MAX_HUMAN
ID MAX_HUMAN Reviewed; 160 AA.
AC P61244; A6NH73; A8K265; A8K4G4; A8K824; P25912; P52163; Q14803; Q96CY8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Protein max {ECO:0000305};
DE AltName: Full=Class D basic helix-loop-helix protein 4;
DE Short=bHLHd4;
DE AltName: Full=Myc-associated factor X {ECO:0000312|HGNC:HGNC:6913};
GN Name=MAX {ECO:0000312|HGNC:HGNC:6913}; Synonyms=BHLHD4;
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] (ISOFORMS 1 AND 2).
RX PubMed=2006410; DOI=10.1126/science.2006410;
RA Blackwood E.M., Eisenman R.N.;
RT "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-
RT binding complex with Myc.";
RL Science 251:1211-1217(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8426752;
RA Vaestrik I., Koskinen P.J., Alitalo R., Maekelae T.P.;
RT "Alternative mRNA forms and open reading frames of the max gene.";
RL Oncogene 8:503-507(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=1566084; DOI=10.1126/science.256.5055.373;
RA Maekelae T.P., Koskinen P.J., Vaestrik I., Alitalo K.;
RT "Alternative forms of Max as enhancers or suppressors of Myc-ras
RT cotransformation.";
RL Science 256:373-377(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Mammary gland, Thalamus, and Thymus;
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=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
RC TISSUE=Brain, Lung, and Uterus;
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 IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MGA; EUHMTASE1; BAT8; CBX3;
RP RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
RX PubMed=12004135; DOI=10.1126/science.1069861;
RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT genes in G0 cells.";
RL Science 296:1132-1136(2002).
RN [9]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [10]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP ACETYLATION AT LYS-66; LYS-153 AND LYS-154, AND MUTAGENESIS OF LYS-66;
RP LYS-153 AND LYS-154.
RX PubMed=17217336; DOI=10.1042/bj20061593;
RA Faiola F., Wu Y.-T., Pan S., Zhang K., Farina A., Martinez E.;
RT "Max is acetylated by p300 at several nuclear localization residues.";
RL Biochem. J. 403:397-407(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND
RP SER-11 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM
RP 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
RP INVOLVEMENT IN PCC, VARIANTS PCC ASN-23; 33-ARG--SER-160 DEL;
RP 75-ARG--SER-160 DEL AND PRO-94, AND VARIANT LEU-142.
RX PubMed=21685915; DOI=10.1038/ng.861;
RA Comino-Mendez I., Gracia-Aznarez F.J., Schiavi F., Landa I.,
RA Leandro-Garcia L.J., Leton R., Honrado E., Ramos-Medina R., Caronia D.,
RA Pita G., Gomez-Grana A., de Cubas A.A., Inglada-Perez L., Maliszewska A.,
RA Taschin E., Bobisse S., Pica G., Loli P., Hernandez-Lavado R., Diaz J.A.,
RA Gomez-Morales M., Gonzalez-Neira A., Roncador G., Rodriguez-Antona C.,
RA Benitez J., Mannelli M., Opocher G., Robledo M., Cascon A.;
RT "Exome sequencing identifies MAX mutations as a cause of hereditary
RT pheochromocytoma.";
RL Nat. Genet. 43:663-667(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM
RP 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP VARIANTS PCC LEU-9; TRP-25; 33-ARG--SER-160 DEL; CYS-35; 47-ARG--SER-52
RP DEL; TRP-60; SER-71; VAL-74; 75-ARG--SER-160 DEL; 82-GLN--SER-160 DEL;
RP PRO-90 AND PRO-102.
RX PubMed=22452945; DOI=10.1158/1078-0432.ccr-12-0160;
RA Burnichon N., Cascon A., Schiavi F., Morales N.P., Comino-Mendez I.,
RA Abermil N., Inglada-Perez L., de Cubas A.A., Amar L., Barontini M.,
RA de Quiros S.B., Bertherat J., Bignon Y.J., Blok M.J., Bobisse S.,
RA Borrego S., Castellano M., Chanson P., Chiara M.D., Corssmit E.P.,
RA Giacche M., de Krijger R.R., Ercolino T., Girerd X., Gomez-Garcia E.B.,
RA Gomez-Grana A., Guilhem I., Hes F.J., Honrado E., Korpershoek E.,
RA Lenders J.W., Leton R., Mensenkamp A.R., Merlo A., Mori L., Murat A.,
RA Pierre P., Plouin P.F., Prodanov T., Quesada-Charneco M., Qin N.,
RA Rapizzi E., Raymond V., Reisch N., Roncador G., Ruiz-Ferrer M., Schillo F.,
RA Stegmann A.P., Suarez C., Taschin E., Timmers H.J., Tops C.M., Urioste M.,
RA Beuschlein F., Pacak K., Mannelli M., Dahia P.L., Opocher G.,
RA Eisenhofer G., Gimenez-Roqueplo A.P., Robledo M.;
RT "MAX mutations cause hereditary and sporadic pheochromocytoma and
RT paraganglioma.";
RL Clin. Cancer Res. 18:2828-2837(2012).
RN [22]
RP VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60;
RP SER-71; VAL-74; PRO-90; PRO-94; PRO-102 AND PRO-102, CHARACTERIZATION OF
RP VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60;
RP SER-71; VAL-74; PRO-90; PRO-94 AND PRO-102, FUNCTION, VARIANTS THR-114 AND
RP LEU-142, AND CHARACTERIZATION OF VARIANTS THR-114 AND LEU-142.
RX PubMed=26070438; DOI=10.1007/s00109-015-1306-y;
RA Comino-Mendez I., Leandro-Garcia L.J., Montoya G., Inglada-Perez L.,
RA de Cubas A.A., Curras-Freixes M., Tysoe C., Izatt L., Leton R.,
RA Gomez-Grana A., Mancikova V., Apellaniz-Ruiz M., Mannelli M., Schiavi F.,
RA Favier J., Gimenez-Roqueplo A.P., Timmers H.J., Roncador G., Garcia J.F.,
RA Rodriguez-Antona C., Robledo M., Cascon A.;
RT "Functional and in silico assessment of MAX variants of unknown
RT significance.";
RL J. Mol. Med. 93:1247-1255(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-107.
RX PubMed=8479534; DOI=10.1038/363038a0;
RA Ferre-D'Amare A.R., Prendergast G.C., Ziff E.B., Burley S.K.;
RT "Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.";
RL Nature 363:38-45(1993).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9115440; DOI=10.1016/s0969-2126(97)00207-4;
RA Brownlie P., Ceska T., Lamers M., Romier C., Stier G., Teo H., Suck D.;
RT "The crystal structure of an intact human Max-DNA complex: new insights
RT into mechanisms of transcriptional control.";
RL Structure 5:509-520(1997).
CC -!- FUNCTION: Transcription regulator. Forms a sequence-specific DNA-
CC binding protein complex with MYC or MAD which recognizes the core
CC sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional
CC activator, whereas the MAD:MAX complex is a repressor. May repress
CC transcription via the recruitment of a chromatin remodeling complex
CC containing H3 'Lys-9' histone methyltransferase activity. Represses MYC
CC transcriptional activity from E-box elements.
CC {ECO:0000269|PubMed:26070438}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MYC or MAD. Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9.
CC The heterodimer MYC:MAX interacts with ABI1; the interaction may
CC enhance MYC:MAX transcriptional activity. {ECO:0000269|PubMed:12004135,
CC ECO:0000269|PubMed:15960975}.
CC -!- INTERACTION:
CC P61244; Q8N9N5: BANP; NbExp=3; IntAct=EBI-751711, EBI-744695;
CC P61244; O75461: E2F6; NbExp=4; IntAct=EBI-751711, EBI-749694;
CC P61244; P29692: EEF1D; NbExp=2; IntAct=EBI-751711, EBI-358607;
CC P61244; Q99814: EPAS1; NbExp=2; IntAct=EBI-751711, EBI-447470;
CC P61244; Q01167: FOXK2; NbExp=4; IntAct=EBI-751711, EBI-2509991;
CC P61244; P02794: FTH1; NbExp=2; IntAct=EBI-751711, EBI-713259;
CC P61244; Q9UBS5: GABBR1; NbExp=3; IntAct=EBI-751711, EBI-724156;
CC P61244; Q969R5: L3MBTL2; NbExp=6; IntAct=EBI-751711, EBI-739909;
CC P61244; P49916: LIG3; NbExp=2; IntAct=EBI-751711, EBI-1753381;
CC P61244; O75367: MACROH2A1; NbExp=2; IntAct=EBI-751711, EBI-2868511;
CC P61244; P51608: MECP2; NbExp=2; IntAct=EBI-751711, EBI-1189067;
CC P61244; Q8IWI9: MGA; NbExp=5; IntAct=EBI-751711, EBI-2815196;
CC P61244; Q05195: MXD1; NbExp=3; IntAct=EBI-751711, EBI-8833637;
CC P61244; P50539: MXI1; NbExp=6; IntAct=EBI-751711, EBI-752241;
CC P61244; P01106: MYC; NbExp=38; IntAct=EBI-751711, EBI-447544;
CC P61244; P04198: MYCN; NbExp=10; IntAct=EBI-751711, EBI-878369;
CC P61244; Q9H8W4: PLEKHF2; NbExp=4; IntAct=EBI-751711, EBI-742388;
CC P61244; P05549: TFAP2A; NbExp=2; IntAct=EBI-751711, EBI-347351;
CC P61244; Q14186: TFDP1; NbExp=5; IntAct=EBI-751711, EBI-749713;
CC P61244; Q9H3U1: UNC45A; NbExp=4; IntAct=EBI-751711, EBI-1048763;
CC P61244; Q8IV63: VRK3; NbExp=2; IntAct=EBI-751711, EBI-1058605;
CC P61244; P18887: XRCC1; NbExp=2; IntAct=EBI-751711, EBI-947466;
CC P61244-2; P50539: MXI1; NbExp=3; IntAct=EBI-10218525, EBI-752241;
CC P61244-2; Q9H3U1: UNC45A; NbExp=3; IntAct=EBI-10218525, EBI-1048763;
CC P61244-4; P28799: GRN; NbExp=3; IntAct=EBI-25848049, EBI-747754;
CC P61244-4; P04792: HSPB1; NbExp=3; IntAct=EBI-25848049, EBI-352682;
CC P61244-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25848049, EBI-10975473;
CC P61244-4; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25848049, EBI-25882629;
CC P61244-4; O60260-5: PRKN; NbExp=3; IntAct=EBI-25848049, EBI-21251460;
CC P61244-4; P60891: PRPS1; NbExp=3; IntAct=EBI-25848049, EBI-749195;
CC P61244-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25848049, EBI-396669;
CC P61244-4; O76024: WFS1; NbExp=3; IntAct=EBI-25848049, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Long;
CC IsoId=P61244-1, P25912-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P61244-2, P25912-2;
CC Sequence=VSP_002117;
CC Name=3; Synonyms=Delta-Max;
CC IsoId=P61244-3, P25912-3;
CC Sequence=VSP_002118;
CC Name=4;
CC IsoId=P61244-4; Sequence=VSP_043183;
CC Name=5;
CC IsoId=P61244-5; Sequence=VSP_043430;
CC Name=6;
CC IsoId=P61244-6; Sequence=VSP_047661;
CC -!- TISSUE SPECIFICITY: High levels found in the brain, heart and lung
CC while lower levels are seen in the liver, kidney and skeletal muscle.
CC -!- PTM: Reversible lysine acetylation might regulate the nuclear-
CC cytoplasmic shuttling of specific Max complexes.
CC {ECO:0000269|PubMed:17217336}.
CC -!- DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-producing
CC tumor of chromaffin tissue of the adrenal medulla or sympathetic
CC paraganglia. The cardinal symptom, reflecting the increased secretion
CC of epinephrine and norepinephrine, is hypertension, which may be
CC persistent or intermittent. {ECO:0000269|PubMed:21685915,
CC ECO:0000269|PubMed:22452945, ECO:0000269|PubMed:26070438}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; M64240; AAA36200.1; -; mRNA.
DR EMBL; M64240; AAA36201.1; -; mRNA.
DR EMBL; X66867; CAA47337.1; -; Genomic_DNA.
DR EMBL; X66867; CAA47338.1; -; Genomic_DNA.
DR EMBL; X66867; CAA47339.1; -; Genomic_DNA.
DR EMBL; X60287; CAA42827.1; -; mRNA.
DR EMBL; AK290130; BAF82819.1; -; mRNA.
DR EMBL; AK290929; BAF83618.1; -; mRNA.
DR EMBL; AK292189; BAF84878.1; -; mRNA.
DR EMBL; AK292630; BAF85319.1; -; mRNA.
DR EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80899.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW80901.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW80903.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW80904.1; -; Genomic_DNA.
DR EMBL; BC003525; AAH03525.1; -; mRNA.
DR EMBL; BC004516; AAH04516.1; -; mRNA.
DR EMBL; BC013669; AAH13669.1; -; mRNA.
DR EMBL; BC027924; AAH27924.1; -; mRNA.
DR CCDS; CCDS41965.1; -. [P61244-3]
DR CCDS; CCDS9770.1; -. [P61244-6]
DR CCDS; CCDS9771.1; -.
DR CCDS; CCDS9772.1; -. [P61244-2]
DR CCDS; CCDS9774.1; -. [P61244-5]
DR PIR; A38431; A38431.
DR PIR; A42611; A42611.
DR PIR; B38431; B38431.
DR PIR; S33118; S33118.
DR RefSeq; NP_001257997.1; NM_001271068.1.
DR RefSeq; NP_002373.3; NM_002382.4. [P61244-1]
DR RefSeq; NP_660087.1; NM_145112.2. [P61244-2]
DR RefSeq; NP_660088.1; NM_145113.2. [P61244-3]
DR RefSeq; NP_660089.1; NM_145114.2. [P61244-5]
DR RefSeq; NP_932061.1; NM_197957.3. [P61244-6]
DR PDB; 1AN2; X-ray; 2.90 A; A=22-107.
DR PDB; 1HLO; X-ray; 2.80 A; A/B=4-92.
DR PDB; 1NKP; X-ray; 1.80 A; B/E=23-102.
DR PDB; 1NLW; X-ray; 2.00 A; B/E=24-99.
DR PDB; 1R05; NMR; -; A/B=22-103.
DR PDB; 5EYO; X-ray; 2.39 A; A/C=22-107.
DR PDB; 6G6J; X-ray; 2.25 A; B/D=22-103.
DR PDB; 6G6K; X-ray; 1.35 A; B/D=22-103.
DR PDB; 6G6L; X-ray; 2.20 A; B/D/F/H=22-103.
DR PDBsum; 1AN2; -.
DR PDBsum; 1HLO; -.
DR PDBsum; 1NKP; -.
DR PDBsum; 1NLW; -.
DR PDBsum; 1R05; -.
DR PDBsum; 5EYO; -.
DR PDBsum; 6G6J; -.
DR PDBsum; 6G6K; -.
DR PDBsum; 6G6L; -.
DR AlphaFoldDB; P61244; -.
DR BMRB; P61244; -.
DR SASBDB; P61244; -.
DR SMR; P61244; -.
DR BioGRID; 110319; 213.
DR ComplexPortal; CPX-104; Transcriptional repressor Mad-Max complex.
DR ComplexPortal; CPX-91; Transcriptional activator Myc-Max complex.
DR CORUM; P61244; -.
DR DIP; DIP-28145N; -.
DR IntAct; P61244; 121.
DR MINT; P61244; -.
DR STRING; 9606.ENSP00000351490; -.
DR BindingDB; P61244; -.
DR ChEMBL; CHEMBL1250363; -.
DR iPTMnet; P61244; -.
DR PhosphoSitePlus; P61244; -.
DR BioMuta; MAX; -.
DR DMDM; 47117704; -.
DR EPD; P61244; -.
DR jPOST; P61244; -.
DR MassIVE; P61244; -.
DR MaxQB; P61244; -.
DR PaxDb; P61244; -.
DR PeptideAtlas; P61244; -.
DR PRIDE; P61244; -.
DR ProteomicsDB; 1183; -.
DR ProteomicsDB; 57281; -.
DR ProteomicsDB; 57282; -. [P61244-2]
DR ProteomicsDB; 57283; -. [P61244-3]
DR ProteomicsDB; 57284; -. [P61244-4]
DR ProteomicsDB; 57285; -. [P61244-5]
DR Antibodypedia; 159; 570 antibodies from 39 providers.
DR DNASU; 4149; -.
DR Ensembl; ENST00000246163.2; ENSP00000246163.2; ENSG00000125952.20. [P61244-5]
DR Ensembl; ENST00000284165.10; ENSP00000284165.6; ENSG00000125952.20. [P61244-4]
DR Ensembl; ENST00000341653.6; ENSP00000342482.2; ENSG00000125952.20. [P61244-6]
DR Ensembl; ENST00000358402.8; ENSP00000351175.4; ENSG00000125952.20. [P61244-2]
DR Ensembl; ENST00000358664.9; ENSP00000351490.4; ENSG00000125952.20. [P61244-1]
DR Ensembl; ENST00000394606.6; ENSP00000378104.2; ENSG00000125952.20. [P61244-3]
DR Ensembl; ENST00000553928.5; ENSP00000451907.1; ENSG00000125952.20. [P61244-3]
DR Ensembl; ENST00000556979.5; ENSP00000452378.1; ENSG00000125952.20. [P61244-3]
DR Ensembl; ENST00000618858.4; ENSP00000480127.1; ENSG00000125952.20. [P61244-3]
DR GeneID; 4149; -.
DR KEGG; hsa:4149; -.
DR MANE-Select; ENST00000358664.9; ENSP00000351490.4; NM_002382.5; NP_002373.3.
DR UCSC; uc001xic.3; human.
DR CTD; 4149; -.
DR DisGeNET; 4149; -.
DR GeneCards; MAX; -.
DR GeneReviews; MAX; -.
DR HGNC; HGNC:6913; MAX.
DR HPA; ENSG00000125952; Low tissue specificity.
DR MalaCards; MAX; -.
DR MIM; 154950; gene.
DR MIM; 171300; phenotype.
DR neXtProt; NX_P61244; -.
DR OpenTargets; ENSG00000125952; -.
DR Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
DR PharmGKB; PA30656; -.
DR VEuPathDB; HostDB:ENSG00000125952; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00530000064011; -.
DR HOGENOM; CLU_2541927_0_0_1; -.
DR InParanoid; P61244; -.
DR OMA; QIQTNYS; -.
DR OrthoDB; 1545748at2759; -.
DR PhylomeDB; P61244; -.
DR TreeFam; TF318841; -.
DR PathwayCommons; P61244; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; P61244; -.
DR SIGNOR; P61244; -.
DR BioGRID-ORCS; 4149; 561 hits in 1121 CRISPR screens.
DR ChiTaRS; MAX; human.
DR EvolutionaryTrace; P61244; -.
DR GeneWiki; MAX_(gene); -.
DR GenomeRNAi; 4149; -.
DR Pharos; P61244; Tbio.
DR PRO; PR:P61244; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P61244; protein.
DR Bgee; ENSG00000125952; Expressed in monocyte and 205 other tissues.
DR ExpressionAtlas; P61244; baseline and differential.
DR Genevisible; P61244; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0070443; C:Mad-Max complex; IPI:ComplexPortal.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0071943; C:Myc-Max complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR GO; GO:0003677; F:DNA binding; IDA:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR DisProt; DP00084; -.
DR DisProt; DP01097; -. [P61244-2]
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR037933; MAX-like.
DR PANTHER; PTHR10328; PTHR10328; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Cell projection; Disease variant; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..160
FT /note="Protein max"
FT /id="PRO_0000127269"
FT DOMAIN 23..74
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..102
FT /note="Leucine-zipper"
FT REGION 103..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..156
FT /note="Nuclear localization signal"
FT COMPBIAS 13..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000305|PubMed:17217336"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17217336"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17217336"
FT VAR_SEQ 13..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2006410"
FT /id="VSP_002117"
FT VAR_SEQ 58..160
FT /note="ASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSA
FT QLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS -> LYFL
FT FWKLCTPVLHRQSLMQKCHTFISSYQVHKKKECKI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043430"
FT VAR_SEQ 58..160
FT /note="ASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSA
FT QLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS -> GTKM
FT KLTLPPVFPYEHLPFPTVFCHG (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_047661"
FT VAR_SEQ 99..160
FT /note="VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQ
FT SRKKLRMEAS -> GESES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1566084"
FT /id="VSP_002118"
FT VAR_SEQ 99..160
FT /note="VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQ
FT SRKKLRMEAS -> GEHPSSWGSWPCCAPARSGFGTWACRVRASHGVCAQ (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043183"
FT VARIANT 9
FT /note="V -> L (in PCC; does not repress MYC transcriptional
FT activity; dbSNP:rs201743423)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079347"
FT VARIANT 23
FT /note="D -> N (in PCC; unknown pathological significance;
FT does not affect MYC transcriptional activity)"
FT /evidence="ECO:0000269|PubMed:21685915,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079348"
FT VARIANT 25
FT /note="R -> W (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079349"
FT VARIANT 33..160
FT /note="Missing (in PCC; does not repress MYC
FT transcriptional activity)"
FT /evidence="ECO:0000269|PubMed:21685915,
FT ECO:0000269|PubMed:22452945, ECO:0000269|PubMed:26070438"
FT /id="VAR_079350"
FT VARIANT 35
FT /note="R -> C (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079351"
FT VARIANT 47..52
FT /note="Missing (in PCC; unknown pathological significance;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:22452945"
FT /id="VAR_079352"
FT VARIANT 60
FT /note="R -> W (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079353"
FT VARIANT 71
FT /note="I -> S (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079354"
FT VARIANT 74
FT /note="M -> V (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079355"
FT VARIANT 75..160
FT /note="Missing (in PCC; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:21685915,
FT ECO:0000269|PubMed:22452945"
FT /id="VAR_079356"
FT VARIANT 82..160
FT /note="Missing (in PCC; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:22452945"
FT /id="VAR_079357"
FT VARIANT 90
FT /note="R -> P (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079358"
FT VARIANT 94
FT /note="L -> P (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:21685915,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079359"
FT VARIANT 102
FT /note="L -> P (in PCC; does not repress MYC transcriptional
FT activity)"
FT /evidence="ECO:0000269|PubMed:22452945,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079360"
FT VARIANT 114
FT /note="N -> T (does not affect MYC transcriptional
FT activity; dbSNP:rs772912674)"
FT /evidence="ECO:0000269|PubMed:26070438"
FT /id="VAR_079361"
FT VARIANT 142
FT /note="S -> L (does not affect MYC transcriptional
FT activity; dbSNP:rs760147253)"
FT /evidence="ECO:0000269|PubMed:21685915,
FT ECO:0000269|PubMed:26070438"
FT /id="VAR_079362"
FT MUTAGEN 66
FT /note="K->Q: Kept nuclear localization. Loss of nuclear
FT localization; when associated with Q-153 and Q-154."
FT /evidence="ECO:0000269|PubMed:17217336"
FT MUTAGEN 66
FT /note="K->R: Loss of acetylation, kept nuclear
FT localization; when associated with R-153 and R-154."
FT /evidence="ECO:0000269|PubMed:17217336"
FT MUTAGEN 153
FT /note="K->Q: Loss of nuclear localization; when associated
FT with Q-66 and Q-154. Kept nuclear localization; when
FT associated with Q-154."
FT /evidence="ECO:0000269|PubMed:17217336"
FT MUTAGEN 153
FT /note="K->R: Loss of acetylation, kept nuclear
FT localization; when associated with R-66 and R-154."
FT /evidence="ECO:0000269|PubMed:17217336"
FT MUTAGEN 154
FT /note="K->Q: Loss of nuclear localization; when associated
FT with Q-66 and Q-153. Kept nuclear localization; when
FT associated with Q-153."
FT /evidence="ECO:0000269|PubMed:17217336"
FT MUTAGEN 154
FT /note="K->R: Loss of acetylation, kept nuclear
FT localization; when associated with R-66 and R-153."
FT /evidence="ECO:0000269|PubMed:17217336"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:1HLO"
FT HELIX 27..49
FT /evidence="ECO:0007829|PDB:6G6K"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:6G6K"
FT HELIX 60..100
FT /evidence="ECO:0007829|PDB:6G6K"
FT INIT_MET P61244-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P61244-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P61244-2:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P61244-2:11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 160 AA; 18275 MW; EB10F3137727A56F CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN
SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS
