PubMed:20864041,
CC ECO:0000269|PubMed:29225034}.
CC -!- SUBUNIT: Interacts (via MAGE domain) with RING-type zinc finger-
CC containing E3 ubiquitin-protein ligases LNX1, TRIM27 and NSMCE1; the
CC interaction is direct. {ECO:0000269|PubMed:20864041,
CC ECO:0000269|PubMed:29225034}.
CC -!- INTERACTION:
CC Q9HAY2; Q99750: MDFI; NbExp=4; IntAct=EBI-5525855, EBI-724076;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11313144}.
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DR EMBL; AF295378; AAG30208.1; -; mRNA.
DR EMBL; AC107294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010056; AAH10056.1; -; mRNA.
DR EMBL; AF320910; AAG38606.1; -; mRNA.
DR CCDS; CCDS3269.1; -.
DR RefSeq; NP_071432.2; NM_022149.4.
DR AlphaFoldDB; Q9HAY2; -.
DR SMR; Q9HAY2; -.
DR BioGRID; 122067; 35.
DR IntAct; Q9HAY2; 6.
DR STRING; 9606.ENSP00000315064; -.
DR iPTMnet; Q9HAY2; -.
DR PhosphoSitePlus; Q9HAY2; -.
DR BioMuta; MAGEF1; -.
DR DMDM; 300669649; -.
DR EPD; Q9HAY2; -.
DR MassIVE; Q9HAY2; -.
DR PaxDb; Q9HAY2; -.
DR PeptideAtlas; Q9HAY2; -.
DR PRIDE; Q9HAY2; -.
DR ProteomicsDB; 81457; -.
DR Antibodypedia; 33826; 167 antibodies from 28 providers.
DR DNASU; 64110; -.
DR Ensembl; ENST00000317897.5; ENSP00000315064.3; ENSG00000177383.5.
DR GeneID; 64110; -.
DR KEGG; hsa:64110; -.
DR MANE-Select; ENST00000317897.5; ENSP00000315064.3; NM_022149.5; NP_071432.2.
DR UCSC; uc003fpa.4; human.
DR CTD; 64110; -.
DR DisGeNET; 64110; -.
DR GeneCards; MAGEF1; -.
DR HGNC; HGNC:29639; MAGEF1.
DR HPA; ENSG00000177383; Low tissue specificity.
DR MIM; 609267; gene.
DR neXtProt; NX_Q9HAY2; -.
DR OpenTargets; ENSG00000177383; -.
DR PharmGKB; PA134920978; -.
DR VEuPathDB; HostDB:ENSG00000177383; -.
DR eggNOG; KOG4562; Eukaryota.
DR GeneTree; ENSGT00940000163736; -.
DR HOGENOM; CLU_039582_2_0_1; -.
DR InParanoid; Q9HAY2; -.
DR OMA; TNPPEYE; -.
DR OrthoDB; 1195799at2759; -.
DR PhylomeDB; Q9HAY2; -.
DR TreeFam; TF328505; -.
DR PathwayCommons; Q9HAY2; -.
DR SignaLink; Q9HAY2; -.
DR BioGRID-ORCS; 64110; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; MAGEF1; human.
DR GenomeRNAi; 64110; -.
DR Pharos; Q9HAY2; Tdark.
DR PRO; PR:Q9HAY2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HAY2; protein.
DR Bgee; ENSG00000177383; Expressed in ganglionic eminence and 191 other tissues.
DR Genevisible; Q9HAY2; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA: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; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR Pfam; PF01454; MAGE; 1.
DR SMART; SM01373; MAGE; 1.
DR PROSITE; PS50838; MAGE; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Tumor antigen; Ubl conjugation pathway.
FT CHAIN 1..307
FT /note="Melanoma-associated antigen F1"
FT /id="PRO_0000156732"
FT DOMAIN 76..277
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 93
FT /note="K -> R (in dbSNP:rs34540780)"
FT /id="VAR_057651"
FT MUTAGEN 87..88
FT /note="Missing: Loss of interaction with NSMCE1."
FT /evidence="ECO:0000269|PubMed:29225034"
FT CONFLICT 66
FT /note="A -> S (in Ref. 1; AAG30208, 2; AAG38606 and 3;
FT AAH10056)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="E -> EE (in Ref. 1; AAG30208, 2; AAG38606 and 3;
FT AAH10056)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="E -> A (in Ref. 1; AAG30208, 2; AAG38606 and 3;
FT AAH10056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35222 MW; 8CB673B3FF7921EE CRC64;
MLQTPESRGL PVPQAEGEKD GGHDGETRAP TASQERPKEE LGAGREEGAA EPALTRKGAR
ALAAKALARR RAYRRLNRTV AELVQFLLVK DKKKSPITRS EMVKYVIGDL KILFPDIIAR
AAEHLRYVFG FELKQFDRKH HTYILINKLK PLEEEEEEDL GGDGPRLGLL MMILGLIYMR
GNSAREAQVW EMLRRLGVQP SKYHFLFGYP KRLIMEDFVQ QRYLSYRRVP HTNPPEYEFS
WGPRSNLEIS KMEVLGFVAK LHKKEPQHWP VQYREALADE ADRARAKARA EASMRARASA
RAGIHLW
