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P10242 (MYB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional activator Myb
Alternative name(s):
Proto-oncogene c-Myb
Gene names
Name:MYB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.

Subunit structure

Binds MYBBP1A. Interacts with HIPK2, MAF and NLK By similarity. Binds to HIPK1. Ref.15 Ref.16

Subcellular location

Nucleus Ref.16.

Induction

Negatively regulated by microRNA-155 (miR-155). Ref.18

Domain

Comprised of 3 domains; an N-terminal DNA-binding domain, a centrally located transcriptional activation domain and a C-terminal domain involved in transcriptional repression (Ref.14). Ref.14

Post-translational modification

Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation Probable. Ref.15

Phosphorylated by NLK on multiple sites, which induces proteasomal degradation By similarity. Ref.16

Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels. Ref.16

Sequence similarities

Contains 3 HTH myb-type DNA-binding domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB

embryonic digestive tract development

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20531406. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20531406. Source: BHF-UCL

positive regulation of T-helper cell differentiation

Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB

positive regulation of histone H3-K4 methylation

Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB

positive regulation of histone H3-K9 methylation

Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20484083. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.14. Source: UniProtKB

thymus development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear matrix

Non-traceable author statement Ref.12. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 18093978PubMed 20484083. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10242-1)

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: P10242-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-316: Missing.
Isoform 3 (identifier: P10242-3)

The sequence of this isoform differs from the canonical sequence as follows:
     317-350: TQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGE → LCGPLLNSDIFSDWAANWDGSLCFATYIVNQQRQ
     351-640: Missing.
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: P10242-4)

The sequence of this isoform differs from the canonical sequence as follows:
     401-401: S → SDSSSWCDLS...VKSLPFSPSQ
Isoform 5 (identifier: P10242-5)

The sequence of this isoform differs from the canonical sequence as follows:
     402-402: F → M
     403-640: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 6 (identifier: P10242-6)

The sequence of this isoform differs from the canonical sequence as follows:
     567-640: NILTSSVLMA...NAFSARTLVM → TGVQWHDFGS...LRFNGTSIRR
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 7 (identifier: P10242-7)

The sequence of this isoform differs from the canonical sequence as follows:
     314-316: Missing.
     401-401: S → SDSSSWCDLS...VKSLPFSPSQ
Isoform 8 (identifier: P10242-8)

The sequence of this isoform differs from the canonical sequence as follows:
     386-401: VKNLLEFAETLQFIDS → DSSSWCDLSS...VKSLPFSPSQ
Isoform 9 (identifier: P10242-9)

The sequence of this isoform differs from the canonical sequence as follows:
     282-316: Missing.
Isoform 10 (identifier: P10242-10)

The sequence of this isoform differs from the canonical sequence as follows:
     530-566: Missing.
Isoform 11 (identifier: P10242-11)

The sequence of this isoform differs from the canonical sequence as follows:
     317-401: Missing.
Isoform 12 (identifier: P10242-12)

The sequence of this isoform differs from the canonical sequence as follows:
     317-640: TQNHTCSYPG...NAFSARTLVM → VRLSSCA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 640640Transcriptional activator Myb
PRO_0000197048

Regions

Domain35 – 8652HTH myb-type 1
Domain87 – 14256HTH myb-type 2
Domain143 – 19351HTH myb-type 3
DNA binding63 – 8624H-T-H motif By similarity
DNA binding115 – 13824H-T-H motif By similarity
DNA binding166 – 18924H-T-H motif By similarity
Region90 – 193104Interaction with HIPK2 and NLK By similarity
Region275 – 32753Transcription activation domain (PubMed:2189102)
Region328 – 465138Negative regulatory domain By similarity
Region376 – 39722Leucine-zipper

Amino acid modifications

Modified residue4711N6-acetyllysine Ref.17
Modified residue4801N6-acetyllysine Ref.17

Natural variations

Alternative sequence282 – 31635Missing in isoform 9.
VSP_046658
Alternative sequence314 – 3163Missing in isoform 2 and isoform 7.
VSP_003293
Alternative sequence317 – 640324TQNHT…RTLVM → VRLSSCA in isoform 12.
VSP_053389
Alternative sequence317 – 40185Missing in isoform 11.
VSP_046659
Alternative sequence317 – 35034TQNHT…SCLGE → LCGPLLNSDIFSDWAANWDG SLCFATYIVNQQRQ in isoform 3.
VSP_003294
Alternative sequence351 – 640290Missing in isoform 3.
VSP_003295
Alternative sequence386 – 40116VKNLL…QFIDS → DSSSWCDLSSFEFFEEADFS PSQHHTGKALQLQQREGNGT KPAGEPSPRVNKRMLSESSL DPPKVLPPARHSTIPLVILR KKRGQASPLATGDCSSFIFA DVSSSTPKRSPVKSLPFSPS Q in isoform 8.
VSP_046660
Alternative sequence4011S → SDSSSWCDLSSFEFFEEADF SPSQHHTGKALQLQQREGNG TKPAGEPSPRVNKRMLSESS LDPPKVLPPARHSTIPLVIL RKKRGQASPLATGDCSSFIF ADVSSSTPKRSPVKSLPFSP SQ in isoform 4 and isoform 7.
VSP_003296
Alternative sequence4021F → M in isoform 5.
VSP_003297
Alternative sequence403 – 640238Missing in isoform 5.
VSP_003298
Alternative sequence530 – 56637Missing in isoform 10.
VSP_046661
Alternative sequence567 – 64074NILTS…RTLVM → TGVQWHDFGSLQPLPPGFKR FSCLSLPRSWDYRHPPPRPA NFEFLVETGFLHVGQAGLEL LTSGDLPASASQSARITGVS HRARPEYSYKLRFNGTSIRR in isoform 6.
VSP_003299
Natural variant3361T → I.
Corresponds to variant rs2229999 [ dbSNP | Ensembl ].
VAR_050188
Natural variant4221T → N.
Corresponds to variant rs2230000 [ dbSNP | Ensembl ].
VAR_050189

Experimental info

Sequence conflict5111I → F in AAA52032. Ref.1
Sequence conflict5111I → F in AY787447. Ref.6
Sequence conflict5111I → F in AY787448. Ref.6
Sequence conflict5631A → R in AAA52032. Ref.1
Sequence conflict5631A → R in AY787447. Ref.6
Sequence conflict5631A → R in AY787448. Ref.6
Isoform 4:
Sequence conflict4331L → F in CAA35503. Ref.8

Sequences

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

Last modified November 1, 1997. Version 2.
Checksum: FD5E6694020426ED

FASTA64072,341
        10         20         30         40         50         60 
MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 

        70         80         90        100        110        120 
DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 

       130        140        150        160        170        180 
HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 

       190        200        210        220        230        240 
IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 

       250        260        270        280        290        300 
NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 

       310        320        330        340        350        360 
LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD 

       370        380        390        400        410        420 
PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE NSDLEMPSLT 

       430        440        450        460        470        480 
STPLIGHKLT VTTPFHRDQT VKTQKENTVF RTPAIKRSIL ESSPRTPTPF KHALAAQEIK 

       490        500        510        520        530        540 
YGPLKMLPQT PSHLVEDLQD VIKQESDESG IVAEFQENGP PLLKKIKQEV ESPTDKSGNF 

       550        560        570        580        590        600 
FCSHHWEGDS LNTQLFTQTS PVADAPNILT SSVLMAPASE DEDNVLKAFT VPKNRSLASP 

       610        620        630        640 
LQPCSSTWEP ASCGKMEEQM TSSSQARKYV NAFSARTLVM 

« Hide

Isoform 2 [UniParc].

Checksum: 75D8144FEEC381C5
Show »

FASTA63772,032
Isoform 3 [UniParc].

Checksum: 60632631CFEE51FF
Show »

FASTA35040,620
Isoform 4 [UniParc].

Checksum: 9D11661393B1A85B
Show »

FASTA76185,475
Isoform 5 [UniParc].

Checksum: 331FC406EC1C335C
Show »

FASTA40246,065
Isoform 6 [UniParc].

Checksum: BF91C8F858EA12DF
Show »

FASTA66675,526
Isoform 7 [UniParc].

Checksum: 0F2142F19B9D4E48
Show »

FASTA75885,166
Isoform 8 [UniParc].

Checksum: 9B6C4EBD083ED7CF
Show »

FASTA74583,626
Isoform 9 [UniParc].

Checksum: 6078B295869F3BDA
Show »

FASTA60568,135
Isoform 10 [UniParc].

Checksum: 560AF3F759C690F1
Show »

FASTA60368,308
Isoform 11 [UniParc].

Checksum: D29BCA8DD3CDA8FE
Show »

FASTA55563,198
Isoform 12 [UniParc].

Checksum: 52D7B7EA3EDB98E1
Show »

FASTA32337,507

References

« Hide 'large scale' references
[1]"Human c-myb protooncogene: nucleotide sequence of cDNA and organization of the genomic locus."
Majello B., Kenyon L.C., Dalla-Favera R.
Proc. Natl. Acad. Sci. U.S.A. 83:9636-9640(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Alternative splicing of the human c-myb gene."
Westin E.H., Gorse K.M., Clarke M.F.
Oncogene 5:1117-1124(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Genome annotation of a 1.5 Mb region of human chromosome 6q23 encompassing a quantitative trait locus for fetal hemoglobin expression in adults."
Close J.P., Game L., Clark B., Bergounioux J., Gerovassili A., Thein S.L.
BMC Genomics 5:33-33(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
[4]"Characterization of the complete sequence structure of the human c-myb gene."
Westin E.H., Gorse K.M.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6).
Tissue: Liver and Placenta.
[5]Gaillard C., Perbal B.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"Complex RNA splicing produces multiple forms of c-Myb with distinct transcriptional activities."
O'Rourke J.P. Jr., Ness S.A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 8; 9; 10 AND 11), ALTERNATIVE SPLICING.
[7]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM 1).
Tissue: Testis.
[10]"Identification of a second promoter in the human c-myb proto-oncogene."
Jacobs S.M., Gorse K.M., Westin E.H.
Oncogene 9:227-235(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1).
[11]"Positive autoregulation of c-myb expression via Myb binding sites in the 5' flanking region of the human c-myb gene."
Nicolaides N.C., Gualdi R., Casadevall C., Manzella L., Calabretta B.
Mol. Cell. Biol. 11:6166-6176(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[12]"Studies of the human c-myb gene and its product in human acute leukemias."
Slamon D.J., Boone T.C., Murdock D.C., Keith D.E., Press M.F., Larson R.A., Souza L.M.
Science 233:347-351(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-640 (ISOFORMS 1 AND 12).
[13]"Identification of alternatively spliced transcripts for human c-myb: molecular cloning and sequence analysis of human c-myb exon 9A sequences."
Dasgupta P., Reddy E.P.
Oncogene 4:1419-1423(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[14]"Transcriptional activation by human c-myb and v-myb genes."
Kalkbrenner F., Guehmann S., Moelling K.
Oncogene 5:657-661(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[15]"p53 suppresses the c-Myb-induced activation of heat shock transcription factor 3."
Tanikawa J., Ichikawa-Iwata E., Kanei-Ishii C., Nakai A., Matsuzawa S., Reed J.C., Ishii S.
J. Biol. Chem. 275:15578-15585(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[16]"HIPK1 interacts with c-Myb and modulates its activity through phosphorylation."
Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M., Gabrielsen O.S.
Biochem. Biophys. Res. Commun. 388:150-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY HIPK1, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"BCL6 positively regulates AID and germinal center gene expression via repression of miR-155."
Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C., Dalla-Favera R.
J. Exp. Med. 209:2455-2465(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15024 mRNA. Translation: AAA52032.1.
X52125 mRNA. Translation: CAA36371.1.
AJ606319 mRNA. Translation: CAE55170.1.
AJ606320 mRNA. Translation: CAE55171.1.
AJ616791 mRNA. Translation: CAF04482.1.
AJ616791 mRNA. Translation: CAF04479.1.
U22376 Genomic DNA. Translation: AAB49034.1.
U22376 Genomic DNA. Translation: AAB49035.1.
U22376 Genomic DNA. Translation: AAB49036.1.
U22376 Genomic DNA. Translation: AAB49037.1.
U22376 Genomic DNA. Translation: AAB49038.1.
U22376 Genomic DNA. Translation: AAB49039.1.
AF104863 mRNA. Translation: AAC96326.1.
AY787443 mRNA. No translation available.
AY787447 mRNA. No translation available.
AY787448 mRNA. No translation available.
AY787461 mRNA. No translation available.
AY787468 mRNA. No translation available.
AL023693 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW47969.1.
CH471051 Genomic DNA. Translation: EAW47973.1.
BC064955 mRNA. Translation: AAH64955.1.
M13665 mRNA. Translation: AAA52030.1.
M13666 mRNA. Translation: AAA52031.1.
X17469 mRNA. Translation: CAA35503.1.
CCDSCCDS47481.1. [P10242-4]
CCDS47482.1. [P10242-2]
CCDS5174.1. [P10242-1]
CCDS55058.1. [P10242-7]
CCDS55059.1. [P10242-8]
CCDS55060.1. [P10242-10]
CCDS55061.1. [P10242-11]
CCDS55062.1. [P10242-9]
PIRTVHUMB. A26661.
RefSeqNP_001123644.1. NM_001130172.1. [P10242-2]
NP_001123645.1. NM_001130173.1. [P10242-4]
NP_001155128.1. NM_001161656.1. [P10242-7]
NP_001155129.1. NM_001161657.1. [P10242-11]
NP_001155130.1. NM_001161658.1. [P10242-8]
NP_001155131.1. NM_001161659.1. [P10242-10]
NP_001155132.1. NM_001161660.1. [P10242-9]
NP_005366.2. NM_005375.2. [P10242-1]
XP_006715558.1. XM_006715495.1.
UniGeneHs.606320.

3D structure databases

ProteinModelPortalP10242.
SMRP10242. Positions 38-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110687. 50 interactions.
DIPDIP-1057N.
IntActP10242. 33 interactions.
MINTMINT-6772664.
STRING9606.ENSP00000339992.

PTM databases

PhosphoSiteP10242.

Polymorphism databases

DMDM2815504.

Proteomic databases

MaxQBP10242.
PaxDbP10242.
PRIDEP10242.

Protocols and materials databases

DNASU4602.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341911; ENSP00000339992; ENSG00000118513. [P10242-4]
ENST00000367812; ENSP00000356786; ENSG00000118513. [P10242-6]
ENST00000367814; ENSP00000356788; ENSG00000118513. [P10242-1]
ENST00000430686; ENSP00000390460; ENSG00000118513.
ENST00000442647; ENSP00000410825; ENSG00000118513. [P10242-2]
ENST00000525369; ENSP00000435938; ENSG00000118513. [P10242-11]
ENST00000525477; ENSP00000437081; ENSG00000118513. [P10242-3]
ENST00000525514; ENSP00000435578; ENSG00000118513. [P10242-3]
ENST00000528774; ENSP00000434723; ENSG00000118513. [P10242-7]
ENST00000529586; ENSP00000437264; ENSG00000118513. [P10242-3]
ENST00000533384; ENSP00000432811; ENSG00000118513. [P10242-5]
ENST00000533624; ENSP00000436605; ENSG00000118513. [P10242-9]
ENST00000533808; ENSP00000435293; ENSG00000118513. [P10242-5]
ENST00000533837; ENSP00000434639; ENSG00000118513. [P10242-5]
ENST00000534044; ENSP00000435055; ENSG00000118513. [P10242-10]
ENST00000534121; ENSP00000432851; ENSG00000118513. [P10242-8]
GeneID4602.
KEGGhsa:4602.
UCSCuc003qfc.3. human. [P10242-1]
uc003qfh.3. human. [P10242-4]
uc003qfu.3. human. [P10242-2]

Organism-specific databases

CTD4602.
GeneCardsGC06P135503.
HGNCHGNC:7545. MYB.
HPACAB017704.
MIM189990. gene.
neXtProtNX_P10242.
Orphanet86849. Acute basophilic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBPA31345.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5147.
HOVERGENHBG007964.
KOK09420.
OMAHGCLPEE.
OrthoDBEOG7H791P.
PhylomeDBP10242.
TreeFamTF326257.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SignaLinkP10242.

Gene expression databases

ArrayExpressP10242.
BgeeP10242.
CleanExHS_MYB.
GenevestigatorP10242.

Family and domain databases

Gene3D1.10.10.60. 3 hits.
InterProIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR012642. Tscrpt_reg_Wos2-domain.
[Graphical view]
PfamPF09316. Cmyb_C. 1 hit.
PF07988. LMSTEN. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 3 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51294. HTH_MYB. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYB. human.
GeneWikiMYB_(gene).
GenomeRNAi4602.
NextBio17700.
PROP10242.
SOURCESearch...

Entry information

Entry nameMYB_HUMAN
AccessionPrimary (citable) accession number: P10242
Secondary accession number(s): E9PI07 expand/collapse secondary AC list , E9PLZ5, E9PNA4, E9PNL6, E9PRS2, P78391, P78392, P78525, P78526, Q14023, Q14024, Q708E4, Q708E7, Q9UE83
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 152 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM