Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein max (Class D basic helix-loop-helix protein 4) (bHLHd4) (Myc-associated factor X)

 MAX_HUMAN               Reviewed;         160 AA.
P61244; A6NH73; A8K265; A8K4G4; A8K824; P25912; P52163; Q14803;
Q96CY8;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 1.
30-AUG-2017, entry version 160.
RecName: Full=Protein max;
AltName: Full=Class D basic helix-loop-helix protein 4;
Short=bHLHd4;
AltName: Full=Myc-associated factor X;
Name=MAX; Synonyms=BHLHD4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=2006410; DOI=10.1126/science.2006410;
Blackwood E.M., Eisenman R.N.;
"Max: a helix-loop-helix zipper protein that forms a sequence-specific
DNA-binding complex with Myc.";
Science 251:1211-1217(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8426752;
Vaestrik I., Koskinen P.J., Alitalo R., Maekelae T.P.;
"Alternative mRNA forms and open reading frames of the max gene.";
Oncogene 8:503-507(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=1566084; DOI=10.1126/science.256.5055.373;
Maekelae T.P., Koskinen P.J., Vaestrik I., Alitalo K.;
"Alternative forms of Max as enhancers or suppressors of Myc-ras
cotransformation.";
Science 256:373-377(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Mammary gland, Thalamus, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
TISSUE=Brain, Lung, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MGA; EUHMTASE1; BAT8;
CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
PubMed=12004135; DOI=10.1126/science.1069861;
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
"A complex with chromatin modifiers that occupies E2F- and Myc-
responsive genes in G0 cells.";
Science 296:1132-1136(2002).
[9]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[10]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
ACETYLATION AT LYS-66; LYS-153 AND LYS-154, AND MUTAGENESIS OF LYS-66;
LYS-153 AND LYS-154.
PubMed=17217336; DOI=10.1042/BJ20061593;
Faiola F., Wu Y.-T., Pan S., Zhang K., Farina A., Martinez E.;
"Max is acetylated by p300 at several nuclear localization residues.";
Biochem. J. 403:397-407(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE
ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2
AND SER-11 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
(ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INVOLVEMENT IN PCC.
PubMed=21685915; DOI=10.1038/ng.861;
Comino-Mendez I., Gracia-Aznarez F.J., Schiavi F., Landa I.,
Leandro-Garcia L.J., Leton R., Honrado E., Ramos-Medina R.,
Caronia D., Pita G., Gomez-Grana A., de Cubas A.A., Inglada-Perez L.,
Maliszewska A., Taschin E., Bobisse S., Pica G., Loli P.,
Hernandez-Lavado R., Diaz J.A., Gomez-Morales M., Gonzalez-Neira A.,
Roncador G., Rodriguez-Antona C., Benitez J., Mannelli M., Opocher G.,
Robledo M., Cascon A.;
"Exome sequencing identifies MAX mutations as a cause of hereditary
pheochromocytoma.";
Nat. Genet. 43:663-667(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE
ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2
(ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS],
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-107.
PubMed=8479534; DOI=10.1038/363038a0;
Ferre-D'Amare A.R., Prendergast G.C., Ziff E.B., Burley S.K.;
"Recognition by Max of its cognate DNA through a dimeric b/HLH/Z
domain.";
Nature 363:38-45(1993).
[22]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=9115440; DOI=10.1016/S0969-2126(97)00207-4;
Brownlie P., Ceska T., Lamers M., Romier C., Stier G., Teo H.,
Suck D.;
"The crystal structure of an intact human Max-DNA complex: new
insights into mechanisms of transcriptional control.";
Structure 5:509-520(1997).
-!- FUNCTION: Transcription regulator. Forms a sequence-specific DNA-
binding protein complex with MYC or MAD which recognizes the core
sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional
activator, whereas the MAD:MAX complex is a repressor. May repress
transcription via the recruitment of a chromatin remodeling
complex containing H3 'Lys-9' histone methyltransferase activity.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a heterodimer with MYC or MAD. Part of
the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX,
TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2.
Component of some MLL1/MLL complex, at least composed of the core
components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31,
RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7,
TAF9 and TEX10. Interacts with SPAG9. The heterodimer MYC:MAX
interacts with ABI1; the interaction may enhance MYC:MAX
transcriptional activity. {ECO:0000269|PubMed:12004135,
ECO:0000269|PubMed:15960975}.
-!- INTERACTION:
Q8N9N5:BANP; NbExp=3; IntAct=EBI-751711, EBI-744695;
O75461:E2F6; NbExp=4; IntAct=EBI-751711, EBI-749694;
P29692:EEF1D; NbExp=2; IntAct=EBI-751711, EBI-358607;
Q99814:EPAS1; NbExp=2; IntAct=EBI-751711, EBI-447470;
Q01167:FOXK2; NbExp=4; IntAct=EBI-751711, EBI-2509991;
P02794:FTH1; NbExp=2; IntAct=EBI-751711, EBI-713259;
Q9UBS5:GABBR1; NbExp=3; IntAct=EBI-751711, EBI-724156;
O75367:H2AFY; NbExp=2; IntAct=EBI-751711, EBI-2868511;
Q969R5:L3MBTL2; NbExp=5; IntAct=EBI-751711, EBI-739909;
P49916:LIG3; NbExp=2; IntAct=EBI-751711, EBI-1753381;
P51608:MECP2; NbExp=2; IntAct=EBI-751711, EBI-1189067;
Q8IWI9:MGA; NbExp=4; IntAct=EBI-751711, EBI-2815196;
Q05195:MXD1; NbExp=3; IntAct=EBI-751711, EBI-8833637;
P50539:MXI1; NbExp=6; IntAct=EBI-751711, EBI-752241;
P01106:MYC; NbExp=31; IntAct=EBI-751711, EBI-447544;
P04198:MYCN; NbExp=9; IntAct=EBI-751711, EBI-878369;
Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-751711, EBI-742388;
P05549:TFAP2A; NbExp=2; IntAct=EBI-751711, EBI-347351;
Q14186:TFDP1; NbExp=4; IntAct=EBI-751711, EBI-749713;
Q9H3U1:UNC45A; NbExp=3; IntAct=EBI-10218525, EBI-1048763;
Q8IV63:VRK3; NbExp=2; IntAct=EBI-751711, EBI-1058605;
P18887:XRCC1; NbExp=2; IntAct=EBI-751711, EBI-947466;
-!- SUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Long;
IsoId=P61244-1, P25912-1;
Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P61244-2, P25912-2;
Sequence=VSP_002117;
Note=Contains a phosphoserine at position 2. Initiator Met-1 is
removed. Contains a N-acetylserine at position 2. Contains a
phosphoserine at position 11. {ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692};
Name=3; Synonyms=Delta-Max;
IsoId=P61244-3, P25912-3;
Sequence=VSP_002118;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=P61244-4; Sequence=VSP_043183;
Name=5;
IsoId=P61244-5; Sequence=VSP_043430;
Note=No experimental confirmation available.;
Name=6;
IsoId=P61244-6; Sequence=VSP_047661;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High levels found in the brain, heart and lung
while lower levels are seen in the liver, kidney and skeletal
muscle.
-!- PTM: Reversible lysine acetylation might regulate the nuclear-
cytoplasmic shuttling of specific Max complexes.
{ECO:0000269|PubMed:17217336}.
-!- DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-
producing tumor of chromaffin tissue of the adrenal medulla or
sympathetic paraganglia. The cardinal symptom, reflecting the
increased secretion of epinephrine and norepinephrine, is
hypertension, which may be persistent or intermittent.
{ECO:0000269|PubMed:21685915}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M64240; AAA36200.1; -; mRNA.
EMBL; M64240; AAA36201.1; -; mRNA.
EMBL; X66867; CAA47337.1; -; Genomic_DNA.
EMBL; X66867; CAA47338.1; -; Genomic_DNA.
EMBL; X66867; CAA47339.1; -; Genomic_DNA.
EMBL; X60287; CAA42827.1; -; mRNA.
EMBL; AK290130; BAF82819.1; -; mRNA.
EMBL; AK290929; BAF83618.1; -; mRNA.
EMBL; AK292189; BAF84878.1; -; mRNA.
EMBL; AK292630; BAF85319.1; -; mRNA.
EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW80899.1; -; Genomic_DNA.
EMBL; CH471061; EAW80901.1; -; Genomic_DNA.
EMBL; CH471061; EAW80903.1; -; Genomic_DNA.
EMBL; CH471061; EAW80904.1; -; Genomic_DNA.
EMBL; BC003525; AAH03525.1; -; mRNA.
EMBL; BC004516; AAH04516.1; -; mRNA.
EMBL; BC013669; AAH13669.1; -; mRNA.
EMBL; BC027924; AAH27924.1; -; mRNA.
CCDS; CCDS41965.1; -. [P61244-3]
CCDS; CCDS9770.1; -. [P61244-6]
CCDS; CCDS9771.1; -.
CCDS; CCDS9772.1; -. [P61244-2]
CCDS; CCDS9774.1; -. [P61244-5]
PIR; A38431; A38431.
PIR; A42611; A42611.
PIR; B38431; B38431.
PIR; S33118; S33118.
RefSeq; NP_001257997.1; NM_001271068.1.
RefSeq; NP_002373.3; NM_002382.4. [P61244-1]
RefSeq; NP_660087.1; NM_145112.2. [P61244-2]
RefSeq; NP_660088.1; NM_145113.2. [P61244-3]
RefSeq; NP_660089.1; NM_145114.2. [P61244-5]
RefSeq; NP_932061.1; NM_197957.3. [P61244-6]
UniGene; Hs.285354; -.
PDB; 1AN2; X-ray; 2.90 A; A=22-107.
PDB; 1HLO; X-ray; 2.80 A; A/B=20-92.
PDB; 1NKP; X-ray; 1.80 A; B/E=23-102.
PDB; 1NLW; X-ray; 2.00 A; B/E=24-99.
PDB; 1R05; NMR; -; A/B=22-103.
PDB; 5EYO; X-ray; 2.39 A; A/C=22-107.
PDBsum; 1AN2; -.
PDBsum; 1HLO; -.
PDBsum; 1NKP; -.
PDBsum; 1NLW; -.
PDBsum; 1R05; -.
PDBsum; 5EYO; -.
DisProt; DP00084; -.
DisProt; DP01097; -.
ProteinModelPortal; P61244; -.
SMR; P61244; -.
BioGrid; 110319; 99.
DIP; DIP-28145N; -.
IntAct; P61244; 99.
MINT; MINT-1468374; -.
STRING; 9606.ENSP00000351490; -.
BindingDB; P61244; -.
ChEMBL; CHEMBL1250363; -.
iPTMnet; P61244; -.
PhosphoSitePlus; P61244; -.
DMDM; 47117704; -.
EPD; P61244; -.
MaxQB; P61244; -.
PaxDb; P61244; -.
PeptideAtlas; P61244; -.
PRIDE; P61244; -.
DNASU; 4149; -.
Ensembl; ENST00000246163; ENSP00000246163; ENSG00000125952. [P61244-5]
Ensembl; ENST00000284165; ENSP00000284165; ENSG00000125952. [P61244-4]
Ensembl; ENST00000341653; ENSP00000342482; ENSG00000125952. [P61244-6]
Ensembl; ENST00000358402; ENSP00000351175; ENSG00000125952. [P61244-2]
Ensembl; ENST00000358664; ENSP00000351490; ENSG00000125952. [P61244-1]
Ensembl; ENST00000394606; ENSP00000378104; ENSG00000125952. [P61244-3]
Ensembl; ENST00000553928; ENSP00000451907; ENSG00000125952. [P61244-3]
Ensembl; ENST00000556979; ENSP00000452378; ENSG00000125952. [P61244-3]
Ensembl; ENST00000618858; ENSP00000480127; ENSG00000125952. [P61244-3]
GeneID; 4149; -.
KEGG; hsa:4149; -.
UCSC; uc001xic.3; human.
CTD; 4149; -.
DisGeNET; 4149; -.
GeneCards; MAX; -.
GeneReviews; MAX; -.
HGNC; HGNC:6913; MAX.
HPA; CAB000328; -.
HPA; HPA003474; -.
MalaCards; MAX; -.
MIM; 154950; gene.
MIM; 171300; phenotype.
neXtProt; NX_P61244; -.
OpenTargets; ENSG00000125952; -.
Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
PharmGKB; PA30656; -.
eggNOG; KOG2483; Eukaryota.
eggNOG; ENOG4111V1C; LUCA.
GeneTree; ENSGT00530000064011; -.
HOGENOM; HOG000293257; -.
HOVERGEN; HBG008542; -.
InParanoid; P61244; -.
KO; K04453; -.
OMA; RHTSTAN; -.
OrthoDB; EOG091G1312; -.
PhylomeDB; P61244; -.
TreeFam; TF318841; -.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
SignaLink; P61244; -.
SIGNOR; P61244; -.
ChiTaRS; MAX; human.
EvolutionaryTrace; P61244; -.
GeneWiki; MAX_(gene); -.
GenomeRNAi; 4149; -.
PMAP-CutDB; P61244; -.
PRO; PR:P61244; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000125952; -.
CleanEx; HS_MAX; -.
ExpressionAtlas; P61244; baseline and differential.
Genevisible; P61244; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:NTNU_SB.
GO; GO:0003677; F:DNA binding; IMP:CAFA.
GO; GO:0070888; F:E-box binding; IMP:CAFA.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Cell projection; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CHAIN 2 160 Protein max.
/FTId=PRO_0000127269.
DOMAIN 23 74 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 81 102 Leucine-zipper.
MOTIF 152 156 Nuclear localization signal.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 66 66 N6-acetyllysine.
{ECO:0000305|PubMed:17217336}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 153 153 N6-acetyllysine.
{ECO:0000269|PubMed:17217336}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000269|PubMed:17217336}.
VAR_SEQ 13 21 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2006410}.
/FTId=VSP_002117.
VAR_SEQ 58 160 ASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQ
VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSD
SSSESEPEEPQSRKKLRMEAS -> LYFLFWKLCTPVLHRQ
SLMQKCHTFISSYQVHKKKECKI (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043430.
VAR_SEQ 58 160 ASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQ
VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSD
SSSESEPEEPQSRKKLRMEAS -> GTKMKLTLPPVFPYEH
LPFPTVFCHG (in isoform 6). {ECO:0000305}.
/FTId=VSP_047661.
VAR_SEQ 99 160 VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSD
SSSESEPEEPQSRKKLRMEAS -> GESES (in
isoform 3). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:1566084}.
/FTId=VSP_002118.
VAR_SEQ 99 160 VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSD
SSSESEPEEPQSRKKLRMEAS -> GEHPSSWGSWPCCAPA
RSGFGTWACRVRASHGVCAQ (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043183.
MUTAGEN 66 66 K->Q: Kept nuclear localization. Loss of
nuclear localization; when associated
with Q-153 and Q-154.
{ECO:0000269|PubMed:17217336}.
MUTAGEN 66 66 K->R: Loss of acetylation, kept nuclear
localization; when associated with R-153
and R-154. {ECO:0000269|PubMed:17217336}.
MUTAGEN 153 153 K->Q: Loss of nuclear localization; when
associated with Q-66 and Q-154. Kept
nuclear localization; when associated
with Q-154.
{ECO:0000269|PubMed:17217336}.
MUTAGEN 153 153 K->R: Loss of acetylation, kept nuclear
localization; when associated with R-66
and R-154. {ECO:0000269|PubMed:17217336}.
MUTAGEN 154 154 K->Q: Loss of nuclear localization; when
associated with Q-66 and Q-153. Kept
nuclear localization; when associated
with Q-153.
{ECO:0000269|PubMed:17217336}.
MUTAGEN 154 154 K->R: Loss of acetylation, kept nuclear
localization; when associated with R-66
and R-153. {ECO:0000269|PubMed:17217336}.
HELIX 24 47 {ECO:0000244|PDB:1NKP}.
HELIX 51 53 {ECO:0000244|PDB:1NKP}.
HELIX 60 100 {ECO:0000244|PDB:1NKP}.
SEQUENCE 160 AA; 18275 MW; EB10F3137727A56F CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN
SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS


Related products :

Catalog number Product name Quantity
U0404h CLIA bHLHd4,BHLHD4,Class D basic helix-loop-helix protein 4,Homo sapiens,Human,MAX,Myc-associated factor X,Protein max 96T
E0404h ELISA bHLHd4,BHLHD4,Class D basic helix-loop-helix protein 4,Homo sapiens,Human,MAX,Myc-associated factor X,Protein max 96T
E0404h ELISA kit bHLHd4,BHLHD4,Class D basic helix-loop-helix protein 4,Homo sapiens,Human,MAX,Myc-associated factor X,Protein max 96T
EIAAB37697 Basic helix-loop-helix transcription factor scleraxis,bHLHa41,BHLHA41,bHLHa48,Class A basic helix-loop-helix protein 41,Class A basic helix-loop-helix protein 48,Homo sapiens,Human,SCX,SCXA
U2004h CLIA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alph 96T
E2004h ELISA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF- 96T
E2004h ELISA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alp 96T
U2004h CLIA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2 96T
EIAAB28826 bHLHb1,BHLHB1,bHLHe19,BHLHE19,Class B basic helix-loop-helix protein 1,Class E basic helix-loop-helix protein 19,Homo sapiens,Human,OLIG2,Oligo2,Oligodendrocyte transcription factor 2,PRKCBP2,Protein
EIAAB28821 bHLHb6,BHLHB6,bHLHe21,BHLHE21,Class B basic helix-loop-helix protein 6,Class E basic helix-loop-helix protein 21,Homo sapiens,Human,OLIG1,Oligo1,Oligodendrocyte transcription factor 1
EIAAB28828 bHLHb7,BHLHB7,bHLHe20,BHLHE20,Class B basic helix-loop-helix protein 7,Class E basic helix-loop-helix protein 20,Homo sapiens,Human,OLIG3,Oligo3,Oligodendrocyte transcription factor 3
U0798h CLIA ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible factor 96T
EIAAB27132 bHLHa6,BHLHA6,Class A basic helix-loop-helix protein 6,Homo sapiens,Human,NeuroD3,NEUROD3,NEUROG1,Neurogenic basic-helix-loop-helix protein,Neurogenic differentiation factor 3,Neurogenin-1,NGN,NGN1,NG
E0798h ELISA ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible facto 96T
E0798h ELISA kit ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible 96T
E0255h ELISA kit ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
U0255h CLIA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
E0255h ELISA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
EIAAB14718 Basic helix-loop-helix protein N-twist,bHLHa31,BHLHA31,Class A basic helix-loop-helix protein 31,Fer3-like protein,FERD3L,Homo sapiens,Human,NATO3,Nephew of atonal 3,Neuronal twist,NTWIST
EIAAB27612 Basic-helix-loop-helix-PAS protein MOP5,bHLHe11,BHLHE11,Class E basic helix-loop-helix protein 11,Homo sapiens,Human,Member of PAS protein 5,MOP5,Neuronal PAS domain-containing protein 1,Neuronal PAS1
EIAAB27615 Basic-helix-loop-helix-PAS protein MOP4,bHLHe9,BHLHE9,Class E basic helix-loop-helix protein 9,Homo sapiens,Human,Member of PAS protein 4,MOP4,Neuronal PAS domain-containing protein 2,Neuronal PAS2,NP
EIAAB27618 Basic-helix-loop-helix-PAS protein MOP6,bHLHe12,BHLHE12,Class E basic helix-loop-helix protein 12,Homo sapiens,Human,Member of PAS protein 6,MOP6,Neuronal PAS domain-containing protein 3,Neuronal PAS3
EIAAB27130 Ath4c,Helix-loop-helix protein mATH-4C,mATH4C,Mouse,Mus musculus,NeuroD3,Neurod3,Neurog1,Neurogenic basic-helix-loop-helix protein,Neurogenic differentiation factor 3,Neurogenin-1,Ngn,Ngn1,NGN-1
EIAAB24971 bHLHd13,BHLHD13,Class D basic helix-loop-helix protein 13,Homo sapiens,Human,Max-like bHLHZip protein,Max-like protein X,MLX,Protein BigMax,TCFL4,Transcription factor-like protein 4
LF-PA40832 anti-Basic-helix-loop-helix-PAS Protein, Rabbit polyclonal to Basic-helix-loop-helix-PAS Protein, Isotype IgG, Host Rabbit 50 ug


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur