P61244 (MAX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein max

Alternative name(s):
Class D basic helix-loop-helix protein 4
Short name=bHLHd4
Myc-associated factor X

Gene names

Name:	MAX
Synonyms:	BHLHD4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	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 MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9. Ref.8 Ref.10
Subcellular location	Nucleus.
Tissue specificity	High levels found in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle.
Post-translational modification	Reversible lysine acetylation might regulate the nuclear-cytoplasmic shuttling of specific Max complexes.
Sequence similarities	Belongs to the MAX family. Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to starvation Inferred from electronic annotation. Source: Compara negative regulation of gene expression Inferred from electronic annotation. Source: Compara neuron apoptotic process Inferred from electronic annotation. Source: Compara protein complex assembly Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara retina development in camera-type eye Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement PubMed 8425218. Source: ProtInc
Cellular_component	MLL1 complex Inferred from direct assay Ref.10. Source: UniProtKB PML body Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay. Source: HPA dendrite Inferred from electronic annotation. Source: Compara
Molecular_function	sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc transcription coactivator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EPAS1	Q99814	2	EBI-751711,EBI-447470
FTH1	P02794	2	EBI-751711,EBI-713259
GABBR1	Q9UBS5	3	EBI-751711,EBI-724156
MAD1L1	Q9Y6D9	2	EBI-751711,EBI-742610
MYC	P01106	21	EBI-751711,EBI-447544

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P61244-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P61244-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     13-21: Missing.

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.

Isoform 3 (identifier: P61244-3)

Also known as: Delta-Max;

The sequence of this isoform differs from the canonical sequence as follows:
     99-160: VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS → GESES

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: P61244-4)

The sequence of this isoform differs from the canonical sequence as follows:
     99-160: VRALEKARSS...SRKKLRMEAS → GEHPSSWGSW...VRASHGVCAQ

Isoform 5 (identifier: P61244-5)

The sequence of this isoform differs from the canonical sequence as follows:
     58-160: ASRAQILDKA...SRKKLRMEAS → LYFLFWKLCT...QVHKKKECKI

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.15

Chain

2 – 160

159

Protein max

PRO_0000127269

Regions

Domain

23 – 74

52

bHLH

Region

81 – 102

22

Leucine-zipper

Motif

152 – 156

5

Nuclear localization signal

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.15 Ref.17

Modified residue

2

1

Phosphoserine Ref.12 Ref.14 Ref.15 Ref.17

Modified residue

11

1

Phosphoserine Ref.12 Ref.15 Ref.17

Modified residue

66

1

N6-acetyllysine Probable

Modified residue

153

1

N6-acetyllysine; alternate Ref.13

Modified residue

154

1

N6-acetyllysine; alternate Ref.13

Natural variations

Alternative sequence

13 – 21

9

Missing in isoform 2.

VSP_002117

Alternative sequence

58 – 160

103

ASRAQ…RMEAS → LYFLFWKLCTPVLHRQSLMQ KCHTFISSYQVHKKKECKI in isoform 5.

VSP_043430

Alternative sequence

99 – 160

62

VRALE…RMEAS → GESES in isoform 3.

VSP_002118

Alternative sequence

99 – 160

62

VRALE…RMEAS → GEHPSSWGSWPCCAPARSGF GTWACRVRASHGVCAQ in isoform 4.

VSP_043183

Experimental info

Mutagenesis

66

1

K → Q: Kept nuclear localization. Loss of nuclear localization; when associated with Q-153 and Q-154. Ref.13

Mutagenesis

66

1

K → R: Loss of acetylation, kept nuclear localization; when associated with R-153 and R-154. Ref.13

Mutagenesis

153

1

K → Q: Loss of nuclear localization; when associated with Q-66 and Q-154. Kept nuclear localization; when associated with Q-154. Ref.13

Mutagenesis

153

1

K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-154. Ref.13

Mutagenesis

154

1

K → Q: Loss of nuclear localization; when associated with Q-66 and Q-153. Kept nuclear localization; when associated with Q-153. Ref.13

Mutagenesis

154

1

K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-153. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

160

Helix Strand Turn

Details...

Helix

24 – 47

24

Helix

51 – 53

3

Helix

60 – 100

41

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified May 10, 2004. Version 1. Checksum: EB10F3137727A56F	FASTA	160	18,275
	10 20 30 40 50 60 MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR 70 80 90 100 110 120 AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN 130 140 150 160 SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS
	Isoform 2 (Short) [UniParc] [UniParc]. Checksum: CB69F6F5F39793FA	FASTA	151	17,202
	10 20 30 40 50 60 MSDNDDIEVE SDADKRAHHN ALERKRRDHI KDSFHSLRDS VPSLQGEKAS RAQILDKATE 70 80 90 100 110 120 YIQYMRRKNH THQQDIDDLK RQNALLEQQV RALEKARSSA QLQTNYPSSD NSLYTNAKGS 130 140 150 TISAFDGGSD SSSESEPEEP QSRKKLRMEA S
	Isoform 3 (Delta-Max) [UniParc] [UniParc]. Checksum: 49DC1A0441FFA301	FASTA	103	12,099
	10 20 30 40 50 60 MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR 70 80 90 100 AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQGE SES
	Isoform 4 [UniParc]. Checksum: A2FFD0B98CF93275	FASTA	134	15,395
	10 20 30 40 50 60 MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR 70 80 90 100 110 120 AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQGE HPSSWGSWPC CAPARSGFGT 130 WACRVRASHG VCAQ
	Isoform 5 [UniParc]. Checksum: D380F721DCF2D6C8	FASTA	96	11,455
	10 20 30 40 50 60 MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKLYF 70 80 90 LFWKLCTPVL HRQSLMQKCH TFISSYQVHK KKECKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc." Blackwood E.M., Eisenman R.N. Science 251:1211-1217(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"Alternative mRNA forms and open reading frames of the max gene." Vaestrik I., Koskinen P.J., Alitalo R., Maekelae T.P. Oncogene 8:503-507(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation." Maekelae T.P., Koskinen P.J., Vaestrik I., Alitalo K. Science 256:373-377(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). Tissue: Mammary gland, Thalamus and Thymus.
[5]	"The DNA sequence and analysis of human chromosome 14." 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. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5). Tissue: Brain, Lung and Uterus.
[8]	"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells." Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y. Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MGA; EUHMTASE1; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
[9]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[10]	"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF." 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. Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Max is acetylated by p300 at several nuclear localization residues." Faiola F., Wu Y.-T., Pan S., Zhang K., Farina A., Martinez E. Biochem. J. 403:397-407(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-66; LYS-153 AND LYS-154, MUTAGENESIS OF LYS-66; LYS-153 AND LYS-154.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, MASS SPECTROMETRY.
[18]	"Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain." Ferre-D'Amare A.R., Prendergast G.C., Ziff E.B., Burley S.K. Nature 363:38-45(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-107.
[19]	"The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control." Brownlie P., Ceska T., Lamers M., Romier C., Stier G., Teo H., Suck D. Structure 5:509-520(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64240 mRNA. Translation: AAA36200.1.
M64240 mRNA. Translation: AAA36201.1.
X66867 Genomic DNA. Translation: CAA47337.1.
X66867 Genomic DNA. Translation: CAA47338.1.
X66867 Genomic DNA. Translation: CAA47339.1.
X60287 mRNA. Translation: CAA42827.1.
AK290130 mRNA. Translation: BAF82819.1.
AK290929 mRNA. Translation: BAF83618.1.
AK292189 mRNA. Translation: BAF84878.1.
AK292630 mRNA. Translation: BAF85319.1.
AL139022 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80899.1.
CH471061 Genomic DNA. Translation: EAW80901.1.
CH471061 Genomic DNA. Translation: EAW80903.1.
CH471061 Genomic DNA. Translation: EAW80904.1.
BC003525 mRNA. Translation: AAH03525.1.
BC004516 mRNA. Translation: AAH04516.1.
BC013669 mRNA. Translation: AAH13669.1.
BC027924 mRNA. Translation: AAH27924.1.

IPI

IPI00018214.
IPI00060723.
IPI00157813.
IPI00158128.
IPI00219929.

PIR

A38431.
A42611.
B38431.
S33118.

RefSeq

NP_001257997.1. NM_001271068.1.
NP_002373.3. NM_002382.4.
NP_660087.1. NM_145112.2.
NP_660088.1. NM_145113.2.
NP_660089.1. NM_145114.2.
NP_932061.1. NM_197957.3.

UniGene

Hs.285354.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AN2	X-ray	2.90	A	22-107	[»]
1HLO	X-ray	2.80	A/B	22-92	[»]
1NKP	X-ray	1.80	B/E	23-102	[»]
1NLW	X-ray	2.00	B/E	24-99	[»]
1R05	NMR	-	A/B	22-103	[»]

ProteinModelPortal

P61244.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28145N.

IntAct

P61244. 43 interactions.

MINT

MINT-257220.

STRING

9606.ENSP00000351490.

PTM databases

PhosphoSite

P61244.

Polymorphism databases

DMDM

47117704.

Proteomic databases

PaxDb

P61244.

PRIDE

P61244.

Protocols and materials databases

DNASU

4149.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000246163; ENSP00000246163; ENSG00000125952.
ENST00000284165; ENSP00000284165; ENSG00000125952.
ENST00000358402; ENSP00000351175; ENSG00000125952.
ENST00000358664; ENSP00000351490; ENSG00000125952.
ENST00000394606; ENSP00000378104; ENSG00000125952.
ENST00000553928; ENSP00000451907; ENSG00000125952.
ENST00000556979; ENSP00000452378; ENSG00000125952.

GeneID

4149.

KEGG

hsa:4149.

UCSC

uc001xie.1. human.
uc001xif.1. human.
uc001xig.1. human.

Organism-specific databases

CTD

4149.

GeneCards

GC14M065472.

HGNC

HGNC:6913. MAX.

HPA

CAB000328.
HPA003474.

MIM

154950. gene.

neXtProt

NX_P61244.

Orphanet

29072. Hereditary pheochromocytoma-paraganglioma.

PharmGKB

PA30656.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG239807.

HOGENOM

HOG000293257.

HOVERGEN

HBG008542.

InParanoid

P61244.

KO

K04453.

OMA

ANYSSSD.

PhylomeDB

P61244.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpress

P61244.

Bgee

P61244.

CleanEx

HS_MAX.

Genevestigator

P61244.

GermOnline

ENSG00000125952. Homo sapiens.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
[Graphical view]

Pfam

PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P61244.

ChEMBL

CHEMBL1250363.

ChiTaRS

MAX. human.

EvolutionaryTrace

P61244.

GenomeRNAi

4149.

NextBio

16302.

PMAP-CutDB

P61244.

SOURCE

Search...

Entry information

Entry name

MAX_HUMAN

Accession

Primary (citable) accession number: P61244
Secondary accession number(s): A8K265 , A8K4G4, A8K824, P25912, P52163, Q14803, Q96CY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.