GenomeNet

Database: UniProt
Entry: P61244
LinkDB: P61244
Original site: P61244 
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   29-SEP-2021, entry version 194.
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=36; 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}.
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; 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   BMRB; P61244; -.
DR   SMR; P61244; -.
DR   BioGRID; 110319; 187.
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; 116.
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; 564 antibodies.
DR   DNASU; 4149; -.
DR   Ensembl; ENST00000246163; ENSP00000246163; ENSG00000125952. [P61244-5]
DR   Ensembl; ENST00000284165; ENSP00000284165; ENSG00000125952. [P61244-4]
DR   Ensembl; ENST00000341653; ENSP00000342482; ENSG00000125952. [P61244-6]
DR   Ensembl; ENST00000358402; ENSP00000351175; ENSG00000125952. [P61244-2]
DR   Ensembl; ENST00000358664; ENSP00000351490; ENSG00000125952. [P61244-1]
DR   Ensembl; ENST00000394606; ENSP00000378104; ENSG00000125952. [P61244-3]
DR   Ensembl; ENST00000553928; ENSP00000451907; ENSG00000125952. [P61244-3]
DR   Ensembl; ENST00000556979; ENSP00000452378; ENSG00000125952. [P61244-3]
DR   Ensembl; ENST00000618858; ENSP00000480127; ENSG00000125952. [P61244-3]
DR   GeneID; 4149; -.
DR   KEGG; hsa:4149; -.
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; 549 hits in 1053 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 253 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:0071339; C:MLL1 complex; IDA:UniProtKB.
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: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: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.
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
//
DBGET integrated database retrieval system