MAX MYC associated factor X [Homo sapiens] - Gene

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Summary

Official Symbol: MAXprovided by HGNC
Official Full Name: MYC associated factor Xprovided by HGNC
Primary source: HGNC:6913
See related: Ensembl:ENSG00000125952; HPRD:01113; MIM:154950; Vega:OTTHUMG00000142809
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: orf1; bHLHd4; bHLHd5; bHLHd6; bHLHd7; bHLHd8; MGC10775; MGC11225; MGC18164; MGC34679; MGC36767
Summary: The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown. [provided by RefSeq, Jul 2008]

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Genomic context

Location :: 14q23

Sequence :: Chromosome: 14; NC_000014.8 (65472892..65569227, complement)

See MAX in Epigenomics, MapViewer

Chromosome 14 - NC_000014.8 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

The E-box binding factors Max/Mnt, MITF, and USF1 act coordinately with FoxO to regulate expression of proapoptotic and cell cycle control genes by phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3 signaling.
Title: The E-box binding factors Max/Mnt, MITF, and USF1 act coordinately with FoxO to regulate expression of proapoptotic and cell cycle control genes by phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3 signaling.
The transcription factors Max and RXRalpha bind directly to the miR-193a promoter and inhibit miR-193a expression during transformation, thereby activating the PLAU and K-Ras oncogenes.
Title: Inhibition of miR-193a expression by Max and RXRα activates K-Ras and PLAU to mediate distinct aspects of cellular transformation.
MAX mutations are associated with hereditary pheochromocytoma.
Title: Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma.
Enforced miR-22 expression presumably lowers Max levels available for Myc binding, which differentially influenced the transcription of downstream targets of the Myc-Max complex.
Title: Differentiation-associated miR-22 represses Max expression and inhibits cell cycle progression.
The switch from Mnt-Max to Myc-Max during bile duct ligation (cholestasis) and in hepatocytes treated with lithocholic acid is responsible for the induction in p53 and cyclin D1 expression and contributes to apoptosis.
Title: Switch from Mnt-Max to Myc-Max induces p53 and cyclin D1 expression and apoptosis during cholestasis in mouse and human hepatocytes.
Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)
Title: Genome-wide association study of anthropometric traits in Korcula Island, Croatia.
Max as a novel co-activator of C/EBPalpha functions, thereby suggesting a possible link between C/EBPalpha and Myc-Max-Mad network.
Title: Proteomic discovery of Max as a novel interacting partner of C/EBPalpha: a Myc/Max/Mad link.
C6-cer inhibited the DNA-binding function of the c-Myc/Max oncogene
Title: Regulation of the sphingosine-recycling pathway for ceramide generation by oxidative stress, and its role in controlling c-Myc/Max function.
Binding affinities & thermodynamics of dimerization of Max-Max homodimer & c-Myc-Max & Mad-Max heterodimers were determined.c-Myc & Max form most stable heterodimer.Polylysine had little effect, polyglutamic acid stabilized both heterodimers & homodimers.
Title: Thermodynamics of protein-protein interactions of cMyc, Max, and Mad: effect of polyions on protein dimerization.
X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors.
Title: X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors.

Submit: New GeneRIF Correction See all (13)

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Phenotypes

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Genome-wide association study of anthropometric traits in Korcula Island, Croatia.

Multiple loci influence erythrocyte phenotypes in the CHARGE Consortium.

Pheochromocytoma, susceptibility to

MIM: 171300

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HIV-1 protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	HIV-1 gp120 downregulates expression of c-Myc, Max, and 14-3-3epsilon proteins, and decreases phosphorylation of ATP-dependent tyrosine kinases (Akt) at Ser-473 in human mesangial cells (HMC)	PubMed

Go to the HIV-1, Human Protein Interaction Database

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Products	Interactant	Other Gene	Source	Pubs	Description
NP_002373.3	NP_000242.1	MSH2	BIND	PubMed	Max interacts with MSH2. This is a modeled interaction between Max from an unspecified source and human MSH2.
NP_002373.3	NP_002348.1	MXD1	BIND	PubMed	Max interacts with Mad1.
NP_002373.3	NP_005953.3	MXI1	BIND	PubMed	Max interacts with Mxi1.
NP_002373.3	NP_002458.1	MYC	BIND	PubMed	Myc interacts with Max. This interaction was modeled on a demonstrated interaction between human Myc and Max from an unspecified source.
P61244	P51878	CASP5	HPRD	PubMed
P61244	P55210	CASP7	HPRD	PubMed
P61244	P68400	CSNK2A1	HPRD	PubMed
P61244	Q99814	EPAS1	HPRD	PubMed
P61244	Q16665	HIF1A	HPRD	PubMed
P61244	Q9Y6D9	MAD1L1	HPRD	PubMed
P61244	Q16539	MAPK14	HPRD	PubMed
P61244	P61244	MAX	HPRD	PubMed
P61244	Q99583	MNT	HPRD	PubMed
P61244	P43246	MSH2	HPRD	PubMed
P61244	Q05195	MXD1	HPRD	PubMed
P61244	Q9BW11	MXD3	HPRD	PubMed
P61244	Q14582	MXD4	HPRD	PubMed
P61244	P01106	MYC	HPRD	PubMed
P61244	P12524	MYCL1	HPRD	PubMed
P61244	P04198	MYCN	HPRD	PubMed
P61244	Q9H8W4	PLEKHF2	HPRD	PubMed
P61244	P84022	SMAD3	HPRD	PubMed
P61244	Q13485	SMAD4	HPRD	PubMed
P61244	Q8TAD8	SNIP1	HPRD	PubMed
P61244	O60271	SPAG9	HPRD	PubMed
P61244	P28347	TEAD1	HPRD	PubMed
P61244	Q9Y4A5	TRRAP	HPRD	PubMed
P61244	L-myc-2 protein		HPRD	PubMed
BioGRID:110319	BioGRID:116108	BRD8	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western
BioGRID:110319	BioGRID:107343	CCNT1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:107479	CEBPA	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western; Reconstituted Complex
BioGRID:110319	BioGRID:113300	CLIP2	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:116183	COPS5	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:107903	CUX1	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:121004	DMAP1	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western
BioGRID:110319	BioGRID:108347	EP300	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity
BioGRID:110319	BioGRID:121676	EP400	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western
BioGRID:110319	BioGRID:108348	EPAS1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:109338	HIF1A	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:109433	HNRNPU	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:109535	HSPA1A	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110319	BioGRID:108918	KAT2A	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:115779	KAT5	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western
BioGRID:110319	BioGRID:113870	KDM5C	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110319	BioGRID:113971	MAD1L1	BioGRID	PubMed	Reconstituted Complex
BioGRID:110319	BioGRID:110319	MAX	BioGRID	PubMed	Affinity Capture-Western; Co-crystal Structure; Reconstituted Complex
BioGRID:110319	BioGRID:116870	MGA	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:110478	MNT	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:110319	BioGRID:110573	MSH2	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:110319	BioGRID:110259	MXD1	BioGRID	PubMed	Affinity Capture-Western; Co-crystal Structure; Reconstituted Complex; Two-hybrid
BioGRID:110319	BioGRID:123658	MXD3	BioGRID	PubMed	Reconstituted Complex; Two-hybrid
BioGRID:110319	BioGRID:115854	MXD4	BioGRID	PubMed	Reconstituted Complex; Two-hybrid
BioGRID:110319	BioGRID:110686	MXI1	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:110319	BioGRID:110694	MYC	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western; Co-crystal Structure; FRET; Reconstituted Complex; Two-hybrid
BioGRID:110319	BioGRID:110695	MYCL1	BioGRID	PubMed	Reconstituted Complex
BioGRID:110319	BioGRID:110698	MYCN	BioGRID	PubMed	Affinity Capture-MS; Reconstituted Complex
BioGRID:110319	BioGRID:123896	PCGF6	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110319	BioGRID:111310	PIM1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:119982	PLEKHA5	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:122791	PLEKHF2	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:110263	SMAD3	BioGRID	PubMed	Reconstituted Complex
BioGRID:110319	BioGRID:110264	SMAD4	BioGRID	PubMed	Reconstituted Complex
BioGRID:110319	BioGRID:114505	SPAG9	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:110319	BioGRID:112735	TAF1	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:112862	TEAD1	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:110319	BioGRID:113900	TRRAP	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western
BioGRID:110319	BioGRID:120901	TXLNG	BioGRID	PubMed	Two-hybrid
BioGRID:110319	BioGRID:116272	WDR5	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110319	BioGRID:113360	YY1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110319	BioGRID:113503	ZBTB17	BioGRID	PubMed	Reconstituted Complex

Function	Evidence Code	Pubs
protein binding	IPI Inferred from Physical Interaction more info	PubMed
protein complex binding	IEA Inferred from Electronic Annotation more info
protein heterodimerization activity	IEA Inferred from Electronic Annotation more info
protein homodimerization activity	IEA Inferred from Electronic Annotation more info
sequence-specific DNA binding	IEA Inferred from Electronic Annotation more info
sequence-specific DNA binding transcription factor activity	IEA Inferred from Electronic Annotation more info
transcription coactivator activity	TAS Traceable Author Statement more info	PubMed
transcription cofactor activity	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
cellular response to peptide hormone stimulus	IEA Inferred from Electronic Annotation more info
cellular response to starvation	IEA Inferred from Electronic Annotation more info
negative regulation of gene expression	IEA Inferred from Electronic Annotation more info
neuron apoptosis	IEA Inferred from Electronic Annotation more info
protein complex assembly	IEA Inferred from Electronic Annotation more info
regulation of transcription, DNA-dependent	TAS Traceable Author Statement more info	PubMed
response to axon injury	IEA Inferred from Electronic Annotation more info
response to insulin stimulus	IEA Inferred from Electronic Annotation more info
response to organic nitrogen	IEA Inferred from Electronic Annotation more info
retina development in camera-type eye	IEA Inferred from Electronic Annotation more info
transcription from RNA polymerase II promoter	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
MLL1 complex	IDA Inferred from Direct Assay more info	PubMed
PML body	IEA Inferred from Electronic Annotation more info
cytoplasm	IDA Inferred from Direct Assay more info	PubMed
dendrite	IEA Inferred from Electronic Annotation more info
NOT nucleolus	IDA Inferred from Direct Assay more info	PubMed
nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

Preferred Names: protein max

Names: protein max; helix-loop-helix zipper protein; class D basic helix-loop-helix protein 4

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NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_029830.1 RefSeqGene

Range

5001..101336

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_002382.3 → NP_002373.3 protein max isoform a

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the predominant isoform (a) which is also known as the long form.

Source sequence(s)

BC004516, BC013669, BC025685

Consensus CDS

CCDS9771.1

UniProtKB/Swiss-Prot

P61244

UniProtKB/TrEMBL

Q8TAX8

Related

ENSP00000351490, OTTHUMP00000183462, ENST00000358664, OTTHUMT00000286386

Conserved Domains (1) summary

cd00083
Location:23 – 79
Blast Score: 118

HLH; Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, ...
NM_145112.1 → NP_660087.1 protein max isoform b

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks an in-frame segment compared to variant 1, resulting in a shorter protein (isoform b, also known as the short form).

Source sequence(s)

BC013669, BC025685

Consensus CDS

CCDS9772.1

UniProtKB/Swiss-Prot

P61244

UniProtKB/TrEMBL

Q8TAX8

Related

ENSP00000351175, OTTHUMP00000183461, ENST00000358402, OTTHUMT00000286385

Conserved Domains (1) summary

cd00083
Location:12 – 70
Blast Score: 118

HLH; Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, ...
NM_145113.1 → NP_660088.1 protein max isoform c

Status: REVIEWED

Source sequence(s)

BC013669, BC025685, X60287

Consensus CDS

CCDS41965.1

UniProtKB/Swiss-Prot

P61244

UniProtKB/TrEMBL

Q8TAX8

Related

ENSP00000451907, OTTHUMP00000246626, ENST00000553928, OTTHUMT00000414535

Conserved Domains (1) summary

cd00083
Location:23 – 79
Blast Score: 116

HLH; Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, ...
NM_145114.1 → NP_660089.1 protein max isoform d

Status: REVIEWED

Description

Transcript Variant: This variant (4) differs in the 3' UTR and has multiple coding region differences, compared to variant 1. The resulting protein (isoform d) has a distinct C-terminus, compared to isoform a.

Source sequence(s)

BC013669

Consensus CDS

CCDS9774.1

Related

ENSP00000246163, OTTHUMP00000183465, ENST00000246163, OTTHUMT00000286389

Conserved Domains (1) summary

cl00081
Location:24 – 58
Blast Score: 120

HLH; Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, ...
NM_145116.1 → NP_660092.1 protein max isoform e

Status: REVIEWED

Description

Transcript Variant: This variant (5) uses an alternate splice site in the 3' coding region and lacks a downstream exon, compared to variant 1. The resulting protein (isoform e) has a distinct C-terminus, compared to isoform a.

Source sequence(s)

BC013669, X66867

Consensus CDS

CCDS9773.1

Related

ENSP00000284165, OTTHUMP00000183464, ENST00000284165, OTTHUMT00000286388

Conserved Domains (1) summary

cd00083
Location:23 – 79
Blast Score: 140

HLH; Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, ...
NM_197957.2 → NP_932061.1 protein max isoform f

Status: REVIEWED

Description

Transcript Variant: This variant (6) differs in the 3' UTR and coding sequence compared to variant 1, that causes a frameshift. The resulting isoform (f) is shorter and has a distinct C-terminus compared to isoform a.

Source sequence(s)

AI652319, AI917842, BC013669

Consensus CDS

CCDS9770.1

UniProtKB/TrEMBL

A6NH73

Related

ENSP00000342482, OTTHUMP00000183463, ENST00000341653, OTTHUMT00000286387

Conserved Domains (1) summary

cd00083
Location:23 – 57
Blast Score: 98

HLH; Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, ...

RefSeqs of Annotated Genomes: Build 37.3

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000014.8 Reference GRCh37.p5 Primary Assembly

Range

65472892..65569227, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000146.1 Alternate HuRef

Range

45642227..45738483, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AL139022.4 (3674..100009)	None
genomic	CH471061.1	EAW80898.1
		EAW80899.1
		EAW80900.1
		EAW80901.1
		EAW80902.1
		EAW80903.1
		EAW80904.1
		EAW80905.1
		EAW80906.1
genomic	X66867.1	CAA47337.1
		CAA47338.1
		CAA47339.1
genomic	X66867.1	CAA47337.1
		CAA47338.1
		CAA47339.1
mRNA	AI652319.1	None
mRNA	AI655674.1	None
mRNA	AI917842.1	None
mRNA	AK290130.1	BAF82819.1
mRNA	AK290929.1	BAF83618.1
mRNA	AK292189.1	BAF84878.1
mRNA	AK292630.1	BAF85319.1
mRNA	AK303412.1	BAG64465.1
mRNA	AL833643.1	None
mRNA	AY353088.1	AAQ57210.1
mRNA	BC003525.1	AAH03525.1
mRNA	BC004516.2	AAH04516.1
mRNA	BC013669.1	AAH13669.1
mRNA	BC025685.1	AAH25685.1
mRNA	BC027924.1	AAH27924.1
mRNA	BC036092.1	AAH36092.1
mRNA	CR542191.1	CAG46988.1
mRNA	M64240.1	AAA36200.1
		AAA36201.1
mRNA	X60287.1	CAA42827.1
other-genetic	JF432558.1	ADZ15775.1

Protein Accession	Links
Protein Accession	GenPept Link	UniProtKB Link
P61244.1	GenPept	UniProtKB/Swiss-Prot:P61244
Q6V3B1	GenPept	UniProtKB/TrEMBL:Q6V3B1
Q8IYC6	GenPept	UniProtKB/TrEMBL:Q8IYC6
Q8TAX8	GenPept	UniProtKB/TrEMBL:Q8TAX8