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P61244 (MAX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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. Ref.8 Ref.10

Subcellular location

Nucleus. Cell projectiondendrite By similarity.

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. Ref.13

Sequence similarities

Belongs to the MAX family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell projection
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 8425218. Source: ProtInc

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.10. Source: UniProtKB

PML body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 15358760. Source: BHF-UCL

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15674325. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

transcription cofactor activity

Traceable author statement PubMed 8425218. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 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.
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.
Isoform 6 (identifier: P61244-6)

The sequence of this isoform differs from the canonical sequence as follows:
     58-160: ASRAQILDKA...SRKKLRMEAS → GTKMKLTLPPVFPYEHLPFPTVFCHG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 160159Protein max
PRO_0000127269

Regions

Domain23 – 7452bHLH
Region81 – 10222Leucine-zipper
Motif152 – 1565Nuclear localization signal

Amino acid modifications

Modified residue21N-acetylserine Ref.15 Ref.16 Ref.18
Modified residue21Phosphoserine Ref.12 Ref.14 Ref.16 Ref.18
Modified residue111Phosphoserine Ref.12 Ref.16 Ref.18
Modified residue661N6-acetyllysine Probable
Modified residue1531N6-acetyllysine Ref.13
Modified residue1541N6-acetyllysine Ref.13

Natural variations

Alternative sequence13 – 219Missing in isoform 2.
VSP_002117
Alternative sequence58 – 160103ASRAQ…RMEAS → LYFLFWKLCTPVLHRQSLMQ KCHTFISSYQVHKKKECKI in isoform 5.
VSP_043430
Alternative sequence58 – 160103ASRAQ…RMEAS → GTKMKLTLPPVFPYEHLPFP TVFCHG in isoform 6.
VSP_047661
Alternative sequence99 – 16062VRALE…RMEAS → GESES in isoform 3.
VSP_002118
Alternative sequence99 – 16062VRALE…RMEAS → GEHPSSWGSWPCCAPARSGF GTWACRVRASHGVCAQ in isoform 4.
VSP_043183

Experimental info

Mutagenesis661K → Q: Kept nuclear localization. Loss of nuclear localization; when associated with Q-153 and Q-154. Ref.13
Mutagenesis661K → R: Loss of acetylation, kept nuclear localization; when associated with R-153 and R-154. Ref.13
Mutagenesis1531K → Q: Loss of nuclear localization; when associated with Q-66 and Q-154. Kept nuclear localization; when associated with Q-154. Ref.13
Mutagenesis1531K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-154. Ref.13
Mutagenesis1541K → Q: Loss of nuclear localization; when associated with Q-66 and Q-153. Kept nuclear localization; when associated with Q-153. Ref.13
Mutagenesis1541K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-153. Ref.13

Secondary structure

....... 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: EB10F3137727A56F

FASTA16018,275
        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 

« Hide

Isoform 2 (Short) [UniParc] [UniParc].

Checksum: CB69F6F5F39793FA
Show »

FASTA15117,202
Isoform 3 (Delta-Max) [UniParc] [UniParc].

Checksum: 49DC1A0441FFA301
Show »

FASTA10312,099
Isoform 4 [UniParc].

Checksum: A2FFD0B98CF93275
Show »

FASTA13415,395
Isoform 5 [UniParc].

Checksum: D380F721DCF2D6C8
Show »

FASTA9611,455
Isoform 6 [UniParc].

Checksum: FE0E966237003D47
Show »

FASTA839,599

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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.
[20]"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.
CCDSCCDS41965.1. [P61244-3]
CCDS9770.1. [P61244-6]
CCDS9771.1.
CCDS9772.1. [P61244-2]
CCDS9774.1. [P61244-5]
PIRA38431.
A42611.
B38431.
S33118.
RefSeqNP_001257997.1. NM_001271068.1.
NP_002373.3. NM_002382.4. [P61244-1]
NP_660087.1. NM_145112.2. [P61244-2]
NP_660088.1. NM_145113.2. [P61244-3]
NP_660089.1. NM_145114.2. [P61244-5]
NP_932061.1. NM_197957.3. [P61244-6]
UniGeneHs.285354.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AN2X-ray2.90A22-107[»]
1HLOX-ray2.80A/B20-92[»]
1NKPX-ray1.80B/E23-102[»]
1NLWX-ray2.00B/E24-99[»]
1R05NMR-A/B22-103[»]
DisProtDP00084.
ProteinModelPortalP61244.
SMRP61244. Positions 23-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110319. 62 interactions.
DIPDIP-28145N.
IntActP61244. 43 interactions.
MINTMINT-1468374.
STRING9606.ENSP00000351490.

Chemistry

BindingDBP61244.
ChEMBLCHEMBL1250363.

PTM databases

PhosphoSiteP61244.

Polymorphism databases

DMDM47117704.

Proteomic databases

MaxQBP61244.
PaxDbP61244.
PRIDEP61244.

Protocols and materials databases

DNASU4149.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246163; ENSP00000246163; ENSG00000125952. [P61244-5]
ENST00000284165; ENSP00000284165; ENSG00000125952. [P61244-4]
ENST00000341653; ENSP00000342482; ENSG00000125952. [P61244-6]
ENST00000358402; ENSP00000351175; ENSG00000125952. [P61244-2]
ENST00000358664; ENSP00000351490; ENSG00000125952. [P61244-1]
ENST00000394606; ENSP00000378104; ENSG00000125952. [P61244-3]
ENST00000553928; ENSP00000451907; ENSG00000125952. [P61244-3]
ENST00000556979; ENSP00000452378; ENSG00000125952. [P61244-3]
GeneID4149.
KEGGhsa:4149.
UCSCuc001xie.2. human. [P61244-3]
uc001xif.2. human.
uc001xig.2. human. [P61244-2]
uc001xij.2. human. [P61244-4]
uc001xik.4. human. [P61244-5]

Organism-specific databases

CTD4149.
GeneCardsGC14M065472.
GeneReviewsMAX.
HGNCHGNC:6913. MAX.
HPACAB000328.
HPA003474.
MIM154950. gene.
neXtProtNX_P61244.
Orphanet29072. Hereditary pheochromocytoma-paraganglioma.
PharmGKBPA30656.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239807.
HOGENOMHOG000293257.
HOVERGENHBG008542.
InParanoidP61244.
KOK04453.
OMAFPYEHLP.
OrthoDBEOG7XPZ7J.
PhylomeDBP61244.
TreeFamTF318841.

Enzyme and pathway databases

SignaLinkP61244.

Gene expression databases

ArrayExpressP61244.
BgeeP61244.
CleanExHS_MAX.
GenevestigatorP61244.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAX. human.
EvolutionaryTraceP61244.
GeneWikiMAX_(gene).
GenomeRNAi4149.
NextBio16302.
PMAP-CutDBP61244.
PROP61244.
SOURCESearch...

Entry information

Entry nameMAX_HUMAN
AccessionPrimary (citable) accession number: P61244
Secondary accession number(s): A6NH73 expand/collapse secondary AC list , 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: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM